ID ADK_HUMAN STANDARD; PRT; 362 AA.
AC P55263; O00741; O00742; Q16710; Q9BTN2;
DT 01-OCT-1996 (Rel. 34, Created)
DT 30-MAY-2000 (Rel. 39, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Adenosine kinase (EC 2.7.1.20) (AK) (Adenosine 5'-phosphotransferase).
GN ADK.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A., AND SEQUENCE OF 94-133; 175-200 AND 272-289.
RC TISSUE=Liver;
RX MEDLINE=96165550; PubMed=8577746;
RA Spychala J., Datta N.S., Takabayashi K., Datta M., Fox I.H.,
RA Gribbin T., Mitchell B.S.;
RT "Cloning of human adenosine kinase cDNA: sequence similarity to
RT microbial ribokinases and fructokinases.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:1232-1237(1996).
RN [2]
RP SEQUENCE FROM N.A., AND CHARACTERIZATION.
RX MEDLINE=97075030; PubMed=8917457;
RA Singh B., Hao W., Wu Z.-C., Eigl B., Gupta R.S.;
RT "Cloning and characterization of cDNA for adenosine kinase from
RT mammalian (Chinese hamster, mouse, human and rat) species. High
RT frequency mutants of Chinese hamster ovary cells involve structural
RT alterations in the gene.";
RL Eur. J. Biochem. 241:564-571(1996).
RN [3]
RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING.
RX MEDLINE=97224402; PubMed=9070863;
RA McNally T., Helfrich R.J., Cowart M., Dorwin S.A., Meuth J.L.,
RA Idler K.B., Klute K.A., Simmer R.L., Kowaluk E.A., Halbert D.N.;
RT "Cloning and expression of the adenosine kinase gene from rat and
RT human tissues.";
RL Biochem. Biophys. Res. Commun. 231:645-650(1997).
RN [4]
RP SEQUENCE FROM N.A. (ISOFORM SHORT).
RC TISSUE=Skin;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF SHORT ISOFORM.
RX MEDLINE=99060037; PubMed=9843365;
RA Mathews I.I., Erion M.D., Ealick S.E.;
RT "Structure of human adenosine kinase at 1.5-A resolution.";
RL Biochemistry 37:15607-15620(1998).
RN [6]
RP PHOSPHORYLATION OF TYR-77.
RX MEDLINE=22107313; PubMed=12112843;
RA Maguire P.B., Wynne K.J., Harney D.F., O'Donoghue N.M., Stephens G.,
RA Fitzgerald D.J.;
RT "Identification of the phosphotyrosine proteome from thrombin
RT activated platelets.";
RL Proteomics 2:642-648(2002).
CC -!- FUNCTION: ATP dependent phosphorylation of adenosine and other
CC related nucleoside analogs to monophosphate derivatives. Serves as
CC a potential regulator of concentrations of extracellular adenosine
CC and intracellular adenine nucleotides.
CC -!- CATALYTIC ACTIVITY: ATP + adenosine = ADP + AMP.
CC -!- COFACTOR: Magnesium.
CC -!- PATHWAY: Purine salvage.
CC -!- SUBUNIT: Monomer.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P55263-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P55263-2; Sequence=VSP_004668;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highest level in placenta,
CC liver, muscle and kidney.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase pfkB family.
CC -!- CAUTION: Ref.2 sequence differs from that shown due to a
CC frameshift in position 17.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
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DR EMBL; U50196; AAA97893.1; -.
DR EMBL; U33936; AAB01689.1; ALT_FRAME.
DR EMBL; U90338; AAB50234.1; -.
DR EMBL; U90339; AAB50235.1; -.
DR EMBL; BC003568; AAH03568.1; -.
DR PIR; JC5363; JC5363.
DR PIR; JC5364; JC5364.
DR PDB; 1BX4; 13-OCT-99.
DR Genew; HGNC:257; ADK.
DR GK; P55263; -.
DR MIM; 102750; -.
DR GO; GO:0004001; F:adenosine kinase activity; TAS.
DR GO; GO:0009156; P:ribonucleoside monophosphate biosynthesis; TAS.
DR InterPro; IPR001805; Adenokinase.
DR InterPro; IPR002173; PfkB.
DR Pfam; PF00294; pfkB; 1.
DR PRINTS; PR00989; ADENOKINASE.
DR PROSITE; PS00583; PFKB_KINASES_1; FALSE_NEG.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
KW Transferase; Kinase; Purine salvage; Magnesium; Alternative splicing;
KW Phosphorylation; 3D-structure.
FT ACT_SITE 317 317
FT MOD_RES 77 77 PHOSPHORYLATION.
FT VARSPLIC 1 21 MAAAEEEPKPKKLKVEAPQAL -> MTSV (in isoform
FT Short).
FT /FTId=VSP_004668.
FT CONFLICT 21 21 L -> V (in Ref. 2).
FT CONFLICT 98 98 H -> A (IN REF. 1; AA SEQUENCE).
FT CONFLICT 133 133 N -> D (in Ref. 2).
FT CONFLICT 171 171 K -> R (in Ref. 2).
FT CONFLICT 190 190 T -> H (in Ref. 1).
FT CONFLICT 219 219 I -> F (in Ref. 4).
FT CONFLICT 273 273 S -> V (IN REF. 1; AA SEQUENCE).
FT CONFLICT 289 289 I -> N (IN REF. 1; AA SEQUENCE).
FT CONFLICT 307 307 K -> R (in Ref. 2).
FT TURN 23 24
FT STRAND 26 29
FT STRAND 33 39
FT HELIX 42 47
FT TURN 48 49
FT STRAND 54 57
FT HELIX 60 62
FT HELIX 63 72
FT STRAND 76 80
FT HELIX 82 94
FT TURN 98 99
FT STRAND 101 108
FT HELIX 111 122
FT TURN 123 124
FT STRAND 126 132
FT STRAND 139 145
FT TURN 146 147
FT STRAND 148 154
FT HELIX 156 160
FT HELIX 163 165
FT TURN 166 168
FT HELIX 170 178
FT STRAND 181 185
FT HELIX 186 190
FT TURN 191 191
FT HELIX 193 205
FT TURN 206 207
FT STRAND 209 213
FT HELIX 217 222
FT TURN 223 223
FT HELIX 224 230
FT HELIX 231 233
FT STRAND 236 240
FT HELIX 241 250
FT TURN 251 252
FT HELIX 258 266
FT TURN 267 267
FT TURN 273 274
FT STRAND 278 283
FT TURN 284 285
FT STRAND 286 291
FT STRAND 296 299
FT TURN 307 308
FT HELIX 312 327
FT TURN 328 330
FT HELIX 333 347
FT TURN 348 349
SQ SEQUENCE 362 AA; 40545 MW; 48AA4925865BFE70 CRC64;
MAAAEEEPKP KKLKVEAPQA LRENILFGMG NPLLDISAVV DKDFLDKYSL KPNDQILAED
KHKELFDELV KKFKVEYHAG GSTQNSIKVA QWMIQQPHKA ATFFGCIGID KFGEILKRKA
AEAHVDAHYY EQNEQPTGTC AACITGDNRS LIANLAAANC YKKEKHLDLE KNWMLVEKAR
VCYIAGFFLT VSPESVLKVA HHASENNRIF TLNLSAPFIS QFYKESLMKV MPYVDILFGN
ETEAATFARE QGFETKDIKE IAKKTQALPK MNSKRQRIVI FTQGRDDTIM ATESEVTAFA
VLDQDQKEII DTNGAGDAFV GGFLSQLVSD KPLTECIRAG HYAASIIIRR TGCTFPEKPD
FH
//
ID ATM_HUMAN STANDARD; PRT; 3056 AA.
AC Q13315; O15429; Q12758; Q16551; Q93007; Q9NP02; Q9UCX7;
DT 16-OCT-2001 (Rel. 40, Created)
DT 16-OCT-2001 (Rel. 40, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Serine-protein kinase ATM (EC 2.7.1.37) (Ataxia telangiectasia
DE mutated) (A-T, mutated).
GN ATM.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RX MEDLINE=96154672; PubMed=8589678;
RA Savitsky K., Sfez S., Tagle D.A., Ziv Y., Sartiel A., Collins F.S.,
RA Shiloh Y., Rotman G.;
RT "The complete sequence of the coding region of the ATM gene reveals
RT similarity to cell cycle regulators in different species.";
RL Hum. Mol. Genet. 4:2025-2032(1995).
RN [2]
RP SEQUENCE FROM N.A.
RX MEDLINE=97343327; PubMed=9199932;
RA Platzer M., Rotman G., Bauer D., Uziel T., Savitsky K., Bar-Shira A.,
RA Gilad S., Shiloh Y., Rosenthal A.;
RT "Ataxia-telangiectasia locus: sequence analysis of 184 kb of human
RT genomic DNA containing the entire ATM gene.";
RL Genome Res. 7:592-605(1997).
RN [3]
RP SEQUENCE OF 1-24 FROM N.A.
RX MEDLINE=97263790; PubMed=9108147;
RA Savitsky K., Platzer M., Uziel T., Gilad S., Sartiel A., Rosenthal A.,
RA Elroy-Stein O., Shiloh Y., Rotman G.;
RT "Ataxia-telangiectasia: structural diversity of untranslated sequences
RT suggests complex post-transcriptional regulation of ATM gene
RT expression.";
RL Nucleic Acids Res. 25:1678-1684(1997).
RN [4]
RP SEQUENCE OF 1-1369 FROM N.A., AND VARIANT AT 2546-SER--ILE-2548 DEL.
RX MEDLINE=96381439; PubMed=8789452;
RA Byrd P.J., McConville C.M., Cooper P., Parkhill J., Stankovic T.,
RA McGuire G.M., Thick J.A., Taylor A.M.R.;
RT "Mutations revealed by sequencing the 5' half of the gene for ataxia
RT telangiectasia.";
RL Hum. Mol. Genet. 5:145-149(1996).
RN [5]
RP SEQUENCE OF 1-2756 FROM N.A., AND VARIANT MCL LYS-750.
RA Rieder M.J., Livingston R.J., Daniels M.R., Montoya M.A., Chung M.-W.,
RA Miyamoto K.E., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D.,
RA Schackwitz W.S., Sherwood J.K., Witrak L.A., Nickerson D.A.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SEQUENCE OF 1349-3056 FROM N.A., AND VARIANT ASN-3003.
RX MEDLINE=96105020; PubMed=8521392;
RA Rasio D., Negrini M., Croce C.M.;
RT "Genomic organization of the ATM locus involved in ataxia-
RT telangiectasia.";
RL Cancer Res. 55:6053-6057(1995).
RN [7]
RP SEQUENCE OF 1349-3056 FROM N.A., AND VARIANTS AT 2427-LEU-ARG-2428
RP DEL; 2546-SER--ILE-2548 DEL AND SER-2860 DEL.
RC TISSUE=Fibroblast;
RX MEDLINE=95312868; PubMed=7792600;
RA Savitsky K., Bar-Shira A., Gilad S., Rotman G., Ziv Y., Vanagaite L.,
RA Tagle D.A., Smith S., Uziel T., Sfez S., Ashkenazi M., Pecker I.,
RA Frydman M., Harnik R., Patanjali S.R., Simmons A., Clines G.A.,
RA Sartiel A., Gatti R.A., Chessa L., Sanal O., Lavin M.F.,
RA Jaspers N.G.J., Taylor A.M.R., Arlett C.F., Miki T., Weissman S.M.,
RA Lovett M., Collins F.S., Shiloh Y.;
RT "A single ataxia telangiectasia gene with a product similar to PI-3
RT kinase.";
RL Science 268:1749-1753(1995).
RN [8]
RP PARTIAL SEQUENCE FROM N.A., AND VARIANTS CYS-49; ARG-1054; PHE-1420;
RP ILE-2079 AND ALA-2287.
RX MEDLINE=96275738; PubMed=8665503;
RA Vorechovsky I., Rasio D., Luo L., Monaco C., Hammarstroem L.,
RA Webster A.D.B., Zaloudik J., Barbanti-Brodano G., James M.R.,
RA Russo G., Croce C.M., Negrini M.;
RT "The ATM gene and susceptibility to breast cancer: analysis of 38
RT breast tumors reveals no evidence for mutation.";
RL Cancer Res. 56:2726-2732(1996).
RN [9]
RP PHOSPHORYLATION.
RX MEDLINE=97126018; PubMed=8969240;
RA Chen G., Lee E.Y.-H.P.;
RT "The product of the ATM gene is a 370-kDa nuclear phosphoprotein.";
RL J. Biol. Chem. 271:33693-33697(1996).
RN [10]
RP SUBCELLULAR LOCATION.
RX MEDLINE=97203148; PubMed=9050866;
RA Brown K.D., Ziv Y., Sadanandan S.N., Chessa L., Collins F.S.,
RA Shiloh Y., Tagle D.A.;
RT "The ataxia-telangiectasia gene product, a constitutively expressed
RT nuclear protein that is not up-regulated following genome damage.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:1840-1845(1997).
RN [11]
RP SUBCELLULAR LOCATION, AND VARIANTS AT 2546-SER--ILE-2548 DEL AND
RP TYR-2824.
RX MEDLINE=97294602; PubMed=9150358;
RA Watters D., Khanna K.K., Beamish H., Birrell G., Spring K., Kedar P.,
RA Gatei M., Stenzel D., Hobson K., Kozlov S., Zhang N., Farrell A.,
RA Ramsay J., Gatti R.A., Lavin M.F.;
RT "Cellular localisation of the ataxia-telangiectasia (ATM) gene product
RT and discrimination between mutated and normal forms.";
RL Oncogene 14:1911-1921(1997).
RN [12]
RP KINASE ACTIVITY.
RX MEDLINE=97141775; PubMed=8988033;
RA Jung M., Kondratyev A., Lee S.A., Dimtchev A., Dritschilo A.;
RT "ATM gene product phosphorylates I kappa B-alpha.";
RL Cancer Res. 57:24-27(1997).
RN [13]
RP C-ABL BINDING.
RX MEDLINE=97311400; PubMed=9168117;
RA Shafman T., Khanna K.K., Kedar P., Spring K., Kozlov S., Yen T.,
RA Hobson K., Gatei M., Zhang N., Watters D., Egerton M., Shiloh Y.,
RA Kharbanda S., Kufe D., Lavin M.F.;
RT "Interaction between ATM protein and c-Abl in response to DNA
RT damage.";
RL Nature 387:520-523(1997).
RN [14]
RP P53 BINDING, AND KINASE ACTIVITY.
RX MEDLINE=99057351; PubMed=9843217;
RA Khanna K.K., Keating K.E., Kozlov S., Scott S., Gatei M., Hobson K.,
RA Taya Y., Gabrielli B., Chan D., Lees-Miller S.P., Lavin M.F.;
RT "ATM associates with and phosphorylates p53: mapping the region of
RT interaction.";
RL Nat. Genet. 20:398-400(1998).
RN [15]
RP BETA-ADAPTIN BINDING.
RX MEDLINE=98374320; PubMed=9707615;
RA Lim D.-S., Kirsch D.G., Canman C.E., Ahn J.-H., Ziv Y., Newman L.S.,
RA Darnell R.B., Shiloh Y., Kastan M.B.;
RT "ATM binds to beta-adaptin in cytoplasmic vesicles.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:10146-10151(1998).
RN [16]
RP PHOSPHORYLATION OF P53.
RX MEDLINE=98404273; PubMed=9733514;
RA Banin S., Moyal L., Shieh S.-Y., Taya Y., Anderson C.W., Chessa L.,
RA Smorodinsky N.I., Prives C., Reiss Y., Shiloh Y., Ziv Y.;
RT "Enhanced phosphorylation of p53 by ATM in response to DNA damage.";
RL Science 281:1674-1677(1998).
RN [17]
RP PHOSPHORYLATION OF P53, AND MUTAGENESIS OF ASP-2870 AND ASN-2875.
RX MEDLINE=98404274; PubMed=9733515;
RA Canman C.E., Lim D.-S., Cimprich K.A., Taya Y., Tamai K.,
RA Sakaguchi K., Appella E., Kastan M.B., Siliciano J.D.;
RT "Activation of the ATM kinase by ionizing radiation and
RT phosphorylation of p53.";
RL Science 281:1677-1679(1998).
RN [18]
RP DNA BINDING.
RX MEDLINE=99432198; PubMed=10500142;
RA Smith G.C.M., Cary R.B., Lakin N.D., Hann B.C., Teo S.-H., Chen D.J.,
RA Jackson S.P.;
RT "Purification and DNA binding properties of the ataxia-telangiectasia
RT gene product ATM.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:11134-11139(1999).
RN [19]
RP PHOSPHORYLATION OF BRCA1.
RX MEDLINE=20018333; PubMed=10550055;
RA Cortez D., Wang Y., Qin J., Elledge S.J.;
RT "Requirement of ATM-dependent phosphorylation of brca1 in the DNA
RT damage response to double-strand breaks.";
RL Science 286:1162-1166(1999).
RN [20]
RP IDENTIFICATION OF ATM AS MEMBER OF BASC.
RX MEDLINE=20245492; PubMed=10783165;
RA Wang Y., Cortez D., Yazdi P., Neff N., Elledge S.J., Qin J.;
RT "BASC, a super complex of BRCA1-associated proteins involved in the
RT recognition and repair of aberrant DNA structures.";
RL Genes Dev. 14:927-939(2000).
RN [21]
RP PHOSPHORYLATION OF NIBRIN.
RX MEDLINE=20227312; PubMed=10766245;
RA Lim D.-S., Kim S.-T., Xu B., Maser R.S., Lin J., Petrini J.H.J.,
RA Kastan M.B.;
RT "ATM phosphorylates p95/nbs1 in an S-phase checkpoint pathway.";
RL Nature 404:613-617(2000).
RN [22]
RP PHOSPHORYLATION OF NIBRIN.
RX MEDLINE=20296355; PubMed=10839545;
RA Wu X., Ranganathan V., Weisman D.S., Heine W.F., Ciccone D.N.,
RA O'Neill T.B., Crick K.E., Pierce K.A., Lane W.S., Rathbun G.,
RA Livingston D.M., Weaver D.T.;
RT "ATM phosphorylation of Nijmegen breakage syndrome protein is required
RT in a DNA damage response.";
RL Nature 405:477-482(2000).
RN [23]
RP PHOSPHORYLATION OF NIBRIN.
RX MEDLINE=20264381; PubMed=10802669;
RA Gatei M., Young D., Cerosaletti K.M., Desai-Mehta A., Spring K.,
RA Kozlov S., Lavin M.F., Gatti R.A., Concannon P., Khanna K.K.;
RT "ATM-dependent phosphorylation of nibrin in response to radiation
RT exposure.";
RL Nat. Genet. 25:115-119(2000).
RN [24]
RP PHOSPHORYLATION OF CTIP.
RX MEDLINE=20365735; PubMed=10910365;
RA Li S., Ting N.S.Y., Zheng L., Chen P.-L., Ziv Y., Shiloh Y.,
RA Lee E.Y.-H.P., Lee W.-H.;
RT "Functional link of BRCA1 and ataxia telangiectasia gene product in
RT DNA damage response.";
RL Nature 406:210-215(2000).
RN [25]
RP PHOSPHORYLATION OF TERF1.
RX MEDLINE=21369915; PubMed=11375976;
RA Kishi S., Zhou X.Z., Ziv Y., Khoo C., Hill D.E., Shiloh Y., Lu K.P.;
RT "Telomeric protein Pin2/TRF1 as an important ATM target in response to
RT double strand DNA breaks.";
RL J. Biol. Chem. 276:29282-29291(2001).
RN [26]
RP PHOSPHORYLATION BY ARK5.
RX MEDLINE=22393479; PubMed=12409306;
RA Suzuki A., Kusakai G.-I., Kishimoto A., Lu J., Ogura T., Lavin M.F.,
RA Esumi H.;
RT "Identification of a novel protein kinase mediating Akt survival
RT signaling to the ATM protein.";
RL J. Biol. Chem. 278:48-53(2003).
RN [27]
RP VARIANTS AT GLY-2424; 2546-SER--ILE-2548 DEL AND CYS-2827.
RX MEDLINE=96335701; PubMed=8755918;
RA McConville C.M., Stankovic T., Byrd P.J., McGuire G.M., Yao Q.-Y.,
RA Lennox G.G., Taylor A.M.R.;
RT "Mutations associated with variant phenotypes in
RT ataxia-telangiectasia.";
RL Am. J. Hum. Genet. 59:320-330(1996).
RN [28]
RP VARIANT AT 2546-SER--ILE-2548 DEL, AND VARIANT ILE-2438.
RX MEDLINE=96404417; PubMed=8808599;
RA Wright J., Teraoka S., Onengut S., Tolun A., Gatti R.A., Ochs H.D.,
RA Concannon P.;
RT "A high frequency of distinct ATM gene mutations in ataxia-
RT telangiectasia.";
RL Am. J. Hum. Genet. 59:839-846(1996).
RN [29]
RP VARIANTS AT 705-PHE--PRO-707 AND 2546-SER--ILE-2548 DEL, AND
RP VARIANTS CYS-49; LEU-858; ARG-1054; PHE-1420 AND ARG-1691.
RX MEDLINE=96390593; PubMed=8797579;
RA Vorechovsky I., Luo L., Lindblom A., Negrini M., Webster A.D.B.,
RA Croce C.M., Hammarstroem L.;
RT "ATM mutations in cancer families.";
RL Cancer Res. 56:4130-4133(1996).
RN [30]
RP VARIANT AT 705-PHE--PRO-707, AND VARIANTS LEU-858 AND ARG-1054.
RX MEDLINE=97196780; PubMed=9043869;
RA Vorechovsky I., Luo L., Prudente S., Chessa L., Russo G., Kanariou M.,
RA James M.R., Negrini M., Webster A.D.B., Hammarstroem L.;
RT "Exon-scanning mutation analysis of the ATM gene in patients with
RT ataxia-telangiectasia.";
RL Eur. J. Hum. Genet. 4:352-355(1996).
RN [31]
RP VARIANT AT ARG-2867.
RX MEDLINE=96305462; PubMed=8698354;
RA Baumer A., Bernthaler U., Wolz W., Hoehn H., Schindler D.;
RT "New mutations in the ataxia telangiectasia gene.";
RL Hum. Genet. 98:246-249(1996).
RN [32]
RP VARIANTS AT 2427-LEU-ARG-2428 DEL; 2546-SER--ILE-2548 DEL; SER-2860
RP DEL AND GLY-2904.
RX MEDLINE=96254972; PubMed=8845835;
RA Gilad S., Khosravi R., Shkedy D., Uziel T., Ziv Y., Savitsky K.,
RA Rotman G., Smith S., Chessa L., Jorgensen T.J., Harnik R., Frydman M.,
RA Sanal O., Portnoi S., Goldwicz Z., Jaspers N.G.J., Gatti R.A.,
RA Lenoir G., Lavin M.F., Tatsumi K., Wegner R.-D., Shiloh Y.,
RA Bar-Shira A.;
RT "Predominance of null mutations in ataxia-telangiectasia.";
RL Hum. Mol. Genet. 5:433-439(1996).
RN [33]
RP VARIANTS TPLL THR-1407; HIS-1682; HIS-1910; LYS-2164; SER-2396;
RP GLY-2424; PRO-2442; 2546-SER--ILE-2548 DEL; ALA-2695; ARG-2722;
RP VAL-2725; LEU-2732; LYS-2810 DEL; 2871-ARG-HIS-2872 DELINS SER
RP AND VAL-2890, AND VARIANTS BNHL VAL-1040; SER-1463 AND CYS-2832.
RX MEDLINE=97434220; PubMed=9288106;
RA Vorechovsky I., Luo L., Dyer M.J.S., Catovsky D., Amlot P.L.,
RA Yaxley J.C., Foroni L., Hammarstroem L., Webster A.D.B.,
RA Yuille M.A.R.;
RT "Clustering of missense mutations in the ataxia-telangiectasia gene in
RT a sporadic T-cell leukaemia.";
RL Nat. Genet. 17:96-99(1997).
RN [34]
RP VARIANTS TPLL GLY-2725; PRO-3006 AND CYS-3008.
RX MEDLINE=97475207; PubMed=9334731;
RA Stilgenbauer S., Schaffner C., Litterst A., Liebisch P., Gilad S.,
RA Bar-Shira A., James M.R., Lichter P., Doehner H.;
RT "Biallelic mutations in the ATM gene in T-prolymphocytic leukemia.";
RL Nat. Med. 3:1155-1159(1997).
RN [35]
RP VARIANT AT CYS-2832.
RX MEDLINE=98107941; PubMed=9443866;
RA Telatar M., Teraoka S., Wang Z., Chun H.H., Liang T.,
RA Castellvi-Bel S., Udar N., Borresen-Dale A.-L., Chessa L.,
RA Bernatowska-Matuszkiewicz E., Porras O., Watanabe M., Junker A.,
RA Concannon P., Gatti R.A.;
RT "Ataxia-telangiectasia: identification and detection of founder-effect
RT mutations in the ATM gene in ethnic populations.";
RL Am. J. Hum. Genet. 62:86-97(1998).
RN [36]
RP VARIANTS AT LEU-292; ASP-768; GLN-1001; ARG-1691; ILE-1743; GLY-2424;
RP 2427-LEU-ARG-2428 DEL; 2546-SER--ILE-2548 DEL; ASP-2554; GLY-2668
RP AND CYS-2827.
RX MEDLINE=98130536; PubMed=9463314;
RA Stankovic T., Kidd A.M.J., Sutcliffe A., McGuire G.M., Robinson P.,
RA Weber P., Bedenham T., Bradwell A.R., Easton D.F., Lennox G.G.,
RA Haites N., Byrd P.J., Taylor A.M.R.;
RT "ATM mutations and phenotypes in ataxia-telangiectasia families in the
RT British Isles: expression of mutant ATM and the risk of leukemia,
RT lymphoma, and breast cancer.";
RL Am. J. Hum. Genet. 62:334-345(1998).
RN [37]
RP VARIANT AT 1812-ALA-PHE-1813 DELINS VAL.
RX MEDLINE=98163439; PubMed=9497252;
RA Gilad S., Chessa L., Khosravi R., Russell P., Galanty Y., Piane M.,
RA Gatti R.A., Jorgensen T.J., Shiloh Y., Bar-Shira A.;
RT "Genotype-phenotype relationships in ataxia-telangiectasia and
RT variants.";
RL Am. J. Hum. Genet. 62:551-561(1998).
RN [38]
RP VARIANT AT PRO-2656.
RX MEDLINE=98111350; PubMed=9450874;
RA Toyoshima M., Hara T., Zhang H., Yamamoto T., Akaboshi S., Nanba E.,
RA Ohno K., Hori N., Sato K., Takeshita K.;
RT "Ataxia-telangiectasia without immunodeficiency: novel point mutations
RT within and adjacent to the phosphatidylinositol 3-kinase-like
RT domain.";
RL Am. J. Med. Genet. 75:141-144(1998).
RN [39]
RP VARIANT TPLL GLY-2486.
RX MEDLINE=98241437; PubMed=9573030;
RA Stoppa-Lyonnet D., Soulier J., Lauge A., Dastot H., Garand R.,
RA Sigaux F., Stern M.-H.;
RT "Inactivation of the ATM gene in T-cell prolymphocytic leukemias.";
RL Blood 91:3920-3926(1998).
RN [40]
RP VARIANTS AT 2855-ARG-ILE-2856 AND CYS-3008, AND VARIANT VAL-1853.
RX MEDLINE=99091900; PubMed=9872980;
RA Hacia J.G., Sun B., Hunt N., Edgemon K., Mosbrook D., Robbins C.,
RA Fodor S.P.A., Tagle D.A., Collins F.S.;
RT "Strategies for mutational analysis of the large multiexon ATM gene
RT using high-density oligonucleotide arrays.";
RL Genome Res. 8:1245-1258(1998).
RN [41]
RP VARIANT AT 2625-GLU-PRO-2626.
RX MEDLINE=98180886; PubMed=9521587;
RA van Belzen M.J., Hiel J.A.P., Weemaes C.M.R., Gabreeels F.J.M.,
RA van Engelen B.G.M., Smeets D.F.C.M., van den Heuvel L.P.W.J.;
RT "A double missense mutation in the ATM gene of a Dutch family with
RT ataxia telangiectasia.";
RL Hum. Genet. 102:187-191(1998).
RN [42]
RP VARIANT AT LEU-2829, AND VARIANTS GLU-126; ASP-514 AND ASN-1853.
RX MEDLINE=98375694; PubMed=9711876;
RA Sasaki T., Tian H., Kukita Y., Inazuka M., Tahira T., Imai T.,
RA Yamauchi M., Saito T., Hori T., Hashimoto-Tamaoki T., Komatsu K.,
RA Nikaido O., Hayashi K.;
RT "ATM mutations in patients with ataxia telangiectasia screened by a
RT hierarchical strategy.";
RL Hum. Mutat. 12:186-195(1998).
RN [43]
RP VARIANTS AT ASP-1091 AND ARG-1566, AND VARIANTS LEU-858 AND ARG-1054.
RX MEDLINE=99006895; PubMed=9792409;
RA Broeks A., de Klein A., Floore A.N., Muijtjens M., Kleijer W.J.,
RA Jaspers N.G.J., van 't Veer L.J.;
RT "ATM germline mutations in classical ataxia-telangiectasia patients in
RT the Dutch population.";
RL Hum. Mutat. 12:330-337(1998).
RN [44]
RP VARIANTS AT ARG-2491 AND GLY-2909.
RX MEDLINE=99006896; PubMed=9792410;
RA Fukao T., Song X.-Q., Yoshida T., Tashita H., Kaneko H., Teramoto T.,
RA Inoue R., Katamura K., Mayumi M., Hiratani M., Taniguchi N., Arai J.,
RA Wakiguchi H., Bar-Shira A., Shiloh Y., Kondo N.;
RT "Ataxia-telangiectasia in the Japanese population: identification of
RT R1917X, W2491R, R2909G, IVS33+2T-->A, and 7883del5, the latter two
RT being relatively common mutations.";
RL Hum. Mutat. 12:338-343(1998).
RN [45]
RP VARIANTS TPLL GLY-2139; VAL-2890 AND CYS-3008.
RX MEDLINE=98147367; PubMed=9488043;
RA Yuille M.A.R., Coignet L.J.A., Abraham S.M., Yaqub F., Luo L.,
RA Matutes E., Brito-Babapulle V., Vorechovsky I., Dyer M.J.S.,
RA Catovsky D.;
RT "ATM is usually rearranged in T-cell prolymphocytic leukaemia.";
RL Oncogene 16:789-796(1998).
RN [46]
RP ERRATUM.
RA Yuille M.A.R., Coignet L.J.A., Abraham S.M., Yaqub F., Luo L.,
RA Matutes E., Brito-Babapulle V., Vorechovsky I., Dyer M.J.S.,
RA Catovsky D.;
RL Oncogene 16:2955-2955(1998).
RN [47]
RP VARIANTS BCLL VAL-1853; ARG-1953; PRO-2420; HIS-3008 AND ASN-3018,
RP VARIANTS MCL LYS-2418 INS AND GLY-2423, AND VARIANT ASN-1853.
RX MEDLINE=99326327; PubMed=10397742;
RA Schaffner C., Stilgenbauer S., Rappold G.A., Doehner H., Lichter P.;
RT "Somatic ATM mutations indicate a pathogenic role of ATM in B-cell
RT chronic lymphocytic leukemia.";
RL Blood 94:748-753(1999).
RN [48]
RP VARIANTS BCLL CYS-332; ARG-1691 AND GLY-2424.
RX MEDLINE=99107196; PubMed=9892178;
RA Bullrich F., Rasio D., Kitada S., Starostik P., Kipps T., Keating M.,
RA Albitar M., Reed J.C., Croce C.M.;
RT "ATM mutations in B-cell chronic lymphocytic leukemia.";
RL Cancer Res. 59:24-27(1999).
RN [49]
RP VARIANT AT PRO-1465.
RX MEDLINE=99250766; PubMed=10234507;
RA Izatt L., Vessey C., Hodgson S.V., Solomon E.;
RT "Rapid and efficient ATM mutation detection by fluorescent chemical
RT cleavage of mismatch: identification of four novel mutations.";
RL Eur. J. Hum. Genet. 7:310-320(1999).
RN [50]
RP VARIANTS CYS-49; LEU-182; PRO-707; LEU-858; PHE-1420; ALA-1570;
RP ASN-1853 AND SER-2765.
RX MEDLINE=20005806; PubMed=10534763;
RA Izatt L., Greenman J., Hodgson S.V., Ellis D., Watts S., Scott G.,
RA Jacobs C., Liebmann R., Zvelebil M.J., Mathew C., Solomon E.;
RT "Identification of germline missense mutations and rare allelic
RT variants in the ATM gene in early-onset breast cancer.";
RL Genes Chromosomes Cancer 26:286-294(1999).
RN [51]
RP VARIANTS AT SER-570; CYS-785; GLY-1913; GLY-2016; ASP-2067; CYS-2227;
RP ASP-2470; VAL-2662 DEL; PRO-2849 AND ARG-2867, AND VARIANTS CYS-49;
RP LEU-858; ARG-1054; ASN-1853 AND VAL-1853.
RX MEDLINE=99105918; PubMed=9887333;
RA Sandoval N., Platzer M., Rosenthal A., Doerk T., Bendix R.,
RA Skawran B., Stuhrmann M., Wegner R.-D., Sperling K., Banin S.,
RA Shiloh Y., Baumer A., Bernthaler U., Sennefelder H., Brohm M.,
RA Weber B.H.F., Schindler D.;
RT "Characterization of ATM gene mutations in 66 ataxia telangiectasia
RT families.";
RL Hum. Mol. Genet. 8:69-79(1999).
RN [52]
RP VARIANTS AT, AND VARIANTS ASN-1454 AND ASN-1853.
RX MEDLINE=99355715; PubMed=10425038;
RA Castellvi-Bel S., Sheikhavandi S., Telatar M., Tai L.-Q., Hwang M.J.,
RA Wang Z., Yang Z., Cheng R., Gatti R.A.;
RT "New mutations, polymorphisms, and rare variants in the ATM gene
RT detected by a novel SSCP strategy.";
RL Hum. Mutat. 14:156-162(1999).
RN [53]
RP VARIANTS BCLL THR-350; THR-352; ARG-1054; LYS-2274 AND ALA-2695, AND
RP VARIANT ASN-3003.
RX MEDLINE=99146552; PubMed=10023947;
RA Stankovic T., Weber P., Stewart G., Bedenham T., Murray J., Byrd P.J.,
RA Moss P.A.H., Taylor A.M.R.;
RT "Inactivation of ataxia telangiectasia mutated gene in B-cell chronic
RT lymphocytic leukaemia.";
RL Lancet 353:26-29(1999).
RN [54]
RP VARIANT ARG-1054.
RX MEDLINE=99231468; PubMed=10217116;
RA Vorechovsky I., Luo L., Ortmann E., Steinmann D., Doerk T.;
RT "Missense mutations at ATM gene and cancer risk.";
RL Lancet 353:1276-1276(1999).
RN [55]
RP ERRATUM.
RA Vorechovsky I., Luo L., Ortmann E., Steinmann D., Doerk T.;
RL Lancet 354:780-780(1999).
RN [56]
RP VARIANTS AT GLU-224; VAL-323; PRO-1420; CYS-2218; 2546-SER--ILE-2548
RP DEL; GLN-2625; CYS-2832; 2855-ARG-ILE-2856 AND CYS-3008, AND VARIANTS
RP VAL-1853 AND ILE-2438.
RX MEDLINE=20275351; PubMed=10817650;
RA Li A., Swift M.;
RT "Mutations at the ataxia-telangiectasia locus and clinical phenotypes
RT of A-T patients.";
RL Am. J. Med. Genet. 92:170-177(2000).
RN [57]
RP VARIANTS AT.
RX MEDLINE=20334897; PubMed=10873394;
RA Becker-Catania S.G., Chen G., Hwang M.J., Wang Z., Sun X., Sanal O.,
RA Bernatowska-Matuszkiewicz E., Chessa L., Lee E.Y.-H.P., Gatti R.A.;
RT "Ataxia-telangiectasia: phenotype/genotype studies of ATM protein
RT expression, mutations, and radiosensitivity.";
RL Mol. Genet. Metab. 70:122-133(2000).
RN [58]
RP VARIANTS MCL LYS-750; LYS-2418 INS; GLY-2423 AND CYS-3008.
RX MEDLINE=20183964; PubMed=10706620;
RA Schaffner C., Idler I., Stilgenbauer S., Doehner H., Lichter P.;
RT "Mantle cell lymphoma is characterized by inactivation of the ATM
RT gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:2773-2778(2000).
CC -!- FUNCTION: Involved in signal transduction, cell cycle control and
CC DNA repair. May function as a tumor suppressor. Necessary for
CC activation of ABL1 and SAPK. Phosphorylates p53, NFKBIA, BRCA1,
CC CTIP, NIBRIN (NBS1), TERF1, and RAD9. May play a role in vesicle
CC and/or protein transport. Inhibited by wortmaninn. Could play a
CC role in T-cell development, gonad and neurological function.
CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC -!- SUBUNIT: Exists in monomeric and tetrameric state. Binds DNA ends,
CC P53, ABL1, BRCA1, NIBRIN (NBS1) and TERF1. Part of the BRCA1-
CC associated genome surveillance complex (BASC), which contains
CC BRCA1, MSH2, MSH6, MLH1, ATM, BLM, PMS2 and the RAD50-MRE11-NBS1
CC protein complex. This association could be a dynamic process
CC changing throughout the cell cycle and within subnuclear domains.
CC -!- SUBCELLULAR LOCATION: Primarily nuclear. Found also in endocytic
CC vesicles in association with beta-adaptin.
CC -!- TISSUE SPECIFICITY: Found in pancreas, kidney, skeletal muscle,
CC liver, lung, placenta, brain, heart, spleen, thymus, testis,
CC ovary, small intestine, colon and leukocytes.
CC -!- INDUCTION: By ionizing radiation.
CC -!- PTM: Phosphorylated by ARK5.
CC -!- DISEASE: Defects in ATM are the cause of ataxia talangiectasia
CC (AT) [MIM:208900]; also known as Louis-Bar syndrome, which
CC includes four complementation groups: A, C, D and E. This rare
CC recessive disorder is characterized by progressive cerebellar
CC ataxia, dilation of the blood vessels in the conjunctiva and
CC eyeballs, immunodeficiency, growth retardation and sexual
CC immaturity. AT patients have a strong predisposition to cancer;
CC about 30% of patients develop tumors, particularly lymphomas and
CC leukemias. Cells from affected individuals are highly sensitive to
CC damage by ionizing radiation and resistant to inhibition of DNA
CC synthesis following irradiation.
CC -!- DISEASE: Defects in ATM contribute to T-cell acute lymphoblastic
CC leukemia (TALL) and T-prolymphocytic leukemia (TPLL). TPLL is
CC characterized by a high white blood cell count, with a
CC predominance of prolymphocytes, marked splenomegaly,
CC lymphadenopathy, skin lesions and serous effusion. The clinical
CC course is highly aggressive, with poor response to chemoterapy and
CC short survival time. TPLL occurs both in adults as a sporadic
CC disease and in younger AT patients.
CC -!- DISEASE: Defects in ATM contribute to B-cell non-Hodgkin's
CC lymphomas (BNHL), including mantle cell lymphoma (MCL).
CC -!- DISEASE: Defects in ATM contribute to B-cell chronic lymphocytic
CC leukemia (BCLL). BCLL is the commonest form of leukemia in the
CC elderly. It is characterized by the accumulation of mature CD5+ B
CC lymphocytes, lymphadenopathy, immunodeficiency and bone marrow
CC failure.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC -!- DATABASE: NAME=Ataxia talangiectasia mutation db;
CC WWW="http://www.vmresearch.org/atm.htm".
CC -!- DATABASE: NAME=Atlas Genet. Cytogenet. Oncol. Haematol.;
CC WWW="http://www.infobiogen.fr/services/chromcancer/Genes/ATM123.html".
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; U33841; AAC50289.1; -.
DR EMBL; U82828; AAB65827.1; -.
DR EMBL; U67092; AAC51298.1; -.
DR EMBL; AY220758; AAO26044.1; -.
DR EMBL; U55757; AAB38309.1; -.
DR EMBL; U55704; AAB38309.1; JOINED.
DR EMBL; U55705; AAB38309.1; JOINED.
DR EMBL; U55707; AAB38309.1; JOINED.
DR EMBL; U55708; AAB38309.1; JOINED.
DR EMBL; U55709; AAB38309.1; JOINED.
DR EMBL; U55710; AAB38309.1; JOINED.
DR EMBL; U55711; AAB38309.1; JOINED.
DR EMBL; U55712; AAB38309.1; JOINED.
DR EMBL; U55713; AAB38309.1; JOINED.
DR EMBL; U55714; AAB38309.1; JOINED.
DR EMBL; U55715; AAB38309.1; JOINED.
DR EMBL; U55716; AAB38309.1; JOINED.
DR EMBL; U55717; AAB38309.1; JOINED.
DR EMBL; U55718; AAB38309.1; JOINED.
DR EMBL; U55719; AAB38309.1; JOINED.
DR EMBL; U55720; AAB38309.1; JOINED.
DR EMBL; U55721; AAB38309.1; JOINED.
DR EMBL; U55722; AAB38309.1; JOINED.
DR EMBL; U55723; AAB38309.1; JOINED.
DR EMBL; U55724; AAB38309.1; JOINED.
DR EMBL; U55725; AAB38309.1; JOINED.
DR EMBL; U55726; AAB38309.1; JOINED.
DR EMBL; U55727; AAB38309.1; JOINED.
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DR EMBL; U55730; AAB38309.1; JOINED.
DR EMBL; U55731; AAB38309.1; JOINED.
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DR EMBL; U55749; AAB38309.1; JOINED.
DR EMBL; U55750; AAB38309.1; JOINED.
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DR EMBL; U55756; AAB38309.1; JOINED.
DR EMBL; U55757; AAB38310.1; -.
DR EMBL; U55726; AAB38310.1; JOINED.
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DR EMBL; U55734; AAB38310.1; JOINED.
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DR EMBL; U55750; AAB38310.1; JOINED.
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DR EMBL; U55753; AAB38310.1; JOINED.
DR EMBL; U55754; AAB38310.1; JOINED.
DR EMBL; U55755; AAB38310.1; JOINED.
DR EMBL; U55756; AAB38310.1; JOINED.
DR EMBL; U26455; AAA86520.1; -.
DR EMBL; X91196; CAA62603.1; -.
DR PIR; A43100; A43100.
DR Genew; HGNC:795; ATM.
DR GK; Q13315; -.
DR MIM; 607585; -.
DR MIM; 208900; -.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; TAS.
DR GO; GO:0006281; P:DNA repair; TAS.
DR GO; GO:0007131; P:meiotic recombination; TAS.
DR GO; GO:0000074; P:regulation of cell cycle; TAS.
DR GO; GO:0007165; P:signal transduction; TAS.
DR InterPro; IPR003151; FAT.
DR InterPro; IPR003152; FATC.
DR InterPro; IPR000403; PI3_PI4_kinase.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM00146; PI3Kc; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
KW Transferase; Kinase; Nuclear protein; Cell cycle; DNA repair;
KW DNA-binding; Phosphorylation; Polymorphism; Disease mutation;
KW Anti-oncogene.
FT DOMAIN 1373 1382 C-ABL-BINDING.
FT DOMAIN 1966 2566 FAT.
FT DOMAIN 2712 3056 PI3K/PI4K.
FT VARIANT 49 49 S -> C (in dbSNP:1800054).
FT /FTId=VAR_010798.
FT VARIANT 126 126 D -> E.
FT /FTId=VAR_010799.
FT VARIANT 182 182 V -> L.
FT /FTId=VAR_010800.
FT VARIANT 224 224 K -> E (in AT).
FT /FTId=VAR_010801.
FT VARIANT 292 292 P -> L (in AT; associated with lymphoma).
FT /FTId=VAR_010802.
FT VARIANT 323 323 I -> V (in AT).
FT /FTId=VAR_010803.
FT VARIANT 332 332 Y -> C (in B-cell chronic lymphocytic
FT leukemia).
FT /FTId=VAR_010804.
FT VARIANT 350 350 A -> T (in B-cell chronic lymphocytic
FT leukemia).
FT /FTId=VAR_010805.
FT VARIANT 352 352 I -> T (in B-cell chronic lymphocytic
FT leukemia).
FT /FTId=VAR_010806.
FT VARIANT 514 514 G -> D.
FT /FTId=VAR_010807.
FT VARIANT 570 570 F -> S (in AT).
FT /FTId=VAR_010808.
FT VARIANT 705 707 YSS -> FIP (in AT; might be associated
FT with susceptibility to cancer).
FT /FTId=VAR_010809.
FT VARIANT 707 707 S -> P.
FT /FTId=VAR_010810.
FT VARIANT 750 750 N -> K (in mantle cell lymphoma).
FT /FTId=VAR_010811.
FT VARIANT 768 768 N -> D (in AT).
FT /FTId=VAR_010812.
FT VARIANT 785 785 R -> C (in AT).
FT /FTId=VAR_010813.
FT VARIANT 858 858 F -> L (rare polymorphism;
FT dbSNP:1800056).
FT /FTId=VAR_010814.
FT VARIANT 950 950 L -> R (in AT).
FT /FTId=VAR_010815.
FT VARIANT 1001 1001 L -> Q (in AT; associated with T-cell
FT acute lymphoblastic leukemia).
FT /FTId=VAR_010816.
FT VARIANT 1040 1040 M -> V (in B-cell non-Hodgkin's
FT lymphoma).
FT /FTId=VAR_010817.
FT VARIANT 1054 1054 P -> R (in dbSNP:1800057).
FT /FTId=VAR_010818.
FT VARIANT 1082 1082 H -> L (in AT).
FT /FTId=VAR_010819.
FT VARIANT 1091 1091 E -> D (in AT).
FT /FTId=VAR_010820.
FT VARIANT 1407 1407 I -> T (in T-prolymphocytic leukemia).
FT /FTId=VAR_010821.
FT VARIANT 1420 1420 L -> F (rare polymorphism;
FT dbSNP:1800058).
FT /FTId=VAR_010822.
FT VARIANT 1420 1420 L -> P (in AT).
FT /FTId=VAR_010823.
FT VARIANT 1454 1454 K -> N.
FT /FTId=VAR_010824.
FT VARIANT 1463 1463 F -> S (in B-cell non-Hodgkin's
FT lymphoma).
FT /FTId=VAR_010825.
FT VARIANT 1465 1465 L -> P (in AT).
FT /FTId=VAR_010826.
FT VARIANT 1566 1566 P -> R (in AT).
FT /FTId=VAR_010827.
FT VARIANT 1570 1570 V -> A.
FT /FTId=VAR_010828.
FT VARIANT 1682 1682 D -> H (in T-prolymphocytic leukemia).
FT /FTId=VAR_010829.
FT VARIANT 1691 1691 S -> R (in AT and B-cell chronic
FT lymphocytic leukemia; could be a rare
FT polymorphism; dbSNP:1800059).
FT /FTId=VAR_010830.
FT VARIANT 1743 1743 T -> I (in AT; associated with
FT preleukemic T-cell proliferation).
FT /FTId=VAR_010831.
FT VARIANT 1812 1813 AF -> V (in AT).
FT /FTId=VAR_010832.
FT VARIANT 1853 1853 D -> N (common polymorphism;
FT dbSNP:1801516).
FT /FTId=VAR_010833.
FT VARIANT 1853 1853 D -> V (might contribute to B-cell
FT chronic lymphocytic leukemia;
FT dbSNP:1801673).
FT /FTId=VAR_010834.
FT VARIANT 1910 1910 L -> H (in T-prolymphocytic leukemia).
FT /FTId=VAR_010835.
FT VARIANT 1913 1913 V -> G (in AT).
FT /FTId=VAR_010836.
FT VARIANT 1953 1953 T -> R (in B-cell chronic lymphocytic
FT leukemia).
FT /FTId=VAR_010837.
FT VARIANT 2016 2016 D -> G (in AT).
FT /FTId=VAR_010838.
FT VARIANT 2063 2063 G -> E (in AT).
FT /FTId=VAR_010839.
FT VARIANT 2067 2067 A -> D (in AT).
FT /FTId=VAR_010840.
FT VARIANT 2079 2079 V -> I (in dbSNP:1800060).
FT /FTId=VAR_010841.
FT VARIANT 2139 2139 E -> G (in T-prolymphocytic leukemia;
FT somatic mutation).
FT /FTId=VAR_010842.
FT VARIANT 2164 2164 E -> K (in T-prolymphocytic leukemia).
FT /FTId=VAR_010843.
FT VARIANT 2218 2218 S -> C (in AT).
FT /FTId=VAR_010844.
FT VARIANT 2224 2227 MALR -> IS (in AT).
FT /FTId=VAR_010845.
FT VARIANT 2227 2227 R -> C (in AT).
FT /FTId=VAR_010846.
FT VARIANT 2246 2252 CIKDILT -> H (in AT).
FT /FTId=VAR_010847.
FT VARIANT 2274 2274 A -> K (in B-cell chronic lymphocytic
FT leukemia).
FT /FTId=VAR_010848.
FT VARIANT 2287 2287 G -> A (in dbSNP:1800061).
FT /FTId=VAR_010849.
FT VARIANT 2396 2396 T -> S (in T-prolymphocytic leukemia).
FT /FTId=VAR_010850.
FT VARIANT 2418 2418 K -> KK (in mantle cell lymphoma).
FT /FTId=VAR_010851.
FT VARIANT 2420 2420 A -> P (in B-cell chronic lymphocytic
FT leukemia).
FT /FTId=VAR_010852.
FT VARIANT 2423 2423 E -> G (in mantle cell lymphoma).
FT /FTId=VAR_010853.
FT VARIANT 2424 2424 V -> G (in AT, B-cell chronic lymphocytic
FT leukemia and T-prolymphocytic leukemia;
FT associated with increased risk for breast
FT cancer).
FT /FTId=VAR_010854.
FT VARIANT 2427 2428 Missing (in AT; associated with T-
FT prolymphocytic leukemia).
FT /FTId=VAR_010855.
FT VARIANT 2438 2438 T -> I.
FT /FTId=VAR_010856.
FT VARIANT 2442 2442 Q -> P (in T-prolymphocytic leukemia).
FT /FTId=VAR_010857.
FT VARIANT 2470 2470 Y -> D (in AT).
FT /FTId=VAR_010858.
FT VARIANT 2486 2486 R -> G (in T-prolymphocytic leukemia).
FT /FTId=VAR_010859.
FT VARIANT 2491 2491 W -> R (in AT).
FT /FTId=VAR_010860.
FT VARIANT 2546 2548 Missing (in AT, T-prolymphocytic leukemia
FT and T-cell acute lymphoblastic leukemia).
FT /FTId=VAR_010861.
FT VARIANT 2554 2554 H -> D (in AT).
FT /FTId=VAR_010862.
FT VARIANT 2625 2625 D -> Q (in AT; requires 2 nucleotide
FT substitutions).
FT /FTId=VAR_010863.
FT VARIANT 2625 2626 DA -> EP (in AT).
FT /FTId=VAR_010864.
FT VARIANT 2656 2656 L -> P (in AT; partial functional loss).
FT /FTId=VAR_010865.
FT VARIANT 2662 2662 Missing (in AT).
FT /FTId=VAR_010866.
FT VARIANT 2663 2663 Missing (in AT).
FT /FTId=VAR_010867.
FT VARIANT 2668 2668 E -> G (in AT).
FT /FTId=VAR_010868.
FT VARIANT 2695 2695 G -> A (in T-prolymphocytic leukemia and
FT B-cell chronic lymphocytic leukemia).
FT /FTId=VAR_010869.
FT VARIANT 2702 2702 I -> R (in AT).
FT /FTId=VAR_010870.
FT VARIANT 2722 2722 L -> R (in T-prolymphocytic leukemia).
FT /FTId=VAR_010871.
FT VARIANT 2725 2725 D -> G (in T-prolymphocytic leukemia).
FT /FTId=VAR_010872.
FT VARIANT 2725 2725 D -> V (in T-prolymphocytic leukemia).
FT /FTId=VAR_010873.
FT VARIANT 2726 2726 A -> V (in AT).
FT /FTId=VAR_010874.
FT VARIANT 2732 2732 F -> L (in T-prolymphocytic leukemia).
FT /FTId=VAR_010875.
FT VARIANT 2765 2765 G -> S (may contribute to breast cancer).
FT /FTId=VAR_010876.
FT VARIANT 2810 2810 Missing (in T-prolymphocytic leukemia).
FT /FTId=VAR_010877.
FT VARIANT 2824 2824 C -> Y (in AT).
FT /FTId=VAR_010878.
FT VARIANT 2827 2827 F -> C (in AT; mild).
FT /FTId=VAR_010879.
FT VARIANT 2829 2829 P -> L (in AT).
FT /FTId=VAR_010880.
FT VARIANT 2832 2832 R -> C (in AT and B-cell non-Hodgkin's
FT lymphoma).
FT /FTId=VAR_010881.
FT VARIANT 2849 2849 R -> P (in AT).
FT /FTId=VAR_010882.
FT VARIANT 2855 2855 S -> R (in AT).
FT /FTId=VAR_010883.
FT VARIANT 2855 2856 SV -> RI (in AT).
FT /FTId=VAR_010884.
FT VARIANT 2860 2860 Missing (in AT).
FT /FTId=VAR_010885.
FT VARIANT 2867 2867 G -> R (in AT).
FT /FTId=VAR_010886.
FT VARIANT 2871 2872 RH -> S (in T-prolymphocytic leukemia).
FT /FTId=VAR_010887.
FT VARIANT 2890 2890 L -> V (in T-prolymphocytic leukemia).
FT /FTId=VAR_010888.
FT VARIANT 2904 2904 E -> G (in AT).
FT /FTId=VAR_010889.
FT VARIANT 2909 2909 R -> G (in AT).
FT /FTId=VAR_010890.
FT VARIANT 3003 3003 D -> N.
FT /FTId=VAR_010891.
FT VARIANT 3006 3006 A -> P (in T-prolymphocytic leukemia).
FT /FTId=VAR_010892.
FT VARIANT 3008 3008 R -> C (in AT, T-prolymphocytic leukemia
FT and mantle cell lymphoma).
FT /FTId=VAR_010893.
FT VARIANT 3008 3008 R -> H (in B-cell chronic lymphocytic
FT leukemia).
FT /FTId=VAR_010894.
FT VARIANT 3018 3018 K -> N (in B-cell chronic lymphocytic
FT leukemia).
FT /FTId=VAR_010895.
FT MUTAGEN 2870 2870 D->A: LOSS OF KINASE ACTIVITY.
FT MUTAGEN 2875 2875 N->K: LOSS OF KINASE ACTIVITY.
FT CONFLICT 46 46 H -> N (in Ref. 4).
FT CONFLICT 56 56 N -> I (in Ref. 4).
FT CONFLICT 313 313 Y -> N (in Ref. 4).
FT CONFLICT 488 488 W -> G (in Ref. 4).
FT CONFLICT 554 554 A -> T (IN REF. 2, 4, 5 AND 8).
FT CONFLICT 754 754 Q -> K (in Ref. 4).
FT CONFLICT 887 887 E -> G (in Ref. 4).
FT CONFLICT 1003 1003 Q -> L (in Ref. 4).
FT CONFLICT 1049 1049 L -> W (in Ref. 4).
FT CONFLICT 1089 1089 A -> V (in Ref. 4).
SQ SEQUENCE 3056 AA; 350641 MW; 9AB9F31BBD58B08D CRC64;
MSLVLNDLLI CCRQLEHDRA TERKKEVEKF KRLIRDPETI KHLDRHSDSK QGKYLNWDAV
FRFLQKYIQK ETECLRIAKP NVSASTQASR QKKMQEISSL VKYFIKCANR RAPRLKCQEL
LNYIMDTVKD SSNGAIYGAD CSNILLKDIL SVRKYWCEIS QQQWLELFSV YFRLYLKPSQ
DVHRVLVARI IHAVTKGCCS QTDGLNSKFL DFFSKAIQCA RQEKSSSGLN HILAALTIFL
KTLAVNFRIR VCELGDEILP TLLYIWTQHR LNDSLKEVII ELFQLQIYIH HPKGAKTQEK
GAYESTKWRS ILYNLYDLLV NEISHIGSRG KYSSGFRNIA VKENLIELMA DICHQVFNED
TRSLEISQSY TTTQRESSDY SVPCKRKKIE LGWEVIKDHL QKSQNDFDLV PWLQIATQLI
SKYPASLPNC ELSPLLMILS QLLPQQRHGE RTPYVLRCLT EVALCQDKRS NLESSQKSDL
LKLWNKIWCI TFRGISSEQI QAENFGLLGA IIQGSLVEVD REFWKLFTGS ACRPSCPAVC
CLTLALTTSI VPGAVKMGIE QNMCEVNRSF SLKESIMKWL LFYQLEGDLE NSTEVPPILH
SNFPHLVLEK ILVSLTMKNC KAAMNFFQSV PECEHHQKDK EELSFSEVEE LFLQTTFDKM
DFLTIVRECG IEKHQSSIGF SVHQNLKESL DRCLLGLSEQ LLNNYSSEIT NSETLVRCSR
LLVGVLGCYC YMGVIAEEEA YKSELFQKAN SLMQCAGESI TLFKNKTNEE FRIGSLRNMM
QLCTRCLSNC TKKSPNKIAS GFFLRLLTSK LMNDIADICK SLASFIKKPF DRGEVESMED
DTNGNLMEVE DQSSMNLFND YPDSSVSDAN EPGESQSTIG AINPLAEEYL SKQDLLFLDM
LKFLCLCVTT AQTNTVSFRA ADIRRKLLML IDSSTLEPTK SLHLHMYLML LKELPGEEYP
LPMEDVLELL KPLSNVCSLY RRDQDVCKTI LNHVLHVVKN LGQSNMDSEN TRDAQGQFLT
VIGAFWHLTK ERKYIFSVRM ALVNCLKTLL EADPYSKWAI LNVMGKDFPV NEVFTQFLAD
NHHQVRMLAA ESINRLFQDT KGDSSRLLKA LPLKLQQTAF ENAYLKAQEG MREMSHSAEN
PETLDEIYNR KSVLLTLIAV VLSCSPICEK QALFALCKSV KENGLEPHLV KKVLEKVSET
FGYRRLEDFM ASHLDYLVLE WLNLQDTEYN LSSFPFILLN YTNIEDFYRS CYKVLIPHLV
IRSHFDEVKS IANQIQEDWK SLLTDCFPKI LVNILPYFAY EGTRDSGMAQ QRETATKVYD
MLKSENLLGK QIDHLFISNL PEIVVELLMT LHEPANSSAS QSTDLCDFSG DLDPAPNPPH
FPSHVIKATF AYISNCHKTK LKSILEILSK SPDSYQKILL AICEQAAETN NVYKKHRILK
IYHLFVSLLL KDIKSGLGGA WAFVLRDVIY TLIHYINQRP SCIMDVSLRS FSLCCDLLSQ
VCQTAVTYCK DALENHLHVI VGTLIPLVYE QVEVQKQVLD LLKYLVIDNK DNENLYITIK
LLDPFPDHVV FKDLRITQQK IKYSRGPFSL LEEINHFLSV SVYDALPLTR LEGLKDLRRQ
LELHKDQMVD IMRASQDNPQ DGIMVKLVVN LLQLSKMAIN HTGEKEVLEA VGSCLGEVGP
IDFSTIAIQH SKDASYTKAL KLFEDKELQW TFIMLTYLNN TLVEDCVKVR SAAVTCLKNI
LATKTGHSFW EIYKMTTDPM LAYLQPFRTS RKKFLEVPRF DKENPFEGLD DINLWIPLSE
NHDIWIKTLT CAFLDSGGTK CEILQLLKPM CEVKTDFCQT VLPYLIHDIL LQDTNESWRN
LLSTHVQGFF TSCLRHFSQT SRSTTPANLD SESEHFFRCC LDKKSQRTML AVVDYMRRQK
RPSSGTIFND AFWLDLNYLE VAKVAQSCAA HFTALLYAEI YADKKSMDDQ EKRSLAFEEG
SQSTTISSLS EKSKEETGIS LQDLLLEIYR SIGEPDSLYG CGGGKMLQPI TRLRTYEHEA
MWGKALVTYD LETAIPSSTR QAGIIQALQN LGLCHILSVY LKGLDYENKD WCPELEELHY
QAAWRNMQWD HCTSVSKEVE GTSYHESLYN ALQSLRDREF STFYESLKYA RVKEVEEMCK
RSLESVYSLY PTLSRLQAIG ELESIGELFS RSVTHRQLSE VYIKWQKHSQ LLKDSDFSFQ
EPIMALRTVI LEILMEKEMD NSQRECIKDI LTKHLVELSI LARTFKNTQL PERAIFQIKQ
YNSVSCGVSE WQLEEAQVFW AKKEQSLALS ILKQMIKKLD ASCAANNPSL KLTYTECLRV
CGNWLAETCL ENPAVIMQTY LEKAVEVAGN YDGESSDELR NGKMKAFLSL ARFSDTQYQR
IENYMKSSEF ENKQALLKRA KEEVGLLREH KIQTNRYTVK VQRELELDEL ALRALKEDRK
RFLCKAVENY INCLLSGEEH DMWVFRLCSL WLENSGVSEV NGMMKRDGMK IPTYKFLPLM
YQLAARMGTK MMGGLGFHEV LNNLISRISM DHPHHTLFII LALANANRDE FLTKPEVARR
SRITKNVPKQ SSQLDEDRTE AANRIICTIR SRRPQMVRSV EALCDAYIIL ANLDATQWKT
QRKGINIPAD QPITKLKNLE DVVVPTMEIK VDHTGEYGNL VTIQSFKAEF RLAGGVNLPK
IIDCVGSDGK ERRQLVKGRD DLRQDAVMQQ VFQMCNTLLQ RNTETRKRKL TICTYKVVPL
SQRSGVLEWC TGTVPIGEFL VNNEDGAHKR YRPNDFSAFQ CQKKMMEVQK KSFEEKYEVF
MDVCQNFQPV FRYFCMEKFL DPAIWFEKRL AYTRSVATSS IVGYILGLGD RHVQNILINE
QSAELVHIDL GVAFEQGKIL PTPETVPFRL TRDIVDGMGI TGVEGVFRRC CEKTMEVMRN
SQETLLTIVE VLLYDPLFDW TMNPLKALYL QQRPEDETEL HPTLNADDQE CKRNLSDIDQ
SFDKVAERVL MRLQEKLKGV EEGTVLSVGG QVNLLIQQAI DPKNLSRLFP GWKAWV
//
ID BCKD_HUMAN STANDARD; PRT; 412 AA.
AC O14874; Q96IN5;
DT 15-JUL-1998 (Rel. 36, Created)
DT 28-FEB-2003 (Rel. 41, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE [3-methyl-2-oxobutanoate dehydrogenase [lipoamide]] kinase,
DE mitochondrial precursor (EC 2.7.1.115) (Branched-chain alpha-ketoacid
DE dehydrogenase kinase) (BCKDHKIN) (BCKD-kinase).
GN BCKDK.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RA Chuang J.C., Cox R.P., Chuang D.T.;
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SEQUENCE FROM N.A.
RC TISSUE=Placenta;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC -!- FUNCTION: Catalyzes the phosphorylation and inactivation of the
CC branched-chain alpha-ketoacid dehydrogenase complex, the key
CC regulatory enzyme of the valine, leucine and isoleucine catabolic
CC pathways. Key enzyme that regulate the activity state of the BCKD
CC complex (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + [3-methyl-2-oxobutanoate dehydrogenase
CC (lipoamide)] = ADP + [3-methyl-2-oxobutanoate dehydrogenase
CC (lipoamide)] phosphate.
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SUBCELLULAR LOCATION: Mitochondrial matrix.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: Autophosphorylated (By similarity).
CC -!- SIMILARITY: Belongs to the PDK/BCKDK protein kinase family.
CC -!- SIMILARITY: Contains 1 histidine kinase domain.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AF026548; AAB82714.1; -.
DR EMBL; BC007363; AAH07363.1; -.
DR InterPro; IPR003594; ATPbind_ATPase.
DR InterPro; IPR004358; Bact_sens_pr_C.
DR InterPro; IPR005467; His_kinase.
DR Pfam; PF02518; HATPase_c; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
KW Kinase; Transferase; Transit peptide; Mitochondrion; Phosphorylation.
FT TRANSIT 1 30 Mitochondrion (By similarity).
FT CHAIN 31 412 [3-METHYL-2-OXOBUTANOATE DEHYDROGENASE
FT [LIPOAMIDE]] KINASE.
FT DOMAIN 159 404 HISTIDINE KINASE.
FT MOD_RES 52 52 PHOSPHORYLATION (AUTO-) (BY SIMILARITY).
FT CONFLICT 218 218 V -> F (in Ref. 1).
SQ SEQUENCE 412 AA; 46360 MW; AC97CF5D151FEFB4 CRC64;
MILASVLRSG PGGGLPLRPL LGPALALRAR STSATDTHHV EMARERSKTV TSFYNQSAID
AAAEKPSVRL TPTMMLYAGR SQDGSHLLKS ARYLQQELPV RIAHRIKGFR CLPFIIGCNP
TILHVHELYI RAFQKLTDFP PIKDQADEAQ YCQLVRQLLD DHKDVVTLLA EGLRESRKHI
EDEKLVRYFL DKTLTSRLGI RMLATHHLAL HEDKPDFVGI ICTRLSPKKI IEKWVDFARR
LCEHKYGNAP RVRINGHVAA RFPFIPMPLD YILPELLKNA MRATMESHLD TPYNVPDVVI
TIANNDVDLI IRISDRGGGI AHKDLDRVMD YHFTTAEAST QDPRISPLFG HLDMHSGAQS
GPMHGFGFGL PTSRAYAEYL GGSLQLQSLQ GIGTDVYLRL RHIDGREESF RI
//
ID C43B_HUMAN STANDARD; PRT; 624 AA.
AC Q9Y5P4; Q96Q85; Q96Q88; Q9H2S7; Q9H2S8;
DT 28-FEB-2003 (Rel. 41, Created)
DT 28-FEB-2003 (Rel. 41, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE Goodpasture antigen-binding protein (EC 2.7.1.37) (GPBP) (Collagen
DE type IV alpha 3 binding protein) (StAR-related lipid transfer protein
DE 11) (StARD11) (START domain-containing protein 11).
GN COL4A3BP OR STARD11.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A. (ISOFORM 1), AND CHARACTERIZATION.
RX MEDLINE=99230287; PubMed=10212244;
RA Raya A., Revert F., Navarro S., Saus J.;
RT "Characterization of a novel type of Serine/Threonine kinase that
RT specifically phosphorylates the human goodpasture antigen.";
RL J. Biol. Chem. 274:12642-12649(1999).
RN [2]
RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 2).
RX MEDLINE=20568301; PubMed=11007769;
RA Raya A., Revert-Ros F., Martinez-Martinez P., Navarro S., Rosello E.,
RA Vieites B., Granero F., Forteza J., Saus J.;
RT "Goodpasture antigen-binding protein, the kinase that phosphorylates
RT the Goodpasture antigen, is an alternatively spliced variant
RT implicated in autoimmune pathogenesis.";
RL J. Biol. Chem. 275:40392-40399(2000).
RN [3]
RP SEQUENCE FROM N.A. (ISOFORM 2).
RC TISSUE=Placenta;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [4]
RP SEQUENCE OF 1-77 FROM N.A.
RA Ogi T., Yamamoto Y., Ohmori H.;
RT "Homo sapiens genomic sequence, containing DINB1 & GPBP gene.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phosphorylates on Ser and Thr residues the Goodpasture
CC autoantigen (in vitro). Isoform 2 seems to be less active.
CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC -!- SUBUNIT: Interacts with COL4A3.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y5P4-1; Sequence=Displayed;
CC Name=2; Synonyms=Delta26, GPBPD26;
CC IsoId=Q9Y5P4-2; Sequence=VSP_006276;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Contains 1 PH domain.
CC -!- SIMILARITY: Contains 1 START domain.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AF136450; AAD30288.1; -.
DR EMBL; AF232930; AAG42046.1; -.
DR EMBL; AF232935; AAG42051.1; -.
DR EMBL; BC000102; AAH00102.1; -.
DR EMBL; AB036934; BAB58974.1; -.
DR EMBL; AB036936; BAB58977.1; -.
DR Genew; HGNC:2205; COL4A3BP.
DR MIM; 604677; -.
DR GO; GO:0004672; F:protein kinase activity; TAS.
DR GO; GO:0006955; P:immune response; NAS.
DR GO; GO:0006468; P:protein amino acid phosphorylation; TAS.
DR InterPro; IPR001849; PH.
DR InterPro; IPR002913; START.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF01852; START; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00234; START; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50848; START; 1.
KW Transferase; Kinase; Serine/threonine-protein kinase; Coiled coil;
KW Alternative splicing.
FT DOMAIN 23 117 PH.
FT DOMAIN 263 303 COILED COIL (POTENTIAL).
FT DOMAIN 389 618 START.
FT VARSPLIC 371 396 Missing (in isoform 2).
FT /FTId=VSP_006276.
SQ SEQUENCE 624 AA; 70834 MW; A125162492AC5A0E CRC64;
MSDNQSWNSS GSEEDPETES GPPVERCGVL SKWTNYIHGW QDRWVVLKNN ALSYYKSEDE
TEYGCRGSIC LSKAVITPHD FDECRFDISV NDSVWYLRAQ DPDHRQQWID AIEQHKTESG
YGSESSLRRH GSMVSLVSGA SGYSATSTSS FKKGHSLREK LAEMETFRDI LCRQVDTLQK
YFDACADAVS KDELQRDKVV EDDEDDFPTT RSDGDFLHST NGNKEKLFPH VTPKGINGID
FKGEAITFKA TTAGILATLS HCIELMVKRE DSWQKRLDKE TEKKRRTEEA YKNAMTELKK
KSHFGGPDYE EGPNSLINEE EFFDAVEAAL DRQDKIEEQS QSEKVRLHWP TSLPSGDAFS
SVGTHRFVQK PYSRSSSMSS IDLVSASDDV HRFSSQVEEM VQNHMTYSLQ DVGGDANWQL
VVEEGEMKVY RREVEENGIV LDPLKATHAV KGVTGHEVCN YFWNVDVRND WETTIENFHV
VETLADNAII IYQTHKRVWP ASQRDVLYLS VIRKIPALTE NDPETWIVCN FSVDHDSAPL
NNRCVRAKIN VAMICQTLVS PPEGNQEISR DNILCKITYV ANVNPGGWAP ASVLRAVAKR
EYPKFLKRFT SYVQEKTAGK PILF
//
ID CARL_HUMAN STANDARD; PRT; 478 AA.
AC Q9UHJ6;
DT 16-OCT-2001 (Rel. 40, Created)
DT 16-OCT-2001 (Rel. 40, Last sequence update)
DT 16-OCT-2001 (Rel. 40, Last annotation update)
DE Carbohydrate kinase-like protein (EC 2.7.1.-).
GN CARKL.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RC TISSUE=Fetal kidney;
RX MEDLINE=20138496; PubMed=10673275;
RA Touchman J.W., Anikster Y., Dietrich N.L., Maduro V.V., McDowell G.,
RA Shotelersuk V., Bouffard G.G., Beckstrom-Sternberg S.M., Gahl W.A.,
RA Green E.D.;
RT "The genomic region encompassing the nephropathic cystinosis gene
RT (CTNS): complete sequencing of a 200-kb segment and discovery of a
RT novel gene within the common cystinosis-causing deletion.";
RL Genome Res. 10:165-173(2000).
CC -!- SUBCELLULAR LOCATION: Cytoplasmic (Potential).
CC -!- TISSUE SPECIFICITY: Strongly expressed in liver, kidney and
CC pancreas. Expressed at lower levels in placenta and heart. Very
CC weakly expressed in lung and brain.
CC -!- SIMILARITY: Belongs to the fucokinase / gluconokinase /
CC glycerokinase / xylulokinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AF163573; AAF24936.1; -.
DR EMBL; AF168787; AAF43103.1; -.
DR Genew; HGNC:1492; CARKL.
DR MIM; 605060; -.
DR GO; GO:0005975; P:carbohydrate metabolism; TAS.
DR InterPro; IPR000577; FGGY_kin.
DR Pfam; PF00370; FGGY; 1.
DR PROSITE; PS00933; FGGY_KINASES_1; FALSE_NEG.
DR PROSITE; PS00445; FGGY_KINASES_2; FALSE_NEG.
KW Transferase; Kinase.
SQ SEQUENCE 478 AA; 51503 MW; 3A7D0B3FBE86AC1C CRC64;
MAARPITLGI DLGTTSVKAA LLRAAPDDPS GFAVLASCAR AARAEAAVES AVAGPQGREQ
DVSRILQALH ECLAALPRPQ LRSVVGIGVS GQMHGVVFWK TGQGCEWTEG GITPVFEPRA
VSHLVTWQDG RCSSEFLASL PQPKSHLSVA TGFGCATIFW LLKYRPEFLK SYDAAGTIHD
YVVAMLCGLP RPLMSDQNAA SWGYFNTQSQ SWNVKTLRSS GFPVHLLPDI AEPGSVAGRT
SHMWFEIPKG TQVGVALGDL QASVYSCMAQ RTDAVLNIST SVQLAASMPS GFQPAQTPDP
TAPVAYFPYF NRTYLGVAAS LNGGNVLATF VHMLVQWMAD LGLEVEESTV YSRMIQAAVQ
QRDTHLTITP TVLGERHLPD QLASVTRISS SDLSLGHVTR ALCRGIVQNL HSMLPIQQLQ
EWGVERVMGS GSALSRNDVL KQEVQRAFPL PMSFGQDVDA AVGAALVMLR RHLNQKES
//
ID CEK1_HUMAN STANDARD; PRT; 537 AA.
AC Q8TCT0; Q9BYB3; Q9UGE5;
DT 10-OCT-2003 (Rel. 42, Created)
DT 10-OCT-2003 (Rel. 42, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE Ceramide kinase (EC 2.7.1.138) (Acylsphingosine kinase) (hCERK) (Lipid
DE kinase 4) (LK4).
GN CERK OR KIAA1646.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A., AND CHARACTERIZATION.
RC TISSUE=Leukemia;
RX MEDLINE=22075121; PubMed=11956206;
RA Sugiura M., Kono K., Liu H., Shimizugawa T., Minekura H., Spiegel S.,
RA Kohama T.;
RT "Ceramide kinase, a novel lipid kinase. Molecular cloning and
RT functional characterization.";
RL J. Biol. Chem. 277:23294-23300(2002).
RN [2]
RP SEQUENCE FROM N.A.
RA Van Veldhoven P.P.;
RT "A search for lipid kinases.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SEQUENCE FROM N.A.
RX MEDLINE=20057165; PubMed=10591208;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [4]
RP SEQUENCE OF 57-537 FROM N.A.
RC TISSUE=Brain;
RX MEDLINE=21156230; PubMed=11258795;
RA Hirosawa M., Nagase T., Murahashi Y., Kikuno R., Ohara O.;
RT "Identification of novel transcribed sequences on human chromosome 22
RT by expressed sequence tag mapping.";
RL DNA Res. 8:1-9(2001).
CC -!- FUNCTION: Catalyzes specifically the phosphorylation of ceramide
CC to form ceramide 1-phosphate. Acts efficiently on natural and
CC analog ceramides (C6, C8, C16 ceramides, and C8-dihydroceramide),
CC to a lesser extent on C2-ceramide and C6-dihydroceramide, but not
CC on other lipids, such as various sphingosines.
CC -!- CATALYTIC ACTIVITY: ATP + ceramide = ADP + ceramide 1-phosphate.
CC -!- COFACTOR: Calcium and magnesium.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic and membrane-associated.
CC -!- TISSUE SPECIFICITY: High level expression in heart, brain,
CC skeletal muscle, kidney and liver; moderate in peripheral blood
CC leukocytes and thymus; very low in spleen, small intestine,
CC placenta and lung.
CC -!- MISCELLANEOUS: Optimal pH is 6.0-7.5.
CC -!- SIMILARITY: Contains 1 DAGKc domain.
CC -!- CAUTION: Ref.3 sequence differs from that shown due to
CC erroneous gene model prediction. An additional exon may exist
CC between amino acid positions 168 and 169.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AB079066; BAC01154.1; -.
DR EMBL; AJ457828; CAD29884.1; -.
DR EMBL; AL096766; CAB62977.1; ALT_SEQ.
DR EMBL; AL118516; -; NOT_ANNOTATED_CDS.
DR EMBL; AB051433; BAB33316.1; -.
DR Genew; HGNC:19256; CERK.
DR GO; GO:0000299; C:integral to membrane of membrane fraction; IDA.
DR GO; GO:0004685; F:calcium/calmodulin-dependent protein kinase...; IDA.
DR GO; GO:0001729; F:ceramide kinase activity; IDA.
DR GO; GO:0000287; F:magnesium ion binding; IDA.
DR GO; GO:0006672; P:ceramide metabolism; TAS.
DR InterPro; IPR001206; DAGKc.
DR Pfam; PF00781; DAGKc; 1.
DR ProDom; PD005043; DAGKc; 1.
KW Transferase; Kinase; Calcium; Magnesium.
FT DOMAIN 132 278 DAGKC.
SQ SEQUENCE 537 AA; 59977 MW; 3DBFC0ED8D679F7F CRC64;
MGATGAAEPL QSVLWVKQQR CAVSLEPARA LLRWWRSPGP GAGAPGADAC SVPVSEIIAV
EETDVHGKHQ GSGKWQKMEK PYAFTVHCVK RARRHRWKWA QVTFWCPEEQ LCHLWLQTLR
EMLEKLTSRP KHLLVFINPF GGKGQGKRIY ERKVAPLFTL ASITTDIIVT EHANQAKETL
YEINIDKYDG IVCVGGDGMF SEVLHGLIGR TQRSAGVDQN HPRAVLVPSS LRIGIIPAGS
TDCVCYSTVG TSDAETSALH IVVGDSLAMD VSSVHHNSTL LRYSVSLLGY GFYGDIIKDS
EKKRWLGLAR YDFSGLKTFL SHHCYEGTVS FLPAQHTVGS PRDRKPCRAG CFVCRQSKQQ
LEEEQKKALY GLEAAEDVEE WQVVCGKFLA INATNMSCAC RRSPRGLSPA AHLGDGSSDL
ILIRKCSRFN FLRFLIRHTN QQDQFDFTFV EVYRVKKFQF TSKHMEDEDS DLKEGGKKRF
GHICSSHPSC CCTVSNSSWN CDGEVLHSPA IEVRVHCQLV RLFARGIEEN PKPDSHS
//
ID COAS_HUMAN STANDARD; PRT; 564 AA.
AC Q13057; Q8NBM7; Q8NEW1; Q8WXD4; Q9NRM3;
DT 01-NOV-1997 (Rel. 35, Created)
DT 10-OCT-2003 (Rel. 42, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE Bifunctional coenzyme A synthase (CoA synthase) (NBP) (POV-2)
DE [Includes: Phosphopantetheine adenylyltransferase (EC 2.7.7.3)
DE (Pantetheine-phosphate adenylyltransferase) (PPAT) (Dephospho-CoA
DE pyrophosphorylase); Dephospho-CoA kinase (EC 2.7.1.24) (DPCK)
DE (Dephosphocoenzyme A kinase) (DPCOAK)].
GN COASY.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A., FUNCTION, AND TISSUE SPECIFICITY.
RX MEDLINE=22050577; PubMed=11923312;
RA Daugherty M., Polanuyer B., Farrell M., Scholle M., Lykidis A.,
RA de Crecy-Lagard V., Osterman A.;
RT "Complete reconstitution of the human coenzyme A biosynthetic pathway
RT via comparative genomics.";
RL J. Biol. Chem. 277:21431-21439(2002).
RN [2]
RP SEQUENCE FROM N.A., AND SUBUNIT.
RX MEDLINE=22067063; PubMed=11994049;
RA Aghajanian S., Worrall D.M.;
RT "Identification and characterization of the gene encoding the human
RT phosphopantetheine adenylyltransferase and dephospho-CoA kinase
RT bifunctional enzyme (CoA synthase).";
RL Biochem. J. 365:13-18(2002).
RN [3]
RP SEQUENCE FROM N.A.
RA Ota T., Nishikawa T., Suzuki Y., Kawai-Hio Y., Hayashi K., Ishii S.,
RA Saito K., Yamamoto J., Wakamatsu A., Nagai T., Nakamura Y.,
RA Nagahari K., Sugano S., Isogai T.;
RT "HRI human cDNA sequencing project.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SEQUENCE OF 165-564 FROM N.A.
RA Zhu Y.-B., Han Y.;
RT "Molecular cloning of a NBP gene cDNA.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SEQUENCE OF 332-564 FROM N.A.
RC TISSUE=Ovary;
RX MEDLINE=96070985; PubMed=8529999;
RA Montagna M., Serova O., Sylla B.S., Feunteun J., Lenoir G.M.;
RT "A 100-kb physical and transcriptional map around the EDH17B2 gene:
RT identification of three novel genes and a pseudogene of a human
RT homologue of the rat PRL-1 tyrosine phosphatase.";
RL Hum. Genet. 96:532-538(1995).
RN [6]
RP SEQUENCE OF 340-564 FROM N.A.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP SEQUENCE OF 93-564 FROM N.A.
RC TISSUE=Colon, and Muscle;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC -!- FUNCTION: Bifunctional enzyme that catalyzes the fourth and fifth
CC sequential steps of CoA biosynthetic pathway. The fourth reaction
CC is catalyzed by the phosphopantetheine adenylyltransferase, coded
CC by the coaD domain; the fifth reaction is catalyzed by the
CC dephospho-CoA kinase, coded by the coaE domain. May act as a point
CC of CoA biosynthesis regulation.
CC -!- CATALYTIC ACTIVITY: ATP + pantetheine 4'-phosphate = diphosphate +
CC 3'-dephospho-CoA.
CC -!- CATALYTIC ACTIVITY: ATP + dephospho-CoA = ADP + CoA.
CC -!- PATHWAY: Coenzyme A (CoA) biosynthesis; fourth step.
CC -!- PATHWAY: Coenzyme A (CoA) biosynthesis; fifth (last) step.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic (By similarity).
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined including
CC brain, heart, skeletal muscle, colon, thymus, spleen, kidney,
CC liver, small intestine, placenta, lung and peripheral blood
CC leukocyte. Lowest expression in peripheral blood leukocytes and
CC highest in kidney and liver.
CC -!- MISCELLANEOUS: For the PPAT reaction, the Km for 4'-
CC phoshopantetheine and ATP are 7.6 +/-1.3 and 145 +/-29.8 mM,
CC respectively. For the DPCK reaction, the Km for dephospho-CoA and
CC ATP are 16.7 +/-1.92 and 34.4 +/-6.6 mM, respectively.
CC -!- SIMILARITY: In the central section; belongs to the eukaryotic
CC coaD family.
CC -!- SIMILARITY: In the C-terminal section; belongs to the coaE family.
CC -!- CAUTION: Ref.3 sequence differs from that shown due to a
CC frameshift in position 315.
CC -!- CAUTION: Ref.5 sequence differs from that shown due to a
CC frameshift in position 535.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AF453478; AAL50813.1; -.
DR EMBL; AY094602; AAM19996.1; -.
DR EMBL; AK075415; BAC11605.1; ALT_FRAME.
DR EMBL; AF208536; AAF87955.1; ALT_INIT.
DR EMBL; U18919; AAA69699.1; ALT_FRAME.
DR EMBL; BT007168; AAP35832.1; -.
DR EMBL; BC006354; AAH06354.1; ALT_INIT.
DR EMBL; BC020985; AAH20985.1; ALT_INIT.
DR GO; GO:0000166; F:nucleotide binding; NAS.
DR InterPro; IPR004820; Cytidylyltransf.
DR InterPro; IPR004821; Cyt_tran_rel.
DR InterPro; IPR001977; Depp_CoAkinase.
DR Pfam; PF01121; CoaE; 1.
DR Pfam; PF01467; CTP_transf_2; 1.
DR ProDom; PD003329; Depp_CoAkinase; 1.
DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
DR TIGRFAMs; TIGR00152; TIGR00152; 1.
DR PROSITE; PS01294; COAE; 1.
KW Coenzyme A biosynthesis; Multifunctional enzyme; Transferase; Kinase;
KW Nucleotidyltransferase; ATP-binding.
FT DOMAIN 180 358 PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE.
FT DOMAIN 359 564 DEPHOSPHO-COA KINASE.
FT NP_BIND 365 372 ATP (Potential).
FT CONFLICT 55 55 S -> Y (in Ref. 1 and 3).
SQ SEQUENCE 564 AA; 62328 MW; 7DC9E93B356C5DB7 CRC64;
MAVFRSGLLV LTTPLASLAP RLASILTSAA RLVNHTLYVH LQPGMSLEGP AQPQSSPVQA
TFEVLDFITH LYAGADVHRH LDVRILLTNI RTKSTFLPPL PTSVQNLAHP PEVVLTDFQT
LDGSQYNPVK QQLVRYATSC YSCCPRLASV LLYSDYGIGE VPVEPLDVPL PSTIRPASPV
AGSPKQPVRG YYRGAVGGTF DRLHNAHKVL LSVACILAQE QLVVGVADKD LLKSKLLPEL
LQPYTERVEH LSEFLVDIKP SLTFDVIPLL DPYGPAGSDP SLEFLVVSEE TYRGGMAINR
FRLENDLEEL ALYQIQLLKD LRHTENEEDK VSSSSFRQRM LGNLLRPPYE RPELPTCLYV
IGLTGISGSG KSSIAQRLKG LGAFVIDSDH LGHRAYAPGG PAYQPVVEAF GTDILHKDGI
INRKVLGSRV FGNKKQLKIL TDIMWPIIAK LAREEMDRAV AEGKRVCVID AAVLLEAGWQ
NLVHEVWTAV IPETEAVRRI VERDGLSEAA AQSRLQSQMS GQQLVEQSHV VLSTLWEPHI
TQRQVEKAWA LLQKRIPKTH QALD
//
ID DCK_HUMAN STANDARD; PRT; 260 AA.
AC P27707;
DT 01-AUG-1992 (Rel. 23, Created)
DT 01-AUG-1992 (Rel. 23, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Deoxycytidine kinase (EC 2.7.1.74) (dCK).
GN DCK.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A., AND SEQUENCE OF 58-70; 119-127 AND 189-192.
RX MEDLINE=91142207; PubMed=1996353;
RA Chottiner E.G., Shewach D.S., Datta N.S., Ashcraft E., Gribbin D.,
RA Ginsburg D., Fox I.H., Mitchell B.S.;
RT "Cloning and expression of human deoxycytidine kinase cDNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:1531-1535(1991).
RN [2]
RP PARTIAL SEQUENCE, AND CHARACTERIZATION.
RX MEDLINE=91192170; PubMed=2013338;
RA Eriksson S., Cederlund E., Bergman T., Joernvall H., Bohman C.;
RT "Characterization of human deoxycytidine kinase. Correlation with
RT cDNA sequences.";
RL FEBS Lett. 280:363-366(1991).
RN [3]
RP SUBCELLULAR LOCATION.
RX MEDLINE=98004502; PubMed=9342341;
RA Johansson M., Brismar S., Karlsson A.;
RT "Human deoxycytidine kinase is located in the cell nucleus.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:11941-11945(1997).
CC -!- FUNCTION: Required for the phosphorylation of several
CC deoxyribonucleosides and certain nucleoside analogs widely
CC employed as antiviral and chemotherapeutic agents.
CC -!- CATALYTIC ACTIVITY: NTP + deoxycytidine = NDP + dCMP.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Nuclear.
CC -!- SIMILARITY: Belongs to the DCK/DGK family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; M60527; AAA35752.1; -.
DR PIR; A38585; A38585.
DR PDB; 1P5Z; 01-JUL-03.
DR Genew; HGNC:2704; DCK.
DR GK; P27707; -.
DR MIM; 125450; -.
DR GO; GO:0004137; F:deoxycytidine kinase activity; TAS.
DR GO; GO:0006220; P:pyrimidine nucleotide metabolism; TAS.
DR InterPro; IPR002624; dNK.
DR Pfam; PF01712; dNK; 1.
KW Transferase; Kinase; ATP-binding; Nuclear protein; 3D-structure.
FT NP_BIND 28 35 ATP (Probable).
SQ SEQUENCE 260 AA; 30518 MW; 626B9D2D6BED8DBC CRC64;
MATPPKRSCP SFSASSEGTR IKKISIEGNI AAGKSTFVNI LKQLCEDWEV VPEPVARWCN
VQSTQDEFEE LTMSQKNGGN VLQMMYEKPE RWSFTFQTYA CLSRIRAQLA SLNGKLKDAE
KPVLFFERSV YSDRYIFASN LYESECMNET EWTIYQDWHD WMNNQFGQSL ELDGIIYLQA
TPETCLHRIY LRGRNEEQGI PLEYLEKLHY KHESWLLHRT LKTNFDYLQE VPILTLDVNE
DFKDKYESLV EKVKEFLSTL
//
ID DGK_HUMAN STANDARD; PRT; 277 AA.
AC Q16854; P78532; Q16759; Q96BC1;
DT 01-NOV-1997 (Rel. 35, Created)
DT 28-FEB-2003 (Rel. 41, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Deoxyguanosine kinase, mitochondrial precursor (EC 2.7.1.113) (dGK).
GN DGUOK OR DGK.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RC TISSUE=Brain;
RX MEDLINE=96293511; PubMed=8692979;
RA Johansson M., Karlsson A.;
RT "Cloning and expression of human deoxyguanosine kinase cDNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:7258-7262(1996).
RN [2]
RP SEQUENCE FROM N.A.
RC TISSUE=B-cell;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [3]
RP SEQUENCE OF 18-277 FROM N.A.
RC TISSUE=Brain;
RX MEDLINE=96314545; PubMed=8706825;
RA Wang L., Hellman U., Eriksson S.;
RT "Cloning and expression of human mitochondrial deoxyguanosine kinase
RT cDNA.";
RL FEBS Lett. 390:39-43(1996).
RN [4]
RP SEQUENCE OF 1-47 FROM N.A.
RA Stegmann A.P.A., Mitchell B.S.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for the phosphorylation of several
CC deoxyribonucleosides and certain nucleoside analogs widely
CC employed as antiviral and chemotherapeutic agents.
CC -!- CATALYTIC ACTIVITY: ATP + deoxyguanosine = ADP + dGMP.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Mitochondrial.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q16854-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16854-2; Sequence=VSP_003025;
CC Name=3;
CC IsoId=Q16854-3; Sequence=VSP_003024;
CC Name=4;
CC IsoId=Q16854-4; Sequence=VSP_003024, VSP_003025;
CC Name=5;
CC IsoId=Q16854-5; Sequence=VSP_003024, VSP_003026;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highest expression in muscle,
CC brain, liver and lymphoid tissues.
CC -!- SIMILARITY: Belongs to the DCK/DGK family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; U41668; AAC50624.1; -.
DR EMBL; BC015757; AAH15757.1; -.
DR EMBL; X97386; CAA66054.1; -.
DR EMBL; U81499; AAB39858.1; -.
DR PIR; JC6142; JC6142.
DR PIR; S71315; S71315.
DR PDB; 1JAG; 05-DEC-01.
DR Genew; HGNC:2858; DGUOK.
DR GK; Q16854; -.
DR MIM; 601465; -.
DR GO; GO:0005739; C:mitochondrion; TAS.
DR GO; GO:0004138; F:deoxyguanosine kinase activity; TAS.
DR GO; GO:0008617; P:guanosine metabolism; TAS.
DR InterPro; IPR002624; dNK.
DR Pfam; PF01712; dNK; 1.
KW Transferase; Kinase; ATP-binding; Mitochondrion; Transit peptide;
KW Alternative splicing; 3D-structure.
FT TRANSIT 1 39 Mitochondrion (Potential).
FT CHAIN 40 277 DEOXYGUANOSINE KINASE.
FT NP_BIND 45 52 ATP (Potential).
FT VARSPLIC 48 85 Missing (in isoform 3, isoform 4 and
FT isoform 5).
FT /FTId=VSP_003024.
FT VARSPLIC 149 236 Missing (in isoform 2 and isoform 4).
FT /FTId=VSP_003025.
FT VARSPLIC 47 47 I -> IGNILKQIRGRAPIQET (in isoform 5).
FT /FTId=VSP_003026.
FT CONFLICT 83 83 T -> N (in Ref. 1).
FT CONFLICT 159 159 G -> D (in Ref. 3).
FT CONFLICT 212 212 K -> E (in Ref. 3).
FT STRAND 39 45
FT TURN 47 48
FT HELIX 51 61
FT TURN 63 64
FT STRAND 66 68
FT HELIX 72 74
FT TURN 75 75
FT HELIX 95 101
FT HELIX 103 123
FT HELIX 128 131
FT STRAND 137 141
FT HELIX 144 149
FT TURN 150 150
FT HELIX 151 157
FT TURN 158 159
FT HELIX 163 179
FT HELIX 181 184
FT STRAND 188 193
FT HELIX 196 205
FT TURN 209 213
FT HELIX 216 230
FT TURN 231 231
FT TURN 240 241
FT HELIX 242 244
FT STRAND 247 251
FT TURN 256 258
FT HELIX 260 275
FT TURN 276 277
SQ SEQUENCE 277 AA; 32056 MW; 53E4514BFC2CB5E5 CRC64;
MAAGRLFLSR LRAPFSSMAK SPLEGVSSSR GLHAGRGPRR LSIEGNIAVG KSTFVKLLTK
TYPEWHVATE PVATWQNIQA AGTQKACTAQ SLGNLLDMMY REPARWSYTF QTFSFLSRLK
VQLEPFPEKL LQARKPVQIF ERSVYSDRYI FAKNLFENGS LSDIEWHIYQ DWHSFLLWEF
ASRITLHGFI YLQASPQVCL KRLYQRAREE EKGIELAYLE QLHGQHEAWL IHKTTKLHFE
ALMNIPVLVL DVNDDFSEEV TKQEDLMREV NTFVKNL
//
ID E2K1_HUMAN STANDARD; PRT; 630 AA.
AC Q9BQI3; Q8NBW3; Q9HC02; Q9NYE0; Q9P0V6; Q9P1J5; Q9P2H8; Q9UHG4;
DT 16-OCT-2001 (Rel. 40, Created)
DT 10-OCT-2003 (Rel. 42, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE Eukaryotic translation initiation factor 2 alpha kinase 1
DE (EC 2.7.1.37) (Heme-regulated eukaryotic initiation factor eIF-2-alpha
DE kinase) (Heme-regulated inhibitor) (Heme-controlled repressor)
DE (HCR) (Hemin-sensitive initiation factor-2 alpha kinase) (PRO1362).
GN EIF2AK1 OR HRI OR KIAA1369.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A. (ISOFORM 1).
RC TISSUE=Dermal papilla;
RX MEDLINE=20550853; PubMed=11101152;
RA Hwang S.-Y., Kim M.-K., Kim J.-C.;
RT "Cloning of hHRI, human heme-regulated eukaryotic initiation factor
RT 2alpha kinase: down-regulated in epithelial ovarian cancers.";
RL Mol. Cells 10:584-591(2000).
RN [2]
RP SEQUENCE FROM N.A. (ISOFORM 1).
RC TISSUE=Skin;
RA Cannon G., Naik S.M., Boss J.M., Caughman S.W.;
RT "Cloning of the human heme-regulated eukaryotic initiation factor 2-
RT alpha kinase from TNF-alpha stimulated dermal microvascular
RT endothelial cells.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SEQUENCE FROM N.A. (ISOFORM 1).
RC TISSUE=Brain;
RX MEDLINE=20181126; PubMed=10718198;
RA Nagase T., Kikuno R., Ishikawa K.-I., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI.
RT The complete sequences of 150 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [4]
RP SEQUENCE FROM N.A. (ISOFORM 1).
RC TISSUE=Hypothalamus;
RX MEDLINE=20402571; PubMed=10931946;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [5]
RP SEQUENCE FROM N.A. (ISOFORM 2).
RC TISSUE=Amygdala;
RX MEDLINE=21154917; PubMed=11230166;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [6]
RP SEQUENCE FROM N.A. (ISOFORM 2).
RC TISSUE=Bone marrow;
RX MEDLINE=22279635; PubMed=12391722;
RA Omasa T., Chen Y.-G., Mantalaris A., Tsai Y.C., Wu J.H.;
RT "Molecular cloning and sequencing of the human heme-regulated
RT eukaryotic initiation factor 2 alpha (eIF-2 alpha) kinase from bone
RT marrow culture.";
RL DNA Seq. 13:133-137(2002).
RN [7]
RP SEQUENCE FROM N.A. (ISOFORM 1), AND VARIANT ARG-558.
RC TISSUE=Placenta;
RA Isogai T., Ota T., Nishikawa T., Hayashi K., Otsuki T., Sugiyama T.,
RA Suzuki Y., Nagai K., Sugano S., Ishii S., Kawai-Hio Y., Saito K.,
RA Yamamoto J., Wakamatsu A., Nakamura Y., Kojima S., Nagahari K.,
RA Masuho Y., Ono T., Okano K., Yoshikawa Y., Aotsuka S., Sasaki N.,
RA Hattori A., Okumura K., Iwayanagi T., Ninomiya K.;
RT "NEDO human cDNA sequencing project.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP SEQUENCE FROM N.A. (ISOFORM 2).
RC TISSUE=Amygdala;
RA Ottenwaelder B., Obermaier B., Mewes H.-W., Gassenhuber J.,
RA Wiemann S.;
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP SEQUENCE FROM N.A. (ISOFORM 1).
RC TISSUE=Ovary;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [10]
RP SEQUENCE OF 450-630 FROM N.A., AND VARIANT ARG-558.
RC TISSUE=Liver;
RA Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Ouyang S., Luo L., Bi J.,
RA Liu M., He F.;
RT "Functional prediction of the coding sequences of 121 new genes
RT deduced by analysis of cDNA clones from human fetal liver.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP INTERACTION WITH CDC37 AND THE HSP90 COMPLEX.
RX MEDLINE=20576356; PubMed=11036079;
RA Shao J., Grammatikakis N., Scroggins B.T., Uma S., Huang W.,
RA Chen J.-J., Hartson S.D., Matts R.L.;
RT "Hsp90 regulates p50(cdc37) function during the biogenesis of the
RT active conformation of the heme-regulated eIF2 alpha kinase.";
RL J. Biol. Chem. 276:206-214(2001).
CC -!- FUNCTION: Mediates down-regulation of protein synthesis in
CC response to various stress conditions by the phosphorylation of
CC EIF2S1 at Ser-48 and Ser-51. Protein synthesis is inhibited at the
CC level of initiation (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC -!- ENZYME REGULATION: Hemin inactivates EIF2AK1 by promoting the
CC formation of a disulfide-linked homodimer. Binding of nitric oxide
CC (NO) to the heme iron in the N-terminal heme-binding domain
CC activates the kinase activity, while binding of carbon monoxide
CC (CO) suppresses kinase activity (By similarity).
CC -!- SUBUNIT: Synthesized in an inactive form that binds to the N-
CC terminal domain of CDC37. Has to be associated with a multiprotein
CC complex containing Hsp90, CDC37 and PPP5C for maturation and
CC activation by autophosporylation. The phosphatase PPP5C modulates
CC this activation. Homodimer; non-covalently bound in the absence of
CC hemin. Converted to an inactive disulfide linked homodimer in the
CC presence of hemin (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BQI3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BQI3-2; Sequence=VSP_007589;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Detected in heart, brain, placenta, lung,
CC liver, skeletal muscle, pancreas, kidney, spleen, muscle and
CC stomach.
CC -!- PTM: Activated by autophosphorylation; phosphorylated
CC predominantly on serine and threonine residues, but also on
CC tyrosine residues (By similarity).
CC -!- MISCELLANEOUS: Can bind 2 molecules of heme per polypeptide chain
CC (By similarity).
CC -!- SIMILARITY: Belongs to the Ser/Thr protein kinase family. GCN2
CC subfamily.
CC -!- SIMILARITY: Contains 2 heme regulatory motif (HRM) repeats.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AF255050; AAF70289.1; -.
DR EMBL; AF181071; AAF18391.1; -.
DR EMBL; AB037790; BAA92607.1; ALT_INIT.
DR EMBL; AF183414; AAG09683.1; -.
DR EMBL; AL136563; CAB66498.1; -.
DR EMBL; AF147094; AAF66736.1; -.
DR EMBL; AK075192; BAC11461.1; -.
DR EMBL; AL834494; CAD39152.1; -.
DR EMBL; BC006524; AAH06524.1; -.
DR EMBL; AF116634; AAF71057.1; ALT_INIT.
DR GO; GO:0004694; F:eukaryotic translation initiation factor 2a...; IDA.
DR GO; GO:0020037; F:heme binding; ISS.
DR GO; GO:0042803; F:protein homodimerization activity; ISS.
DR GO; GO:0046777; P:autophosphorylation; ISS.
DR GO; GO:0046986; P:negative regulation of hemoglobin biosynthesis; ISS.
DR GO; GO:0045993; P:negative regulation of translational initia...; NAS.
DR GO; GO:0009605; P:response to external stimulus; IEP.
DR GO; GO:0006950; P:response to stress; IEP.
DR InterPro; IPR000719; Prot_kinase.
DR InterPro; IPR008271; Ser_thr_pkin_AS.
DR Pfam; PF00069; pkinase; 1.
DR ProDom; PD000001; Prot_kinase; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
KW Transferase; Kinase; Serine/threonine-protein kinase;
KW Protein synthesis inhibitor; ATP-binding; Repeat; Phosphorylation;
KW Alternative splicing; Polymorphism.
FT DOMAIN 167 582 PROTEIN KINASE.
FT NP_BIND 173 181 ATP (By similarity).
FT BINDING 196 196 ATP (By similarity).
FT ACT_SITE 441 441 By similarity.
FT MOD_RES 487 487 PHOSPHORYLATION (AUTO-) (BY SIMILARITY).
FT REPEAT 409 414 HRM 1.
FT REPEAT 551 556 HRM 2.
FT VARSPLIC 244 244 Missing (in isoform 2).
FT /FTId=VSP_007589.
FT VARIANT 558 558 K -> R (in dbSNP:2640).
FT /FTId=VAR_015732.
FT CONFLICT 2 2 Q -> L (in Ref. 2).
FT CONFLICT 24 32 PPAIDFPAE -> RRHRLSRR (in Ref. 1).
FT CONFLICT 137 137 Q -> R (in Ref. 1).
FT CONFLICT 171 171 A -> V (in Ref. 2).
FT CONFLICT 206 206 T -> P (in Ref. 6).
SQ SEQUENCE 630 AA; 71106 MW; D63021651806620B CRC64;
MQGGNSGVRK REEEGDGAGA VAAPPAIDFP AEGPDPEYDE SDVPAEIQVL KEPLQQPTFP
FAVANQLLLV SLLEHLSHVH EPNPLRSRQV FKLLCQTFIK MGLLSSFTCS DEFSSLRLHH
NRAITHLMRS AKERVRQDPC EDISRIQKIR SREVALEAQT SRYLNEFEEL AILGKGGYGR
VYKVRNKLDG QYYAIKKILI KGATKTVCMK VLREVKVLAG LQHPNIVGYH TAWIEHVHVI
QPRADRAAIE LPSLEVLSDQ EEDREQCGVK NDESSSSSII FAEPTPEKEK RFGESDTENQ
NNKSVKYTTN LVIRESGELE STLELQENGL AGLSASSIVE QQLPLRRNSH LEESFTSTEE
SSEENVNFLG QTEAQYHLML HIQMQLCELS LWDWIVERNK RGREYVDESA CPYVMANVAT
KIFQELVEGV FYIHNMGIVH RDLKPRNIFL HGPDQQVKIG DFGLACTDIL QKNTDWTNRN
GKRTPTHTSR VGTCLYASPE QLEGSEYDAK SDMYSLGVVL LELFQPFGTE MERAEVLTGL
RTGQLPESLR KRCPVQAKYI QHLTRRNSSQ RPSAIQLLQS ELFQNSGNVN LTLQMKIIEQ
EKEIAELKKQ LNLLSQDKGV RDDGKDGGVG
//
ID EKI1_HUMAN STANDARD; PRT; 452 AA.
AC Q9HBU6;
DT 16-OCT-2001 (Rel. 40, Created)
DT 16-OCT-2001 (Rel. 40, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Ethanolamine kinase (EC 2.7.1.82) (EKI).
GN EKI1.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RX MEDLINE=21125782; PubMed=11044454;
RA Lykidis A., Wang J., Karim M.A., Jackowski S.;
RT "Overexpression of a mammalian ethanolamine-specific kinase
RT accelerates the CDP-ethanolamine pathway.";
RL J. Biol. Chem. 276:2174-2179(2001).
RN [2]
RP SEQUENCE OF 10-258 FROM N.A.
RC TISSUE=Brain;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC -!- FUNCTION: Highly specific for ethanolamine phosphorylation. May be
CC a rate-controlling step in phosphatidylethanolamine biosynthesis.
CC -!- CATALYTIC ACTIVITY: ATP + ethanolamine = ADP + O-
CC phosphoethanolamine.
CC -!- PATHWAY: Phosphatidylethanolamine biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic.
CC -!- TISSUE SPECIFICITY: Expressed in kidney, liver, placenta, heart,
CC leukocyte, ovary and testis.
CC -!- SIMILARITY: Belongs to the choline/ethanolamine kinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AF207600; AAF71220.2; -.
DR EMBL; BC006111; AAH06111.1; ALT_INIT.
DR GO; GO:0005737; C:cytoplasm; NAS.
DR GO; GO:0004305; F:ethanolamine kinase activity; IDA.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthesis; IDA.
DR InterPro; IPR002573; Choline_kinase.
DR Pfam; PF01633; Choline_kinase; 1.
KW Transferase; Kinase.
FT ACT_SITE 308 308 By similarity.
FT DOMAIN 73 83 POLY-VAL.
FT CONFLICT 228 258 RLIARQLAKIHAIHAHNGWIPKSNLWLKMGK -> SLSSLT
FT LCKGKTTRCFGLTGCRGSRLLLSFF (in Ref. 2).
SQ SEQUENCE 452 AA; 50968 MW; 9AF29EAC556ED91F CRC64;
MLCGRPRSSS DNRNFLRERA GLSSAAVQTR IGNSAASRRS PAARPPVPAP PALPRGRPGT
EGSTSLSAPA VLVVAVAVVV VVVSAVAWAM ANYIHVPPGS PEVPKLNVTV QDQEEHRCRE
GALSLLQHLR PHWDPQEVTL QLFTDGITNK LIGCYVGNTM EDVVLVRIYG NKTELLVDRD
EEVKSFRVLQ AHGCAPQLYC TFNNGLCYEF IQGEALDPKH VCNPAIFRLI ARQLAKIHAI
HAHNGWIPKS NLWLKMGKYF SLIPTGFADE DINKRFLSDI PSSQILQEEM TWMKEILSNL
GSPVVLCHND LLCKNIIYNE KQGDVQFIDY EYSGYNYLAY DIGNHFNEFA GVSDVDYSLY
PDRELQSQWL RAYLEAYKEF KGFGTEVTEK EVEILFIQVN QFALASHFFW GLWALIQAKY
STIEFDFLGY AIVRFNQYFK MKPEVTALKV PE
//
ID EKI2_HUMAN STANDARD; PRT; 394 AA.
AC Q9NVF9;
DT 16-OCT-2001 (Rel. 40, Created)
DT 16-OCT-2001 (Rel. 40, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE Ethanolamine kinase-like protein EKI2 (FLJ10761).
GN EKI2.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RA Isogai T., Ota T., Hayashi K., Sugiyama T., Otsuki T., Suzuki Y.,
RA Nishikawa T., Nagai K., Sugano S., Ishibashi T., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Ishii S., Kawai Y.,
RA Saito K., Yamamoto J., Wakamatsu A., Nakamura Y., Nagahari K.,
RA Masuho Y., Kanehori K.;
RT "NEDO human cDNA sequencing project.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP TISSUE SPECIFICITY.
RX MEDLINE=21125782; PubMed=11044454;
RA Lykidis A., Wang J., Karim M.A., Jackowski S.;
RT "Overexpression of a mammalian ethanolamine-specific kinase
RT accelerates the CDP-ethanolamine pathway.";
RL J. Biol. Chem. 276:2174-2179(2001).
CC -!- SIMILARITY: Belongs to the choline/ethanolamine kinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AK001623; BAA91793.1; -.
DR GO; GO:0004103; F:choline kinase activity; NAS.
DR InterPro; IPR002573; Choline_kinase.
DR Pfam; PF01633; Choline_kinase; 1.
KW Transferase; Kinase.
FT ACT_SITE 247 247 By similarity.
SQ SEQUENCE 394 AA; 44871 MW; 5B0D2C035622A81B CRC64;
MAVPPSAPQQ RASFHLRRHT PCPQCSWGME EKAAASASCR EPPGPPRAAA VAYFGISVDP
DDILPGALRL IQELRPHWKP EQVRTKRFTD GITNKLVACY VEEDMQDCVL VRVYGERTEL
LVDRENEVRN FQLLRAHSCA PKLYCTFQNG LCYEYMQGVA LEPEHIREPR LFRLIALEMA
KIHTIHANGS LPKPILWHKM HNYFTLVKNE INPSLSADVP KVEVLERELA WLKEHLSQLE
SPVVFCHNDL LCKNIIYDSI KGHVRFIDYE YAGYNYQAFD IGNHFNEFAG VNEVDYCLYP
ARETQLQWLH YYLQAQKGMA VTPREVQRLY VQVNKFALGP SCVSSTMTAS LQCCRVGNRH
GEIARLTLSG LFPGVSLLLG SLGPHPEPVL HHRL
//
ID F261_HUMAN STANDARD; PRT; 471 AA.
AC P16118; Q99951;
DT 01-APR-1990 (Rel. 14, Created)
DT 01-NOV-1997 (Rel. 35, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 1 (6PF-2-K/Fru-
DE 2,6-P2ASE liver isozyme) [Includes: 6-phosphofructo-2-kinase
DE (EC 2.7.1.105); Fructose-2,6-bisphosphatase (EC 3.1.3.46)].
GN PFKFB1 OR PFRX OR F6PK.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RC TISSUE=Liver;
RX MEDLINE=90301497; PubMed=2163524;
RA Lange A.J., Pilkis S.J.;
RT "Sequence of human liver 6-phosphofructo-2-kinase/fructose-2,6-
RT bisphosphatase.";
RL Nucleic Acids Res. 18:3652-3652(1990).
RN [2]
RP SEQUENCE OF 94-471 FROM N.A.
RC TISSUE=Liver;
RX MEDLINE=88240421; PubMed=2837207;
RA Algaier J., Uyeda K.;
RT "Molecular cloning, sequence analysis, and expression of a human liver
RT cDNA coding for fructose-6-P,2-kinase:fructose-2,6-bisphosphatase.";
RL Biochem. Biophys. Res. Commun. 153:328-333(1988).
RN [3]
RP SEQUENCE OF 1-409 FROM N.A.
RA Isherwood J.;
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate.
CC -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D-
CC fructose 2,6-bisphosphate.
CC -!- CATALYTIC ACTIVITY: D-fructose 2,6-bisphosphate + H(2)O = D-
CC fructose 6-phosphate + phosphate.
CC -!- ENZYME REGULATION: Phosphorylation results in inhibition of the
CC kinase activity.
CC -!- SUBUNIT: Homodimer.
CC -!- TISSUE SPECIFICITY: Liver.
CC -!- SIMILARITY: In the C-terminal section; belongs to the
CC phosphoglycerate mutase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; X52638; CAA36861.1; -.
DR EMBL; M19938; AAA35818.1; -.
DR EMBL; Z83821; -; NOT_ANNOTATED_CDS.
DR PIR; S12732; S12732.
DR PDB; 1K6M; 11-DEC-02.
DR Genew; HGNC:8872; PFKFB1.
DR GK; P16118; -.
DR MIM; 311790; -.
DR InterPro; IPR003094; 6Pfruct_kin.
DR InterPro; IPR001345; PG/BPGM_mutase.
DR Pfam; PF01591; 6PF2K; 1.
DR Pfam; PF00300; PGAM; 1.
DR PRINTS; PR00991; 6PFRUCTKNASE.
DR ProDom; PD002665; 6Pfruct_kin; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
KW Multifunctional enzyme; Transferase; Kinase; Hydrolase; ATP-binding;
KW Phosphorylation; Multigene family; 3D-structure.
FT DOMAIN 1 250 6-PHOSPHOFRUCTO-2-KINASE.
FT DOMAIN 251 471 FRUCTOSE-2,6-BISPHOSPHATASE.
FT MOD_RES 33 33 PHOSPHORYLATION (BY PKA) (BY SIMILARITY).
FT NP_BIND 49 56 ATP (Potential).
FT BINDING 105 105 FRUCTOSE-6-PHOSPHATE (BY SIMILARITY).
FT ACT_SITE 131 131 Potential.
FT ACT_SITE 161 161 Potential.
FT BINDING 196 196 FRUCTOSE-6-PHOSPHATE (BY SIMILARITY).
FT ACT_SITE 259 259 TELE-PHOSPHOHISTIDINE INTERMEDIATE
FT (BY SIMILARITY).
FT ACT_SITE 328 328 Potential.
FT ACT_SITE 393 393 PROTON DONOR (BY SIMILARITY).
FT CONFLICT 305 305 H -> R (in Ref. 1).
FT CONFLICT 359 359 R -> H (in Ref. 2).
FT CONFLICT 397 398 MR -> HA (in Ref. 2).
FT STRAND 43 48
FT TURN 51 52
FT HELIX 55 68
FT TURN 69 70
FT STRAND 73 77
FT HELIX 78 83
FT TURN 84 84
FT HELIX 91 94
FT TURN 96 97
FT HELIX 99 121
FT TURN 122 122
FT STRAND 127 131
FT HELIX 137 150
FT TURN 151 151
FT STRAND 153 160
FT HELIX 164 175
FT TURN 176 177
FT TURN 180 181
FT HELIX 187 202
FT TURN 203 203
FT TURN 209 214
FT STRAND 217 221
FT TURN 222 225
FT STRAND 226 230
FT HELIX 235 244
FT TURN 245 246
FT STRAND 254 258
FT STRAND 262 262
FT HELIX 263 266
FT TURN 267 268
FT STRAND 269 269
FT STRAND 276 276
FT HELIX 278 294
FT TURN 295 295
FT STRAND 300 303
FT HELIX 307 314
FT TURN 315 316
FT STRAND 321 322
FT HELIX 324 326
FT HELIX 332 334
FT TURN 335 336
FT STRAND 338 338
FT HELIX 339 345
FT HELIX 347 355
FT TURN 357 359
FT TURN 363 364
FT HELIX 368 384
FT STRAND 388 392
FT HELIX 394 405
FT TURN 406 406
FT TURN 409 411
FT HELIX 412 414
FT TURN 419 420
FT STRAND 421 427
FT STRAND 432 438
FT TURN 456 457
FT HELIX 460 464
FT TURN 465 466
SQ SEQUENCE 471 AA; 54681 MW; C4FF081A295FB7D3 CRC64;
MSPEMGELTQ TRLQKIWIPH SSGSSRLQRR RGSSIPQFTN SPTMVIMVGL PARGKTYIST
KLTRYLNWIG TPTKVFNLGQ YRREAVSYKN YEFFLPDNME ALQIRKQCAL AALKDVHNYL
SHEEGHVAVF DATNTTRERR SLILQFAKEH GYKVFFIESI CNDPGIIAEN IRQVKLGSPD
YIDCDREKVL EDFLKRIECY EVNYQPLDEE LDSHLSYIKI FDVGTRYMVN RVQDHIQSRT
VYYLMNIHVT PRSIYLCRHG ESELNIRGRI GGDSGLSVRG KQYAYALANF IQSQGISSLK
VWTSHMKRTI QTAEALGVPY EQWKALNEID AGVCEEMTYE EIQEHYPEEF ALRDQDKYRY
RYPKGESYED LVQRLEPVIM ELERQENVLV ICHQAVMRCL LAYFLDKSSD ELPYLKCPLH
TVLKLTPVAY GCKVESIYLN VEAVNTHREK PENVDITREP EEALDTVPAH Y
//
ID F262_HUMAN STANDARD; PRT; 505 AA.
AC O60825; O60824; Q9H3P1;
DT 16-OCT-2001 (Rel. 40, Created)
DT 16-OCT-2001 (Rel. 40, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2 (6PF-2-K/Fru-
DE 2,6-P2ASE heart-type isozyme) (PFK-2/FBPase-2) [Includes: 6-
DE phosphofructo-2-kinase (EC 2.7.1.105); Fructose-2,6-bisphosphatase
DE (EC 3.1.3.46)].
GN PFKFB2.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A. (ISOFORM 1).
RX MEDLINE=98314509; PubMed=9652401;
RA Heine-Suner D., Diaz-Guillen M.A., Lange A.J.,
RA Rodriguez de Cordoba S.;
RT "Sequence and structure of the human 6-phosphofructo-2-
RT kinase/fructose-2,6-bisphosphatase heart isoform gene (PFKFB2).";
RL Eur. J. Biochem. 254:103-110(1998).
RN [2]
RP SEQUENCE FROM N.A. (ISOFORM 2).
RC TISSUE=Heart;
RX MEDLINE=21269186; PubMed=11374908;
RA Soejima H., Kawamoto S., Akai J., Miyoshi O., Arai Y., Morohka T.,
RA Matsuo S., Niikawa N., Kimura A., Okubo K., Mukai T.;
RT "Isolation of novel heart-specific genes using the BodyMap database.";
RL Genomics 74:115-120(2001).
RN [3]
RP SEQUENCE FROM N.A. (ISOFORM 2).
RA Matsutani A.;
RT "Human insulinoma PFK2/F26DPase.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate.
CC -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D-
CC fructose 2,6-bisphosphate.
CC -!- CATALYTIC ACTIVITY: D-fructose 2,6-bisphosphate + H(2)O = D-
CC fructose 6-phosphate + phosphate.
CC -!- ENZYME REGULATION: Phosphorylation results in the activation of
CC the kinase activity.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O60825-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60825-2; Sequence=VSP_004675;
CC -!- TISSUE SPECIFICITY: Heart.
CC -!- SIMILARITY: In the C-terminal section; belongs to the
CC phosphoglycerate mutase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AJ005577; CAA06605.1; -.
DR EMBL; AJ005578; CAA06606.1; -.
DR EMBL; AB044805; BAB19681.1; -.
DR EMBL; AF470623; AAL99386.1; -.
DR HSSP; P07953; 1TIP.
DR Genew; HGNC:8873; PFKFB2.
DR GK; O60825; -.
DR MIM; 171835; -.
DR GO; GO:0003873; F:6-phosphofructo-2-kinase activity; TAS.
DR GO; GO:0006000; P:fructose metabolism; TAS.
DR InterPro; IPR003094; 6Pfruct_kin.
DR InterPro; IPR001345; PG/BPGM_mutase.
DR Pfam; PF01591; 6PF2K; 1.
DR Pfam; PF00300; PGAM; 1.
DR PRINTS; PR00991; 6PFRUCTKNASE.
DR ProDom; PD002665; 6Pfruct_kin; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
KW Multifunctional enzyme; Transferase; Kinase; Hydrolase; ATP-binding;
KW Phosphorylation; Alternative splicing; Multigene family.
FT DOMAIN 1 248 6-PHOSPHOFRUCTO-2-KINASE.
FT DOMAIN 249 505 FRUCTOSE-2,6-BISPHOSPHATASE.
FT MOD_RES 29 29 PHOSPHORYLATION (BY PKA) (BY SIMILARITY).
FT NP_BIND 45 52 ATP (Potential).
FT BINDING 102 102 FRUCTOSE-6-PHOSPHATE (BY SIMILARITY).
FT BINDING 193 193 FRUCTOSE-6-PHOSPHATE (BY SIMILARITY).
FT ACT_SITE 128 128 Potential.
FT ACT_SITE 158 158 Potential.
FT ACT_SITE 257 257 TELE-PHOSPHOHISTIDINE INTERMEDIATE
FT (BY SIMILARITY).
FT ACT_SITE 326 326 Potential.
FT ACT_SITE 391 391 PROTON DONOR (BY SIMILARITY).
FT MOD_RES 466 466 PHOSPHORYLATION (BY PKA) (BY SIMILARITY).
FT MOD_RES 475 475 PHOSPHORYLATION (BY PKC) (BY SIMILARITY).
FT VARSPLIC 451 505 NNFPKNQTPVRMRRNSFTPLSSSNTIRRPRNYSVGSRPLKP
FT LSPLRAQDMQEGAD -> AAETTLAVRRRPSAASLMLPC
FT (in isoform 2).
FT /FTId=VSP_004675.
FT CONFLICT 28 28 Missing (IN REF. 1; CAA06605).
FT CONFLICT 303 304 QL -> HV (IN REF. 1; CAA06606).
FT CONFLICT 372 372 R -> L (IN REF. 1; CAA06606).
FT CONFLICT 396 396 R -> H (IN REF. 1; CAA06606).
FT CONFLICT 406 406 G -> D (IN REF. 1; CAA06606).
FT CONFLICT 427 427 A -> T (IN REF. 1; CAA06606).
SQ SEQUENCE 505 AA; 58476 MW; 5CD6A933A7EBF604 CRC64;
MSGASSSEQN NNSYETKTPN LRMSEKKCSW ASYMTNSPTL IVMIGLPARG KTYVSKKLTR
YLNWIGVPTK VFNLGVYRRE AVKSYKSYDF FRHDNEEAMK IRKQCALVAL EDVKAYLTEE
NGQIAVFDAT NTTRERRDMI LNFAEQNSFK VFFVESVCDD PDVIAANILE VKVSSPDYPE
RNRENVMEDF LKRIECYKVT YRPLDPDNYD KDLSFIKVIN VGQRFLVNRV QDYIQSKIVY
YLMNIHVQPR TIYLCRHGES EFNLLGKIGG DSGLSVRGKQ FAQALRKFLE EQEITDLKVW
TSQLKRTIQT AESLGVPYEQ WKILNEIDAG VCEEMTYAEI EKRYPEEFAL RDQEKYLYRY
PGGESYQDLV QRLEPVIMEL ERQGNVLVIS HQAVMRCLLA YFLDKGADEL PYLRCPLHTI
FKLTPVAYGC KVETIKLNVE AVNTHRDKPT NNFPKNQTPV RMRRNSFTPL SSSNTIRRPR
NYSVGSRPLK PLSPLRAQDM QEGAD
//
ID F263_HUMAN STANDARD; PRT; 520 AA.
AC Q16875; O43622; O75902;
DT 15-JUL-1998 (Rel. 36, Created)
DT 15-JUL-1998 (Rel. 36, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 3 (6PF-2-K/Fru-
DE 2,6-P2ASE brain/placenta-type isozyme) (iPFK-2) [Includes: 6-
DE phosphofructo-2-kinase (EC 2.7.1.105); Fructose-2,6-bisphosphatase
DE (EC 3.1.3.46)].
GN PFKFB3.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A. (ISOFORM 1).
RC TISSUE=Placenta;
RX MEDLINE=96271013; PubMed=8830046;
RA Sakai A., Kato M., Fukasawa M., Ishiguro M., Furuya E., Sakakibara R.;
RT "Cloning of cDNA encoding for a novel isozyme of fructose
RT 6-phosphate, 2-kinase/fructose 2,6-bisphosphatase from human
RT placenta.";
RL J. Biochem. 119:506-511(1996).
RN [2]
RP SEQUENCE FROM N.A. (ISOFORM 1).
RC TISSUE=Brain;
RX MEDLINE=99172090; PubMed=10072580;
RA Manzano A., Rosa J.L., Ventura F., Perez J.X., Nadal M., Estivill X.,
RA Ambrosio S., Gil J., Bartrons R.;
RT "Molecular cloning, expression, and chromosomal localization of a
RT ubiquitously expressed human 6-phosphofructo-2-kinase/ fructose-2,
RT 6-bisphosphatase gene (PFKFB3).";
RL Cytogenet. Cell Genet. 83:214-217(1998).
RN [3]
RP SEQUENCE FROM N.A. (ISOFORM 1).
RC TISSUE=Brain;
RA El-Maghrabi M.R.;
RT "Human brain 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SEQUENCE FROM N.A. (ISOFORM 2).
RC TISSUE=Skeletal muscle;
RX MEDLINE=99179012; PubMed=10077634;
RA Chesney J., Mitchell R.A., Benigni F., Bacher M., Spiegel L.,
RA Al-Abed Y., Han J.H., Metz C., Bucala R.;
RT "An inducible gene product for 6-phosphofructo-2-kinase with an AU-
RT rich instability element: role in tumor cell glycolysis and the
RT Warburg effect.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:3047-3052(1999).
RN [5]
RP SEQUENCE FROM N.A. (ISOFORM 1).
RC TISSUE=Testis;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC -!- FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate.
CC -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D-
CC fructose 2,6-bisphosphate.
CC -!- CATALYTIC ACTIVITY: D-fructose 2,6-bisphosphate + H(2)O = D-
CC fructose 6-phosphate + phosphate.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q16875-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16875-2; Sequence=VSP_004680;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: In the C-terminal section; belongs to the
CC phosphoglycerate mutase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; D49817; BAA08624.1; -.
DR EMBL; AF109735; AAD08818.1; -.
DR EMBL; AF041831; AAB99795.1; -.
DR EMBL; AF041823; AAB99795.1; JOINED.
DR EMBL; AF041824; AAB99795.1; JOINED.
DR EMBL; AF041825; AAB99795.1; JOINED.
DR EMBL; AF041826; AAB99795.1; JOINED.
DR EMBL; AF041827; AAB99795.1; JOINED.
DR EMBL; AF041828; AAB99795.1; JOINED.
DR EMBL; AF041829; AAB99795.1; JOINED.
DR EMBL; AF041830; AAB99795.1; JOINED.
DR EMBL; AF056320; AAC62000.1; -.
DR EMBL; BC040482; AAH40482.1; -.
DR PIR; JC4626; JC4626.
DR HSSP; P07953; 1FBT.
DR Genew; HGNC:8874; PFKFB3.
DR GK; Q16875; -.
DR MIM; 605319; -.
DR GO; GO:0003873; F:6-phosphofructo-2-kinase activity; NAS.
DR GO; GO:0006003; P:fructose 2,6-bisphosphate metabolism; NAS.
DR InterPro; IPR003094; 6Pfruct_kin.
DR InterPro; IPR001345; PG/BPGM_mutase.
DR Pfam; PF01591; 6PF2K; 1.
DR Pfam; PF00300; PGAM; 1.
DR PRINTS; PR00991; 6PFRUCTKNASE.
DR ProDom; PD002665; 6Pfruct_kin; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
KW Multifunctional enzyme; Transferase; Kinase; Hydrolase; ATP-binding;
KW Phosphorylation; Multigene family; Alternative splicing.
FT DOMAIN 1 245 6-PHOSPHOFRUCTO-2-KINASE.
FT DOMAIN 246 520 FRUCTOSE-2,6-BISPHOSPHATASE.
FT NP_BIND 42 49 ATP (By similarity).
FT BINDING 99 99 FRUCTOSE-6-PHOSPHATE (BY SIMILARITY).
FT BINDING 190 190 FRUCTOSE-6-PHOSPHATE (BY SIMILARITY).
FT ACT_SITE 125 125 Potential.
FT ACT_SITE 155 155 Potential.
FT ACT_SITE 254 254 TELE-PHOSPHOHISTIDINE INTERMEDIATE
FT (BY SIMILARITY).
FT ACT_SITE 323 323 Potential.
FT ACT_SITE 388 388 PROTON DONOR (BY SIMILARITY).
FT MOD_RES 461 461 PHOSPHORYLATION (BY PKA) (BY SIMILARITY).
FT MOD_RES 471 471 PHOSPHORYLATION (BY PKC) (BY SIMILARITY).
FT VARSPLIC 506 520 NMKGSRSSADSSRKH -> PLLGQACLT (in isoform
FT 2).
FT /FTId=VSP_004680.
FT CONFLICT 136 136 M -> V (in Ref. 3).
FT CONFLICT 141 141 A -> G (in Ref. 4).
SQ SEQUENCE 520 AA; 59609 MW; A7675A4ADC376879 CRC64;
MPLELTQSRV QKIWVPVDHR PSLPRSCGPK LTNSPTVIVM VGLPARGKTY ISKKLTRYLN
WIGVPTKVFN VGEYRREAVK QYSSYNFFRP DNEEAMKVRK QCALAALRDV KSYLAKEGGQ
IAVFDATNTT RERRHMILHF AKENDFKAFF IESVCDDPTV VASNIMEVKI SSPDYKDCNS
AEAMDDFMKR ISCYEASYQP LDPDKCDRDL SLIKVIDVGR RFLVNRVQDH IQSRIVYYLM
NIHVQPRTIY LCRHGENEHN LQGRIGGDSG LSSRGKKFAS ALSKFVEEQN LKDLRVWTSQ
LKSTIQTAEA LRLPYEQWKA LNEIDAGVCE ELTYEEIRDT YPEEYALREQ DKYYYRYPTG
ESYQDLVQRL EPVIMELERQ ENVLVICHQA VLRCLLAYFL DKSAEEMPYL KCPLHTVLKL
TPVAYGCRVE SIYLNVESVC THRERSEDAK KGPNPLMRRN SVTPLASPEP TKKPRINSFE
EHVASTSAAL PSCLPPEVPT QLPGQNMKGS RSSADSSRKH
//
ID F264_HUMAN STANDARD; PRT; 468 AA.
AC Q16877;
DT 15-JUL-1998 (Rel. 36, Created)
DT 30-MAY-2000 (Rel. 39, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 4 (6PF-2-K/Fru-
DE 2,6-P2ASE testis-type isozyme) [Includes: 6-phosphofructo-2-kinase
DE (EC 2.7.1.105); Fructose-2,6-bisphosphatase (EC 3.1.3.46)].
GN PFKFB4.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RA Sakakibara R.;
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SEQUENCE FROM N.A.
RC TISSUE=Testis;
RX MEDLINE=99196986; PubMed=10095107;
RA Manzano A., Perez J.X., Nadal M., Estivill X., Lange A., Bartrons R.;
RT "Cloning, expression and chromosomal localization of a human testis
RT 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase gene.";
RL Gene 229:83-89(1999).
RN [3]
RP SEQUENCE FROM N.A.
RC TISSUE=Placenta;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [4]
RP SEQUENCE OF 356-468 FROM N.A.
RC TISSUE=Placenta;
RX MEDLINE=96271013; PubMed=8830046;
RA Sakai A., Kato M., Fukasawa M., Ishiguro M., Furuya E., Sakakibara R.;
RT "Cloning of cDNA encoding for a novel isozyme of fructose 6-phosphate,
RT 2-kinase/fructose 2,6-bisphosphatase from human placenta.";
RL J. Biochem. 119:506-511(1996).
CC -!- FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate.
CC -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D-
CC fructose 2,6-bisphosphate.
CC -!- CATALYTIC ACTIVITY: D-fructose 2,6-bisphosphate + H(2)O = D-
CC fructose 6-phosphate + phosphate.
CC -!- ENZYME REGULATION: The most important regulatory mechanism of
CC these opposing activities is by phosphorylation and
CC dephosphorylation of the enzyme (By similarity).
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SIMILARITY: In the C-terminal section; belongs to the
CC phosphoglycerate mutase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; D49818; BAA18921.1; -.
DR EMBL; AF108765; AAD09427.1; -.
DR EMBL; BC010269; AAH10269.1; -.
DR Genew; HGNC:8875; PFKFB4.
DR GK; Q16877; -.
DR MIM; 605320; -.
DR GO; GO:0003873; F:6-phosphofructo-2-kinase activity; NAS.
DR GO; GO:0006003; P:fructose 2,6-bisphosphate metabolism; NAS.
DR InterPro; IPR003094; 6Pfruct_kin.
DR InterPro; IPR001345; PG/BPGM_mutase.
DR Pfam; PF01591; 6PF2K; 1.
DR Pfam; PF00300; PGAM; 1.
DR PRINTS; PR00991; 6PFRUCTKNASE.
DR ProDom; PD002665; 6Pfruct_kin; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
KW Multifunctional enzyme; Transferase; Kinase; Hydrolase; ATP-binding;
KW Phosphorylation; Multigene family.
FT INIT_MET 0 0 By similarity.
FT DOMAIN 1 248 6-PHOSPHOFRUCTO-2-KINASE.
FT DOMAIN 249 468 FRUCTOSE-2,6-BISPHOSPHATASE.
FT NP_BIND 45 52 ATP (By similarity).
FT BINDING 102 102 FRUCTOSE-6-PHOSPHATE (BY SIMILARITY).
FT BINDING 193 193 FRUCTOSE-6-PHOSPHATE (BY SIMILARITY).
FT ACT_SITE 128 128 Potential.
FT ACT_SITE 158 158 Potential.
FT ACT_SITE 256 256 TELE-PHOSPHOHISTIDINE INTERMEDIATE
FT (BY SIMILARITY).
FT ACT_SITE 325 325 Potential.
FT ACT_SITE 390 390 PROTON DONOR (BY SIMILARITY).
FT MOD_RES 443 443 PHOSPHORYLATION (BY PKC) (POTENTIAL).
SQ SEQUENCE 468 AA; 53908 MW; DB96CD59913BDCCB CRC64;
ASPRELTQNP LKKIWMPYSN GRPALHACQR GVCMTNCPTL IVMVGLPARG KTYISKKLTR
YLNWIGVPTR EFNVGQYRRD VVKTYKSFEF FLPDNEEGLK IRKQCALAAL RDVRRFLSEE
GGHVAVFDAT NTTRERRATI FNFGEQNGYK TFFVESICVD PEVIAANIVQ VKLGSPDYVN
RDSDEATEDF MRRIECYENS YESLDEDLDR DLSYIKIMDV GQSYVVNRVA DHIQSRIVYY
LMNIHVTPRS IYLCRHGESE LNLKGRIGGD PGLSPRGREF AKSLAQFISD QNIKDLKVWT
SQMKRTIQTA EALGVPYEQW KVLNEIDAGV CEEMTYEEIQ DNYPLEFALR DQDKYRYRYP
KGESYEDLVQ RLEPVIMELE RQENVLVICH QAVMRCLLAY FLDKAAEQLP YLKCPLHTVL
KLTPVAYGCK VESIFLNVAA VNTHRDRPQN VDISRPPEEA LVTVPAHQ
//
ID FN3K_HUMAN STANDARD; PRT; 309 AA.
AC Q9H479;
DT 16-OCT-2001 (Rel. 40, Created)
DT 16-OCT-2001 (Rel. 40, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE Fructosamine-3-kinase (EC 2.7.1.-).
GN FN3K.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A., PARTIAL SEQUENCE, ACETYLATION, AND
RP CHARACTERIZATION.
RC TISSUE=Kidney;
RX MEDLINE=20468660; PubMed=11016445;
RA Delpierre G., Rider M.H., Collard F., Stroobant V., Vanstapel F.,
RA Santos H., Van Schaftingen E.;
RT "Identification, cloning, and heterologous expression of a mammalian
RT fructosamine-3-kinase.";
RL Diabetes 49:1627-1634(2000).
RN [2]
RP SEQUENCE FROM N.A.
RC TISSUE=Brain;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC -!- FUNCTION: May initiate a process leading to the deglycation of
CC fructoselysine and of glycated proteins. May play a role in the
CC phosphorylation of 1-deoxy-1-morpholinofructose (DMF),
CC fructoselysine, fructoseglycine, fructose and glycated lysozyme.
CC -!- SUBUNIT: Monomer (Probable).
CC -!- TISSUE SPECIFICITY: Expressed in erythrocytes.
CC -!- SIMILARITY: Belongs to the fructosamine kinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AJ404615; CAC16393.1; -.
DR EMBL; BC042680; AAH42680.1; -.
DR GO; GO:0030387; F:fructosamine-3-kinase activity; NAS.
DR GO; GO:0030393; P:fructoselysine metabolism; NAS.
DR InterPro; IPR005581; Fructosamin_kin.
DR Pfam; PF03881; Fructosamin_kin; 1.
KW Transferase; Kinase; Acetylation.
FT MOD_RES 1 1 ACETYLATION.
SQ SEQUENCE 309 AA; 35171 MW; BA886A86655DE28F CRC64;
MEQLLRAELR TATLRAFGGP GAGCISEGRA YDTDAGPVFV KVNRRTQARQ MFEGEVASLE
ALRSTGLVRV PRPMKVIDLP GGGAAFVMEH LKMKSLSSQA SKLGEQMADL HLYNQKLREK
LKEEENTVGR RGEGAEPQYV DKFGFHTVTC CGFIPQVNEW QDDWPTFFAR HRLQAQLDLI
EKDYADREAR ELWSRLQVKI PDLFCGLEIV PALLHGDLWS GNVAEDDVGP IIYDPASFYG
HSEFELAIAL MFGGFPRSFF TAYHRKIPKA PGFDQRLLLY QLFNYLNHWN HFGREYRSPS
LGTMRRLLK
//
ID FN3X_HUMAN STANDARD; PRT; 309 AA.
AC Q9HA64; Q9H0U7;
DT 16-OCT-2001 (Rel. 40, Created)
DT 16-OCT-2001 (Rel. 40, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE Hypothetical fructosamine kinase-like protein FLJ12171/DKFZp564D202.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RC TISSUE=Mammary gland;
RA Isogai T., Ota T., Hayashi K., Sugiyama T., Otsuki T., Suzuki Y.,
RA Nishikawa T., Nagai K., Sugano S., Shiratori A., Sudo H.,
RA Wagatsuma M., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Chiba Y., Ishida S., Murakawa K., Ono Y., Takiguchi S.,
RA Watanabe S., Kimura K., Murakami K., Ishii S., Kawai Y., Saito K.,
RA Yamamoto J., Wakamatsu A., Nakamura Y., Nagahari K., Masuho Y.,
RA Ninomiya K., Iwayanagi T.;
RT "NEDO human cDNA sequencing project.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SEQUENCE OF 1-197 FROM N.A.
RC TISSUE=Brain;
RX MEDLINE=21154917; PubMed=11230166;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP SEQUENCE OF 136-309 FROM N.A.
RC TISSUE=Placenta;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC -!- SIMILARITY: Belongs to the fructosamine kinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AK022233; BAB13992.1; -.
DR EMBL; AL136631; CAB66566.1; -.
DR EMBL; BC001458; AAH01458.1; -.
DR InterPro; IPR005581; Fructosamin_kin.
DR Pfam; PF03881; Fructosamin_kin; 1.
KW Hypothetical protein; Transferase; Kinase.
FT CONFLICT 129 129 G -> W (in Ref. 2).
FT CONFLICT 136 138 ERP -> HEA (in Ref. 3).
FT CONFLICT 265 265 G -> C (in Ref. 3).
FT CONFLICT 278 278 R -> Q (in Ref. 3).
SQ SEQUENCE 309 AA; 34440 MW; C34ED1C5BB2A7FF0 CRC64;
MEELLRRELG CSSVRATGHS GGGCISQGRS YDTDQGRVFV KVNPKAEARR MFEGEMASLT
AILKTNTVKV PKPIKVLDAP GGGSVLVMEH MDMRHLSSHA AKLGAQLADL HLDNKKLGEM
RLKEAGTVGR GGGQEERPFV ARFGFDVVTC CGYLPQVNDW QEDWVVFYAR QRIQPQMDMV
EKESGDREAL QLWSALQLKI PDLFRDLEII PALLHGDLWG GNVAEDSSGP VIFDPASFYG
HSEYELAIAG MFGGFSSSFY SAYHGKIPKA PGFEKRLRLY QLFHYLNHWN HFGSGYRGSS
LNIMRNLVK
//
ID FRAP_HUMAN STANDARD; PRT; 2549 AA.
AC P42345; Q9Y4I3;
DT 01-NOV-1995 (Rel. 32, Created)
DT 01-NOV-1995 (Rel. 32, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE FKBP-rapamycin associated protein (FRAP) (Rapamycin target protein).
GN FRAP1 OR FRAP OR FRAP2.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RC TISSUE=Brain;
RX MEDLINE=94277209; PubMed=8008069;
RA Brown E.J., Albers M.W., Shin T.B., Ichikawa K., Keith C.T.,
RA Lane W.S., Schreiber S.L.;
RT "A mammalian protein targeted by G1-arresting rapamycin-receptor
RT complex.";
RL Nature 369:756-758(1994).
RN [2]
RP SEQUENCE FROM N.A.
RX MEDLINE=98317532; PubMed=9653645;
RA Onyango P., Lubyova B., Gardellin P., Kurzbauer R., Weith A.;
RT "Molecular cloning and expression analysis of five novel genes in
RT chromosome 1p36.";
RL Genomics 50:187-198(1998).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 2018-2112.
RX MEDLINE=96279639; PubMed=8662507;
RA Choi J., Chen J., Schreiber S.L., Clardy J.;
RT "Structure of the FKBP12-rapamycin complex interacting with the
RT binding domain of human FRAP.";
RL Science 273:239-242(1996).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 2018-2112.
RX MEDLINE=99190960; PubMed=10089303;
RA Liang J., Choi J., Clardy J.;
RT "Refined structure of the FKBP12-rapamycin-FRB ternary complex at 2.2
RT A resolution.";
RL Acta Crystallogr. D 55:736-744(1999).
CC -!- FUNCTION: ACTS AS THE TARGET FOR THE CELL-CYCLE ARREST AND
CC IMMUNOSUPPRESSIVE EFFECTS OF THE FKBP12-RAPAMYCIN COMPLEX.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC -!- SIMILARITY: Contains 8 HEAT repeats.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; L34075; AAA58486.1; -.
DR EMBL; U88966; AAC39933.1; -.
DR PIR; S45340; S45340.
DR PDB; 1AUE; 18-NOV-98.
DR PDB; 1FAP; 23-JUL-97.
DR PDB; 1NSG; 18-MAR-98.
DR PDB; 2FAP; 09-AUG-99.
DR PDB; 3FAP; 13-SEP-00.
DR PDB; 4FAP; 13-SEP-00.
DR Genew; HGNC:3942; FRAP1.
DR MIM; 601231; -.
DR GO; GO:0000074; P:regulation of cell cycle; TAS.
DR InterPro; IPR008938; ARM.
DR InterPro; IPR003151; FAT.
DR InterPro; IPR003152; FATC.
DR InterPro; IPR000357; HEAT.
DR InterPro; IPR000403; PI3_PI4_kinase.
DR InterPro; IPR008940; Prenyl_trans.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM00146; PI3Kc; 1.
DR PROSITE; PS50077; HEAT_REPEAT; FALSE_NEG.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
KW Transferase; Kinase; Repeat; 3D-structure.
FT REPEAT 16 53 HEAT 1.
FT REPEAT 650 688 HEAT 2.
FT REPEAT 859 897 HEAT 3.
FT REPEAT 988 1025 HEAT 4.
FT REPEAT 1069 1106 HEAT 5.
FT REPEAT 1109 1148 HEAT 6.
FT REPEAT 1150 1186 HEAT 7.
FT DOMAIN 1382 1982 FAT.
FT REPEAT 1933 1970 HEAT 8.
FT DOMAIN 2182 2549 PI3K/PI4K.
FT CONFLICT 353 353 K -> N (in Ref. 2).
FT CONFLICT 359 359 S -> N (in Ref. 2).
FT CONFLICT 364 364 D -> N (in Ref. 2).
FT CONFLICT 390 390 M -> L (in Ref. 2).
FT CONFLICT 430 430 R -> L (in Ref. 2).
FT CONFLICT 455 457 VLD -> GVE (in Ref. 2).
FT CONFLICT 461 461 A -> G (in Ref. 2).
FT CONFLICT 482 484 VFT -> FFN (in Ref. 2).
FT CONFLICT 489 489 L -> V (in Ref. 2).
FT CONFLICT 513 513 L -> I (in Ref. 2).
FT CONFLICT 539 539 L -> V (in Ref. 2).
FT CONFLICT 553 553 R -> C (in Ref. 2).
FT CONFLICT 956 999 MRIFRDQSLSHHHTMVVQAITFIFKSLGLKCVQFLPQVMPT
FT FLN -> ADLPRPVTLSSSHHGCPGHHLHLQVPGTQMCAVP
FT APGHAHVPY (in Ref. 2).
FT CONFLICT 1075 1075 I -> S (in Ref. 2).
FT HELIX 2023 2039
FT TURN 2040 2041
FT HELIX 2044 2060
FT HELIX 2065 2091
FT HELIX 2094 2111
SQ SEQUENCE 2549 AA; 288888 MW; 7D9AD6E784882AB4 CRC64;
MLGTGPAAAT TAATTSSNVS VLQQFASGLK SRNEETRAKA AKELQHYVTM ELREMSQEES
TRFYDQLNHH IFELVSSSDA NERKGGILAI ASLIGVEGGN ATRIGRFANY LRNLLPSNDP
VVMEMASKAI GRLAMAGDTF TAEYVEFEVK RALEWLGADR NEGRRHAAVL VLRELAISVP
TFFFQQVQPF FDNIFVAVWD PKQAIREGAV AALRACLILT TQREPKEMQK PQWYRHTFEE
AEKGFDETLA KEKGMNRDDR IHGALLILNE LVRISSMEGE RLREEMEEIT QQQLVHDKYC
KDLMGFGTKP RHITPFTSFQ AVQPQQSNAL VGLLGYSSHQ GLMGFGTSPS PAKSTLVESR
CCRDLMEEKF DQVCQWVLKC RNSKNSLIQM TILNLLPRLA AFRPSAFTDT QYLQDTMNHV
LSCVKKEKER TAAFQALGLL SVAVRSEFKV YLPRVLDIIR AALPPKDFAH KRQKAMQVDA
TVFTCISMLA RAMGPGIQQD IKELLEPMLA VGLSPALTAV LYDLSRQIPQ LKKDIQDGLL
KMLSLVLMHK PLRHPGMPKG LAHQLASPGL TTLPEASDVG SITLALRTLG SFEFEGHSLT
QFVRHCADHF LNSEHKEIRM EAARTCSRLL TPSIHLISGH AHVVSQTAVQ VVADVLSKLL
VVGITDPDPD IRYCVLASLD ERFDAHLAQA ENLQALFVAL NDQVFEIREL AICTVGRLSS
MNPAFVMPFL RKMLIQILTE LEHSGIGRIK EQSARMLGHL VSNAPRLIRP YMEPILKALI
LKLKDPDPDP NPGVINNVLA TIGELAQVSG LEMRKWVDEL FIIIMDMLQD SSLLAKRQVA
LWTLGQLVAS TGYVVEPYRK YPTLLEVLLN FLKTEQNQGT RREAIRVLGL LGALDPYKHK
VNIGMIDQSR DASAVSLSES KSSQDSSDYS TSEMLVNMGN LPLDEFYPAV SMVALMRIFR
DQSLSHHHTM VVQAITFIFK SLGLKCVQFL PQVMPTFLNV IRVCDGAIRE FLFQQLGMLV
SFVKSHIRPY MDEIVTLMRE FWVMNTSIQS TIILLIEQIV VALGGEFKLY LPQLIPHMLR
VFMHDNSPGR IVSIKLLAAI QLFGANLDDY LHLLLPPIVK LFDAPEAPLP SRKAALETVD
RLTESLDFTD YASRIIHPIV RTLDQSPELR STAMDTLSSL VFQLGKKYQI FIPMVNKVLV
RHRINHQRYD VLICRIVKGY TLADEEEDPL IYQHRMLRSG QGDALASGPV ETGPMKKLHV
STINLQKAWG AARRVSKDDW LEWLRRLSLE LLKDSSSPSL RSCWALAQAY NPMARDLFNA
AFVSCWSELN EDQQDELIRS IELALTSQDI AEVTQTLLNL AEFMEHSDKG PLPLRDDNGI
VLLGERAAKC RAYAKALHYK ELEFQKGPTP AILESLISIN NKLQQPEAAA GVLEYAMKHF
GELEIQATWY EKLHEWEDAL VAYDKKMDTN KDDPELMLGR MRCLEALGEW GQLHQQCCEK
WTLVNDETQA KMARMAAAAA WGLGQWDSME EYTCMIPRDT HDGAFYRAVL ALHQDLFSLA
QQCIDKARDL LDAELTAMAG ESYSRAYGAM VSCHMLSELE EVIQYKLVPE RREIIRQIWW
ERLQGCQRIV EDWQKILMVR SLVVSPHEDM RTWLKYASLC GKSGRLALAH KTLVLLLGVD
PSRQLDHPLP TVHPQVTYAY MKNMWKSARK IDAFQHMQHF VQTMQQQAQH AIATEDQQHK
QELHKLMARC FLKLGEWQLN LQGINESTIP KVLQYYSAAT EHDRSWYKAW HAWAVMNFEA
VLHYKHQNQA RDEKKKLRHA SGANITNATT AATTAATATT TASTEGSNSE SEAESTENSP
TPSPLQKKVT EDLSKTLLMY TVPAVQGFFR SISLSRGNNL QDTLRVLTLW FDYGHWPDVN
EALVEGVKAI QIDTWLQVIP QLIARIDTPR PLVGRLIHQL LTDIGRYHPQ ALIYPLTVAS
KSTTTARHNA ANKILKNMCE HSNTLVQQAM MVSEELIRVA ILWHEMWHEG LEEASRLYFG
ERNVKGMFEV LEPLHAMMER GPQTLKETSF NQAYGRDLME AQEWCRKYMK SGNVKDLTQA
WDLYYHVFRR ISKQLPQLTS LELQYVSPKL LMCRDLELAV PGTYDPNQPI IRIQSIAPSL
QVITSKQRPR KLTLMGSNGH EFVFLLKGHE DLRQDERVMQ LFGLVNTLLA NDPTSLRKNL
SIQRYAVIPL STNSGLIGWV PHCDTLHALI RDYREKKKIL LNIEHRIMLR MAPDYDHLTL
MQKVEVFEHA VNNTAGDDLA KLLWLKSPSS EVWFDRRTNY TRSLAVMSMV GYILGLGDRH
PSNLMLDRLS GKILHIDFGD CFEVAMTREK FPEKIPFRLT RMLTNAMEVT GLDGNYRITC
HTVMEVLREH KDSVMAVLEA FVYDPLLNWR LMDTNTKGNK RSRTRTDSYS AGQSVEILDG
VELGEPAHKK TGTTVPESIH SFIGDGLVKP EALNKKAIQI INRVRDKLTG RDFSHDDTLD
VPTQVELLIK QATSHENLCQ CYIGWCPFW
//
ID FUK_HUMAN STANDARD; PRT; 990 AA.
AC Q8N0W3;
DT 28-FEB-2003 (Rel. 41, Created)
DT 28-FEB-2003 (Rel. 41, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE L-fucose kinase (EC 2.7.1.52) (Fucokinase).
GN FUK.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RX MEDLINE=22052376; PubMed=12056818;
RA Hinderlich S., Berger M., Blume A., Chen H., Ghaderi D., Bauer C.;
RT "Identification of human L-fucose kinase amino acid sequence.";
RL Biochem. Biophys. Res. Commun. 294:650-654(2002).
RN [2]
RP SEQUENCE FROM N.A.
RC TISSUE=Uterus;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC -!- FUNCTION: Takes part in the salvage pathway for reutilization of
CC fucose from the degradation of oligosaccharides.
CC -!- CATALYTIC ACTIVITY: ATP + 6-deoxy-L-galactose = ADP + 6-deoxy-L-
CC galactose 1-phosphate.
CC -!- SIMILARITY: BELONGS TO THE GHMP KINASE FAMILY.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AJ441184; CAD29647.1; -.
DR EMBL; BC032542; AAH32542.1; -.
DR InterPro; IPR001174; Galkinase.
DR InterPro; IPR006204; GHMP_kinase.
DR InterPro; IPR006203; GHMPknse_ATP.
DR InterPro; IPR006206; Mev_galkinase.
DR Pfam; PF00288; GHMP_kinases; 1.
DR PRINTS; PR00960; LMBPPROTEIN.
DR PRINTS; PR00959; MEVGALKINASE.
DR PROSITE; PS00627; GHMP_KINASES_ATP; FALSE_NEG.
KW Kinase; Transferase; ATP-binding.
FT NP_BIND 740 751 ATP (Potential).
SQ SEQUENCE 990 AA; 107276 MW; EA97E05A26C51B89 CRC64;
MGRDFPFDDC GRAFTCLPVE NPEAPVEALV CNLDCLLDIM TYRLGPGSPP GVWVCSTDML
LSVPANPGIS WDSFRGARVI ALPGSPAYAQ NHGVYLTDPQ GLVLDIYYQG TEAEIQRCVR
PDGRVPLVSG VVFFSVETAE RLLATHVSPP LDACTYLGLD SGARPVQLSL FFDILHCMAE
NVTREDFLVG RPPELGQGDA DVAGYLQSAR AQLWRELRDQ PLTMAYVSSG SYSYMTSSAS
EFLLSLTLPG APGAQIVHSQ VEEQQLLAAG SSVVSCLLEG PVQLGPGSVL QHCHLQGPIH
IGAGCLVTGL DTAHSKALHG RELRDLVLQG HHTRLHGSPG HAFTLVGRLD SWERQGAGTY
LNVPWSEFFK RTGVRAWDLW DPETLPAEYC LPSARLFPVL HPSRELGPQD LLWMLDHQED
GGEALRAWRA SWRLSWEQLQ PCLDRAATLA SRRDLFFRQA LHKARHVLEA RQDLSLRPLI
WAAVREGCPG PLLATLDQVA AGAGDPGVAA RALACVADVL GCMAEGRGGL RSGPAANPEW
MRPFSYLECG DLAAGVEALA QERDKWLSRP ALLVRAARHY EGAGQILIRQ AVMSAQHFVS
TEQVELPGPG QWVVAECPAR VDFSGGWSDT PPLAYELGGA VLGLAVRVDG RRPIGARARR
IPEPELWLAV GPRQDEMTVK IVCRCLADLR DYCQPHAPGA LLKAAFICAG IVHVHSELQL
SEQLLRTFGG GFELHTWSEL PHGSGLGTSS ILAGTALAAL QRAAGRVVGT EALIHAVLHL
EQVLTTGGGW QDQVGGLMPG IKVGRSRAQL PLKVEVEEVT VPEGFVQKLN DHLLLVYTGK
TRLARNLLQD VLRSWYARLP AVVQNAHSLV RQTEECAEGF RQGSLPLLGQ CLTSYWEQKK
LMAPGCEPLT VRRMMDVLAP HVHGQSLAGA GGGGFLYLLT KEPQQKEALE AVLAKTEGLG
NYSIHLVEVD TQGLSLKLLG TEASTCCPFP
//
ID FYV1_HUMAN STANDARD; PRT; 578 AA.
AC Q9Y2I7;
DT 16-OCT-2001 (Rel. 40, Created)
DT 16-OCT-2001 (Rel. 40, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE FYVE finger-containing phosphoinositide kinase (EC 2.7.1.68) (1-
DE phosphatidylinositol-4-phosphate 5-kinase) (PIP5K) (PtdIns(4)P-5-
DE kinase) (p235) (Fragment).
GN PIP5K3 OR PIKFYVE OR KIAA0981.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RC TISSUE=Brain;
RX MEDLINE=99246063; PubMed=10231032;
RA Nagase T., Ishikawa K.-I., Suyama M., Kikuno R., Hirosawa M.,
RA Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 6:63-70(1999).
CC -!- FUNCTION: SUPPORTS THE INTRACELLULAR PIP POOL AND TO A LESSER
CC EXTENT, THE PI 4,5-P(2) POOL. IT GENERATES PIP FROM PI AND, TO A
CC LESSER EXTENT, PI 4,5-P(2) FROM PI 4-P. THERE ARE INDICATIONS THAT
CC IT PHOSPHORYLATES THE D-5 RATHER THAN THE D-4 POSITION. HAS A ROLE
CC IN ENDOSOME-RELATED MEMBRANE TRAFFICKING (BY SIMILARITY).
CC -!- CATALYTIC ACTIVITY: ATP + 1-phosphatidyl-1D-myo-inositol 4-
CC phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.
CC -!- COFACTOR: Binds 2.2 zinc equivalents per molecule (By similarity).
CC -!- SIMILARITY: Belongs to the PtdIns(4)P-5-kinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AB023198; BAA76825.1; -.
DR Genew; HGNC:23785; PIP5K3.
DR InterPro; IPR002498; PIP5K.
DR Pfam; PF01504; PIP5K; 1.
DR SMART; SM00330; PIPKc; 1.
KW Transferase; Kinase.
FT NON_TER 1 1
SQ SEQUENCE 578 AA; 64554 MW; FCBE9CA1F3AAFC22 CRC64;
PSVPPSPGRL RQGEESKISA MDASPRNISP GLQNGEKEDR FLTTLSSQSS TSSTHLQLPT
PPEVMSEQSV GGPPELDTAS SSEDVFDGHL LGSTDSQVKE KSTMKAIFAN LLPGNSYNPI
PFPFDPDKHY LMYEHERVPI AVCEKEPSSI IAFALSCKEY RNALEELSKA TQWNSAEEGL
PTNSTSDSRP KSSSPIRLPE MSGGQTNRTT ETEPQPTKKA SGMLSFFRGT AGKSPDLSSQ
KRETLRGADS AYYQVGQTGK EGTENQGVEP QDEVDGGDTQ KKQLINPHVE LQFSDANAKF
YCRLYYAGEF HKMREVILDS SEEDFIRSLS HSSPWQARGG KSGAAFYATE DDRFILKQMP
RLEVQSFLDF APHYFNYITN AVQQKRPTAL AKILGVYRIG YKNSQNNTEK KLDLLVMENL
FYGRKMAQVF DLKGSLRNRN VKTDTGKESC DVVLLDENLL KMVRDNPLYI RSHSKAVLRT
SIHSDSHFLS SHLIIDYSLL VGRDDTSNEL VVGIIDYIRT FTWDKKLEMV VKSTGILGGQ
GKMPTVVSPE LYRTRFCEAM DKYFLMVPDH WTGLGLNC
//
ID GAL1_HUMAN STANDARD; PRT; 392 AA.
AC P51570;
DT 01-OCT-1996 (Rel. 34, Created)
DT 01-OCT-1996 (Rel. 34, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE Galactokinase (EC 2.7.1.6) (Galactose kinase).
GN GALK1 OR GALK.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A., AND VARIANT GALACTOSEMIA MET-32.
RX MEDLINE=95400298; PubMed=7670469;
RA Stambolian D., Ai Y., Sidjanin D., Nesburn K., Sathe G., Rosenberg M.,
RA Bergsma D.J.;
RT "Cloning of the galactokinase cDNA and identification of mutations in
RT two families with cataracts.";
RL Nat. Genet. 10:307-312(1995).
RN [2]
RP SEQUENCE FROM N.A.
RX MEDLINE=97064967; PubMed=8908517;
RA Bergsma D.J., Ai Y., Skach W.R., Nesburn K., Anoia E.,
RA van Horn S., Stambolian D.;
RT "Fine structure of the human galactokinase GALK1 gene.";
RL Genome Res. 6:980-985(1996).
RN [3]
RP SEQUENCE FROM N.A.
RC TISSUE=Brain;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [4]
RP CHARACTERIZATION.
RX MEDLINE=95352063; PubMed=7542884;
RA Ai Y., Basu M., Bergsma D.J., Stambolian D.;
RT "Comparison of the enzymatic activities of human galactokinase GALK1
RT and a related human galactokinase protein GK2.";
RL Biochem. Biophys. Res. Commun. 212:687-691(1995).
RN [5]
RP VARIANT GALACTOSEMIA THR-28.
RX MEDLINE=99452591; PubMed=10521295;
RA Kalaydjieva L., Perez-Lezaun A., Angelicheva D., Onengut S., Dye D.,
RA Bosshard N.U., Jordanova A., Savov A., Yanakiev P., Kremensky I.,
RA Radeva B., Hallmayer J., Markov A., Nedkova V., Tournev I., Aneva L.,
RA Gitzelmann R.;
RT "A founder mutation in the GK1 gene is responsible for galactokinase
RT deficiency in Roma (Gypsies).";
RL Am. J. Hum. Genet. 65:1299-1307(1999).
RN [6]
RP VARIANT GALACTOSEMIA VAL-198.
RX MEDLINE=21152290; PubMed=11231902;
RA Okano Y., Asada M., Fujimoto A., Ohtake A., Murayama K., Hsiao K.-J.,
RA Choeh K., Yang Y., Cao Q., Reichardt J.K.V., Niihira S., Imamura T.,
RA Yamano T.;
RT "A genetic factor for age-related cataract: identification and
RT characterization of a novel galactokinase variant, 'Osaka,' in
RT Asians.";
RL Am. J. Hum. Genet. 68:1036-1042(2001).
CC -!- FUNCTION: Major enzyme for galactose metabolism.
CC -!- CATALYTIC ACTIVITY: ATP + D-galactose = ADP + D-galactose 1-
CC phosphate.
CC -!- PATHWAY: Galactose metabolism; first step.
CC -!- DISEASE: Defects in GALK1 are the cause of galactosemia II
CC [MIM:230200], an autosomal recessive deficiency characterized by
CC congenital cataracts during infancy and presenile cataracts in the
CC adult population. The cataracts are secondary to accumulation of
CC galactitol in the lenses.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. GalK subfamily.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; U26401; AAA96147.1; -.
DR EMBL; L76927; AAB51607.1; -.
DR EMBL; BC001166; AAH01166.1; -.
DR Genew; HGNC:4118; GALK1.
DR GK; P51570; -.
DR MIM; 604313; -.
DR MIM; 230200; -.
DR GO; GO:0005737; C:cytoplasm; TAS.
DR GO; GO:0004335; F:galactokinase activity; TAS.
DR GO; GO:0006012; P:galactose metabolism; TAS.
DR InterPro; IPR000705; Galactokinase.
DR InterPro; IPR001174; Galkinase.
DR InterPro; IPR006204; GHMP_kinase.
DR InterPro; IPR006203; GHMPknse_ATP.
DR InterPro; IPR006206; Mev_galkinase.
DR Pfam; PF00288; GHMP_kinases; 1.
DR PRINTS; PR00473; GALCTOKINASE.
DR PRINTS; PR00960; LMBPPROTEIN.
DR PRINTS; PR00959; MEVGALKINASE.
DR TIGRFAMs; TIGR00131; gal_kin; 1.
DR PROSITE; PS00106; GALACTOKINASE; 1.
DR PROSITE; PS00627; GHMP_KINASES_ATP; 1.
KW Transferase; Kinase; Galactose metabolism; ATP-binding;
KW Disease mutation.
FT NP_BIND 134 144 ATP (Potential).
FT VARIANT 28 28 P -> T (in galactosemia II).
FT /FTId=VAR_008514.
FT VARIANT 32 32 V -> M (in galactosemia II).
FT /FTId=VAR_002547.
FT VARIANT 198 198 A -> V (in galactosemia II; mild
FT deficiency; Osaka).
FT /FTId=VAR_015746.
SQ SEQUENCE 392 AA; 42272 MW; 8D7CFF8FDB0E4718 CRC64;
MAALRQPQVA ELLAEARRAF REEFGAEPEL AVSAPGRVNL IGEHTDYNQG LVLPMALELM
TVLVGSPRKD GLVSLLTTSE GADEPQRLQF PLPTAQRSLE PGTPRWANYV KGVIQYYPAA
PLPGFSAVVV SSVPLGGGLS SSASLEVATY TFLQQLCPDS GTIAARAQVC QQAEHSFAGM
PCGIMDQFIS LMGQKGHALL IDCRSLETSL VPLSDPKLAV LITNSNVRHS LASSEYPVRR
RQCEEVARAL GKESLREVQL EELEAARDLV SKEGFRRARH VVGEIRRTAQ AAAALRRGDY
RAFGRLMVES HRSLRDDYEV SCPELDQLVE AALAVPGVYG SRMTGGGFGG CTVTLLEASA
APHAMRHIQE HYGGTATFYL SQAADGAKVL CL
//
ID GAL2_HUMAN STANDARD; PRT; 458 AA.
AC Q01415;
DT 01-JUL-1993 (Rel. 26, Created)
DT 01-JUL-1993 (Rel. 26, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE N-acetylgalactosamine kinase (EC 2.7.1.-) (GalNAc kinase)
DE (Galactokinase 2).
GN GALK2 OR GK2.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RX MEDLINE=93066348; PubMed=1438294;
RA Lee R.T., Peterson C.L., Calman A.F., Herskowitz I., O'Donnell J.J.;
RT "Cloning of a human galactokinase gene (GK2) on chromosome 15 by
RT complementation in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:10887-10891(1992).
RN [2]
RP SEQUENCE FROM N.A.
RC TISSUE=Placenta;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [3]
RP CHARACTERIZATION.
RX MEDLINE=95352063; PubMed=7542884;
RA Ai Y., Basu M., Bergsma D.J., Stambolian D.;
RT "Comparison of the enzymatic activities of human galactokinase GALK1
RT and a related human galactokinase protein GK2.";
RL Biochem. Biophys. Res. Commun. 212:687-691(1995).
RN [4]
RP POSSIBLE FUNCTION.
RX MEDLINE=96394479; PubMed=8798585;
RA Pastuszak I., O'Donnell J., Elbein A.D.;
RT "Identification of the GalNAc kinase amino acid sequence.";
RL J. Biol. Chem. 271:23653-23656(1996).
CC -!- FUNCTION: Acts on GalNac. Also acts as a galactokinase when
CC galactose is present at high concentrations.
CC -!- CATALYTIC ACTIVITY: ATP + N-acetyl-D-galactosamine = ADP + N-
CC acetyl-D-galactosamine 1-phosphate.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. GalK subfamily.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; M84443; AAA58612.1; -.
DR EMBL; BC005141; AAH05141.1; -.
DR PIR; A46366; A46366.
DR Genew; HGNC:4119; GALK2.
DR MIM; 137028; -.
DR GO; GO:0004335; F:galactokinase activity; TAS.
DR GO; GO:0005975; P:carbohydrate metabolism; TAS.
DR InterPro; IPR000705; Galactokinase.
DR InterPro; IPR006204; GHMP_kinase.
DR InterPro; IPR006203; GHMPknse_ATP.
DR InterPro; IPR006206; Mev_galkinase.
DR Pfam; PF00288; GHMP_kinases; 1.
DR PRINTS; PR00473; GALCTOKINASE.
DR PRINTS; PR00959; MEVGALKINASE.
DR TIGRFAMs; TIGR00131; gal_kin; 1.
DR PROSITE; PS00106; GALACTOKINASE; 1.
DR PROSITE; PS00627; GHMP_KINASES_ATP; 1.
KW Transferase; Kinase; ATP-binding.
FT NP_BIND 139 149 ATP (Potential).
SQ SEQUENCE 458 AA; 50378 MW; 192B774938F32947 CRC64;
MATESPATRR VQVAEHPRLL KLKEMFNSKF GSIPKFYVRA PGRVNIIGEH IDYCGYSVLP
MAVEQDVLIA VEPVKTYALQ LANTNPLYPD FSTSANNIQI DKTKPLWHNY FLCGLKGIQE
HFGLSNLTGM NCLVDGNIPP SSGLSSSSAL VCCAGLVTLT VLGRNLSKVE LAEICAKSER
YIGTEGGGMD QSISFLAEEG TAKLIEFSPL RATDVKLPSG AVFVIANSCV EMNKAATSHF
NIRVMECRLA AKLLAKYKSL QWDKVLRLEE VQAKLGISLE EMLLVTEDAL HPEPYNPEEI
CRCLGISLEE LRTQILSPNT QDVLIFKLYQ RAKHVYSEAA RVLQFKKICE EAPENMVQLL
GELMNQSHMS CRDMYECSCP ELDQLVDICR KFGAQGSRLT GAGWGGCTVS MVPADKLPSF
LANVHKAYYQ RSDGSLAPEK QSLFATKPGG GALVLLEA
//
ID GCVK_HCMVA STANDARD; PRT; 707 AA.
AC P16788;
DT 01-AUG-1990 (Rel. 15, Created)
DT 01-AUG-1990 (Rel. 15, Last sequence update)
DT 28-FEB-2003 (Rel. 41, Last annotation update)
DE Ganciclovir kinase (EC 2.7.1.-) (HSRF3 protein).
GN UL97.
OS Human cytomegalovirus (strain AD169).
OC Viruses; dsDNA viruses, no RNA stage; Herpesviridae;
OC Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=10360;
RN [1]
RP SEQUENCE FROM N.A.
RX MEDLINE=90269039; PubMed=2161319;
RA Chee M.S., Bankier A.T., Beck S., Bohni R., Brown C.M., Cerny R.,
RA Horsnell T., Hutchison C.A. III, Kouzarides T., Martignetti J.A.,
RA Preddie E., Satchwell S.C., Tomlinson P., Weston K.M., Barrell B.G.;
RT "Analysis of the protein-coding content of the sequence of human
RT cytomegalovirus strain AD169.";
RL Curr. Top. Microbiol. Immunol. 154:125-169(1990).
RN [2]
RP FUNCTION.
RX MEDLINE=92310592; PubMed=1319559;
RA Littler E., Stuart A.D., Chee M.S.;
RT "Human cytomegalovirus UL97 open reading frame encodes a protein that
RT phosphorylates the antiviral nucleoside analogue ganciclovir.";
RL Nature 358:160-162(1992).
RN [3]
RP FUNCTION.
RX MEDLINE=92310593; PubMed=1319560;
RA Sullivan V., Talarico C.L., Stanat S.C., Davis M., Coen D.M.,
RA Biron K.K.;
RT "A protein kinase homologue controls phosphorylation of ganciclovir
RT in human cytomegalovirus-infected cells.";
RL Nature 358:162-164(1992).
RN [4]
RP ERRATUM.
RX MEDLINE=92396223; PubMed=1326083;
RA Sullivan V., Talarico C.L., Stanat S.C., Davis M., Coen D.M.,
RA Biron K.K.;
RL Nature 359:85-85(1992).
RN [5]
RP ERRATUM.
RA Sullivan V., Talarico C.L., Stanat S.C., Davis M., Coen D.M.,
RA Biron K.K.;
RL Nature 366:756-756(1993).
CC -!- FUNCTION: Phosphorylates the antiviral nucleoside analog
CC ganciclovir.
CC -!- SIMILARITY: Belongs to the Tyr family of protein kinases. HCMV
CC ganciclovir subfamily.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; X17403; CAA35333.1; -.
DR PIR; S09862; QQBEJ5.
DR InterPro; IPR000719; Prot_kinase.
DR InterPro; IPR008266; Tyr_pkinase_AS.
DR ProDom; PD000001; Prot_kinase; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; FALSE_NEG.
KW Transferase; Kinase; ATP-binding.
FT DOMAIN 41 63 ALA-RICH.
FT NP_BIND 337 345 ATP (By similarity).
FT BINDING 359 359 ATP (By similarity).
FT ACT_SITE 456 456 By similarity.
SQ SEQUENCE 707 AA; 78232 MW; 74914183E5A5E03A CRC64;
MSSALRSRAR SASLGTTTQG WDPPPLRRPS RARRRQWMRE AAQAAAQAAV QAAQAAAAQV
AQAHVDENEV VDLMADEAGG GVTTLTTLSS VSTTTVLGHA TFSACVRSDV MRDGEKEDAA
SDKENLRRPV VPSTSSRGSA ASGDGYHGLR CRETSAMWSF EYDRDGDVTS VRRALFTGGS
DPSDSVSGVR GGRKRPLRPP LVSLARTPLC RRRVGGVDAV LEENDVELRA ESQDSAVASG
PGRIPQPLSG SSGEESATAV EADSTSHDDV HCTCSNDQII TTSIRGLTCD PRMFLRLTHP
ELCELSISYL LVYVPKEDDF CHKICYAVDM SDESYRLGQG SFGEVWPLDR YRVVKVARKH
SETVLTVWMS GLIRTRAAGE QQQPPSLVGT GVHRGLLTAT GCCLLHNVTV HRRFHTDMFH
HDQWKLACID SYRRAFCTLA DAIKFLNHQC RVCHFDITPM NVLIDVNPHN PSEIVRAALC
DYSLSEPYPD YNERCVAVFQ ETGTARRIPN CSHRLRECYH PAFRPMPLQK LLICDPHARF
PVAGLRRYCM SELSALGNVL GFCLMRLLDR RGLDEVRMGT EALLFKHAGA ACRALENGKL
THCSDACLLI LAAQMSYGAC LLGEHGAALV SHTLRFVEAK MSSCRVRAFR RFYHECSQTM
LHEYVRKNVE RLLATSDGLY LYNAFRRTTS IICEEDLDGD CRQLFPE
//
ID GCVK_HSV6U STANDARD; PRT; 562 AA.
AC P24446;
DT 01-MAR-1992 (Rel. 21, Created)
DT 01-MAR-1992 (Rel. 21, Last sequence update)
DT 28-FEB-2003 (Rel. 41, Last annotation update)
DE Possible ganciclovir kinase (EC 2.7.1.-).
GN U69 OR 15R.
OS Human herpesvirus (type 6 / strain Uganda-1102) (HHV6).
OC Viruses; dsDNA viruses, no RNA stage; Herpesviridae;
OC Betaherpesvirinae; Roseolovirus.
OX NCBI_TaxID=10370;
RN [1]
RP SEQUENCE FROM N.A.
RX MEDLINE=90080132; PubMed=2152817;
RA Lawrence G.L., Chee M., Craxton M.A., Gompels U.A., Honess R.W.,
RA Barrell B.G.;
RT "Human herpesvirus 6 is closely related to human cytomegalovirus.";
RL J. Virol. 64:287-299(1990).
RN [2]
RP SEQUENCE FROM N.A.
RX MEDLINE=95266321; PubMed=7747482;
RA Gompels U.A., Nicholas J., Lawrence G., Jones M., Thomson B.J.,
RA Martin M.E., Efstathiou S., Craxton M., Macaulay H.A.;
RT "The DNA sequence of human herpesvirus-6: structure, coding content,
RT and genome evolution.";
RL Virology 209:29-51(1995).
CC -!- FUNCTION: Phosphorylates the antiviral nucleoside analog
CC ganciclovir (By similarity).
CC -!- SIMILARITY: Belongs to the Tyr family of protein kinases. HCMV
CC ganciclovir subfamily.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; M68963; AAA65577.1; -.
DR EMBL; X83413; CAA58361.1; -.
DR PIR; E36769; QQBEH5.
DR InterPro; IPR000719; Prot_kinase.
DR InterPro; IPR008266; Tyr_pkinase_AS.
DR ProDom; PD000001; Prot_kinase; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; FALSE_NEG.
KW Transferase; Kinase; ATP-binding; Early protein.
FT NP_BIND 201 209 ATP (By similarity).
FT BINDING 218 218 ATP (By similarity).
FT ACT_SITE 313 313 By similarity.
SQ SEQUENCE 562 AA; 63717 MW; 09111202754CC071 CRC64;
MDNGVETPQG QKTQPINLPP VRKKLRKHEG LGKGVKRKLF AEDSSPLKKQ ISACSDMETL
SSPVKSECES RSASLDESFG KCKHEIACDC SAIEELLCHE SLLDSPMKLS NAHTIFSSNK
WKLELEKIIA SKQIFLDMSE NAELAAYGET LCNLRIFEKI SSPFLFDVQS EERSYSVVYV
PHNKELCGQF CQPEKTMARV LGVGAYGKVF DLDKVAIKTA NEDESVISAF IAGVIRAKSG
ADLLSHECVI NNLLISNSVC MSHKVSLSRT YDIDLHKFED WDVRNVMNYY SVFCKLADAV
RFLNLKCRIN HFDISPMNIF LNHKKEIIFD AVLADYSLSE MHPNYNGTCA IAKEYDKNLQ
LVPISRNKFC DMFNPGFRPL VANAMILVNV CGAFDGENNP LRHCNLDLCA FAQVVLSCVL
RMTDKRGCRE AQLYYEKRLF ALANEACRLN PLKYPFAYRD ACCKVLAEHV VLLGLLFYRD
VVEIYEKLYD FLDERGEFGS RDLFEATFLN NSKLTRRQPI REGLASLQSS EYGEKLLHDL
RELFLINSTA DLDKDTSSLF HM
//
ID GCVK_HSV6Z STANDARD; PRT; 563 AA.
AC P52446; Q9IBR7;
DT 01-OCT-1996 (Rel. 34, Created)
DT 10-OCT-2003 (Rel. 42, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE Possible ganciclovir kinase (EC 2.7.1.-).
GN U69 OR CH2R.
OS Human herpesvirus (type 6 / strain Z29) (HHV6).
OC Viruses; dsDNA viruses, no RNA stage; Herpesviridae;
OC Betaherpesvirinae; Roseolovirus.
OX NCBI_TaxID=36351;
RN [1]
RP SEQUENCE FROM N.A.
RX MEDLINE=99412318; PubMed=10482553;
RA Dominguez G., Dambaugh T.R., Stamey F.R., Dewhurst S., Inoue N.,
RA Pellett P.E.;
RT "Human herpesvirus 6B genome sequence: coding content and comparison
RT with human herpesvirus 6A.";
RL J. Virol. 73:8040-8052(1999).
RN [2]
RP SEQUENCE OF 284-563 FROM N.A.
RX MEDLINE=96195263; PubMed=8634027;
RA Lindquester G.J., Inoue N., Allen R.D., Castelli J.W., Stamey F.R.,
RA Dambaugh T.R., O'Brian J.J., Danovich R.M., Frenkel N., Pellett P.E.;
RT "Restriction endonuclease mapping and molecular cloning of the human
RT herpesvirus 6 variant B strain Z29 genome.";
RL Arch. Virol. 141:367-379(1996).
CC -!- FUNCTION: Phosphorylates the antiviral nucleoside analog
CC ganciclovir (By similarity).
CC -!- SIMILARITY: Belongs to the Tyr family of protein kinases. HCMV
CC ganciclovir subfamily.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AF157706; AAD49670.1; -.
DR InterPro; IPR000719; Prot_kinase.
DR InterPro; IPR008266; Tyr_pkinase_AS.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; FALSE_NEG.
KW Transferase; Kinase; ATP-binding.
FT NP_BIND 202 210 ATP (By similarity).
FT BINDING 219 219 ATP (By similarity).
FT ACT_SITE 314 314 By similarity.
SQ SEQUENCE 563 AA; 63883 MW; 22C6F87A346432C2 CRC64;
MDNGVETPQG QKTQPINLPP DRKRLRKHDG LGKGVKRKLF AEDSSPLKKQ IPACSDMETL
SSPVKFGCKS RSASALDESF GKCKHETACD CSAIEELLCH ESLLDSPMKL SNAHTIFSSD
KWKLELEKII ASKQIFLDMS ENVELVAYGE TLCNLRIFEK ISSPFLFDVQ SEERSYSVVY
VPHNKELCGQ FCQPEKTMAR VLGVGAYGKV FDLDKVAIKT ANEDESVISA FIAGVIRAKS
GADLLSHDCV INNLLISNSV CMDHKVSLSR TYDVDLYKFE DWDVRNVMNY YSVFCKLADA
VRFLNLKCRI NHFDISPMNI FINHKKEIIF DAVLADYSLS EIHPEYNGTC AIAKEYDRNL
QLVPISRNKF CDMFNPGFRP LVANAMILVN VCEAFDGENN PLRHCNLDLC AFAQVVLLCV
LRMTDKRGCR EAQLYYEKRL FALANEACRL NPLRYPFAYR DACCKVLAEH VVLLGLLFYR
DVVDIYEKIY DFLDERGEFG LRDLFEATFL NNSKLTRRQP IRGGLASLQS SEYGEKLLHD
LRALFLITSS ADLDKDTSSL FQM
//
ID GCVK_HSV7J STANDARD; PRT; 546 AA.
AC P52344;
DT 01-OCT-1996 (Rel. 34, Created)
DT 01-OCT-1996 (Rel. 34, Last sequence update)
DT 28-FEB-2003 (Rel. 41, Last annotation update)
DE Possible ganciclovir kinase (EC 2.7.1.-).
GN U69.
OS Human herpesvirus (type 7 / strain JI) (HHV7).
OC Viruses; dsDNA viruses, no RNA stage; Herpesviridae;
OC Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=57278;
RN [1]
RP SEQUENCE FROM N.A.
RA Nicholas J.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phosphorylates the antiviral nucleoside analog
CC ganciclovir (By similarity).
CC -!- SIMILARITY: Belongs to the Tyr family of protein kinases. HCMV
CC ganciclovir subfamily.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; U43400; AAC54730.1; -.
DR PIR; T41970; T41970.
DR InterPro; IPR000719; Prot_kinase.
DR InterPro; IPR008266; Tyr_pkinase_AS.
DR ProDom; PD000001; Prot_kinase; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; FALSE_NEG.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
KW Transferase; Kinase; ATP-binding; Early protein.
FT NP_BIND 185 193 ATP (By similarity).
FT BINDING 202 202 ATP (By similarity).
FT ACT_SITE 297 297 By similarity.
SQ SEQUENCE 546 AA; 62853 MW; 4D75A01FE4695528 CRC64;
MEQLKTPQNQ KTRPRNMLPK KKGKELKKRP CKVKRKLFGS ENIRPNKKIP LASDVDNELE
KKRGSMIRKR SETDLCPDPS VTDLLCHESL TVSPKFERDG LSACTEFENF MDTRKIVLSR
NEKSVTDLSA HYPVLCNLGI FERIHSPFLF SIHIDTQSFS VVYVPHKESS CSQFCEPEKN
MARILGSGSY GMVYDLNNVA IKASDDLESC ISSYVSGVVR AKAGAQLTSR ECVFKSLLIC
NSVCLNHKIS LSKTYDTDLY KFTDWKLENV ENYYSIFCNL AEAVRFLNMV CKINHCDISL
ANILIHHKEG IILEAVLADY SLAEVHPQYN GKCGILRQFD HRIQIVPKSY NKLCDMFNPG
FRPMIAHKII LVEVYAEFDG KGNPVRHCNL DLCALAQVFL LCVIRMLDER GCREAQKYYE
NRLFTYSNEA CTLNPIKYPL EYKDACCKVL AEHLVLFGIL FYREVVDMFE NLYDFLHASG
DLSVRDLLEE TYVNDSRDVR RQPIRYRHAQ LQRHEIGQIL LNDLQQLLSI ITISDLEKDP
YSVFRV
//
ID GKP2_HUMAN STANDARD; PRT; 553 AA.
AC Q14410;
DT 16-OCT-2001 (Rel. 40, Created)
DT 16-OCT-2001 (Rel. 40, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE Glycerol kinase, testis specific 2 (EC 2.7.1.30) (ATP:glycerol 3-
DE phosphotransferase) (Glycerokinase) (GK).
GN GK2 OR GKP2 OR GKTA.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RC TISSUE=Testis;
RX MEDLINE=95078834; PubMed=7987308;
RA Sargent C.A., Young C., Marsh S., Ferguson-Smith M.A., Affara N.A.;
RT "The glycerol kinase gene family: structure of the Xp gene, and
RT related intronless retroposons.";
RL Hum. Mol. Genet. 3:1317-1324(1994).
CC -!- FUNCTION: Key enzyme in the regulation of glycerol uptake and
CC metabolism.
CC -!- CATALYTIC ACTIVITY: ATP + glycerol = ADP + glycerol 3-phosphate.
CC -!- PATHWAY: Glycerol utilization; rate-limiting step.
CC -!- SUBCELLULAR LOCATION: BOUND TO THE MITOCHONDRIAL SURFACE OR
CC CYTOPLASMIC. IN SPERM, THE MAJORITY OF THE ENZYME IS BOUND TO
CC MITOCHONDRIA (BY SIMILARITY).
CC -!- SIMILARITY: Belongs to the fucokinase / gluconokinase /
CC glycerokinase / xylulokinase family.
CC -!- CAUTION: This could be the product of a pseudogene.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; X78712; CAA55365.1; -.
DR PIR; I37417; I37417.
DR HSSP; P08859; 1GLJ.
DR Genew; HGNC:4291; GK2.
DR MIM; 600148; -.
DR GO; GO:0005737; C:cytoplasm; NAS.
DR GO; GO:0005741; C:mitochondrial outer membrane; NAS.
DR GO; GO:0004370; F:glycerol kinase activity; NAS.
DR GO; GO:0006071; P:glycerol metabolism; NAS.
DR InterPro; IPR000577; FGGY_kin.
DR InterPro; IPR005999; Glycerol_kin.
DR Pfam; PF00370; FGGY; 1.
DR Pfam; PF02782; FGGY_C; 1.
DR TIGRFAMs; TIGR01311; glycerol_kin; 1.
DR PROSITE; PS00445; FGGY_KINASES_2; 1.
DR PROSITE; PS00933; FGGY_KINASES_1; 1.
KW Glycerol metabolism; Transferase; Kinase; ATP-binding.
FT NP_BIND 167 179 ATP (Probable).
SQ SEQUENCE 553 AA; 60609 MW; 8CF53B1686BC4AD6 CRC64;
MAAPKTAAVG PLVGAVVQGT NSTRFLVFNS KTAELLSHHK VELTQEFPKE GWVEQDPKEI
LQSVYECIAR TCEKLDELNI DISNIKAVGV SNQRETTVIW DKLTGEPLYN AVVWLDLRTQ
TTVEDLSKKI PGNSNFVKSK TGLPLSTYFS AVKLRWMLDN VRNVQKAVEE GRALFGTIDS
WLIWSLTGGV NGGVHCTDVT NASRTMLFNI HSLEWDKELC DFFEIPMDLL PNVFSSSEIY
GLIKTGALEG VPISGCLGDQ CAALVGQMCF QEGQAKNTYG TGCFLLCNTG RKCVFSEHGL
LTTVAYKLGR EKPAYYALEG SVAIAGAVIR WLRDNLGIIE TSGDIERLAK EVGTSYGCYF
VPAFSGLYAP YWEPSARGIL CGLTQFTNKC HIAFAALEAV CFQTREILEA MNRDCGIPLR
HLQVDGGMTN NKVLMQLQAD ILHIPVIKPF MPETTALGAA MAAGAAEGVS VWSLEPQALS
VLRMERFEPQ IQATESEIRY ATWKKAVMKS MGWVTSQSPE GGDPSIFCSL PLGFFIVSSM
VMLIGARYIS GVP
//
ID GKP3_HUMAN STANDARD; PRT; 553 AA.
AC Q14409;
DT 16-OCT-2001 (Rel. 40, Created)
DT 16-OCT-2001 (Rel. 40, Last sequence update)
DT 28-FEB-2003 (Rel. 41, Last annotation update)
DE Glycerol kinase, testis specific 1 (EC 2.7.1.30) (ATP:glycerol 3-
DE phosphotransferase) (Glycerokinase) (GK).
GN GKP3 OR GKTB.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RC TISSUE=Testis;
RX MEDLINE=95078834; PubMed=7987308;
RA Sargent C.A., Young C., Marsh S., Ferguson-Smith M.A., Affara N.A.;
RT "The glycerol kinase gene family: structure of the Xp gene, and
RT related intronless retroposons.";
RL Hum. Mol. Genet. 3:1317-1324(1994).
CC -!- FUNCTION: Key enzyme in the regulation of glycerol uptake and
CC metabolism.
CC -!- CATALYTIC ACTIVITY: ATP + glycerol = ADP + glycerol 3-phosphate.
CC -!- PATHWAY: Glycerol utilization; rate-limiting step.
CC -!- SUBCELLULAR LOCATION: BOUND TO THE MITOCHONDRIAL SURFACE OR
CC CYTOPLASMIC. IN SPERM, THE MAJORITY OF THE ENZYME IS BOUND TO
CC MITOCHONDRIA (BY SIMILARITY).
CC -!- SIMILARITY: Belongs to the fucokinase / gluconokinase /
CC glycerokinase / xylulokinase family.
CC -!- CAUTION: This could be the product of a pseudogene.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; X78711; CAA55364.1; -.
DR HSSP; P08859; 1GLJ.
DR Genew; HGNC:4292; GKP3.
DR MIM; 600149; -.
DR GO; GO:0005737; C:cytoplasm; NAS.
DR GO; GO:0005741; C:mitochondrial outer membrane; NAS.
DR GO; GO:0004370; F:glycerol kinase activity; NAS.
DR GO; GO:0006071; P:glycerol metabolism; NAS.
DR InterPro; IPR000577; FGGY_kin.
DR InterPro; IPR005999; Glycerol_kin.
DR Pfam; PF00370; FGGY; 1.
DR Pfam; PF02782; FGGY_C; 1.
DR TIGRFAMs; TIGR01311; glycerol_kin; 1.
DR PROSITE; PS00445; FGGY_KINASES_2; 1.
DR PROSITE; PS00933; FGGY_KINASES_1; 1.
KW Glycerol metabolism; Transferase; Kinase; ATP-binding.
FT NP_BIND 167 179 ATP (Probable).
SQ SEQUENCE 553 AA; 60569 MW; A49F57BF5E7E7D01 CRC64;
MAASKKAVLG PLVGAVDQGT SSTRFLVFNS RTAELLSHHQ VEIKQEFPRE GWVEQDPKEI
LHSVYECIEK TCEKLGQLNI GISNIKAIGV SNQRETTVAW DKITGEPLYN AVVWLDLRTQ
STVESLSKRI PGNNNFVKSK TGLPLSTYFS AVKLRWLLDN VRKVQKAVEE KRALFGTIDS
WLIWSLTGGV NGGVHCTDVT NASRTMLFNI HSLEWDKQLC EFFGIPMEIL PHVRSSSEIY
GLMKAGALEG VPISGCLGDQ SAALVGQMCF QIGQAKNTYG TGCFLLCNTG HKCVFSDHGL
LTTVAYKLGR DKPVYYALEG SVAIAGAVIR WLRDNLGIIK TSEEIEKLAK EVGTSYGCYF
VPAFSGLYAP YWEPSARGII CGLTQFTNKC HIAFAALEAV CFQTREILDA MNRDCGIPLS
HLQVDGGMTS NKILMQLQAD ILYIPVVKPL MPETTALGAA MAAGAAEGVD VWSLEPEDLS
AVTMERFEPQ INAEESEIRY STWKKAVMKS MGWVTTQSPE GGDPSVFCSL PLGFFIVSSM
AMLIGARYIS GIP
//
ID GLPK_HUMAN STANDARD; PRT; 524 AA.
AC P32189; Q9UMP0; Q9UMP1;
DT 01-OCT-1993 (Rel. 27, Created)
DT 01-OCT-1996 (Rel. 34, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE Glycerol kinase (EC 2.7.1.30) (ATP:glycerol 3-phosphotransferase)
DE (Glycerokinase) (GK).
GN GK.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A. (ISOFORM 1).
RC TISSUE=Liver;
RX MEDLINE=94004964; PubMed=8401584;
RA Guo W., Worley K.C., Adams V., Mason J., Sylvester-Jackson D.E.,
RA Zhang Y.-H., Towbin J.A., Fogt D.D., Madu S., Wheeler D.A.,
RA McCabe E.R.B.;
RT "Genomic scanning for expressed sequences in Xp21 identifies the
RT glycerol kinase gene.";
RL Nat. Genet. 4:367-372(1993).
RN [2]
RP SEQUENCE FROM N.A. (ISOFORM 2).
RC TISSUE=Fetal brain;
RX MEDLINE=95078834; PubMed=7987308;
RA Sargent C.A., Young C., Marsh S., Ferguson-Smith M.A., Affara N.A.;
RT "The glycerol kinase gene family: structure of the Xp gene, and
RT related intronless retroposons.";
RL Hum. Mol. Genet. 3:1317-1324(1994).
RN [3]
RP SEQUENCE FROM N.A. (ISOFORM 3).
RA Sargent C.A., Kidd A., Moore S., Dean J., Besley G.T.N., Affara N.A.;
RT "Five cases of isolated glycerol kinase deficiency, including two
RT families: failure to find genotype: phenotype correlations.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SEQUENCE FROM N.A. (ISOFORM 1).
RC TISSUE=Blood;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [5]
RP SEQUENCE OF 77-524 FROM N.A. (ISOFORM 3).
RC TISSUE=Fetal brain;
RX MEDLINE=93271973; PubMed=8499912;
RA Sargent C.A., Affara N.A., Bentley E., Pelmear A., Bailey D.M.D.,
RA Davey P., Dow D., Leversha M., Aplin H., Besley G.T.N.,
RA Ferguson-Smith M.A.;
RT "Cloning of the X-linked glycerol kinase deficiency gene and its
RT identification by sequence comparison to the Bacillus subtilis
RT homologue.";
RL Hum. Mol. Genet. 2:97-106(1993).
RN [6]
RP SEQUENCE OF 130-524 FROM N.A. (ISOFORM 1).
RC TISSUE=Fetal liver;
RX MEDLINE=93271953; PubMed=8499898;
RA Walker A.P., Muscatelli F., Monaco A.P.;
RT "Isolation of the human Xp21 glycerol kinase gene by positional
RT cloning.";
RL Hum. Mol. Genet. 2:107-114(1993).
RN [7]
RP VARIANT GKD VAL-440.
RX MEDLINE=96213755; PubMed=8651297;
RA Walker A.P., Muscatelli F., Stafford A.N., Chelly J., Dahl N.,
RA Blomquist H.K., Delanghe J., Willems P.J., Steinmann B., Monaco A.P.;
RT "Mutations and phenotype in isolated glycerol kinase deficiency.";
RL Am. J. Hum. Genet. 58:1205-1211(1996).
RN [8]
RP VARIANT GKD ARG-503.
RX MEDLINE=98383876; PubMed=9719371;
RA Sjarif D.R., Sinke R.J., Duran M., Beemer F.A., Kleijer W.J.,
RA Ploos van Amstel J.K., Poll-The B.T.;
RT "Clinical heterogeneity and novel mutations in the glycerol kinase
RT gene in three families with isolated glycerol kinase deficiency.";
RL J. Med. Genet. 35:650-656(1998).
RN [9]
RP VARIANT GKD ASP-288.
RX MEDLINE=20311538; PubMed=10736265;
RA Gaudet D., Arsenault S., Perusse L., Vohl M.C., St-Pierre J.,
RA Bergeron J., Despres J.P., Dewar K., Daly M.J., Hudson T., Rioux J.D.;
RT "Glycerol as a correlate of impaired glucose tolerance: dissection of
RT a complex system by use of a simple genetic trait.";
RL Am. J. Hum. Genet. 66:1558-1568(2000).
CC -!- FUNCTION: Key enzyme in the regulation of glycerol uptake and
CC metabolism.
CC -!- CATALYTIC ACTIVITY: ATP + glycerol = ADP + glycerol 3-phosphate.
CC -!- PATHWAY: Glycerol utilization; rate-limiting step.
CC -!- SUBCELLULAR LOCATION: BOUND TO THE MITOCHONDRIAL SURFACE OR
CC CYTOPLASMIC. IN SPERM AND FETAL TISSUES, THE MAJORITY OF THE
CC ENZYME IS BOUND TO MITOCHONDRIA, BUT IN ADULT TISSUES, SUCH AS
CC LIVER FOUND IN THE CYTOPLASM.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P32189-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P32189-2; Sequence=VSP_000771;
CC Name=3;
CC IsoId=P32189-3; Sequence=VSP_000770, VSP_000771;
CC -!- TISSUE SPECIFICITY: HIGHLY EXPRESSED IN THE LIVER, KIDNEY AND
CC TESTIS. ISOFORMS 2 AND 3 ARE EXPRESSED SPECIFICALLY IN TESTIS AND
CC FETAL LIVER, BUT NOT IN THE ADULT LIVER.
CC -!- DISEASE: Defects in GK are the cause of GK deficiency (GKD)
CC [MIM:307030]. This disease can be either symptomatic with episodic
CC metabolic and CNS decompensation or asymptomatic with
CC hyperglycerolemia and hyperglyceroluria only.
CC -!- SIMILARITY: Belongs to the fucokinase / gluconokinase /
CC glycerokinase / xylulokinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; L13943; AAA52576.1; -.
DR EMBL; X78211; -; NOT_ANNOTATED_CDS.
DR EMBL; AJ252550; CAB54859.1; -.
DR EMBL; AJ252551; CAB54859.1; JOINED.
DR EMBL; AJ252552; CAB54859.1; JOINED.
DR EMBL; AJ252553; CAB54859.1; JOINED.
DR EMBL; AJ252554; CAB54859.1; JOINED.
DR EMBL; AJ252555; CAB54859.1; JOINED.
DR EMBL; AJ252556; CAB54859.1; JOINED.
DR EMBL; AJ252557; CAB54859.1; JOINED.
DR EMBL; AJ252558; CAB54859.1; JOINED.
DR EMBL; AJ252559; CAB54859.1; JOINED.
DR EMBL; AJ252560; CAB54859.1; JOINED.
DR EMBL; AJ252561; CAB54859.1; JOINED.
DR EMBL; AJ252562; CAB54859.1; JOINED.
DR EMBL; AJ252563; CAB54859.1; JOINED.
DR EMBL; AJ252564; CAB54859.1; JOINED.
DR EMBL; AJ252565; CAB54859.1; JOINED.
DR EMBL; AJ252566; CAB54859.1; JOINED.
DR EMBL; AJ252567; CAB54859.1; JOINED.
DR EMBL; AJ252568; CAB54859.1; JOINED.
DR EMBL; AJ252569; CAB54859.1; JOINED.
DR EMBL; AJ252570; CAB54859.1; JOINED.
DR EMBL; AJ252550; CAB54858.1; -.
DR EMBL; AJ252551; CAB54858.1; JOINED.
DR EMBL; AJ252552; CAB54858.1; JOINED.
DR EMBL; AJ252553; CAB54858.1; JOINED.
DR EMBL; AJ252554; CAB54858.1; JOINED.
DR EMBL; AJ252555; CAB54858.1; JOINED.
DR EMBL; AJ252556; CAB54858.1; JOINED.
DR EMBL; AJ252557; CAB54858.1; JOINED.
DR EMBL; AJ252559; CAB54858.1; JOINED.
DR EMBL; AJ252560; CAB54858.1; JOINED.
DR EMBL; AJ252561; CAB54858.1; JOINED.
DR EMBL; AJ252562; CAB54858.1; JOINED.
DR EMBL; AJ252563; CAB54858.1; JOINED.
DR EMBL; AJ252564; CAB54858.1; JOINED.
DR EMBL; AJ252565; CAB54858.1; JOINED.
DR EMBL; AJ252566; CAB54858.1; JOINED.
DR EMBL; AJ252567; CAB54858.1; JOINED.
DR EMBL; AJ252568; CAB54858.1; JOINED.
DR EMBL; AJ252569; CAB54858.1; JOINED.
DR EMBL; AJ252570; CAB54858.1; JOINED.
DR EMBL; AJ252550; CAB54857.1; -.
DR EMBL; AJ252551; CAB54857.1; JOINED.
DR EMBL; AJ252552; CAB54857.1; JOINED.
DR EMBL; AJ252553; CAB54857.1; JOINED.
DR EMBL; AJ252554; CAB54857.1; JOINED.
DR EMBL; AJ252555; CAB54857.1; JOINED.
DR EMBL; AJ252556; CAB54857.1; JOINED.
DR EMBL; AJ252557; CAB54857.1; JOINED.
DR EMBL; AJ252559; CAB54857.1; JOINED.
DR EMBL; AJ252560; CAB54857.1; JOINED.
DR EMBL; AJ252561; CAB54857.1; JOINED.
DR EMBL; AJ252562; CAB54857.1; JOINED.
DR EMBL; AJ252563; CAB54857.1; JOINED.
DR EMBL; AJ252564; CAB54857.1; JOINED.
DR EMBL; AJ252565; CAB54857.1; JOINED.
DR EMBL; AJ252566; CAB54857.1; JOINED.
DR EMBL; AJ252567; CAB54857.1; JOINED.
DR EMBL; AJ252568; CAB54857.1; JOINED.
DR EMBL; AJ252570; CAB54857.1; JOINED.
DR EMBL; BC037549; AAH37549.1; -.
DR EMBL; X68285; CAA48346.1; -.
DR EMBL; X69886; CAA49512.1; -.
DR PIR; I37427; S36175.
DR HSSP; P08859; 1GLJ.
DR Genew; HGNC:4289; GK.
DR GK; P32189; -.
DR MIM; 307030; -.
DR GO; GO:0005737; C:cytoplasm; NAS.
DR GO; GO:0005741; C:mitochondrial outer membrane; NAS.
DR GO; GO:0004370; F:glycerol kinase activity; NAS.
DR GO; GO:0006071; P:glycerol metabolism; NAS.
DR InterPro; IPR000577; FGGY_kin.
DR InterPro; IPR005999; Glycerol_kin.
DR Pfam; PF00370; FGGY; 1.
DR Pfam; PF02782; FGGY_C; 1.
DR TIGRFAMs; TIGR01311; glycerol_kin; 1.
DR PROSITE; PS00445; FGGY_KINASES_2; 1.
DR PROSITE; PS00933; FGGY_KINASES_1; 1.
KW Glycerol metabolism; Transferase; Kinase; ATP-binding; Polymorphism;
KW Disease mutation; Alternative splicing.
FT NP_BIND 167 179 ATP (Probable).
FT VARSPLIC 244 244 K -> KISHSVK (in isoform 3).
FT /FTId=VSP_000770.
FT VARSPLIC 523 524 IP -> DPSIFCSLPLGFFIVSSMVMLIGARYISGIP (in
FT isoform 2 and isoform 3).
FT /FTId=VSP_000771.
FT VARIANT 185 185 S -> N.
FT /FTId=VAR_001374.
FT VARIANT 232 232 N -> H.
FT /FTId=VAR_001375.
FT VARIANT 288 288 N -> D (in GKD).
FT /FTId=VAR_015433.
FT VARIANT 376 376 A -> T.
FT /FTId=VAR_001376.
FT VARIANT 440 440 D -> V (in GKD).
FT /FTId=VAR_001377.
FT VARIANT 503 503 W -> R (in GKD).
FT /FTId=VAR_010138.
FT CONFLICT 201 210 NASRTMLFNI -> MQVGLCFSTC (in Ref. 5).
FT CONFLICT 459 524 AAMAAGAAEGVGVWSLEPEDLSAVTMERFEPQINAEESEIR
FT YSTWKKAVMKSMGWVTTQSPESGIP -> RLWRQGLQKESA
FT YGVSNPRICLPSRWSGLNLRLMRRKVKFVILHGRKL (IN
FT REF. 5).
SQ SEQUENCE 524 AA; 57489 MW; 0FAA29ADC6054154 CRC64;
MAASKKAVLG PLVGAVDQGT SSTRFLVFNS KTAELLSHHQ VEIKQEFPRE GWVEQDPKEI
LHSVYECIEK TCEKLGQLNI DISNIKAIGV SNQRETTVVW DKITGEPLYN AVVWLDLRTQ
STVESLSKRI PGNNNFVKSK TGLPLSTYFS AVKLRWLLDN VRKVQKAVEE KRALFGTIDS
WLIWSLTGGV NGGVHCTDVT NASRTMLFNI HSLEWDKQLC EFFGIPMEIL PNVRSSSEIY
GLMKAGALEG VPISGCLGDQ SAALVGQMCF QIGQAKNTYG TGCFLLCNTG HKCVFSDHGL
LTTVAYKLGR DKPVYYALEG SVAIAGAVIR WLRDNLGIIK TSEEIEKLAK EVGTSYGCYF
VPAFSGLYAP YWEPSARGII CGLTQFTNKC HIAFAALEAV CFQTREILDA MNRDCGIPLS
HLQVDGGMTS NKILMQLQAD ILYIPVVKPS MPETTALGAA MAAGAAEGVG VWSLEPEDLS
AVTMERFEPQ INAEESEIRY STWKKAVMKS MGWVTTQSPE SGIP
//
ID HXK1_HUMAN STANDARD; PRT; 917 AA.
AC P19367; O43443; O43444; O75574; Q96HC8; Q9NNZ4; Q9NNZ5;
DT 01-NOV-1990 (Rel. 16, Created)
DT 01-NOV-1990 (Rel. 16, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Hexokinase, type I (EC 2.7.1.1) (HK I) (Brain form hexokinase).
GN HK1.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A. (ISOFORM 1).
RX MEDLINE=89087485; PubMed=3207429;
RA Nishi S., Seino S., Bell G.I.;
RT "Human hexokinase: sequences of amino- and carboxyl-terminal halves
RT are homologous.";
RL Biochem. Biophys. Res. Commun. 157:937-943(1988).
RN [2]
RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING.
RX MEDLINE=98198402; PubMed=9531504;
RA Ruzzo A., Andreoni F., Magnani M.;
RT "Structure of the human hexokinase type I gene and nucleotide sequence
RT of the 5' flanking region.";
RL Biochem. J. 331:607-613(1998).
RN [3]
RP SEQUENCE FROM N.A. (ISOFORM 1).
RC TISSUE=Brain;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [4]
RP SEQUENCE OF 287-917 FROM N.A.
RC TISSUE=Placenta;
RX MEDLINE=92344570; PubMed=1637300;
RA Magnani M., Bianchi M., Casabianca A., Stocchi V., Daniele A.,
RA Altruda F., Ferrone M., Silengo L.;
RT "A recombinant human 'mini'-hexokinase is catalytically active and
RT regulated by hexose 6-phosphates.";
RL Biochem. J. 285:193-199(1992).
RN [5]
RP SEQUENCE OF 11-31 AND 103-120.
RC TISSUE=Placenta;
RX MEDLINE=91093173; PubMed=1985912;
RA Magnani M., Serafini G., Bianchi M., Casabianca A., Stocchi V.;
RT "Human hexokinase type I microheterogeneity is due to different
RT amino-terminal sequences.";
RL J. Biol. Chem. 266:502-505(1991).
RN [6]
RP SEQUENCE OF 1-20 FROM N.A. (ISOFORM 2).
RA Murakami K., Piomelli S.;
RT "The erythrocyte-specific hexokinase isozyme (HKR) and the common
RT hexokinase isozyme (HKI) are produced from a single gene by alternate
RT promoters.";
RL Blood 90:272-272(1998).
RN [7]
RP ALTERNATIVE SPLICING.
RX MEDLINE=97180129; PubMed=9028305;
RA Murakami K., Piomelli S.;
RT "Identification of the cDNA for human red blood cell-specific
RT hexokinase isozyme.";
RL Blood 89:762-766(1997).
RN [8]
RP ALTERNATIVE SPLICING.
RX MEDLINE=20435276; PubMed=10978502;
RA Andreoni F., Ruzzo A., Magnani M.;
RT "Structure of the 5' region of the human hexokinase type I (HKI) gene
RT and identification of an additional testis-specific HKI mRNA.";
RL Biochim. Biophys. Acta 1493:19-26(2000).
RN [9]
RP CRYSTALLIZATION.
RX MEDLINE=96326597; PubMed=8706938;
RA Aleshin A.E., Zeng C., Fromm H.J., Honatko R.B.;
RT "Crystallization and preliminary X-ray analysis of human brain
RT hexokinase.";
RL FEBS Lett. 391:9-10(1996).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 16-914.
RX MEDLINE=98154317; PubMed=9493266;
RA Aleshin A.E., Zeng C., Bourenkov G.P., Bartunik H.D., Fromm H.J.,
RA Honzatko R.B.;
RT "The mechanism of regulation of hexokinase: new insights from the
RT crystal structure of recombinant human brain hexokinase complexed
RT with glucose and glucose-6-phosphate.";
RL Structure 6:39-50(1998).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 16-914.
RX MEDLINE=98407979; PubMed=9735292;
RA Aleshin A.E., Zeng C., Bartunik H.D., Fromm H.J., Honzatko R.B.;
RT "Regulation of hexokinase I: crystal structure of recombinant human
RT brain hexokinase complexed with glucose and phosphate.";
RL J. Mol. Biol. 282:345-357(1998).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
RX MEDLINE=20045192; PubMed=10574795;
RA Rosano C., Sabini E., Rizzi M., Deriu D., Murshudov G., Bianchi M.,
RA Serafini G., Magnani M., Bolognesi M.;
RT "Binding of non-catalytic ATP to human hexokinase I highlights the
RT structural components for enzyme-membrane association control.";
RL Structure 7:1427-1437(1999).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX MEDLINE=20223513; PubMed=10686099;
RA Aleshin A.E., Kirby C., Liu X., Bourenkov G.P., Bartunik H.D.,
RA Fromm H.J., Honzatko R.B.;
RT "Crystal structures of mutant monomeric hexokinase I reveal multiple
RT ADP binding sites and conformational changes relevant to allosteric
RT regulation.";
RL J. Mol. Biol. 296:1001-1015(2000).
RN [14]
RP VARIANT ANEMIA SER-529.
RX MEDLINE=95384597; PubMed=7655856;
RA Bianchi M., Magnani M.;
RT "Hexokinase mutations that produce nonspherocytic hemolytic anemia.";
RL Blood Cells Mol. Dis. 21:2-8(1995).
CC -!- CATALYTIC ACTIVITY: ATP + D-hexose = ADP + D-hexose 6-phosphate.
CC -!- ENZYME REGULATION: Hexokinase is an allosteric enzyme inhibited by
CC its product Glc-6-P.
CC -!- PATHWAY: First step of several metabolic pathways.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Bound to the outer mitochondrial membrane.
CC Its hydrophobic N-terminal sequence may be involved in membrane
CC binding.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Common;
CC IsoId=P19367-1; Sequence=Displayed;
CC Name=2; Synonyms=Erythrocyte, R;
CC IsoId=P19367-2; Sequence=VSP_002071;
CC Name=3; Synonyms=TA, TB;
CC IsoId=P19367-3; Sequence=VSP_002072;
CC Name=4; Synonyms=TD;
CC IsoId=P19367-4; Sequence=VSP_002073;
CC -!- TISSUE SPECIFICITY: Isoform 2 is erythrocyte specific; isoforms 3
CC and 4 are testis-specific.
CC -!- DOMAIN: The N- and C-terminal halves of this hexokinase show
CC extensive sequence similarity to each other. The catalytic
CC activity is associated with the C-terminus while regulatory
CC function is associated with the N-terminus.
CC -!- MISCELLANEOUS: In vertebrates there are four major glucose-
CC phosphorylating isoenzymes, designated hexokinase I, II, III and
CC IV (glucokinase).
CC -!- SIMILARITY: Belongs to the hexokinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; M75126; AAA52646.1; -.
DR EMBL; AF016365; AAC15862.1; -.
DR EMBL; AF016349; AAC15862.1; JOINED.
DR EMBL; AF016351; AAC15862.1; JOINED.
DR EMBL; AF016352; AAC15862.1; JOINED.
DR EMBL; AF016353; AAC15862.1; JOINED.
DR EMBL; AF016354; AAC15862.1; JOINED.
DR EMBL; AF016355; AAC15862.1; JOINED.
DR EMBL; AF016356; AAC15862.1; JOINED.
DR EMBL; AF016357; AAC15862.1; JOINED.
DR EMBL; AF016358; AAC15862.1; JOINED.
DR EMBL; AF016359; AAC15862.1; JOINED.
DR EMBL; AF016360; AAC15862.1; JOINED.
DR EMBL; AF016361; AAC15862.1; JOINED.
DR EMBL; AF016362; AAC15862.1; JOINED.
DR EMBL; AF016363; AAC15862.1; JOINED.
DR EMBL; AF016364; AAC15862.1; JOINED.
DR EMBL; AF016365; AAC15863.1; -.
DR EMBL; AF016349; AAC15863.1; JOINED.
DR EMBL; AF016351; AAC15863.1; JOINED.
DR EMBL; AF016352; AAC15863.1; JOINED.
DR EMBL; AF016353; AAC15863.1; JOINED.
DR EMBL; AF016354; AAC15863.1; JOINED.
DR EMBL; AF016355; AAC15863.1; JOINED.
DR EMBL; AF016356; AAC15863.1; JOINED.
DR EMBL; AF016357; AAC15863.1; JOINED.
DR EMBL; AF016358; AAC15863.1; JOINED.
DR EMBL; AF016359; AAC15863.1; JOINED.
DR EMBL; AF016360; AAC15863.1; JOINED.
DR EMBL; AF016361; AAC15863.1; JOINED.
DR EMBL; AF016362; AAC15863.1; JOINED.
DR EMBL; AF016363; AAC15863.1; JOINED.
DR EMBL; AF016364; AAC15863.1; JOINED.
DR EMBL; AF016365; AAF82319.1; -.
DR EMBL; AF163910; AAF82319.1; JOINED.
DR EMBL; AF163911; AAF82319.1; JOINED.
DR EMBL; AF016351; AAF82319.1; JOINED.
DR EMBL; AF016352; AAF82319.1; JOINED.
DR EMBL; AF016353; AAF82319.1; JOINED.
DR EMBL; AF016354; AAF82319.1; JOINED.
DR EMBL; AF016355; AAF82319.1; JOINED.
DR EMBL; AF016356; AAF82319.1; JOINED.
DR EMBL; AF016357; AAF82319.1; JOINED.
DR EMBL; AF016358; AAF82319.1; JOINED.
DR EMBL; AF016359; AAF82319.1; JOINED.
DR EMBL; AF016360; AAF82319.1; JOINED.
DR EMBL; AF016361; AAF82319.1; JOINED.
DR EMBL; AF016362; AAF82319.1; JOINED.
DR EMBL; AF016363; AAF82319.1; JOINED.
DR EMBL; AF016364; AAF82319.1; JOINED.
DR EMBL; AF016365; AAF82320.1; -.
DR EMBL; AF163912; AAF82320.1; JOINED.
DR EMBL; AF016351; AAF82320.1; JOINED.
DR EMBL; AF016352; AAF82320.1; JOINED.
DR EMBL; AF016353; AAF82320.1; JOINED.
DR EMBL; AF016354; AAF82320.1; JOINED.
DR EMBL; AF016355; AAF82320.1; JOINED.
DR EMBL; AF016356; AAF82320.1; JOINED.
DR EMBL; AF016357; AAF82320.1; JOINED.
DR EMBL; AF016358; AAF82320.1; JOINED.
DR EMBL; AF016359; AAF82320.1; JOINED.
DR EMBL; AF016360; AAF82320.1; JOINED.
DR EMBL; AF016361; AAF82320.1; JOINED.
DR EMBL; AF016362; AAF82320.1; JOINED.
DR EMBL; AF016363; AAF82320.1; JOINED.
DR EMBL; AF016364; AAF82320.1; JOINED.
DR EMBL; BC008730; AAH08730.1; -.
DR EMBL; AF029306; AAC00172.1; -.
DR EMBL; X66957; CAA47379.1; -.
DR EMBL; AF073786; AAC25424.1; -.
DR PIR; A31869; A31869.
DR PDB; 1DGK; 08-MAR-00.
DR PDB; 1HKB; 03-JUN-98.
DR PDB; 1HKC; 11-NOV-98.
DR PDB; 1QHA; 10-NOV-99.
DR PDB; 1CZA; 06-MAR-00.
DR GK; P19367; -.
DR Genew; HGNC:4922; HK1.
DR MIM; 142600; -.
DR MIM; 235700; -.
DR GO; GO:0004396; F:hexokinase activity; TAS.
DR GO; GO:0006096; P:glycolysis; TAS.
DR InterPro; IPR001312; Hexokinase.
DR Pfam; PF03727; hexokinase2; 2.
DR Pfam; PF00349; hexokinase; 2.
DR PRINTS; PR00475; HEXOKINASE.
DR ProDom; PD001109; Hexokinase; 2.
DR PROSITE; PS00378; HEXOKINASES; 2.
KW Transferase; Kinase; Glycolysis; Allosteric enzyme; Repeat;
KW ATP-binding; Membrane; Polymorphism; Alternative splicing;
KW 3D-structure.
FT DOMAIN 1 12 HYDROPHOBIC.
FT DOMAIN 13 475 REGULATORY.
FT DOMAIN 476 917 CATALYTIC.
FT DOMAIN 149 175 GLUCOSE-BINDING (POTENTIAL).
FT DOMAIN 597 623 GLUCOSE-BINDING (POTENTIAL).
FT NP_BIND 84 89 ATP (Potential).
FT NP_BIND 532 537 ATP (Potential).
FT BINDING 558 558 ATP (Potential).
FT VARSPLIC 1 21 MIAAQLLAYYFTELKDDQVKK -> MDCEHSLSLPCRGAEA
FT WEIG (in isoform 2).
FT /FTId=VSP_002071.
FT VARSPLIC 1 21 MIAAQLLAYYFTELKDDQVKK -> MGQICQRESATAAEKP
FT KLHLLAESE (in isoform 3).
FT /FTId=VSP_002072.
FT VARSPLIC 1 21 MIAAQLLAYYFTELKDDQVKK -> MAKRALRDF (in
FT isoform 4).
FT /FTId=VSP_002073.
FT VARIANT 529 529 L -> S (in anemia).
FT /FTId=VAR_009878.
FT CONFLICT 730 730 N -> D (in Ref. 2 and 3).
FT CONFLICT 776 776 M -> L (in Ref. 2 and 3).
FT HELIX 18 25
FT TURN 26 26
FT HELIX 27 29
FT HELIX 33 51
FT TURN 53 58
FT STRAND 64 65
FT STRAND 78 85
FT STRAND 90 97
FT STRAND 106 112
FT HELIX 116 119
FT TURN 120 120
FT STRAND 122 122
FT HELIX 123 140
FT TURN 141 142
FT TURN 144 145
FT STRAND 149 154
FT STRAND 158 159
FT TURN 163 164
FT STRAND 167 168
FT TURN 173 174
FT STRAND 178 178
FT TURN 179 182
FT STRAND 184 184
FT HELIX 185 195
FT TURN 197 198
FT STRAND 202 207
FT HELIX 209 220
FT TURN 222 223
FT STRAND 224 230
FT STRAND 234 241
FT HELIX 242 244
FT TURN 246 247
FT STRAND 254 258
FT HELIX 261 263
FT TURN 264 267
FT TURN 269 273
FT HELIX 276 283
FT TURN 284 284
FT TURN 288 289
FT TURN 292 293
FT HELIX 294 297
FT HELIX 299 315
FT TURN 316 317
FT HELIX 320 322
FT TURN 326 329
FT TURN 331 332
FT HELIX 336 342
FT TURN 343 343
FT TURN 345 347
FT HELIX 348 358
FT TURN 359 360
FT HELIX 365 401
FT TURN 402 402
FT STRAND 406 413
FT HELIX 415 419
FT HELIX 423 434
FT TURN 436 437
FT STRAND 438 444
FT TURN 446 449
FT HELIX 450 474
FT HELIX 475 477
FT HELIX 481 499
FT TURN 501 503
FT HELIX 504 506
FT STRAND 512 513
FT STRAND 526 533
FT STRAND 538 546
FT STRAND 552 560
FT HELIX 564 567
FT TURN 568 568
FT STRAND 570 570
FT HELIX 571 588
FT TURN 589 590
FT STRAND 597 602
FT STRAND 606 607
FT TURN 611 612
FT STRAND 615 616
FT TURN 621 622
FT STRAND 626 626
FT TURN 627 627
FT TURN 629 630
FT STRAND 632 632
FT HELIX 633 644
FT STRAND 650 655
FT HELIX 657 666
FT TURN 670 671
FT STRAND 672 678
FT STRAND 682 689
FT HELIX 690 692
FT TURN 694 695
FT STRAND 702 706
FT HELIX 709 711
FT TURN 712 715
FT TURN 717 721
FT HELIX 724 731
FT TURN 732 732
FT TURN 734 737
FT HELIX 740 743
FT TURN 744 745
FT HELIX 747 763
FT TURN 764 765
FT HELIX 768 770
FT HELIX 774 777
FT TURN 779 782
FT HELIX 784 790
FT TURN 791 791
FT TURN 793 794
FT HELIX 797 806
FT TURN 807 808
FT HELIX 813 848
FT TURN 849 850
FT STRAND 854 861
FT HELIX 863 867
FT HELIX 871 882
FT TURN 884 885
FT STRAND 886 892
FT TURN 896 897
FT HELIX 898 905
FT TURN 906 906
FT HELIX 907 910
FT TURN 911 912
SQ SEQUENCE 917 AA; 102502 MW; 150A66D262687501 CRC64;
MIAAQLLAYY FTELKDDQVK KIDKYLYAMR LSDETLIDIM TRFRKEMKNG LSRDFNPTAT
VKMLPTFVRS IPDGSEKGDF IALDLGGSSF RILRVQVNHE KNQNVHMESE VYDTPENIVH
GSGSQLFDHV AECLGDFMEK RKIKDKKLPV GFTFSFPCQQ SKIDEAILIT WTKRFKASGV
EGADVVKLLN KAIKKRGDYD ANIVAVVNDT VGTMMTCGYD DQHCEVGLII GTGTNACYME
ELRHIDLVEG DEGRMCINTE WGAFGDDGSL EDIRTEFDRE IDRGSLNPGK QLFEKMVSGM
YLGELVRLIL VKMAKEGLLF EGRITPELLT RGKFNTSDVS AIEKNKEGLH NAKEILTRLG
VEPSDDDCVS VQHVCTIVSF RSANLVAATL GAILNRLRDN KGTPRLRTTV GVDGSLYKTH
PQYSRRFHKT LRRLVPDSDV RFLLSESGSG KGAAMVTAVA YRLAEQHRQI EETLAHFHLT
KDMLLEVKKR MRAEMELGLR KQTHNNAVVK MLPSFVRRTP DGTENGDFLA LDLGGTNFRV
LLVKIRSGKK RTVEMHNKIY AIPIEIMQGT GEELFDHIVS CISDFLDYMG IKGPRMPLGF
TFSFPCQQTS LDAGILITWT KGFKATDCVG HDVVTLLRDA IKRREEFDLD VVAVVNDTVG
TMMTCAYEEP TCEVGLIVGT GSNACYMEEM KNVEMVEGDQ GQMCINMEWG AFGDNGCLDD
IRTHYDRLVN EYSLNAGKQR YEKMISGMYL GEIVRNILID FTKKGFLFRG QISETMKTRG
IFETKFLSQI ESDRLALLQV RAILQQLGLN STCDDSILVK TVCGVVSRRA AQLCGAGMAA
VVDKIRENRG LDRLNVTVGV DGTLYKLHPH FSRIMHQTVK ELSPKCNVSF LLSEDGSGKG
AALITAVGVR LRTEASS
//
ID HXK2_HUMAN STANDARD; PRT; 917 AA.
AC P52789; Q9UN82;
DT 01-OCT-1996 (Rel. 34, Created)
DT 01-OCT-1996 (Rel. 34, Last sequence update)
DT 28-FEB-2003 (Rel. 41, Last annotation update)
DE Hexokinase, type II (EC 2.7.1.1) (HK II) (Muscle form hexokinase).
GN HK2.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A., AND VARIANT HIS-142.
RC TISSUE=Blood, Muscle, and Placenta;
RX MEDLINE=96238411; PubMed=8786021;
RA Lehto M., Huang X., Davis E.M., Le Beau M.M., Laurila E.,
RA Eriksson K.F., Bell G.I., Groop L.C.;
RT "Human hexokinase II gene: exon-intron organization, mutation
RT screening in NIDDM, and its relationship to muscle hexokinase
RT activity.";
RL Diabetologia 38:1466-1474(1995).
RN [2]
RP SEQUENCE FROM N.A.
RC TISSUE=Skeletal muscle;
RX MEDLINE=94071972; PubMed=8250948;
RA Deeb S.S., Malkki M., Laakso M.;
RT "Human hexokinase II: sequence and homology to other hexokinases.";
RL Biochem. Biophys. Res. Commun. 197:68-74(1993).
RN [3]
RP SEQUENCE FROM N.A.
RC TISSUE=Skeletal muscle;
RA Malkki M., Heikkinen S., Deeb S.S., Laakso M.;
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SEQUENCE OF 614-739 FROM N.A.
RX MEDLINE=94306348; PubMed=7518342;
RA Shinohara Y., Yamamoto K., Kogure K., Ichihara J., Terada H.;
RT "Steady state transcript levels of the type II hexokinase and type 1
RT glucose transporter in human tumor cell lines.";
RL Cancer Lett. 82:27-32(1994).
RN [5]
RP VARIANTS VAL-314; CYS-353 AND GLN-775.
RX MEDLINE=95189031; PubMed=7883120;
RA Laakso M., Malkki M., Deeb S.S.;
RT "Amino acid substitutions in hexokinase II among patients with
RT NIDDM.";
RL Diabetes 44:330-334(1995).
RN [6]
RP VARIANT HIS-142.
RX MEDLINE=95189033; PubMed=7883122;
RA Vidal-Puig A., Printz R.L., Stratton I.M., Granner D.K., Moller D.E.;
RT "Analysis of the hexokinase II gene in subjects with insulin
RT resistance and NIDDM and detection of a Gln142-->His substitution.";
RL Diabetes 44:340-346(1995).
RN [7]
RP VARIANTS HIS-142; PHE-148; GLN-497 AND LYS-844.
RX MEDLINE=95189034; PubMed=7883123;
RA Echwald S.M., Bjoerbaek C., Hansen T., Clausen J.O., Vestergaard H.,
RA Zierath J.R., Printz R.L., Granner D.K., Pedersen O.;
RT "Identification of four amino acid substitutions in hexokinase II and
RT studies of relationships to NIDDM, glucose effectiveness, and insulin
RT sensitivity.";
RL Diabetes 44:347-353(1995).
CC -!- CATALYTIC ACTIVITY: ATP + D-hexose = ADP + D-hexose 6-phosphate.
CC -!- ENZYME REGULATION: Hexokinase is an allosteric enzyme inhibited by
CC its product Glc-6-P.
CC -!- PATHWAY: First step of several metabolic pathways.
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SUBCELLULAR LOCATION: Bound to the outer mitochondrial membrane.
CC Its hydrophobic N-terminal sequence may be involved in membrane
CC binding (By similarity).
CC -!- TISSUE SPECIFICITY: Predominant hexokinase isozyme expressed in
CC insulin-responsive tissues such as skeletal muscle.
CC -!- DOMAIN: The N- and C-terminal halves of this hexokinase show
CC extensive sequence similarity to each other. The catalytic
CC activity is associated with the C-terminus while regulatory
CC function is associated with the N-terminus.
CC -!- POLYMORPHISM: Although found in NIDDM patients, genetic variations
CC of HK2 do not contribute to the disease.
CC -!- MISCELLANEOUS: In vertebrates there are four major glucose-
CC phosphorylating isoenzymes, designated hexokinase I, II, III and
CC IV (glucokinase).
CC -!- SIMILARITY: Belongs to the hexokinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; Z46376; CAA86511.1; -.
DR EMBL; Z46354; CAA86476.2; -.
DR EMBL; Z46355; CAA86476.2; JOINED.
DR EMBL; Z46604; CAA86476.2; JOINED.
DR EMBL; Z46356; CAA86476.2; JOINED.
DR EMBL; Z46357; CAA86476.2; JOINED.
DR EMBL; Z46358; CAA86476.2; JOINED.
DR EMBL; Z46359; CAA86476.2; JOINED.
DR EMBL; Z46360; CAA86476.2; JOINED.
DR EMBL; Z46361; CAA86476.2; JOINED.
DR EMBL; Z46362; CAA86476.2; JOINED.
DR EMBL; Z46363; CAA86476.2; JOINED.
DR EMBL; Z46364; CAA86476.2; JOINED.
DR EMBL; Z46365; CAA86476.2; JOINED.
DR EMBL; Z46366; CAA86476.2; JOINED.
DR EMBL; Z46367; CAA86476.2; JOINED.
DR EMBL; Z46368; CAA86476.2; JOINED.
DR EMBL; Z46369; CAA86476.2; JOINED.
DR EMBL; AF148513; AAD30174.1; -.
DR EMBL; D25412; BAA04999.1; -.
DR EMBL; D25411; BAA04999.1; JOINED.
DR PIR; S48809; JC2025.
DR HSSP; P05708; 1BG3.
DR Genew; HGNC:4923; HK2.
DR GK; P52789; -.
DR MIM; 601125; -.
DR GO; GO:0004396; F:hexokinase activity; TAS.
DR GO; GO:0000074; P:regulation of cell cycle; TAS.
DR InterPro; IPR001312; Hexokinase.
DR Pfam; PF03727; hexokinase2; 2.
DR Pfam; PF00349; hexokinase; 2.
DR PRINTS; PR00475; HEXOKINASE.
DR ProDom; PD001109; Hexokinase; 2.
DR PROSITE; PS00378; HEXOKINASES; 2.
KW Transferase; Kinase; Glycolysis; Allosteric enzyme; Repeat;
KW ATP-binding; Membrane; Polymorphism.
FT DOMAIN 1 12 HYDROPHOBIC.
FT DOMAIN 13 475 REGULATORY.
FT DOMAIN 476 917 CATALYTIC.
FT DOMAIN 149 175 GLUCOSE-BINDING (POTENTIAL).
FT DOMAIN 597 623 GLUCOSE-BINDING (POTENTIAL).
FT NP_BIND 84 89 ATP (Potential).
FT NP_BIND 532 537 ATP (Potential).
FT BINDING 558 558 ATP (Potential).
FT VARIANT 142 142 Q -> H (does not affect activity).
FT /FTId=VAR_003691.
FT VARIANT 148 148 L -> F.
FT /FTId=VAR_010577.
FT VARIANT 314 314 A -> V.
FT /FTId=VAR_010578.
FT VARIANT 353 353 R -> C.
FT /FTId=VAR_010579.
FT VARIANT 497 497 R -> Q.
FT /FTId=VAR_010580.
FT VARIANT 775 775 R -> Q.
FT /FTId=VAR_010581.
FT VARIANT 844 844 R -> K.
FT /FTId=VAR_010582.
FT CONFLICT 12 12 T -> S (in Ref. 2).
FT CONFLICT 406 406 L -> A (in Ref. 2).
FT CONFLICT 634 634 V -> A (in Ref. 2).
FT CONFLICT 803 803 T -> I (IN REF. 1; CAA86476 AND 2).
FT CONFLICT 870 870 Missing (IN REF. 1; CAA86476).
SQ SEQUENCE 917 AA; 102367 MW; 1C7CE801D147E3ED CRC64;
MIASHLLAYF FTELNHDQVQ KVDQYLYHMR LSDETLLEIS KRFRKEMEKG LGATTHPTAA
VKMLPTFVRS TPDGTEHGEF LALDLGGTNF RVLWVKVTDN GLQKVEMENQ IYAIPEDIMR
GSGTQLFDHI AECLANFMDK LQIKDKKLPL GFTFSFPCHQ TKLDESFLVS WTKGFKSSGV
EGRDVVALIR KAIQRRGDFD IDIVAVVNDT VGTMMTCGYD DHNCEIGLIV GTGSNACYME
EMRHIDMVEG DEGRMCINME WGAFGDDGSL NDIRTEFDQE IDMGSLNPGK QLFEKMISGM
YMGELVRLIL VKMAKEELLF GGKLSPELLN TGRFETKDIS DIEGEKDGIR KAREVLMRLG
LDPTQEDCVA THRICQIVST RSASLCAATL AAVLQRIKEN KGEERLRSTI GVDGSVYKKH
PHFAKRLHKT VRRLVPGCDV RFLRSEDGSG KGAAMVTAVA YRLADQHRAR QKTLEHLQLS
HDQLLEVKRR MKVEMERGLS KETHASAPVK MLPTYVCATP DGTEKGDFLA LDLGGTNFRV
LLVRVRNGKW GGVEMHNKIY AIPQEVMHGT GDELFDHIVQ CIADFLEYMG MKGVSLPLGF
TFSFPCQQNS LDESILLKWT KGFKASGCEG EDVVTLLKEA IHRREEFDLD VVAVVNDTVG
TMMTCGFEDP HCEVGLIVGT GSNACYMEEM RNVELVEGEE GRMCVNMEWG AFGDNGCLDD
FRTEFDVAVD ELSLNPGKQR FEKMISGMYL GEIVRNILID FTKRGLLFRG RISERLKTRG
IFETKFLSQI ESDCLALLQV RATLQHLGLE STCDDSIIVK EVCTVVARRA AQLCGAGMAA
VVDRIRENRG LDALKVTVGV DGTLYKLHPH FAKVMHETVK DLAPKCDVSF LQSEDGSGKG
AALITAVACR IREAGQR
//
ID HXK3_HUMAN STANDARD; PRT; 923 AA.
AC P52790;
DT 01-OCT-1996 (Rel. 34, Created)
DT 01-OCT-1996 (Rel. 34, Last sequence update)
DT 28-FEB-2003 (Rel. 41, Last annotation update)
DE Hexokinase type III (EC 2.7.1.1) (HK III).
GN HK3.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RC TISSUE=Liver;
RX MEDLINE=96411670; PubMed=8812439;
RA Furuta H., Nishi S., Le Beau M.M., Fernald A.A., Yano H., Bell G.I.;
RT "Sequence of human hexokinase III cDNA and assignment of the human
RT hexokinase III gene (HK3) to chromosome band 5q35.2 by fluorescence
RT in situ hybridization.";
RL Genomics 36:206-209(1996).
RN [2]
RP SEQUENCE OF 358-923 FROM N.A.
RC TISSUE=Liver;
RX MEDLINE=96351387; PubMed=8717435;
RA Palma F., Agostini D., Mason P., Dacha M., Piccoli G., Biagiarelli B.,
RA Fiorani M., Stocchi V.;
RT "Purification and characterization of the carboxyl-domain of human
RT hexokinase type III expressed as fusion protein.";
RL Mol. Cell. Biochem. 155:23-29(1996).
CC -!- CATALYTIC ACTIVITY: ATP + D-hexose = ADP + D-hexose 6-phosphate.
CC -!- ENZYME REGULATION: Hexokinase is an allosteric enzyme inhibited by
CC its product Glc-6-P.
CC -!- PATHWAY: First step of several metabolic pathways.
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- DOMAIN: The N- and C-terminal halves of this hexokinase show
CC extensive sequence similarity to each other. The catalytic
CC activity is associated with the C-terminus while regulatory
CC function is associated with the N-terminus.
CC -!- MISCELLANEOUS: In vertebrates there are four major glucose-
CC phosphorylating isoenzymes, designated hexokinase I, II, III and
CC IV (glucokinase).
CC -!- SIMILARITY: Belongs to the hexokinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; U51333; AAC50732.1; -.
DR EMBL; U42303; AAC50422.1; -.
DR HSSP; P05708; 1BG3.
DR Genew; HGNC:4925; HK3.
DR GK; P52790; -.
DR MIM; 142570; -.
DR GO; GO:0016020; C:membrane; NAS.
DR GO; GO:0005524; F:ATP binding; NAS.
DR GO; GO:0004396; F:hexokinase activity; NAS.
DR GO; GO:0006096; P:glycolysis; NAS.
DR InterPro; IPR001312; Hexokinase.
DR Pfam; PF00349; hexokinase; 2.
DR Pfam; PF03727; hexokinase2; 2.
DR PRINTS; PR00475; HEXOKINASE.
DR ProDom; PD001109; Hexokinase; 2.
DR PROSITE; PS00378; HEXOKINASES; 1.
KW Transferase; Kinase; Glycolysis; Allosteric enzyme; Repeat;
KW ATP-binding; Membrane.
FT DOMAIN 1 488 REGULATORY.
FT DOMAIN 489 923 CATALYTIC.
FT DOMAIN 162 188 GLUCOSE-BINDING (POTENTIAL).
FT DOMAIN 603 629 GLUCOSE-BINDING (POTENTIAL).
FT NP_BIND 95 100 ATP (Potential).
FT NP_BIND 542 547 ATP (Potential).
FT CONFLICT 420 420 Q -> L (in Ref. 2).
FT CONFLICT 431 431 E -> Q (in Ref. 2).
FT CONFLICT 439 439 V -> I (in Ref. 2).
FT CONFLICT 510 510 K -> R (in Ref. 2).
FT CONFLICT 512 513 LR -> SE (in Ref. 2).
FT CONFLICT 516 516 A -> S (in Ref. 2).
FT CONFLICT 519 519 L -> S (in Ref. 2).
FT CONFLICT 530 531 PD -> LT (in Ref. 2).
FT CONFLICT 577 578 GQ -> AE (in Ref. 2).
FT CONFLICT 604 604 L -> T (in Ref. 2).
FT CONFLICT 708 708 R -> H (in Ref. 2).
FT CONFLICT 718 718 F -> L (in Ref. 2).
FT CONFLICT 728 728 S -> R (in Ref. 2).
FT CONFLICT 750 750 M -> I (in Ref. 2).
FT CONFLICT 831 831 A -> V (in Ref. 2).
FT CONFLICT 836 836 A -> P (in Ref. 2).
FT CONFLICT 853 853 G -> E (in Ref. 2).
FT CONFLICT 918 918 A -> T (in Ref. 2).
SQ SEQUENCE 923 AA; 98919 MW; D4C53841D851B5FB CRC64;
MDSIGSSGLR QGEETLSCSE EGLPGPSDSS ELVQECLQQF KVTRAQLQQI QASLLGSMEQ
ALRGQASPAP AVRMLPTYVG STPHGTEQGD FVVLELGATG ASLRVLWVTL TGIEGHRVEP
RSQEFVIPQE VMLGAGQQLF DFAAHCLSEF LDAQPVNKQG LQLGFSFSFP CHQTGLDRST
LISWTKGFRC SGVEGQDVVQ LLRDAIRRQG AYNIDVVAVV NDTVGTMMGC EPGVRPCEVG
LVVDTGTNAC YMEEARHVAV LDEDRGRVCV SVEWGSLSDD GALGPVLTTF DHTLDHESLN
PGAQRFEKMI GGLYLGELVR LVLAHLARCG VLFGGCTSPA LLSQGSILLE HVAEMEDPST
GAARVHAILQ DLGLSPGASD VELVQHVCAA VCTRAAQLCA AALAAVLSCL QHSREQQTLQ
VAVATGGRVC ERHPRFCSVL QGTVMLLAPE CDVSLIPSVD GGGRGVAMVT AVAARLAAHR
RLLEETLAPF RLNHDQLAAV QAQMRKAMAK GLRGEASSLR MLPTFVRATP DGSERGDFLA
LDLGGTNFRV LLVRVTTGVQ ITSEIYSIPE TVAQGSGQQL FDHIVDCIVD FQQKQGLSGQ
SLPLGFTFSF PCRQLGLDQG ILLNWTKGFK ASDCEGQDVV SLLREAITRR QAVELNVVAI
VNDTVGTMMS CGYEDPRCEI GLIVGTGTNA CYMEELRNVA GVPGDSGRMC INMEWGAFGD
DGSLAMLSTR FDASVDQASI NPGKQRFEKM ISGMYLGEIV RHILLHLTSL GVLFRGQQIQ
RLQTRDIFKT KFLSEIESDS LALRQVRAIL EDLGLPLTSD DALMVLEVCQ AVSQRAAQLC
GAGVAAVVEK IRGNRGLEEL AVSVGVDGTL YKLHPRFSSL VAATVRELAP RCVVTFLQSE
DGSGKGAALV TAVACRLAQL TRV
//
ID HXK4_HUMAN STANDARD; PRT; 465 AA.
AC P35557; Q05810;
DT 01-JUN-1994 (Rel. 29, Created)
DT 01-JUN-1994 (Rel. 29, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Hexokinase D (EC 2.7.1.1) (Hexokinase type IV) (HK IV) (HK4)
DE (Glucokinase).
GN GCK.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RX MEDLINE=92375100; PubMed=1354840;
RA Tanizawa Y., Matsutani A., Chiu K.C., Permutt M.A.;
RT "Human glucokinase gene: isolation, structural characterization, and
RT identification of a microsatellite repeat polymorphism.";
RL Mol. Endocrinol. 6:1070-1081(1992).
RN [2]
RP SEQUENCE FROM N.A.
RX MEDLINE=91334452; PubMed=1871135;
RA Tanizawa Y., Koranyi L.I., Welling C.M., Permutt M.A.;
RT "Human liver glucokinase gene: cloning and sequence determination of
RT two alternatively spliced cDNAs.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:7294-7297(1991).
RN [3]
RP SEQUENCE FROM N.A.
RC TISSUE=Pancreas;
RX MEDLINE=92380355; PubMed=1511800;
RA Nishi S., Stoffel M., Xiang K.S., Shows T.B., Bell G.I., Takeda J.;
RT "Human pancreatic beta-cell glucokinase: cDNA sequence and
RT localization of the polymorphic gene to chromosome 7, band p13.";
RL Diabetologia 35:743-747(1992).
RN [4]
RP SEQUENCE FROM N.A.
RC TISSUE=Pancreas;
RX MEDLINE=92307138; PubMed=1612194;
RA Koranyi L.I., Tanizawa Y., Welling C.M., Rabin D.U., Permutt M.A.;
RT "Human islet glucokinase gene. Isolation and sequence analysis of
RT full-length cDNA.";
RL Diabetes 41:807-811(1992).
RN [5]
RP SEQUENCE FROM N.A., AND VARIANTS MODY2 MET-228 AND ARG-261.
RC TISSUE=Placenta;
RX MEDLINE=92366529; PubMed=1502186;
RA Stoffel M., Froguel P., Takeda J., Zouali H., Vionnet N., Nishi S.,
RA Weber I.T., Harrison R.W., Pilkis S.J., Lesage S., Vaxillaire M.,
RA Velho G., Sun F., Iris F., Passa P., Cohen D., Bell G.I.;
RT "Human glucokinase gene: isolation, characterization, and
RT identification of two missense mutations linked to early-onset
RT non-insulin-dependent (type 2) diabetes mellitus.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:7698-7702(1992).
RN [6]
RP ERRATUM.
RA Stoffel M., Froguel P., Takeda J., Zouali H., Vionnet N., Nishi S.,
RA Weber I.T., Harrison R.W., Pilkis S.J., Lesage S., Vaxillaire M.,
RA Velho G., Sun F., Iris F., Passa P., Cohen D., Bell G.I.;
RL Proc. Natl. Acad. Sci. U.S.A. 89:10562-10562(1992).
RN [7]
RP SEQUENCE FROM N.A., VARIANT THR-107, AND VARIANT MODY2 ARG-261.
RX MEDLINE=93100400; PubMed=1464666;
RA Sakura H., Eto K., Kadowaki H., Simokawa K., Ueno H., Koda N.,
RA Fukushima Y., Akanuma Y., Yazaki Y., Kadowaki T.;
RT "Structure of the human glucokinase gene and identification of a
RT missense mutation in a Japanese patient with early-onset non-insulin-
RT dependent diabetes mellitus.";
RL J. Clin. Endocrinol. Metab. 75:1571-1573(1992).
RN [8]
RP SEQUENCE FROM N.A.
RC TISSUE=Lung;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [9]
RP 3D-STRUCTURE MODELING.
RX MEDLINE=94252471; PubMed=8194664;
RA St Charles R., Harrison R.W., Bell G.I., Pilkis S.J., Weber I.T.;
RT "Molecular model of human beta-cell glucokinase built by analogy to
RT the crystal structure of yeast hexokinase B.";
RL Diabetes 43:784-791(1994).
RN [10]
RP VARIANT MODY2 ARG-299.
RX MEDLINE=93265142; PubMed=1303265;
RA Stoffel M., Patel P., Lo Y.-M.D., Hattersley A.T., Lucassen A.M.,
RA Page R., Bell J.I., Bell G.I., Turner R.C., Wainscoat J.S.;
RT "Missense glucokinase mutation in maturity-onset diabetes of the
RT young and mutation screening in late-onset diabetes.";
RL Nat. Genet. 2:153-156(1992).
RN [11]
RP VARIANT THR-11.
RX MEDLINE=93202338; PubMed=8454109;
RA Chiu K.C., Tanizawa Y., Permutt M.A.;
RT "Glucokinase gene variants in the common form of NIDDM.";
RL Diabetes 42:579-582(1993).
RN [12]
RP VARIANT MODY2 PRO-131.
RX MEDLINE=93266044; PubMed=8495817;
RA Stoffel M., Bell K.L., Blackburn C.L., Powell K.L., Seo T.S.,
RA Takeda J., Vionnet N., Xiang K.-S., Gidh-Jain M., Pilkis S.J.,
RA Ober C., Bell G.I.;
RT "Identification of glucokinase mutations in subjects with gestational
RT diabetes mellitus.";
RL Diabetes 42:937-940(1993).
RN [13]
RP VARIANT ASN-4, AND VARIANTS MODY2 LYS-70; PRO-131; THR-188; ARG-257
RP AND GLU-414.
RX MEDLINE=93315503; PubMed=8325892;
RA Takeda J., Gidh-Jain M., Xu L.Z., Froguel P., Velho G., Vaxillaire M.,
RA Cohen D., Shimada F., Makino H., Nishi S., Stoffel M., Vionnet N.,
RA St Charles R., Harrison R.W., Weber I.T., Bell G.I., Pilkis S.J.;
RT "Structure/function studies of human beta-cell glucokinase. Enzymatic
RT properties of a sequence polymorphism, mutations associated with
RT diabetes, and other site-directed mutants.";
RL J. Biol. Chem. 268:15200-15204(1993).
RN [14]
RP CHARACTERIZATION OF MODY2 VARIANTS.
RX MEDLINE=93189611; PubMed=8446612;
RA Gidh-Jain M., Takeda J., Xu L.Z., Lange A.J., Vionnet N., Stoffel M.,
RA Froguel P., Velho G., Sun D., Cohen D., Patel P., Lo Y.-M.D.,
RA Hattersley A.T., Luthman H., Wedell A., St Charles R., Harrison R.W.,
RA Weber I.T., Bell G.I., Pilkis S.J.;
RT "Glucokinase mutations associated with non-insulin-dependent (type 2)
RT diabetes mellitus have decreased enzymatic activity: implications for
RT structure/function relationships.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:1932-1936(1993).
RN [15]
RP VARIANTS MODY2 TRP-36; MET-209 AND GLU-261.
RX MEDLINE=94222222; PubMed=8168652;
RA Hager J., Blanche H., Sun F., Vionnet N., Vaxillaire M., Poller W.,
RA Cohen D., Czernichow P., Velho G., Robert J.-J., Cohen N., Froguel P.;
RT "Six mutations in the glucokinase gene identified in MODY by using a
RT nonradioactive sensitive screening technique.";
RL Diabetes 43:730-733(1994).
RN [16]
RP VARIANTS MODY2.
RX MEDLINE=97201951; PubMed=9049484;
RA Velho G., Blanche H., Vaxillaire M., Bellanne-Chantelot C.,
RA Pardini V.C., Timsit J., Passa P., Deschamps I., Robert J.-J.,
RA Weber I.T., Marotta D., Pilkis S.J., Lipkind G.M., Bell G.I.,
RA Froguel P.;
RT "Identification of 14 new glucokinase mutations and description of the
RT clinical profile of 42 MODY-2 families.";
RL Diabetologia 40:217-224(1997).
RN [17]
RP VARIANTS MODY2 SER-80; LYS-221 AND CYS-227.
RA Guazzini B., Gaffi D., Mainieri D., Multari G., Cordera R.,
RA Bertolini S., Pozza G., Meschi F., Barbetti F.;
RT "Three novel missense mutations in the glucokinase gene (G80S; E221K;
RT G227C) in Italian subjects with maturity-onset diabetes of the young
RT (MODY).";
RL Hum. Mutat. 12:136-136(1998).
RN [18]
RP VARIANTS MODY2 HIS-108; SER-150; THR-259; ARG-299; TYR-382; THR-384
RP AND CYS-392.
RX MEDLINE=98324778; PubMed=9662401;
RA Hattersley A.T., Beards F., Ballantyne E., Appleton M., Harvey R.,
RA Ellard S.;
RT "Mutations in the glucokinase gene of the fetus result in reduced
RT birth weight.";
RL Nat. Genet. 19:268-270(1998).
RN [19]
RP VARIANT HYPERINSULINISM MET-455.
RX MEDLINE=98084322; PubMed=9435328;
RA Glaser B., Kesavan P., Heyman M., Davis E., Cuesta A., Buchs A.,
RA Stanley C.A., Thornton P.S., Permutt M.A., Matschinsky F.M.,
RA Herold K.C.;
RT "Familial hyperinsulinism caused by an activating glucokinase
RT mutation.";
RL N. Engl. J. Med. 338:226-230(1998).
RN [20]
RP VARIANTS MODY2 THR-110; ASP-119 AND VAL-385.
RX MEDLINE=20053748; PubMed=10588527;
RA Ng M.C.Y., Cockburn B.N., Lindner T.H., Yeung V.T.F., Chow C.-C.,
RA So W.-Y., Li J.K.Y., Lo Y.M.D., Lee Z.S.K., Cockram C.S.,
RA Critchley J.A.J.H., Bell G.I., Chan J.C.N.;
RT "Molecular genetics of diabetes mellitus in Chinese subjects:
RT identification of mutations in glucokinase and hepatocyte nuclear
RT factor-1alpha genes in patients with early-onset type 2 diabetes
RT mellitus/MODY.";
RL Diabet. Med. 16:956-963(1999).
RN [21]
RP VARIANT MODY2 PRO-164.
RX MEDLINE=20560768; PubMed=11106831;
RA Nam J.H., Lee H.C., Kim Y.H., Cha B.S., Song Y.D., Lim S.K., Kim K.R.,
RA Huh K.B.;
RT "Identification of glucokinase mutation in subjects with post-renal
RT transplantation diabetes mellitus.";
RL Diabetes Res. Clin. Pract. 50:169-176(2000).
RN [22]
RP VARIANTS MODY2 LYS-210 AND MET-228.
RX MEDLINE=21245203; PubMed=11372010;
RA Njoelstad P.R., Soevik O., Cuesta-Munoz A., Bjoerkhaug L., Massa O.,
RA Barbetti F., Undlien D.E., Shiota C., Magnuson M.A., Molven A.,
RA Matschinsky F.M., Bell G.I.;
RT "Neonatal diabetes mellitus due to complete glucokinase deficiency.";
RL N. Engl. J. Med. 344:1588-1592(2001).
CC -!- FUNCTION: Catalyzes the initial step in utilization of glucose by
CC the beta-cell and liver at physiological glucose concentration.
CC Glucokinase has a high km for glucose, and so it is effective only
CC when glucose is abundant. The role of GCK is to provide G6P for
CC the synthesis of glycogen. Pancreatic glucokinase plays an
CC important role in modulating insulin secretion. Hepatic
CC glucokinase helps to facilitate the uptake and conversion of
CC glucose by acting as an insulin-sensitive determinant of hepatic
CC glucose usage.
CC -!- CATALYTIC ACTIVITY: ATP + D-hexose = ADP + D-hexose 6-phosphate.
CC -!- ENZYME REGULATION: The use of alternative promoters apparently
CC enables the type IV hexokinase gene to be regulated by insulin in
CC the liver and glucose in the beta cell. This may constitute an
CC important feedback loop for maintaining glucose homeostasis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P35557-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P35557-2; Sequence=VSP_002074;
CC Name=3;
CC IsoId=P35557-3; Sequence=VSP_002075;
CC -!- TISSUE SPECIFICITY: PANCREAS (ISOFORM 1) AND LIVER (ISOFORMS 2 AND
CC 3).
CC -!- DISEASE: Defects in GCK are the cause of maturity-onset diabetes
CC of the young, type II (MODY2) [MIM:125851]. It is a form of
CC noninsulin-dependent diabetes mellitus (NIDDM) characterized by
CC monogenic autosomal dominant transmission and early age of onset.
CC Mutations in GCK result in mild chronic hyperglycemia due to
CC reduced pancreatic beta cell responsiveness to glucose, and
CC decreased net accumulation of hepatic glycogen and increased
CC hepatic gluconeogenesis following meals.
CC -!- DISEASE: Defects in GCK are a cause of hyperinsulinism
CC [MIM:602485]; a familial autosomal dominant disease. It is the
CC most common cause of persistent hypoglycemia in infancy. Unless
CC early and aggressive intervention is undertaken, brain damage from
CC recurrent episodes of hypoglycemia may occur.
CC -!- MISCELLANEOUS: In vertebrates there are four major glucose-
CC phosphorylating isoenzymes, designated hexokinase I, II, III and
CC IV (glucokinase).
CC -!- SIMILARITY: Belongs to the hexokinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; M88011; AAA51824.1; -.
DR EMBL; M69051; AAB59563.1; ALT_SEQ.
DR EMBL; M90298; AAA67541.1; ALT_TERM.
DR EMBL; M90298; AAA67542.1; ALT_TERM.
DR EMBL; M90299; AAA52562.1; -.
DR EMBL; AF041022; AAB97680.1; -.
DR EMBL; AF041012; AAB97680.1; JOINED.
DR EMBL; AF041015; AAB97680.1; JOINED.
DR EMBL; AF041016; AAB97680.1; JOINED.
DR EMBL; AF041017; AAB97680.1; JOINED.
DR EMBL; AF041018; AAB97680.1; JOINED.
DR EMBL; AF041019; AAB97680.1; JOINED.
DR EMBL; AF041020; AAB97680.1; JOINED.
DR EMBL; AF041021; AAB97680.1; JOINED.
DR EMBL; AF041022; AAB97681.1; -.
DR EMBL; AF041013; AAB97681.1; JOINED.
DR EMBL; AF041015; AAB97681.1; JOINED.
DR EMBL; AF041016; AAB97681.1; JOINED.
DR EMBL; AF041017; AAB97681.1; JOINED.
DR EMBL; AF041018; AAB97681.1; JOINED.
DR EMBL; AF041019; AAB97681.1; JOINED.
DR EMBL; AF041020; AAB97681.1; JOINED.
DR EMBL; AF041021; AAB97681.1; JOINED.
DR EMBL; AF041022; AAB97682.1; -.
DR EMBL; AF041014; AAB97682.1; JOINED.
DR EMBL; AF041015; AAB97682.1; JOINED.
DR EMBL; AF041016; AAB97682.1; JOINED.
DR EMBL; AF041017; AAB97682.1; JOINED.
DR EMBL; AF041018; AAB97682.1; JOINED.
DR EMBL; AF041019; AAB97682.1; JOINED.
DR EMBL; AF041020; AAB97682.1; JOINED.
DR EMBL; AF041021; AAB97682.1; JOINED.
DR EMBL; BC001890; AAH01890.1; -.
DR PIR; A46157; A46157.
DR PDB; 1GLK; 30-NOV-94.
DR Genew; HGNC:4195; GCK.
DR GK; P35557; -.
DR MIM; 138079; -.
DR MIM; 125851; -.
DR MIM; 602485; -.
DR GO; GO:0004340; F:glucokinase activity; TAS.
DR InterPro; IPR001312; Hexokinase.
DR Pfam; PF03727; hexokinase2; 1.
DR Pfam; PF00349; hexokinase; 1.
DR PRINTS; PR00475; HEXOKINASE.
DR ProDom; PD001109; Hexokinase; 1.
DR PROSITE; PS00378; HEXOKINASES; 1.
KW Transferase; Kinase; Glycolysis; ATP-binding; Alternative splicing;
KW Disease mutation; Polymorphism; Diabetes mellitus; 3D-structure.
FT NP_BIND 78 83 ATP (Potential).
FT BINDING 104 104 ATP (Potential).
FT DOMAIN 145 171 GLUCOSE-BINDING (POTENTIAL).
FT VARSPLIC 1 15 MLDDRARMEAAKKEK -> MAMDVTRSQAQTALTL (in
FT isoform 2).
FT /FTId=VSP_002074.
FT VARSPLIC 1 15 MLDDRARMEAAKKEK -> MPRPRSQLPQPNSQ (in
FT isoform 3).
FT /FTId=VSP_002075.
FT VARIANT 4 4 D -> N.
FT /FTId=VAR_003692.
FT VARIANT 11 11 A -> T.
FT /FTId=VAR_010583.
FT VARIANT 36 36 R -> W (in MODY2).
FT /FTId=VAR_010584.
FT VARIANT 53 53 A -> S (in MODY2).
FT /FTId=VAR_010585.
FT VARIANT 70 70 E -> K (in MODY2; large increase in Km
FT for glucose).
FT /FTId=VAR_003693.
FT VARIANT 80 80 G -> A (in MODY2).
FT /FTId=VAR_003694.
FT VARIANT 80 80 G -> S (in MODY2).
FT /FTId=VAR_003695.
FT VARIANT 107 107 M -> T.
FT /FTId=VAR_003696.
FT VARIANT 108 108 Y -> H (in MODY2).
FT /FTId=VAR_010586.
FT VARIANT 110 110 I -> T (in MODY2).
FT /FTId=VAR_012352.
FT VARIANT 119 119 A -> D (in MODY2).
FT /FTId=VAR_012353.
FT VARIANT 131 131 S -> P (in MODY2; significant increase in
FT the Km and in the affinity for ATP).
FT /FTId=VAR_003697.
FT VARIANT 137 137 H -> R (in MODY2).
FT /FTId=VAR_010587.
FT VARIANT 150 150 F -> S (in MODY2).
FT /FTId=VAR_010588.
FT VARIANT 164 164 L -> P (in MODY2).
FT /FTId=VAR_012350.
FT VARIANT 168 168 T -> P (in MODY2).
FT /FTId=VAR_010589.
FT VARIANT 175 175 G -> R (in MODY2).
FT /FTId=VAR_003698.
FT VARIANT 182 182 V -> M (in MODY2).
FT /FTId=VAR_003699.
FT VARIANT 188 188 A -> T (in MODY2; large increase in Km
FT for glucose).
FT /FTId=VAR_003700.
FT VARIANT 203 203 V -> A (in MODY2).
FT /FTId=VAR_003701.
FT VARIANT 209 209 T -> M (in MODY2).
FT /FTId=VAR_010590.
FT VARIANT 210 210 M -> K (in MODY2).
FT /FTId=VAR_012351.
FT VARIANT 210 210 M -> T (in MODY2).
FT /FTId=VAR_010591.
FT VARIANT 213 213 C -> R (in MODY2).
FT /FTId=VAR_010592.
FT VARIANT 221 221 E -> K (in MODY2).
FT /FTId=VAR_003702.
FT VARIANT 226 226 V -> M (in MODY2).
FT /FTId=VAR_003703.
FT VARIANT 227 227 G -> C (in MODY2).
FT /FTId=VAR_003704.
FT VARIANT 228 228 T -> M (in MODY2).
FT /FTId=VAR_003705.
FT VARIANT 256 256 E -> K (in MODY2).
FT /FTId=VAR_003706.
FT VARIANT 257 257 W -> R (in MODY2; almost complete loss of
FT activity).
FT /FTId=VAR_003707.
FT VARIANT 259 259 A -> T (in MODY2).
FT /FTId=VAR_010593.
FT VARIANT 261 261 G -> E (in MODY2).
FT /FTId=VAR_010594.
FT VARIANT 261 261 G -> R (in MODY2).
FT /FTId=VAR_003708.
FT VARIANT 279 279 E -> Q (in MODY2).
FT /FTId=VAR_003709.
FT VARIANT 299 299 G -> R (in MODY2).
FT /FTId=VAR_003710.
FT VARIANT 300 300 E -> Q (in MODY2).
FT /FTId=VAR_003711.
FT VARIANT 300 300 E -> K (in MODY2).
FT /FTId=VAR_003712.
FT VARIANT 309 309 L -> P (in MODY2).
FT /FTId=VAR_003713.
FT VARIANT 336 336 S -> L (in MODY2).
FT /FTId=VAR_010595.
FT VARIANT 367 367 V -> M (in MODY2).
FT /FTId=VAR_010596.
FT VARIANT 382 382 C -> Y (in MODY2).
FT /FTId=VAR_010597.
FT VARIANT 384 384 A -> T (in MODY2).
FT /FTId=VAR_010598.
FT VARIANT 385 385 G -> V (in MODY2).
FT /FTId=VAR_012354.
FT VARIANT 392 392 R -> C (in MODY2).
FT /FTId=VAR_010599.
FT VARIANT 414 414 K -> E (in MODY2; large increase in Km
FT for glucose).
FT /FTId=VAR_003714.
FT VARIANT 455 455 V -> M (in hyperinsulinism).
FT /FTId=VAR_003715.
FT MUTAGEN 177 177 E->K: SMALL CHANGE IN ACTIVITY.
FT MUTAGEN 256 256 E->A: INACTIVE ENZYME.
FT MUTAGEN 414 414 K->A: SMALL CHANGE IN ACTIVITY.
FT CONFLICT 107 107 M -> T (in Ref. 2).
SQ SEQUENCE 465 AA; 52191 MW; 094D4A2F78096724 CRC64;
MLDDRARMEA AKKEKVEQIL AEFQLQEEDL KKVMRRMQKE MDRGLRLETH EEASVKMLPT
YVRSTPEGSE VGDFLSLDLG GTNFRVMLVK VGEGEEGQWS VKTKHQMYSI PEDAMTGTAE
MLFDYISECI SDFLDKHQMK HKKLPLGFTF SFPVRHEDID KGILLNWTKG FKASGAEGNN
VVGLLRDAIK RRGDFEMDVV AMVNDTVATM ISCYYEDHQC EVGMIVGTGC NACYMEEMQN
VELVEGDEGR MCVNTEWGAF GDSGELDEFL LEYDRLVDES SANPGQQLYE KLIGGKYMGE
LVRLVLLRLV DENLLFHGEA SEQLRTRGAF ETRFVSQVES DTGDRKQIYN ILSTLGLRPS
TTDCDIVRRA CESVSTRAAH MCSAGLAGVI NRMRESRSED VMRITVGVDG SVYKLHPSFK
ERFHASVRRL TPSCEITFIE SEEGSGRGAA LVSAVACKKA CMLGQ
//
ID IP3K_HUMAN STANDARD; PRT; 461 AA.
AC P23677;
DT 01-NOV-1991 (Rel. 20, Created)
DT 01-NOV-1991 (Rel. 20, Last sequence update)
DT 28-FEB-2003 (Rel. 41, Last annotation update)
DE Inositol-trisphosphate 3-kinase A (EC 2.7.1.127) (Inositol 1,4,5-
DE trisphosphate 3-kinase) (IP3K) (IP3 3-kinase).
GN ITPKA.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RC TISSUE=Brain;
RX MEDLINE=91128380; PubMed=1847047;
RA Takazawa K., Perret J., Dumont J.E., Erneux C.;
RT "Molecular cloning and expression of a human brain inositol 1,4,5-
RT trisphosphate 3-kinase.";
RL Biochem. Biophys. Res. Commun. 174:529-535(1991).
RN [2]
RP SEQUENCE FROM N.A.
RC TISSUE=Brain;
RX MEDLINE=91088302; PubMed=2175886;
RA Takazawa K., Perret J., Dumont J.E., Erneux C.;
RT "Human brain inositol 1,4,5-trisphosphate 3-kinase cDNA sequence.";
RL Nucleic Acids Res. 18:7141-7141(1990).
CC -!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol 1,4,5-trisphosphate =
CC ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate.
CC -!- ENZYME REGULATION: IP3K is activated by calmodulin.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; X54938; CAA38700.1; -.
DR PIR; JN0129; JN0129.
DR Genew; HGNC:6178; ITPKA.
DR MIM; 147521; -.
DR GO; GO:0008440; F:inositol-trisphosphate 3-kinase activity; TAS.
DR GO; GO:0007165; P:signal transduction; TAS.
DR InterPro; IPR005522; IPK.
DR Pfam; PF03770; IPK; 1.
KW Transferase; Kinase; Calmodulin-binding.
FT DOMAIN 287 295 CALMODULIN-BINDING (BY SIMILARITY).
SQ SEQUENCE 461 AA; 51008 MW; 18CA214A091F5B19 CRC64;
MTLPGGPTGM ARPGGARPCS PGLERAPRRS VGELRLLFEA RCAAVAAAAA AGEPRARGAK
RRGGQVPNGL PRAPPAPVIP QLTVTAEEPD VPPTSPGPPE RERDCLPAAG SSHLQQPRRL
STSSVSSTGS SSLLEDSEDD LLSDSESRSR GNVQLEAGED VGQKNHWQKI RTMVNLPVIS
PFKKRYAWVQ LAGHTGSFKA AGTSGLILKR CSEPERYCLA RLMADALRGC VPAFHGVVER
DGESYLQLQD LLDGFDGPCV LDCKMGVRTY LEEELTKARE RPKLRKDMYK KMLAVDPEAP
TEEEHAQRAV TKPRYMQWRE GISSSTTLGF RIEGIKKADG SCSTDFKTTR SREQVLRVFE
EFVQGDEEVL RRYLNRLQQI RDTLEVSEFF RRHEVIGSSL LFVHDHCHRA GVWLIDFGKT
TPLPDGQILD HRRPWEEGNR EDGYLLGLDN LIGILASLAE R
//
ID IP3L_HUMAN STANDARD; PRT; 946 AA.
AC P27987; Q96JS1; Q9UH47;
DT 01-AUG-1992 (Rel. 23, Created)
DT 28-FEB-2003 (Rel. 41, Last sequence update)
DT 28-FEB-2003 (Rel. 41, Last annotation update)
DE Inositol-trisphosphate 3-kinase B (EC 2.7.1.127) (Inositol 1,4,5-
DE trisphosphate 3-kinase) (IP3K) (IP3 3-kinase) (IP3K-B).
GN ITPKB.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RC TISSUE=Hippocampus;
RA Dewaste V.;
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SEQUENCE FROM N.A.
RC TISSUE=Colon;
RA Bertsch U., Suesse S., Frerk S., Fanick W.;
RT "Cloning of the complete protein coding regions for inositol 1,4,5-
RT trisphosphate 3-kinase B-isoforms from rat and human.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SEQUENCE OF 257-946 FROM N.A.
RA Donnelly S.;
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SEQUENCE OF 442-946 FROM N.A.
RC TISSUE=Brain;
RX MEDLINE=91378954; PubMed=1654894;
RA Takazawa K., Perret J., Dumont J.E., Erneux C.;
RT "Molecular cloning and expression of a new putative inositol 1,4,5-
RT trisphosphate 3-kinase isoenzyme.";
RL Biochem. J. 278:883-886(1991).
CC -!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol 1,4,5-trisphosphate =
CC ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate.
CC -!- ENZYME REGULATION: IP3K is activated by calmodulin. Form B
CC is much more sensitive to calcium/calmodulin than form A.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; Y18024; CAB65055.3; -.
DR EMBL; AJ242780; CAC40650.1; -.
DR EMBL; AL365444; CAD20257.1; -.
DR EMBL; X57206; CAA40491.1; ALT_INIT.
DR Genew; HGNC:6179; ITPKB.
DR MIM; 147522; -.
DR GO; GO:0008440; F:inositol-trisphosphate 3-kinase activity; TAS.
DR GO; GO:0007165; P:signal transduction; TAS.
DR InterPro; IPR005522; IPK.
DR Pfam; PF03770; IPK; 1.
KW Transferase; Kinase; Calmodulin-binding.
FT DOMAIN 768 776 CALMODULIN-BINDING (BY SIMILARITY).
FT DOMAIN 599 605 POLY-SER.
FT CONFLICT 173 173 R -> H (in Ref. 2).
FT CONFLICT 210 210 P -> S (in Ref. 2).
FT CONFLICT 297 301 GASLT -> APSFP (in Ref. 2).
FT CONFLICT 408 408 A -> S (in Ref. 2 and 3).
FT CONFLICT 442 443 RV -> IP (in Ref. 4).
FT CONFLICT 552 552 Q -> P (in Ref. 3).
SQ SEQUENCE 946 AA; 102391 MW; 36C0C74679B1EA1D CRC64;
MAVYCYALNS LVIMNSANEM KSGGGPGPSG SETPPPPRRA VLSPGSVFSP GRGASFLFPP
AESLSPEEPR SPGGWRSGRR RLNSSSGSGS GSSGSSVSSP SWAGRLRGDR QQVVAAGTLS
PPGPEEAKRK LRILQRELQN VQVNQKVGMF EAHIQAQSSA IQAPRSPRLG RARSPSPCPF
RSSSQPPGRV LVQGARSEER RTKSWGEQCP ETSGTDSGRK GGPSLCSSQV KKGMPPLPGR
AAPTGSEAQG PSAFVRMEKG IPASPRCGSP TAMEIDKRGS PTPGTRSCLA PSLGLFGASL
TMATEVAARV TSTGPHRPQD LALTEPSGRA RELEDLQPPE ALVERQGQFL GSETSPAPER
GGPRDGEPPG KMGKGYLPCG MPGSGEPEVG KRPEETTVSV QSAESSDALS WSRLPRALAS
VGPEEARSGA PVGGGRWQLS DRVEGGSPTL GLLGGSPSAQ PGTGNVEAGI PSGRMLEPLP
CWDAAKDLKE PQCPPGDRVG VQPGNSRVWQ GTMEKAGLAW TRGTGVQSEG TWESQRQDSD
ALPSPELLPQ DQDKPFLRKA CSPSNIPAVI ITDMGTQEDG ALEETQGSPR GNLPLRKLSS
SSASSTGFSS SYEDSEEDIS SDPERTLDPN SAFLHTLDQQ KPRVSKSWRK IKNMVHWSPF
VMSFKKKYPW IQLAGHAGSF KAAANGRILK KHCESEQRCL DRLMVDVLRP FVPAYHGDVV
KDGERYNQMD DLLADFDSPC VMDCKMGIRT YLEEELTKAR KKPSLRKDMY QKMIEVDPEA
PTEEEKAQRA VTKPRYMQWR ETISSTATLG FRIEGIKKED GTVNRDFKKT KTREQVTEAF
REFTKGNHNI LIAYRDRLKA IRTTLEVSPF FKCHEVIGSS LLFIHDKKEQ AKVWMIDFGK
TTPLPEGQTL QHDVPWQEGN REDGYLSGLN NLVDILTEMS QDAPLA
//
ID K6PF_HUMAN STANDARD; PRT; 779 AA.
AC P08237; Q16814; Q16815;
DT 01-AUG-1988 (Rel. 08, Created)
DT 01-AUG-1988 (Rel. 08, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE 6-phosphofructokinase, muscle type (EC 2.7.1.11) (Phosphofructokinase
DE 1) (Phosphohexokinase) (Phosphofructo-1-kinase isozyme A) (PFK-A)
DE (Phosphofructokinase-M).
GN PFKM.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RC TISSUE=Muscle;
RX MEDLINE=92009225; PubMed=1833270;
RA Yamasaki T., Nakajima H., Kono N., Hotta K., Yamada K., Imai E.,
RA Kuwajima M., Noguchi T., Tanaka T., Tarui S.;
RT "Structure of the entire human muscle phosphofructokinase-encoding
RT gene: a two-promoter system.";
RL Gene 104:277-282(1991).
RN [2]
RP SEQUENCE FROM N.A.
RC TISSUE=Muscle;
RX MEDLINE=89306675; PubMed=2526045;
RA Sharma P.M., Reddy G.R., Vora S., Babior B.M., McLachlan A.;
RT "Cloning and expression of a human muscle phosphofructokinase cDNA.";
RL Gene 77:177-183(1989).
RN [3]
RP SEQUENCE FROM N.A.
RC TISSUE=Muscle;
RX MEDLINE=88030023; PubMed=2822475;
RA Nakajima H., Noguchi T., Yamasaki T., Kono N., Tanaka T., Tarui S.;
RT "Cloning of human muscle phosphofructokinase cDNA.";
RL FEBS Lett. 223:113-116(1987).
RN [4]
RP SEQUENCE FROM N.A. (ISOFORM 1).
RC TISSUE=Brain, and Muscle;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [5]
RP SEQUENCE OF 271-680 FROM N.A. (ISOFORM 2).
RC TISSUE=Muscle;
RX MEDLINE=90264379; PubMed=2140567;
RA Sharma P.M., Reddy G.R., Babior B.M., McLachlan A.;
RT "Alternative splicing of the transcript encoding the human muscle
RT isoenzyme of phosphofructokinase.";
RL J. Biol. Chem. 265:9006-9010(1990).
RN [6]
RP SEQUENCE OF 1-27 FROM N.A.
RC TISSUE=Muscle;
RX MEDLINE=89306652; PubMed=2526044;
RA Valdez B.C., Chen Z., Sosa M.G., Younathan E.S., Chang S.H.;
RT "Human 6-phosphofructo-1-kinase gene has an additional intron
RT upstream of start codon.";
RL Gene 76:167-169(1989).
RN [7]
RP REVIEW ON GSD-VII VARIANTS.
RX MEDLINE=96055509; PubMed=7550225;
RA Raben N., Sherman J.B.;
RT "Mutations in muscle phosphofructokinase gene.";
RL Hum. Mutat. 6:1-6(1995).
RN [8]
RP VARIANTS GSD-VII PRO-38 AND ALA-542.
RX MEDLINE=94234147; PubMed=7513946;
RA Tsujino S., Servidei S., Tonin P., Shanske S., Azan G., DiMauro S.;
RT "Identification of three novel mutations in non-Ashkenazi Italian
RT patients with muscle phosphofructokinase deficiency.";
RL Am. J. Hum. Genet. 54:812-819(1994).
RN [9]
RP VARIANTS GSD-VII GLN-99; ASP-208 AND HIS-695.
RX MEDLINE=95126102; PubMed=7825568;
RA Raben N., Exelbert R., Spiegel R., Sherman J.B., Plotz P.,
RA Heinisch J.J.;
RT "Functional expression of human mutant phosphofructokinase in yeast:
RT genetic defects in French Canadian and Swiss patients with
RT phosphofructokinase deficiency.";
RL Am. J. Hum. Genet. 56:131-141(1995).
RN [10]
RP VARIANT GSD-VII CYS-685.
RX MEDLINE=97044518; PubMed=8889589;
RA Hamaguchi T., Nakajima H., Noguchi T., Nakagawa C., Kuwajima M.,
RA Kono N., Tarui S., Matsuzawa Y.;
RT "Novel missense mutation (W686C) of the phosphofructokinase-M gene in
RT a Japanese patient with a mild form of glycogenosis VII.";
RL Hum. Mutat. 8:273-275(1996).
CC -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D-
CC fructose 1,6-bisphosphate.
CC -!- COFACTOR: Magnesium.
CC -!- ENZYME REGULATION: Allosteric enzyme activated by ADP, AMP, or
CC fructose bisphosphate and inhibited by ATP or citrate.
CC -!- PATHWAY: Key control step of glycolysis.
CC -!- SUBUNIT: Tetramer. Muscle is M4, liver is L4, and red cell is M3L,
CC M2L2, or ML3.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P08237-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P08237-2; Sequence=VSP_004667;
CC -!- DISEASE: Defects in PFKM are the cause of glycogen storage disease
CC VII (GSD-VII) [232800]; also known as Tarui disease. GSD-VII is
CC characterized by exercise intolerance with associated nausea and
CC vomiting. Short bursts of intense activity are particularly
CC difficult. Severe muscle cramps and myoglobinuria develop after
CC vigorous exercise. Most patients obtain a "second wind" when the
CC onset of exercise is followed by a brief rest period. In time
CC patients adjust their activity level and are well compensated.
CC -!- MISCELLANEOUS: In human PFK exists as a system of 3 types of
CC subunits, PFKM (muscle), PFKL (liver) and PFKP (platelet)
CC isoenzymes.
CC -!- SIMILARITY: Belongs to the phosphofructokinase family. Two domains
CC subfamily.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; M59741; AAA82938.1; -.
DR EMBL; M59720; AAA82938.1; JOINED.
DR EMBL; M59721; AAA82938.1; JOINED.
DR EMBL; M59722; AAA82938.1; JOINED.
DR EMBL; M59723; AAA82938.1; JOINED.
DR EMBL; M59724; AAA82938.1; JOINED.
DR EMBL; M59725; AAA82938.1; JOINED.
DR EMBL; M59726; AAA82938.1; JOINED.
DR EMBL; M59727; AAA82938.1; JOINED.
DR EMBL; M59728; AAA82938.1; JOINED.
DR EMBL; M59729; AAA82938.1; JOINED.
DR EMBL; M59730; AAA82938.1; JOINED.
DR EMBL; M59731; AAA82938.1; JOINED.
DR EMBL; M59732; AAA82938.1; JOINED.
DR EMBL; M59733; AAA82938.1; JOINED.
DR EMBL; M59734; AAA82938.1; JOINED.
DR EMBL; M59735; AAA82938.1; JOINED.
DR EMBL; M59736; AAA82938.1; JOINED.
DR EMBL; M59737; AAA82938.1; JOINED.
DR EMBL; M59738; AAA82938.1; JOINED.
DR EMBL; M59739; AAA82938.1; JOINED.
DR EMBL; M59740; AAA82938.1; JOINED.
DR EMBL; M26066; AAA60068.1; -.
DR EMBL; Y00698; CAA68692.1; -.
DR EMBL; BC000534; AAH00534.1; -.
DR EMBL; BC012799; AAH12799.1; -.
DR EMBL; BC013298; AAH13298.1; -.
DR EMBL; BC021203; AAH21203.1; -.
DR EMBL; J05533; AAA79220.1; -.
DR EMBL; M24925; AAA36436.1; -.
DR PIR; A91605; KIHUFM.
DR HSSP; P00512; 3PFK.
DR HSC-2DPAGE; P08237; HUMAN.
DR Genew; HGNC:8877; PFKM.
DR GK; P08237; -.
DR MIM; 232800; -.
DR MIM; 171850; -.
DR GO; GO:0008443; F:phosphofructokinase activity; TAS.
DR GO; GO:0006110; P:regulation of glycolysis; TAS.
DR InterPro; IPR000023; Ppfruckinase.
DR Pfam; PF00365; PFK; 2.
DR PIRSF; PIRSF000533; PFK_euk; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR ProDom; PD000707; Ppfruckinase; 2.
DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
KW Kinase; Transferase; Glycolysis; Repeat; Allosteric enzyme;
KW Phosphorylation; Magnesium; Multigene family; Alternative splicing;
KW Disease mutation; Glycogen storage disease.
FT INIT_MET 0 0
FT MOD_RES 774 774 PHOSPHORYLATION (BY SIMILARITY).
FT VARSPLIC 281 311 Missing (in isoform 2).
FT /FTId=VSP_004667.
FT VARIANT 38 38 R -> L (in GSD-VII; Ashkenazi).
FT /FTId=VAR_006063.
FT VARIANT 38 38 R -> P (in GSD-VII; Italian).
FT /FTId=VAR_006064.
FT VARIANT 99 99 R -> Q (in GSD-VII; Swiss).
FT /FTId=VAR_006065.
FT VARIANT 208 208 G -> D (in GSD-VII; French Canadian).
FT /FTId=VAR_006066.
FT VARIANT 542 542 D -> A (in GSD-VII; Italian).
FT /FTId=VAR_006067.
FT VARIANT 685 685 W -> C (in GSD-VII; Japanese).
FT /FTId=VAR_006068.
FT VARIANT 695 695 R -> H (in GSD-VII; Swiss).
FT /FTId=VAR_006069.
SQ SEQUENCE 779 AA; 85051 MW; 4C9F384A7A5A5750 CRC64;
THEEHHAAKT LGIGKAIAVL TSGGDAQGMN AAVRAVVRVG IFTGARVFFV HEGYQGLVDG
GDHIKEATWE SVSMMLQLGG TVIGSARCKD FREREGRLRA AYNLVKRGIT NLCVIGGDGS
LTGADTFRSE WSDLLSDLQK AGKITDEEAT KSSYLNIVGL VGSIDNDFCG TDMTIGTDSA
LHRIMEIVDA ITTTAQSHQR TFVLEVMGRH CGYLALVTSL SCGADWVFIP ECPPDDDWEE
HLCRRLSETR TRGSRLNIII VAEGAIDKNG KPITSEDIKN LVVKRLGYDT RVTVLGHVQR
GGTPSAFDRI LGSRMGVEAV MALLEGTPDT PACVVSLSGN QAVRLPLMEC VQVTKDVTKA
MDEKKFDEAL KLRGRSFMNN WEVYKLLAHV RPPVSKSGSH TVAVMNVGAP AAGMNAAVRS
TVRIGLIQGN RVLVVHDGFE GLAKGQIEEA GWSYVGGWTG QGGSKLGTKR TLPKKSFEQI
SANITKFNIQ GLVIIGGFEA YTGGLELMEG RKQFDELCIP FVVIPATVSN NVPGSDFSVG
ADTALNTICT TCDRIKQSAA GTKRRVFIIE TMGGYCGYLA TMAGLAAGAD AAYIFEEPFT
IRDLQANVEH LVQKMKTTVK RGLVLRNEKC NENYTTDFIF NLYSEEGKGI FDSRKNVLGH
MQQGGSPTPF DRNFATKMGA KAMNWMSGKI KESYRNGRIF ANTPDSGCVL GMRKRALVFQ
PVAELKDQTD FEHRIPKEQW WLKLRPILKI LAKYEIDLDT SDHAHLEHIT RKRSGEAAV
//
ID K6PL_HUMAN STANDARD; PRT; 780 AA.
AC P17858; Q96IH4;
DT 01-AUG-1990 (Rel. 15, Created)
DT 16-OCT-2001 (Rel. 40, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE 6-phosphofructokinase, liver type (EC 2.7.1.11) (Phosphofructokinase
DE 1) (Phosphohexokinase) (Phosphofructo-1-kinase isozyme B) (PFK-B).
GN PFKL.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RC TISSUE=Liver;
RX MEDLINE=90126227; PubMed=2533063;
RA Levanon D., Danciger E., Dafni N., Bernstein Y., Elson A., Moens W.,
RA Brandeis M., Groner Y.;
RT "The primary structure of human liver type phosphofructokinase and
RT its comparison with other types of PFK.";
RL DNA 8:733-743(1989).
RN [2]
RP SEQUENCE FROM N.A.
RX MEDLINE=90243256; PubMed=2139864;
RA Elson A., Levanon D., Brandeis M., Dafni N., Bernstein Y.,
RA Danciger E., Groner Y.;
RT "The structure of the human liver-type phosphofructokinase gene.";
RL Genomics 7:47-56(1990).
RN [3]
RP SEQUENCE FROM N.A.
RX MEDLINE=20289799; PubMed=10830953;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T.,
RA Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y.,
RA Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K.,
RA Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D.,
RA Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W.,
RA Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S.,
RA Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E.,
RA Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P.,
RA Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H.,
RA Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E.,
RA Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F.,
RA Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [4]
RP SEQUENCE FROM N.A.
RC TISSUE=Kidney;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D-
CC fructose 1,6-bisphosphate.
CC -!- COFACTOR: Magnesium.
CC -!- ENZYME REGULATION: Allosteric enzyme activated by ADP, AMP, or
CC fructose bisphosphate and inhibited by ATP or citrate.
CC -!- PATHWAY: Key control step of glycolysis.
CC -!- SUBUNIT: Tetramer. Muscle is M4, liver is L4, and red cell is M3L,
CC M2L2, or ML3.
CC -!- MISCELLANEOUS: In human PFK exists as a system of 3 types of
CC subunits, PFKM (muscle), PFKL (liver) and PFKP (platelet)
CC isoenzymes.
CC -!- SIMILARITY: Belongs to the phosphofructokinase family. Two domains
CC subfamily.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; X15573; CAA33597.1; -.
DR EMBL; X16911; CAB46744.1; ALT_SEQ.
DR EMBL; X16912; CAB46744.1; JOINED.
DR EMBL; X16913; CAB46744.1; JOINED.
DR EMBL; X16914; CAB46744.1; JOINED.
DR EMBL; X16915; CAB46744.1; JOINED.
DR EMBL; X16916; CAB46744.1; JOINED.
DR EMBL; X16917; CAB46744.1; JOINED.
DR EMBL; X16918; CAB46744.1; JOINED.
DR EMBL; X16919; CAB46744.1; JOINED.
DR EMBL; X16920; CAB46744.1; JOINED.
DR EMBL; X16921; CAB46744.1; JOINED.
DR EMBL; X16922; CAB46744.1; JOINED.
DR EMBL; X16923; CAB46744.1; JOINED.
DR EMBL; X16924; CAB46744.1; JOINED.
DR EMBL; X16925; CAB46744.1; JOINED.
DR EMBL; X16926; CAB46744.1; JOINED.
DR EMBL; X16927; CAB46744.1; JOINED.
DR EMBL; X16928; CAB46744.1; JOINED.
DR EMBL; X16929; CAB46744.1; JOINED.
DR EMBL; X16930; CAB46744.1; JOINED.
DR EMBL; AP001754; BAA95561.1; -.
DR EMBL; BC007536; AAH07536.1; -.
DR HSSP; P00512; 3PFK.
DR Genew; HGNC:8876; PFKL.
DR GK; P17858; -.
DR MIM; 171860; -.
DR MIM; 171850; -.
DR GO; GO:0006000; P:fructose metabolism; TAS.
DR InterPro; IPR000023; Ppfruckinase.
DR Pfam; PF00365; PFK; 2.
DR PIRSF; PIRSF000533; PFK_euk; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR ProDom; PD000707; Ppfruckinase; 2.
DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
KW Kinase; Transferase; Glycolysis; Repeat; Allosteric enzyme;
KW Phosphorylation; Magnesium; Multigene family; Polymorphism.
FT VARIANT 81 81 G -> A.
FT /FTId=VAR_006070.
FT VARIANT 151 151 W -> R.
FT /FTId=VAR_006071.
FT CONFLICT 27 27 A -> R (in Ref. 1 and 2).
FT CONFLICT 89 89 C -> S (in Ref. 1 and 2).
FT CONFLICT 389 389 A -> T (in Ref. 1 and 2).
SQ SEQUENCE 780 AA; 85048 MW; DB8D6CE1E20CC854 CRC64;
MAAVDLEKLR ASGAGKAIGV LTSGGDAQGM NAAVRAVTRM GIYVGAKVFL IYEGYEGLVE
GGENIKQANW LSVSNIIQLG GTIIGSARCK AFTTREGRRA AAYNLVQHGI TNLCVIGGDG
SLTGANIFRS EWGSLLEELV AEGKISETTA WTYSHLNIAG LVGSIDNDFC GTDMTIGTDS
ALHRIMEVID AITTTAQSHQ RTFVLEVMGR HCGYLALVSA LASGADWLFI PEAPPEDGWE
NFMCERLGET RSRGSRLNII IIAEGAIDRN GKPISSSYVK DLVVQRLGFD TRVTVLGHVQ
RGGTPSAFDR ILSSKMGMEA VMALLEATPD TPACVVTLSG NQSVRLPLME CVQMTKEVQK
AMDDKRFDEA TQLRGGSFEN NWNIYKLLAH QKPPKEKSNF SLAILNVGAP AAGMNAAVRS
AVRTGISHGH TVYVVHDGFE GLAKGQVQEV GWHDVAGWLG RGGSMLGTKR TLPKGQLESI
VENIRIYGIH ALLVVGGFEA YEGVLQLVEA RGRYEELCIV MCVIPATISN NVPGTDFSLG
SDTAVNAAME SCDRIKQSAS GTKRRVFIVE TMGGYCGYLA TVTGIAVGAD AAYVFEDPFN
IHDLKVNVEH MTEKMKTDIQ RGLVLRNEKC HDYYTTEFLY NLYSSEGKGV FDCRTNVLGH
LQQGGAPTPF DRNYGTKLGV KAMLWLSEKL REVYRKGRVF ANAPDSACVI GLKKKAVAFS
PVTELKKDTD FEHRMPREQW WLSLRLMLKM LAQYRISMAA YVSGELEHVT RRTLSMDKGF
//
ID K6PP_HUMAN STANDARD; PRT; 784 AA.
AC Q01813;
DT 01-JUL-1993 (Rel. 26, Created)
DT 01-FEB-1996 (Rel. 33, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE 6-phosphofructokinase, type C (EC 2.7.1.11) (Phosphofructokinase
DE 1) (Phosphohexokinase) (Phosphofructo-1-kinase isozyme C) (PFK-C)
DE (6-phosphofructokinase, platelet type).
GN PFKP OR PFKF.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RC TISSUE=Pancreatic islets;
RX MEDLINE=94161770; PubMed=8117307;
RA Eto K., Sakura H., Yasuda K., Hayakawa T., Kawasaki E.,
RA Moriuchi R., Nagataki S., Yazaki Y., Kadowaki T.;
RT "Cloning of a complete protein-coding sequence of human platelet-type
RT phosphofructokinase isozyme from pancreatic islet.";
RL Biochem. Biophys. Res. Commun. 198:990-998(1994).
RN [2]
RP SEQUENCE FROM N.A.
RC TISSUE=Brain, and Placenta;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [3]
RP SEQUENCE OF 484-784 FROM N.A.
RX MEDLINE=92028938; PubMed=1834056;
RA Simpson C.J., Fothergill-Gilmore L.A.;
RT "Isolation and sequence of a cDNA encoding human platelet
RT phosphofructokinase.";
RL Biochem. Biophys. Res. Commun. 180:197-203(1991).
CC -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D-
CC fructose 1,6-bisphosphate.
CC -!- COFACTOR: Magnesium.
CC -!- ENZYME REGULATION: Allosteric enzyme activated by ADP, AMP, or
CC fructose bisphosphate and inhibited by ATP or citrate.
CC -!- PATHWAY: Key control step of glycolysis.
CC -!- SUBUNIT: Tetramer. Muscle is M4, liver is L4, and red cell is M3L,
CC M2L2, or ML3. A subunit composition with a higher proportion of
CC platelet type subunits is found in platelets, brain and
CC fibroblasts.
CC -!- MISCELLANEOUS: In human PFK exists as a system of 3 types of
CC subunits, PFKM (muscle), PFKL (liver) and PFKP (platelet)
CC isoenzymes.
CC -!- SIMILARITY: Belongs to the phosphofructokinase family. Two domains
CC subfamily.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; D25328; BAA04998.1; -.
DR EMBL; BC002536; AAH02536.1; -.
DR EMBL; BC029138; AAH29138.1; -.
DR EMBL; M64784; AAA36435.1; -.
DR PIR; JC2055; JC2055.
DR HSSP; P00512; 3PFK.
DR Genew; HGNC:8878; PFKP.
DR GK; Q01813; -.
DR MIM; 171840; -.
DR GO; GO:0005945; C:6-phosphofructokinase complex; NAS.
DR GO; GO:0003872; F:6-phosphofructokinase activity; TAS.
DR GO; GO:0006096; P:glycolysis; NAS.
DR InterPro; IPR000023; Ppfruckinase.
DR Pfam; PF00365; PFK; 2.
DR PIRSF; PIRSF000533; PFK_euk; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR ProDom; PD000707; Ppfruckinase; 2.
DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
KW Kinase; Transferase; Glycolysis; Repeat; Allosteric enzyme;
KW Phosphorylation; Magnesium; Multigene family.
FT CONFLICT 484 485 PG -> IP (in Ref. 3).
FT CONFLICT 498 498 Missing (in Ref. 3).
FT CONFLICT 699 699 A -> E (in Ref. 3).
SQ SEQUENCE 784 AA; 85596 MW; 22522E77E9AF80F6 CRC64;
MDADDSRAPK GSLRKFLEHL SGAGKAIGVL TSGGDAQGMN AAVRAVVRMG IYVGAKVYFI
YEGYQGMVDG GSNIAEADWE SVSSILQVGG TIIGSARCQA FRTREGRLKA ACNLLQRGIT
NLCVIGGDGS LTGANLFRKE WSGLLEELAR NGQIDKEAVQ KYAYLNVVGM VGSIDNDFCG
TDMTIGTDSA LHRIIEVVDA IMTTAQSHQR TFVLEVMGRH CGYLALVSAL ACGADWVFLP
ESPPEEGWEE QMCVKLSENR ARKKRLNIII VAEGAIDTQN KPITSEKIKE LVVTQLGYDT
RVTILGHVQR GGTPSAFDRI LASRMGVEAV IALLEATPDT PACVVSLNGN HAVRLPLMEC
VQMTQDVQKA MDERRFQDAV RLRGRSFAGN LNTYKRLAIK LPDDQIPKTN CNVAVINVGA
PAAGMNAAVR SAVRVGIADG HRMLAIYDGF DGFAKGQIKE IGWTDVGGWT GQGGSILGTK
RVLPGKYLEE IATQMRTHSI NALLIIGGFE AYLGLLELSA AREKHEEFCV PMVMVPATVS
NNVPGSDFSI GADTALNTIT DTCDRIKQSA SGTKRRVFII ETMGGYCGYL ANMGGLAAGA
DAAYIFEEPF DIRDLQSNVE HLTEKMKTTI QRGLVLRNES CSENYTTDFI YQLYSEEGKG
VFDCRKNVLG HMQQGGAPSP FDRNFGTKIS ARAMEWITAK LKEARGRGKK FTTDDSICVL
GISKRNVIFQ PVAELKKQTD FEHRIPKEQW WLKLRPLMKI LAKYKASYDV SDSGQLEHVQ
PWSV
//
ID KAD1_HUMAN STANDARD; PRT; 194 AA.
AC P00568; Q9BVK9; Q9UQC7;
DT 21-JUL-1986 (Rel. 01, Created)
DT 28-FEB-2003 (Rel. 41, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE Adenylate kinase isoenzyme 1 (EC 2.7.4.3) (ATP-AMP transphosphorylase)
DE (AK1) (Myokinase).
GN AK1.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE.
RC TISSUE=Skeletal muscle;
RX MEDLINE=77003085; PubMed=183954;
RA von Zabern I., Wittmann-Liebold B., Untucht-Grau R., Schirmer R.H.,
RA Pai E.F.;
RT "Primary and tertiary structure of the principal human adenylate
RT kinase.";
RL Eur. J. Biochem. 68:281-290(1976).
RN [2]
RP SEQUENCE FROM N.A., AND VARIANT TRP-128.
RX MEDLINE=89255503; PubMed=2542324;
RA Matsuura S., Igarashi M., Tanizawa Y., Yamada M., Kishi F.,
RA Kajii T., Fujii H., Miwa S., Sakurai M., Nakazawa A.;
RT "Human adenylate kinase deficiency associated with hemolytic anemia.
RT A single base substitution affecting solubility and catalytic
RT activity of the cytosolic adenylate kinase.";
RL J. Biol. Chem. 264:10148-10155(1989).
RN [3]
RP SEQUENCE FROM N.A.
RC TISSUE=Retina;
RA Noma T.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SEQUENCE FROM N.A.
RC TISSUE=Colon;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC -!- FUNCTION: This small ubiquitous enzyme is essential for
CC maintenance and cell growth.
CC -!- CATALYTIC ACTIVITY: ATP + AMP = ADP + ADP.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic.
CC -!- POLYMORPHISM: This enzyme represents the most common of at least
CC five alleles.
CC -!- DISEASE: Deficiency in AK1 is the cause of a form of hemolytic
CC anemia.
CC -!- SIMILARITY: Belongs to the adenylate kinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; J04809; AAA51686.1; -.
DR EMBL; AB021871; BAA78534.1; -.
DR EMBL; BC001116; AAH01116.1; -.
DR PIR; A33508; KIHUA.
DR HSSP; P00571; 3ADK.
DR Genew; HGNC:361; AK1.
DR GK; P00568; -.
DR MIM; 103000; -.
DR GO; GO:0004017; F:adenylate kinase activity; TAS.
DR InterPro; IPR000850; Adenylate_kin.
DR InterPro; IPR006267; Adenylate_kin1.
DR Pfam; PF00406; ADK; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR ProDom; PD000657; Adenylate_kin; 1.
DR TIGRFAMs; TIGR01360; aden_kin_iso1; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; 1.
KW Transferase; Kinase; ATP-binding; Acetylation; Disease mutation.
FT MOD_RES 1 1 ACETYLATION.
FT NP_BIND 15 23 ATP (By similarity).
FT ACT_SITE 36 36
FT ACT_SITE 93 93
FT VARIANT 128 128 R -> W (in hemolytic anemia).
FT /FTId=VAR_004021.
FT CONFLICT 9 9 K -> N (in Ref. 4).
FT CONFLICT 127 127 Q -> R (in Ref. 1).
FT CONFLICT 181 181 S -> E (in Ref. 1).
SQ SEQUENCE 194 AA; 21635 MW; 95EC5AAA92D1F00F CRC64;
MEEKLKKTKI IFVVGGPGSG KGTQCEKIVQ KYGYTHLSTG DLLRSEVSSG SARGKKLSEI
MEKGQLVPLE TVLDMLRDAM VAKVNTSKGF LIDGYPREVQ QGEEFERRIG QPTLLLYVDA
GPETMTQRLL KRGETSGRVD DNEETIKKRL ETYYKATEPV IAFYEKRGIV RKVNAEGSVD
SVFSQVCTHL DALK
//
ID KAD2_HUMAN STANDARD; PRT; 238 AA.
AC P54819; Q16856; Q8TCY2; Q8TCY3;
DT 01-OCT-1996 (Rel. 34, Created)
DT 01-OCT-1996 (Rel. 34, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE Adenylate kinase isoenzyme 2, mitochondrial (EC 2.7.4.3) (ATP-AMP
DE transphosphorylase).
GN AK2 OR ADK2.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A. (ISOFORM 1).
RC TISSUE=Liver;
RX MEDLINE=97000211; PubMed=8843353;
RA Lee Y., Kim J.W., Lee I.A., Kang H.B., Choe Y.K., Lee H.G.,
RA Lim J.S., Kim H.J., Park C., Choe I.S.;
RT "Cloning and characterization of cDNA for human adenylate kinase 2A.";
RL Biochem. Mol. Biol. Int. 39:833-842(1996).
RN [2]
RP SEQUENCE FROM N.A. (ISOFORM 2).
RC TISSUE=Fetal liver;
RX MEDLINE=98162934; PubMed=9504408;
RA Lee Y., Kim J.W., Lee S.M., Kim H.J., Lee K.S., Park C., Choe I.S.;
RT "Cloning and expression of human adenylate kinase 2 isozymes:
RT differential expression of adenylate kinase 1 and 2 in human muscle
RT tissues.";
RL J. Biochem. 123:47-54(1998).
RN [3]
RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 2).
RX MEDLINE=98094237; PubMed=9434148;
RA Noma T., Song S., Yoon Y.-S., Tanaka S., Nakazawa A.;
RT "cDNA cloning and tissue-specific expression of the gene encoding
RT human adenylate kinase isozyme 2.";
RL Biochim. Biophys. Acta 1395:34-39(1998).
RN [4]
RP SEQUENCE FROM N.A. (ISOFORMS 3 AND 4).
RA Guo J.;
RT "Novel isoforms of human adenylate kinase 2.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SEQUENCE FROM N.A. (ISOFORM 1).
RC TISSUE=Uterus;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC -!- FUNCTION: This small ubiquitous enzyme is essential for
CC maintenance and cell growth.
CC -!- CATALYTIC ACTIVITY: ATP + AMP = ADP + ADP.
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SUBCELLULAR LOCATION: Mitochondrial intermembrane space.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=AK2A;
CC IsoId=P54819-1; Sequence=Displayed;
CC Name=2; Synonyms=AK2B;
CC IsoId=P54819-2; Sequence=VSP_002790;
CC Name=3; Synonyms=AK2C;
CC IsoId=P54819-3; Sequence=VSP_002791;
CC Name=4; Synonyms=AK2D;
CC IsoId=P54819-4; Sequence=VSP_002792, VSP_002793, VSP_002794;
CC -!- TISSUE SPECIFICITY: ABUNDANT IN HEART.
CC -!- SIMILARITY: Belongs to the adenylate kinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; U39945; AAC52061.1; -.
DR EMBL; U84371; AAB41790.1; -.
DR EMBL; U54645; AAC13881.1; -.
DR EMBL; AB005621; BAC16747.1; -.
DR EMBL; AB005622; BAC16748.1; -.
DR EMBL; AY080899; AAL87027.1; -.
DR EMBL; AY080900; AAL87028.1; -.
DR EMBL; BC009405; AAH09405.1; -.
DR PIR; G02248; G02248.
DR PIR; JC5893; JC5893.
DR HSSP; P08166; 1AK2.
DR Genew; HGNC:362; AK2.
DR MIM; 103020; -.
DR GO; GO:0004017; F:adenylate kinase activity; TAS.
DR InterPro; IPR006259; Adenyl_kin_sub.
DR InterPro; IPR000850; Adenylate_kin.
DR InterPro; IPR007862; ADK_lid.
DR Pfam; PF00406; ADK; 1.
DR Pfam; PF05191; ADK_lid; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR ProDom; PD000657; Adenylate_kin; 1.
DR TIGRFAMs; TIGR01351; adk; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; 1.
KW Transferase; Kinase; ATP-binding; Mitochondrion; Alternative splicing.
FT INIT_MET 0 0 By similarity.
FT NP_BIND 21 29 ATP (By similarity).
FT VARSPLIC 231 238 CKDLVMFI -> S (in isoform 2).
FT /FTId=VSP_002790.
FT VARSPLIC 177 238 DNEKALKIRLQAYHTQTTPLIEYYRKRGIHSAIDASQTPDV
FT VFASILAAFSKATCKDLVMFI -> IGQAKRSFLRLAKISF
FT DVLIKKALA (in isoform 3).
FT /FTId=VSP_002791.
FT VARSPLIC 1 47 Missing (in isoform 4).
FT /FTId=VSP_002792.
FT VARSPLIC 176 177 DD -> GL (in isoform 4).
FT /FTId=VSP_002793.
FT VARSPLIC 178 238 Missing (in isoform 4).
FT /FTId=VSP_002794.
SQ SEQUENCE 238 AA; 26346 MW; 34B3844F355EC3D1 CRC64;
APSVPAAEPE YPKGIRAVLL GPPGAGKGTQ APRLAENFCV CHLATGDMLR AMVASGSELG
KKLKATMDAG KLVSDEMVVE LIEKNLETPL CKNGFLLDGF PRTVRQAEML DDLMEKRKEK
LDSVIEFSIP DSLLIRRITG RLIHPKSGRS YHEEFNPPKE PMKDDITGEP LIRRSDDNEK
ALKIRLQAYH TQTTPLIEYY RKRGIHSAID ASQTPDVVFA SILAAFSKAT CKDLVMFI
//
ID KAD3_HUMAN STANDARD; PRT; 226 AA.
AC Q9UIJ7; Q9H576; Q9NPB4;
DT 16-OCT-2001 (Rel. 40, Created)
DT 28-FEB-2003 (Rel. 41, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE GTP:AMP phosphotransferase mitochondrial (EC 2.7.4.10) (AK3)
DE (Adenylate kinase 3 alpha like 1).
GN AK3L1 OR AKL3L.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RC TISSUE=Liver;
RA Noma T.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SEQUENCE FROM N.A.
RC TISSUE=Placenta;
RA Isogai T., Ota T., Hayashi K., Sugiyama T., Otsuki T., Suzuki Y.,
RA Nishikawa T., Nagai K., Sugano S., Shiratori A., Sudo H.,
RA Wagatsuma M., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Chiba Y., Ishida S., Murakawa K., Ono Y., Takiguchi S.,
RA Watanabe S., Kimura K., Murakami K., Ishii S., Kawai Y., Saito K.,
RA Yamamoto J., Wakamatsu A., Nakamura Y., Nagahari K., Masuho Y.,
RA Ninomiya K., Iwayanagi T., Aotsuka S., Yoshikawa Y., Matsunawa H.,
RA Sasaki N., Ishibashi T., Fujimori K., Tanai H., Kimata M.,
RA Watanabe M., Hiraoka S., Kanehori K.;
RT "NEDO human cDNA sequencing project.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SEQUENCE FROM N.A.
RC TISSUE=Lymph;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [4]
RP SEQUENCE OF 91-226 FROM N.A.
RA Lloyd D.;
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY: GTP + AMP = GDP + ADP.
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SUBCELLULAR LOCATION: Mitochondrial matrix (By similarity).
CC -!- SIMILARITY: Belongs to the adenylate kinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AB021870; BAA87913.1; -.
DR EMBL; AK001553; BAA91753.1; -.
DR EMBL; AK001951; BAA91996.1; -.
DR EMBL; AK027534; BAB55183.1; -.
DR EMBL; BC013771; AAH13771.1; -.
DR EMBL; AL136231; CAC12706.1; -.
DR HSSP; P08760; 2AK3.
DR Genew; HGNC:17376; AK3L1.
DR InterPro; IPR000850; Adenylate_kin.
DR InterPro; IPR006259; Adenyl_kin_sub.
DR InterPro; IPR007862; ADK_lid.
DR Pfam; PF00406; ADK; 1.
DR Pfam; PF05191; ADK_lid; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR ProDom; PD000657; Adenylate_kin; 1.
DR TIGRFAMs; TIGR01351; adk; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; 1.
KW Transferase; Kinase; GTP-binding; Mitochondrion.
FT INIT_MET 0 0 By similarity.
FT NP_BIND 13 21 GTP (By similarity).
FT CONFLICT 4 4 A -> G (in Ref. 1).
FT CONFLICT 37 37 S -> R (in Ref. 1).
FT CONFLICT 56 56 K -> Q (in Ref. 1).
FT CONFLICT 68 70 DVM -> YVT (in Ref. 1).
SQ SEQUENCE 226 AA; 25434 MW; 9FFD81FEC2C0ACBC CRC64;
GASARLLRAV IMGAPGSGKG TVSSRITTHF ELKHLSSGDL LRDNMLRGTE IGVLAKAFID
QGKLIPDDVM TRLALHELKN LTQYSWLLDG FPRTLPQAEA LDRAYQIDTV INLNVPFEVI
KQRLTARWIH PASGRVYNIE FNPPKTVGID DLTGEPLIQR EDDKPETVIK RLKAYEDQTK
PVLEYYQKKG VLETFSGTET NKIWPYVYAF LQTKVPQRSQ KASVTP
//
ID KAD4_HUMAN STANDARD; PRT; 223 AA.
AC P27144;
DT 01-AUG-1992 (Rel. 23, Created)
DT 01-AUG-1992 (Rel. 23, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE Adenylate kinase isoenzyme 4, mitochondrial (EC 2.7.4.3) (ATP-AMP
DE transphosphorylase).
GN AK3 OR AK4.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RX MEDLINE=92347846; PubMed=1639383;
RA Xu G., O'Connell P., Stevens J., White R.;
RT "Characterization of human adenylate kinase 3 (AK3) cDNA and mapping
RT of the AK3 pseudogene to an intron of the NF1 gene.";
RL Genomics 13:537-542(1992).
RN [2]
RP SEQUENCE FROM N.A.
RC TISSUE=Lung;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC -!- CATALYTIC ACTIVITY: GTP + AMP = GDP + ADP.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Mitochondrial matrix.
CC -!- SIMILARITY: Belongs to the adenylate kinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; X60673; CAA43088.1; -.
DR EMBL; BC016180; AAH16180.1; -.
DR PIR; A42820; KIHUA3.
DR HSSP; P08760; 2AK3.
DR Genew; HGNC:363; AK3.
DR MIM; 103030; -.
DR InterPro; IPR006259; Adenyl_kin_sub.
DR InterPro; IPR000850; Adenylate_kin.
DR InterPro; IPR007862; ADK_lid.
DR Pfam; PF00406; ADK; 1.
DR Pfam; PF05191; ADK_lid; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR ProDom; PD000657; Adenylate_kin; 1.
DR TIGRFAMs; TIGR01351; adk; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; 1.
KW Transferase; Kinase; GTP-binding; Mitochondrion.
FT NP_BIND 12 20 GTP (By similarity).
SQ SEQUENCE 223 AA; 25268 MW; 653341A8EB3BC723 CRC64;
MASKLLRAVI LGPPGSGKGT VCQRIAQNFG LQHLSSGHFL RENIKASTEV GEMAKQYIEK
SLLVPDHVIT RLMMSELENR RGQHWLLDGF PRTLGQAEAL DKICEVDLVI SLNIPFETLK
DRLSRRWIHP PSGRVYNLDF NPPHVHGIDD VTGEPLVQQE DDKPEAVAAR LRQYKDVAKP
VIELYKSRGV LHQFSGTETN KIWPYVYTLF SNKITPIQSK EAY
//
ID KAD5_HUMAN STANDARD; PRT; 198 AA.
AC Q9Y6K8; Q96EC9;
DT 16-OCT-2001 (Rel. 40, Created)
DT 16-OCT-2001 (Rel. 40, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE Adenylate kinase isoenzyme 5 (EC 2.7.4.3) (ATP-AMP
DE transphosphorylase).
GN AK5.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RX MEDLINE=99234026; PubMed=10215863;
RA Van Rompay A.R., Johansson M., Karlsson A.;
RT "Identification of a novel human adenylate kinase. cDNA cloning,
RT expression analysis, chromosome localization and characterization of
RT the recombinant protein.";
RL Eur. J. Biochem. 261:509-517(1999).
RN [2]
RP SEQUENCE FROM N.A.
RC TISSUE=Liver;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC -!- FUNCTION: Active on AMP and dAMP with ATP as a donor. When GTP is
CC used as phosphate donor, the enzyme phosphorylates AMP, CMP, and
CC to a small extent dCMP.
CC -!- CATALYTIC ACTIVITY: ATP + AMP = ADP + ADP.
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasmic.
CC -!- TISSUE SPECIFICITY: Brain specific.
CC -!- SIMILARITY: Belongs to the adenylate kinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AF062595; AAD27956.1; -.
DR EMBL; BC012467; AAH12467.1; -.
DR HSSP; P00571; 3ADK.
DR Genew; HGNC:365; AK5.
DR MIM; 608009; -.
DR GO; GO:0005829; C:cytosol; TAS.
DR GO; GO:0004017; F:adenylate kinase activity; TAS.
DR GO; GO:0006172; P:ADP biosynthesis; TAS.
DR GO; GO:0006173; P:dADP biosynthesis; TAS.
DR GO; GO:0009220; P:pyrimidine ribonucleotide biosynthesis; TAS.
DR InterPro; IPR000850; Adenylate_kin.
DR InterPro; IPR006267; Adenylate_kin1.
DR Pfam; PF00406; ADK; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR ProDom; PD000657; Adenylate_kin; 1.
DR TIGRFAMs; TIGR01360; aden_kin_iso1; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; 1.
KW Transferase; Kinase; ATP-binding.
FT NP_BIND 18 26 ATP (By similarity).
FT NP_BIND 41 70 AMP (By similarity).
FT ACT_SITE 39 39 By similarity.
FT ACT_SITE 96 96 By similarity.
FT CONFLICT 197 197 Missing (in Ref. 2).
SQ SEQUENCE 198 AA; 22087 MW; 8E8FA514CB7C3B58 CRC64;
MGGFMEDLRK CKIIFIIGGP GSGKGTQCEK LVEKYGFTHL STGELLREEL ASESERSKLI
RDIMERGDLV PSGIVLELLK EAMVASLGDT RGFLIDGYPR EVKQGEEFGR RIGDPQLVIC
MDCSADTMTN RLLQRSRSSL PVDDTTKTIA KRLEAYYRAS IPVIAYYETK TQLHKINAEG
TPEDVFLQLC TAIDSIIF
//
ID KAD7_HUMAN STANDARD; PRT; 723 AA.
AC Q96M32; Q8IYP6;
DT 10-OCT-2003 (Rel. 42, Created)
DT 10-OCT-2003 (Rel. 42, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE Putative adenylate kinase 7 (EC 2.7.4.3).
GN AK7.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A., AND VARIANT GLN-102.
RC TISSUE=Testis;
RA Suzuki O., Sasaki N., Aotsuka S., Shoji T., Ichihara T., Shiohata N.,
RA Matsumoto K., Hirano M., Sano S., Nomura R., Yoshikawa Y.,
RA Matsumura Y., Moriya S., Chiba E., Momiyama H., Onogawa S.,
RA Kaeriyama S., Satoh N., Matsunawa H., Takahashi E., Kataoka R.,
RA Kuga N., Kuroda A., Satoh I., Kamata K., Takami S., Terashima Y.,
RA Watanabe M., Sugiyama T., Irie R., Otsuki T., Sato H., Wakamatsu A.,
RA Ishii S., Yamamoto J., Isono Y., Kawai-Hio Y., Saito K., Nishikawa T.,
RA Kimura K., Yamashita H., Matsuo K., Nakamura Y., Sekine M.,
RA Kikuchi H., Kanda K., Wagatsuma M., Murakawa K., Kanehori K.,
RA Takahashi-Fujii A., Oshima A., Sugiyama A., Kawakami B., Suzuki Y.,
RA Sugano S., Nagahari K., Masuho Y., Nagai K., Isogai T.;
RT "NEDO human cDNA sequencing project.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SEQUENCE FROM N.A.
RX PubMed=12508121;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA Quetier F., Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [3]
RP SEQUENCE FROM N.A.
RC TISSUE=Testis;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length human
RT and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC -!- CATALYTIC ACTIVITY: ATP + AMP = ADP + ADP.
CC -!- SIMILARITY: In the central section; belongs to the adenylate
CC kinase family.
CC -!- SIMILARITY: In the C-terminal section; belongs to the dpy-30
CC family.
CC -!- CAUTION: Ref.3 sequence differs from that shown due to a stop
CC codon in position 657.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AK057426; BAB71480.1; -.
DR EMBL; AL163051; -; NOT_ANNOTATED_CDS.
DR EMBL; AL359240; -; NOT_ANNOTATED_CDS.
DR EMBL; BC035256; AAH35256.1; ALT_TERM.
DR Genew; HGNC:20091; AK7.
DR InterPro; IPR007858; Dpy-30.
DR Pfam; PF05186; Dpy-30; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; FALSE_NEG.
KW Transferase; Kinase; ATP-binding; Coiled coil; Polymorphism.
FT DOMAIN 46 458 COILED COIL (POTENTIAL).
FT DOMAIN 366 502 ADENYLATE KINASE.
FT DOMAIN 609 677 COILED COIL (POTENTIAL).
FT DOMAIN 679 723 DPY-30.
FT NP_BIND 374 381 ATP (Potential).
FT DOMAIN 616 674 GLU-RICH.
FT DOMAIN 3 6 POLY-GLU.
FT DOMAIN 51 58 POLY-GLU.
FT DOMAIN 420 432 POLY-GLU.
FT DOMAIN 497 502 POLY-GLU.
FT VARIANT 102 102 R -> Q (in dbSNP:2369679).
FT /FTId=VAR_017059.
FT CONFLICT 272 272 P -> L (in Ref. 1).
FT CONFLICT 410 410 E -> G (in Ref. 1).
FT CONFLICT 605 605 I -> T (in Ref. 3).
FT CONFLICT 657 657 Missing (in Ref. 3).
SQ SEQUENCE 723 AA; 82672 MW; 8E5FE865A9DA0AFB CRC64;
MAEEEETAAL TEKVIRTQRV FINLLDSYSS GNIGKFLSNC VVGASLEEIT EEEEEEDENK
SAMLEASSTK VKEGTFQIVG TLSKPDSPRP DFAVETYSAI SREDLLMRLL ECDVIIYNIT
ESSQQMEEAI WAVSALSEEV SHFEKRKLFI LLSTVMTWAR SKALDPEDSE VPFTEEDYRR
RKSHPNFLDH INAEKMVLKF GKKARKFAAY VVAAGLQYGA EGGMLHTFFK MAWLGEIPAL
PVFGDGTNVI PTIHVLDLAG VIQNVIDHVP KPHYLVAVDE SVHTLEDIVK CISKNTGPGK
IQKIPRENAY LTKDLTQDCL DHLLVNLRME ALFVKENFNI RWAAQTGFVE NINTILKEYK
QSRGLMPIKI CILGPPAVGK SSIAKELAKY YKLHHIQLKD VISEAIAKLE AIVAPNDVGE
GEEEVEEEEE EENVEDAQEL LDGIKESMEQ NAGQLDDQYI IRFMKEKLKS MPCRNQGYIL
DGFPKTYDQA KDLFNQEDEE EEDDVRGRMF PFDKLIIPEF VCALDASDEF LKERVINLPE
SIVAGTHYSQ DRFLRALSNY RDINIDDETV FNYFDELEIH PIHIDVGKLE DAQNRLAIKQ
LIKEIGEPRN YGLTDEEKAE EERKAAEERL AREAAEEAER EHQEAVEMAE KIARWEEWNK
RLEEVKREER ELLEAQSIPL RNYLMTYVMP TLIQGLNECC NVRPEDPVDF LAEYLFKNNP
EAQ
//
ID KCRB_HUMAN STANDARD; PRT; 381 AA.
AC P12277;
DT 01-OCT-1989 (Rel. 12, Created)
DT 01-OCT-1989 (Rel. 12, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE Creatine kinase, B chain (EC 2.7.3.2) (B-CK).
GN CKB OR CKBB.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RX MEDLINE=88085186; PubMed=3692484;
RA Mariman E.C.M., Broers C.A.M., Claesen C.A.A., Tesser G.I.,
RA Wieringa B.;
RT "Structure and expression of the human creatine kinase B gene.";
RL Genomics 1:126-137(1987).
RN [2]
RP SEQUENCE FROM N.A.
RX MEDLINE=87195439; PubMed=2883200;
RA Kaye F.J., McBride O.W., Battey J.F., Gazder A.F., Sausville E.A.;
RT "Human creatine kinase-B complementary DNA. Nucleotide sequence, gene
RT expression in lung cancer, and chromosomal assignment to two distinct
RT loci.";
RL J. Clin. Invest. 79:1412-1420(1987).
RN [3]
RP SEQUENCE FROM N.A.
RX MEDLINE=87213302; PubMed=3034271;
RA Villarreal-Levy G., Ma T.S., Kerner S.A., Roberts R., Perryman M.B.;
RT "Human creatine kinase: isolation and sequence analysis of cDNA
RT clones for the B subunit, development of subunit specific probes and
RT determination of gene copy number.";
RL Biochem. Biophys. Res. Commun. 144:1116-1127(1987).
RN [4]
RP SEQUENCE FROM N.A.
RC TISSUE=Brain;
RX MEDLINE=89366665; PubMed=2771648;
RA Mariman E.C.M., Schepens J.T.G., Wieringa B.;
RT "Complete nucleotide sequence of the human creatine kinase B gene.";
RL Nucleic Acids Res. 17:6385-6385(1989).
RN [5]
RP SEQUENCE FROM N.A.
RC TISSUE=Brain, Eye, and Lung;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [6]
RP SEQUENCE OF 1-97 FROM N.A.
RX MEDLINE=88115393; PubMed=2828370;
RA Daouk G.H., Kaddurah-Daouk R., Putney S., Kingston R., Schimmel P.;
RT "Isolation of a functional human gene for brain creatine kinase.";
RL J. Biol. Chem. 263:2442-2446(1988).
RN [7]
RP MUTAGENESIS OF CYS-283; ASP-340 AND ARG-292.
RX MEDLINE=94242786; PubMed=8186255;
RA Lin L., Perryman M.B., Friedman D., Roberts R., Ma T.S.;
RT "Determination of the catalytic site of creatine kinase by site-
RT directed mutagenesis.";
RL Biochim. Biophys. Acta 1206:97-104(1994).
CC -!- FUNCTION: Reversibly catalyzes the transfer of phosphate between
CC ATP and various phosphogens (e.g. creatine phosphate). Creatine
CC kinase isoenzymes play a central role in energy transduction in
CC tissues with large, fluctuating energy demands, such as skeletal
CC muscle, heart, brain and spermatozoa.
CC -!- CATALYTIC ACTIVITY: ATP + creatine = ADP + phosphocreatine.
CC -!- SUBUNIT: Dimer of identical or nonidentical chains. With MM being
CC the major form in skeletal muscle and myocardium, MB existing in
CC myocardium, and BB existing in many tissues, especially brain.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic.
CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; L47647; AAA76852.1; -.
DR EMBL; X15334; CAA33389.1; -.
DR EMBL; M21243; AAC31758.1; ALT_SEQ.
DR EMBL; M21237; AAC31758.1; JOINED.
DR EMBL; M21238; AAC31758.1; JOINED.
DR EMBL; M21239; AAC31758.1; JOINED.
DR EMBL; M21240; AAC31758.1; JOINED.
DR EMBL; M21241; AAC31758.1; JOINED.
DR EMBL; M21242; AAC31758.1; JOINED.
DR EMBL; M16364; AAA76850.1; -.
DR EMBL; M16451; AAA76851.1; -.
DR EMBL; BC001190; AAH01190.1; -.
DR EMBL; BC004914; AAH04914.1; -.
DR EMBL; BC008323; AAH08323.1; -.
DR EMBL; BC010002; AAH10002.1; -.
DR EMBL; BC019259; AAH19259.1; -.
DR EMBL; BC019281; AAH19281.1; -.
DR EMBL; M22356; AAA52024.1; -.
DR EMBL; M22355; AAA52024.1; JOINED.
DR PIR; S15935; KIHUCB.
DR HSSP; P05122; 1QH4.
DR PHCI-2DPAGE; P12277; -.
DR HSC-2DPAGE; P12277; HUMAN.
DR Genew; HGNC:1991; CKB.
DR MIM; 123280; -.
DR GO; GO:0004111; F:creatine kinase activity; TAS.
DR InterPro; IPR000749; ATP-gua_Ptrans.
DR Pfam; PF00217; ATP-gua_Ptrans; 1.
DR Pfam; PF02807; ATP-gua_PtransN; 1.
DR PROSITE; PS00112; GUANIDO_KINASE; 1.
KW Transferase; Kinase; Multigene family.
FT ACT_SITE 283 283
FT MUTAGEN 283 283 C->S,Y: COMPLETE LOSS OF ACTIVITY.
FT MUTAGEN 292 292 R->H,L,Q: COMPLETE LOSS OF ACTIVITY.
FT MUTAGEN 292 292 R->K: 42% OF WILD-TYPE ACTIVITY.
FT MUTAGEN 340 340 D->E: NO CHANGE IN ACTIVITY.
FT CONFLICT 41 42 EL -> DV (in Ref. 3).
FT CONFLICT 78 78 D -> G (in Ref. 2 and 6).
FT CONFLICT 98 99 GG -> RR (in Ref. 3).
FT CONFLICT 105 106 EH -> DD (in Ref. 3).
FT CONFLICT 130 130 R -> G (in Ref. 2).
FT CONFLICT 132 132 R -> A (in Ref. 3).
FT CONFLICT 215 216 RG -> AR (in Ref. 3).
FT CONFLICT 296 296 H -> D (in Ref. 3).
SQ SEQUENCE 381 AA; 42644 MW; 637AA67A86AE3059 CRC64;
MPFSNSHNAL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG FTLDDVIQTG
VDNPGHPYIM TVGCVAGDEE SYEVFKDLFD PIIEDRHGGY KPSDEHKTDL NPDNLQGGDD
LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE ALSSLDGDLA GRYYALKSMT
EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM
QKGGNMKEVF TRFCTGLTQI ETLFKSKDYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP
NLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL
IEMEQRLEQG QAIDDLMPAQ K
//
ID KCRM_HUMAN STANDARD; PRT; 381 AA.
AC P06732; Q96QL9;
DT 01-JAN-1988 (Rel. 06, Created)
DT 01-NOV-1990 (Rel. 16, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Creatine kinase, M chain (EC 2.7.3.2) (M-CK).
GN CKM OR CKMM.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RX MEDLINE=89034220; PubMed=2903158;
RA Trask R.V., Strauss A.W., Billadello J.J.;
RT "Developmental regulation and tissue-specific expression of the human
RT muscle creatine kinase gene.";
RL J. Biol. Chem. 263:17142-17149(1988).
RN [2]
RP SEQUENCE FROM N.A.
RX MEDLINE=87048887; PubMed=3778496;
RA Perryman M.B., Kerner S.A., Bohlmeyer T.J., Roberts R.;
RT "Isolation and sequence analysis of a full-length cDNA for human M
RT creatine kinase.";
RL Biochem. Biophys. Res. Commun. 140:981-989(1986).
RN [3]
RP SEQUENCE FROM N.A.
RA Lamerdin J.E., McCready P.M., Skowronski E., Viswanathan V.,
RA Burkhart-Schultz K., Gordon L., Dias J., Ramirez M., Stilwagen S.,
RA Phan H., Velasco N., Do L., Regala W., Terry A., Garnes J.,
RA Danganan L., Erler A., Christensen M., Georgescu A., Avila J., Liu S.,
RA Attix C., Andreise T., Trankheim M., Amico-Keller G., Coefield J.,
RA Duarte S., Lucas S., Bruce R., Thomas P., Quan G., Kronmiller B.,
RA Arellano A., Saunders C., Ow D., Nolan M., Trong S., Kobayashi A.,
RA Olsen A.S., Carrano A.V.;
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SEQUENCE FROM N.A.
RC TISSUE=Liver;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [5]
RP SEQUENCE OF 257-327 FROM N.A.
RX MEDLINE=87181666; PubMed=3031982;
RA Nigro J.M., Schweinfest C.W., Rajkovic A., Pavlovic J., Jamal S.,
RA Dottin R.P., Hart J.T., Kamarck M.E., Rae P.M.M., Carty M.D.,
RA Martin-Deleon P.;
RT "cDNA cloning and mapping of the human creatine kinase M gene to
RT 19q13.";
RL Am. J. Hum. Genet. 40:115-125(1987).
RN [6]
RP SEQUENCE OF 1-30 FROM N.A.
RX MEDLINE=90202921; PubMed=1690725;
RA Hamburg R.J., Friedman D.L., Olson E.N., Ma T.S., Cortez M.D.,
RA Goodman C., Puleo P.R., Perryman M.B.;
RT "Muscle creatine kinase isoenzyme expression in adult human brain.";
RL J. Biol. Chem. 265:6403-6409(1990).
CC -!- FUNCTION: Reversibly catalyzes the transfer of phosphate between
CC ATP and various phosphogens (e.g. creatine phosphate). Creatine
CC kinase isoenzymes play a central role in energy transduction in
CC tissues with large, fluctuating energy demands, such as skeletal
CC muscle, heart, brain and spermatozoa.
CC -!- CATALYTIC ACTIVITY: ATP + creatine = ADP + phosphocreatine.
CC -!- SUBUNIT: Dimer of identical or nonidentical chains. With MM being
CC the major form in skeletal muscle and myocardium, MB existing in
CC myocardium, and BB existing in many tissues, especially brain.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic.
CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; M21494; AAA96609.1; -.
DR EMBL; M21488; AAA96609.1; JOINED.
DR EMBL; M21489; AAA96609.1; JOINED.
DR EMBL; M21490; AAA96609.1; JOINED.
DR EMBL; M21491; AAA96609.1; JOINED.
DR EMBL; M21492; AAA96609.1; JOINED.
DR EMBL; M21493; AAA96609.1; JOINED.
DR EMBL; M14780; AAA52025.1; -.
DR EMBL; AC005781; AAC62841.1; -.
DR EMBL; BC007462; AAH07462.1; -.
DR EMBL; M16440; AAA52026.1; ALT_SEQ.
DR PIR; A31793; KIHUCM.
DR PDB; 1I0E; 01-APR-03.
DR HSC-2DPAGE; P06732; HUMAN.
DR Genew; HGNC:1994; CKM.
DR MIM; 123310; -.
DR GO; GO:0004111; F:creatine kinase activity; TAS.
DR InterPro; IPR000749; ATP-gua_Ptrans.
DR Pfam; PF00217; ATP-gua_Ptrans; 1.
DR Pfam; PF02807; ATP-gua_PtransN; 1.
DR PROSITE; PS00112; GUANIDO_KINASE; 1.
KW Transferase; Kinase; Multigene family; 3D-structure.
FT ACT_SITE 283 283 By similarity.
FT CONFLICT 47 47 T -> I (in Ref. 2).
FT CONFLICT 130 130 R -> P (in Ref. 2).
FT CONFLICT 193 193 L -> Q (in Ref. 2).
FT CONFLICT 210 210 D -> H (in Ref. 2).
FT CONFLICT 215 215 R -> P (in Ref. 2).
FT CONFLICT 225 225 F -> L (in Ref. 4).
FT CONFLICT 324 324 G -> A (in Ref. 2).
SQ SEQUENCE 381 AA; 43101 MW; 418FEAD0C2E138C8 CRC64;
MPFGNTHNKF KLNYKPEEEY PDLSKHNNHM AKVLTLELYK KLRDKETPSG FTVDDVIQTG
VDNPGHPFIM TVGCVAGDEE SYEVFKELFD PIISDRHGGY KPTDKHKTDL NHENLKGGDD
LDPNYVLSSR VRTGRSIKGY TLPPHCSRGE RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT
EKEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM
EKGGNMKEVF RRFCVGLQKI EEIFKKAGHP FMWNQHLGYV LTCPSNLGTG LRGGVHVKLA
HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDVSNAD RLGSSEVEQV QLVVDGVKLM
VEMEKKLEKG QSIDDMIPAQ K
//
ID KCRS_HUMAN STANDARD; PRT; 419 AA.
AC P17540; Q8N1E1;
DT 01-AUG-1990 (Rel. 15, Created)
DT 01-AUG-1990 (Rel. 15, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE Creatine kinase, sarcomeric mitochondrial precursor (EC 2.7.3.2) (S-
DE MtCK) (Mib-CK) (Basic-type mitochondrial creatine kinase).
GN CKMT2.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RC TISSUE=Heart;
RX MEDLINE=90216724; PubMed=2324105;
RA Haas R.C., Strauss A.W.;
RT "Separate nuclear genes encode sarcomere-specific and ubiquitous
RT human mitochondrial creatine kinase isoenzymes.";
RL J. Biol. Chem. 265:6921-6927(1990).
RN [2]
RP SEQUENCE FROM N.A.
RC TISSUE=Brain;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [3]
RP SEQUENCE OF 40-65.
RX MEDLINE=89123390; PubMed=2914937;
RA Haas R.C., Korenfeld C., Zhang Z., Perryman B., Roman D.,
RA Strauss A.W.;
RT "Isolation and characterization of the gene and cDNA encoding human
RT mitochondrial creatine kinase.";
RL J. Biol. Chem. 264:2890-2897(1989).
CC -!- FUNCTION: Reversibly catalyzes the transfer of phosphate between
CC ATP and various phosphogens (e.g. creatine phosphate). Creatine
CC kinase isoenzymes play a central role in energy transduction in
CC tissues with large, fluctuating energy demands, such as skeletal
CC muscle, heart, brain and spermatozoa.
CC -!- CATALYTIC ACTIVITY: ATP + creatine = ADP + phosphocreatine.
CC -!- SUBUNIT: Exists as an octamer composed of four MTCK homodimers.
CC -!- SUBCELLULAR LOCATION: Mitochondrial inner membrane; outer side.
CC -!- TISSUE SPECIFICITY: Sarcomere-specific. Found only in heart and
CC skeletal muscles.
CC -!- MISCELLANEOUS: Mitochondrial creatine kinase binds cardiolipin.
CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; J05401; AAA60561.1; -.
DR EMBL; BC029140; AAH29140.1; -.
DR PIR; A35756; A35756.
DR HSSP; P11009; 1CRK.
DR HSC-2DPAGE; P17540; HUMAN.
DR Genew; HGNC:1996; CKMT2.
DR MIM; 123295; -.
DR GO; GO:0005739; C:mitochondrion; TAS.
DR GO; GO:0004111; F:creatine kinase activity; TAS.
DR GO; GO:0006936; P:muscle contraction; TAS.
DR InterPro; IPR000749; ATP-gua_Ptrans.
DR Pfam; PF00217; ATP-gua_Ptrans; 1.
DR Pfam; PF02807; ATP-gua_PtransN; 1.
DR PROSITE; PS00112; GUANIDO_KINASE; 1.
KW Transferase; Kinase; Multigene family; Mitochondrion; Transit peptide.
FT TRANSIT 1 39 Mitochondrion.
FT CHAIN 40 419 CREATINE KINASE, SARCOMERIC
FT MITOCHONDRIAL.
FT DOMAIN 40 64 CARDIOLIPIN-BINDING (BY SIMILARITY).
FT ACT_SITE 317 317 By similarity.
FT CONFLICT 74 74 S -> A (in Ref. 2).
SQ SEQUENCE 419 AA; 47520 MW; F20E8721F93A2996 CRC64;
MASIFSKLLT GRNASLLFAT MGTSVLTTGY LLNRQKVCAE VREQPRLFPP SADYPDLRKH
NNCMAECLTP AIYSKLRNKV TPNGYTLDQC IQTGVDNPGH PFIKTVGMVA GDEESYEVFA
DLFDPVIKLR HNGYDPRVMK HTTDLDASKI TQGQFDEHYV LSSRVRTGRS IRGLSLPPAC
TRAERREVEN VAITALEGLK GDLAGRYYKL SEMTEQDQQR LIDDHFLFDK PVSPLLTCAG
MARDWPDARG IWHNYDKTFL IWINEEDHTR VISMEKGGNM KRVFERFCRG LKEVERLIQE
RGWEFMWNER LGYILTCPSN LGTGLRAGVH VRIPKLSKDP RFSKILENLR LQKRGTGGVD
TAAVADVYDI SNIDRIGRSE VELVQIVIDG VNYLVDCEKK LERGQDIKVP PPLPQFGKK
//
ID KCRU_HUMAN STANDARD; PRT; 417 AA.
AC P12532;
DT 01-OCT-1989 (Rel. 12, Created)
DT 01-OCT-1989 (Rel. 12, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Creatine kinase, ubiquitous mitochondrial precursor (EC 2.7.3.2) (U-
DE MtCK) (Mia-CK) (Acidic-type mitochondrial creatine kinase).
GN CKMT1 OR CKMT.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RX MEDLINE=89123390; PubMed=2914937;
RA Haas R.C., Korenfeld C., Zhang Z., Perryman B., Roman D.,
RA Strauss A.W.;
RT "Isolation and characterization of the gene and cDNA encoding human
RT mitochondrial creatine kinase.";
RL J. Biol. Chem. 264:2890-2897(1989).
RN [2]
RP SEQUENCE FROM N.A.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SEQUENCE FROM N.A.
RC TISSUE=Lung;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC -!- FUNCTION: Reversibly catalyzes the transfer of phosphate between
CC ATP and various phosphogens (e.g. creatine phosphate). Creatine
CC kinase isoenzymes play a central role in energy transduction in
CC tissues with large, fluctuating energy demands, such as skeletal
CC muscle, heart, brain and spermatozoa.
CC -!- CATALYTIC ACTIVITY: ATP + creatine = ADP + phosphocreatine.
CC -!- SUBUNIT: Exists as an octamer composed of four MTCK homodimers.
CC -!- SUBCELLULAR LOCATION: Mitochondrial inner membrane; outer side.
CC -!- MISCELLANEOUS: Mitochondrial creatine kinase binds cardiolipin.
CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; J04469; AAA98744.1; -.
DR EMBL; BT006628; AAP35274.1; -.
DR EMBL; BC001926; AAH01926.1; -.
DR EMBL; BC006467; AAH06467.1; -.
DR PIR; A31431; A30789.
DR PDB; 1QK1; 24-JUL-03.
DR Genew; HGNC:1995; CKMT1.
DR MIM; 123290; -.
DR GO; GO:0005739; C:mitochondrion; TAS.
DR GO; GO:0004111; F:creatine kinase activity; TAS.
DR InterPro; IPR000749; ATP-gua_Ptrans.
DR Pfam; PF00217; ATP-gua_Ptrans; 1.
DR Pfam; PF02807; ATP-gua_PtransN; 1.
DR PROSITE; PS00112; GUANIDO_KINASE; 1.
KW Transferase; Kinase; Multigene family; Mitochondrion; Transit peptide;
KW 3D-structure.
FT TRANSIT 1 39 Mitochondrion.
FT CHAIN 40 417 CREATINE KINASE, UBIQUITOUS
FT MITOCHONDRIAL.
FT DOMAIN 40 64 CARDIOLIPIN-BINDING (BY SIMILARITY).
FT ACT_SITE 316 316 By similarity.
FT TURN 42 43
FT STRAND 46 46
FT HELIX 49 52
FT TURN 57 58
FT STRAND 61 61
FT HELIX 62 66
FT HELIX 69 75
FT TURN 76 77
FT TURN 81 82
FT HELIX 86 95
FT STRAND 104 104
FT TURN 112 113
FT HELIX 114 117
FT TURN 118 118
FT HELIX 119 129
FT TURN 130 132
FT TURN 135 137
FT HELIX 146 148
FT TURN 156 158
FT STRAND 159 168
FT STRAND 170 170
FT TURN 171 172
FT TURN 176 178
FT HELIX 181 195
FT TURN 196 197
FT HELIX 200 202
FT STRAND 204 208
FT HELIX 209 211
FT HELIX 214 223
FT TURN 224 224
FT HELIX 233 236
FT TURN 237 247
FT STRAND 249 253
FT TURN 254 255
FT STRAND 258 262
FT STRAND 268 275
FT HELIX 279 298
FT TURN 299 301
FT STRAND 304 304
FT STRAND 306 307
FT TURN 308 310
FT STRAND 311 312
FT HELIX 317 319
FT STRAND 321 321
FT TURN 322 322
FT STRAND 325 331
FT HELIX 333 337
FT TURN 339 340
FT HELIX 341 348
FT TURN 349 349
FT STRAND 350 353
FT TURN 359 361
FT STRAND 366 371
FT HELIX 379 400
FT TURN 401 403
SQ SEQUENCE 417 AA; 47036 MW; 274DAC2E9A8AD882 CRC64;
MAGPFSRLLS ARPGLRLLAL AGAGSLAAGF LLRPEPVRAA SERRRLYPPS AEYPDLRKHN
NCMASHLTPA VYARLCDKTT PTGWTLDQCI QTGVDNPGHP FIKTVGMVAG DEETYEVFAD
LFDPVIQERH NGYDPRTMKH TTDLDASKIR SGYFDERYVL SSRVRTGRSI RGLSLPPACT
RAERREVERV VVDALSGLKG DLAGRYYRLS EMTEAEQQQL IDDHFLFDKP VSPLLTAAGM
ARDWPDARGI WHNNEKSFLI WVNEEDHTRV ISMEKGGNMK RVFERFCRGL KEVERLIQER
GWEFMWNERL GYILTCPSNL GTGLRAGVHI KLPLLSKDSR FPKILENLRL QKRGTGGVDT
AATGGVFDIS NLDRLGKSEV ELVQLVIDGV NYLIDCERRL ERGQDIRIPT PVIHTKH
//
ID KCY_HUMAN STANDARD; PRT; 196 AA.
AC P30085; Q96C07; Q9UBQ8; Q9UIA2;
DT 01-APR-1993 (Rel. 25, Created)
DT 16-OCT-2001 (Rel. 40, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE UMP-CMP kinase (EC 2.7.4.14) (Cytidylate kinase) (Deoxycytidylate
DE kinase) (Cytidine monophosphate kinase).
GN UCK.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RA Van Rompay A.R., Johansson M., Karlsson A.;
RT "Cloning of human UMP-CMP kinase cDNA.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SEQUENCE FROM N.A.
RC TISSUE=Hypothalamus;
RX MEDLINE=20402571; PubMed=10931946;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [3]
RP SEQUENCE FROM N.A.
RC TISSUE=Pituitary;
RA Song H., Peng Y., Dai M., Huang Q., Mao Y., Zhang Q., Mao M., Fu G.,
RA Luo M., Chen J., Hu R.;
RT "Human UMP-CMP kinase gene.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SEQUENCE FROM N.A.
RA Pearman T., Castro H., Stafforini D.M., Zimmerman G.A., McIntyre T.M.,
RA Prescott S.M.;
RT "Sequence and characterization of a novel human cytidine monophosphate
RT (CMP) kinase.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SEQUENCE FROM N.A.
RC TISSUE=Muscle;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [6]
RP SEQUENCE OF 1-29.
RC TISSUE=Liver;
RX MEDLINE=94147969; PubMed=8313870;
RA Hughes G.J., Frutiger S., Paquet N., Pasquali C., Sanchez J.-C.,
RA Tissot J.-D., Bairoch A., Appel R.D., Hochstrasser D.F.;
RT "Human liver protein map: update 1993.";
RL Electrophoresis 14:1216-1222(1993).
RN [7]
RP SEQUENCE OF 1-10.
RC TISSUE=Liver;
RX MEDLINE=93162045; PubMed=1286669;
RA Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F.,
RA Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R.,
RA Appel R.D., Hughes G.J.;
RT "Human liver protein map: a reference database established by
RT microsequencing and gel comparison.";
RL Electrophoresis 13:992-1001(1992).
CC -!- FUNCTION: Catalyzes specific phosphoryl transfer from ATP to UMP
CC and CMP.
CC -!- CATALYTIC ACTIVITY: ATP + (d)CMP = ADP + (d)CDP.
CC -!- SIMILARITY: Belongs to the adenylate kinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AF070416; AAF17709.1; ALT_INIT.
DR EMBL; AF112216; AAF17204.1; -.
DR EMBL; AF110643; AAD48583.1; -.
DR EMBL; AF259961; AAG22609.1; -.
DR EMBL; BC014961; AAH14961.1; ALT_INIT.
DR HSSP; P20425; 1QF9.
DR SWISS-2DPAGE; P30085; HUMAN.
DR Siena-2DPAGE; P30085; -.
DR GK; P30085; -.
DR GO; GO:0005737; C:cytoplasm; TAS.
DR GO; GO:0005634; C:nucleus; TAS.
DR GO; GO:0004849; F:uridine kinase activity; TAS.
DR GO; GO:0009220; P:pyrimidine ribonucleotide biosynthesis; TAS.
DR InterPro; IPR000850; Adenylate_kin.
DR InterPro; IPR006266; UMP_CMP_kinase.
DR Pfam; PF00406; ADK; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR ProDom; PD000657; Adenylate_kin; 1.
DR TIGRFAMs; TIGR01359; UMP_CMP_kin_fam; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; 1.
KW Transferase; Kinase; Pyrimidine biosynthesis; ATP-binding.
FT NP_BIND 10 18 ATP (By similarity).
FT CONFLICT 27 27 Y -> I (in Ref. 6).
SQ SEQUENCE 196 AA; 22222 MW; 6837B1E6D7543768 CRC64;
MKPLVVFVLG GPGAGKGTQC ARIVEKYGYT HLSAGELLRD ERKNPDSQYG ELIEKYIKEG
KIVPVEITIS LLKREMDQTM AANAQKNKFL IDGFPRNQDN LQGWNKTMDG KADVSFVLFF
DCNNEICIER CLERGKSSGR SDDNRESLEK RIQTYLQSTK PIIDLYEEMG KVKKIDASKS
VDEVFDEVVQ IFDKEG
//
ID KDGA_HUMAN STANDARD; PRT; 735 AA.
AC P23743; O75481; O75482; O75483;
DT 01-NOV-1991 (Rel. 20, Created)
DT 01-NOV-1995 (Rel. 32, Last sequence update)
DT 16-OCT-2001 (Rel. 40, Last annotation update)
DE Diacylglycerol kinase, alpha (EC 2.7.1.107) (Diglyceride kinase) (DGK-
DE alpha) (DAG kinase alpha) (80 kDa diacylglycerol kinase).
GN DGKA OR DAGK1 OR DAGK.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RC TISSUE=Lymphocytes;
RX MEDLINE=91085550; PubMed=2175712;
RA Schaap D., de Widt J., van der Wal J., Vandekerckhove J.,
RA van Damme J., Gussow D., Ploegh H.L., van Blitterswijk W.J.,
RA van der Bendl R.L.;
RT "Purification, cDNA-cloning and expression of human diacylglycerol
RT kinase.";
RL FEBS Lett. 275:151-158(1990).
RN [2]
RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING.
RA Champagne C.M.E., Maeda H., Takashiba S., van Dyke T.E.;
RT "Alternative splicing of diacylglycerol kinase alpha expressed in
RT human neutrophils.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP MAPPING.
RX MEDLINE=94235961; PubMed=8180475;
RA Hart T.C., Champagne C., Zhou J., van Dyke T.E.;
RT "Assignment of the gene for diacylglycerol kinase (DAGK) to human
RT chromosome 12.";
RL Mamm. Genome 5:123-124(1994).
RN [4]
RP MAPPING.
RX MEDLINE=95048385; PubMed=7959783;
RA Hart T.C., Zhou J., Champagne C., van Dyke T.E., Rao P.N.,
RA Pettenati M.J.;
RT "Assignment of the human diacylglycerol kinase gene (DAGK) to 12q13.3
RT using fluorescence in situ hybridization analysis.";
RL Genomics 22:246-247(1994).
CC -!- FUNCTION: Upon cell stimulation converts the second messenger
CC diacylglycerol into phosphatidate, initiating the resynthesis of
CC phosphatidylinositols and attenuating protein kinase C activity.
CC -!- CATALYTIC ACTIVITY: ATP + 1,2-diacylglycerol = ADP + 1,2-
CC diacylglycerol 3-phosphate.
CC -!- ENZYME REGULATION: Stimulated by calcium and phosphatidylserine.
CC Phosphorylated by protein kinase C.
CC -!- SUBUNIT: Monomer.
CC -!- TISSUE SPECIFICITY: Lymphocytes and oligodendroglial cells.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase
CC family.
CC -!- SIMILARITY: Contains 2 zinc-dependent phorbol-ester and DAG
CC binding domains.
CC -!- SIMILARITY: Contains 2 EF-hand calcium-binding domains.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; X62535; CAA44396.1; -.
DR EMBL; AF064769; AAC34804.1; -.
DR EMBL; AF064767; AAC34802.1; -.
DR EMBL; AF064768; AAC34803.1; -.
DR PIR; S12969; S12969.
DR Genew; HGNC:2849; DGKA.
DR MIM; 125855; -.
DR GO; GO:0004143; F:diacylglycerol kinase activity; TAS.
DR GO; GO:0007242; P:intracellular signaling cascade; TAS.
DR InterPro; IPR002219; DAG_PE-bind.
DR InterPro; IPR000756; DAGKa.
DR InterPro; IPR001206; DAGKc.
DR InterPro; IPR002048; EF-hand.
DR Pfam; PF00130; DAG_PE-bind; 2.
DR Pfam; PF00609; DAGKa; 1.
DR Pfam; PF00781; DAGKc; 1.
DR Pfam; PF00036; efhand; 2.
DR ProDom; PD002939; DAGKa; 1.
DR ProDom; PD005043; DAGKc; 1.
DR ProDom; PD000012; EF-hand; 1.
DR SMART; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SMART; SM00054; EFh; 2.
DR PROSITE; PS00479; DAG_PE_BIND_DOM_1; 2.
DR PROSITE; PS50081; DAG_PE_BIND_DOM_2; 2.
DR PROSITE; PS00018; EF_HAND; 2.
KW Transferase; Kinase; Calcium-binding; Phorbol-ester binding;
KW Repeat; Multigene family.
FT CA_BIND 123 134 EF-HAND 1 (PROBABLE).
FT CA_BIND 168 179 EF-HAND 2 (PROBABLE).
FT DOMAIN 206 253 PHORBOL-ESTER AND DAG BINDING 1.
FT DOMAIN 270 319 PHORBOL-ESTER AND DAG BINDING 2.
FT DOMAIN 374 500 CATALYTIC-A (POTENTIAL).
FT DOMAIN 520 701 CATALYTIC-B (POTENTIAL).
FT CONFLICT 339 339 L -> P (in Ref. 2).
FT CONFLICT 379 379 V -> L (in Ref. 2).
FT CONFLICT 385 385 S -> W (in Ref. 2).
FT CONFLICT 684 684 E -> G (in Ref. 2).
FT CONFLICT 699 699 V -> G (in Ref. 2).
FT CONFLICT 715 715 N -> K (in Ref. 2).
SQ SEQUENCE 735 AA; 82672 MW; ACAA0AD19DF4D510 CRC64;
MAKERGLISP SDFAQLQKYM EYSTKKVSDV LKLFEDGEMA KYVQGDAIGY EGFQQFLKIY
LEVDNVPRHL SLALFQSFET GHCLNETNVT KDVVCLNDVS CYFSLLEGGR PEDKLEFTFK
LYDTDRNGIL DSSEVDKIIL QMMRVAEYLD WDVSELRPIL QEMMKEIDYD GSGSVSQAEW
VRAGATTVPL LVLLGLEMTL KDDGQHMWRP KRFPRPVYCN LCESSIGLGK QGLSCNLCKY
TVHDQCAMKA LPCEVSTYAK SRKDIGVQSH VWVRGGCESG RCDRCQKKIR IYHSLTGLHC
VWCHLEIHDD CLQAVGHECD CGLLRDHILP PSSIYPSVLA SGPDRKNSKT SQKTMDDLNL
STSEALRIDP VPNTHPLLVF VNPKSGGKQG QRVLWKFQYI LNPRQVFNLL KDGPEIGLRL
FKDVPDSRIL VCGGDGTVGW ILETIDKANL PVLPPVAVLP LGTGNDLARC LRWGGGYEGQ
NLAKILKDLE MSKVVHMDRW SVEVIPQQTE EKSDPVPFQI INNYFSIGVD ASIAHRFHIM
REKYPEKFNS RMKNKLWYFE FATSESIFST CKKLEESLTV EICGKPLDLS NLSLEGIAVL
NIPSMHGGSN LWGDTRRPHG DIYGINQALG ATAKVITDPD ILKTCVPDLS DKRLEVVGLE
GAIEMGQIYT KLKNAGRRLA KCSEITFHTT KTLPMQIDVE PWMQTPCTIK ITHKNQMPML
MGPPPRSTNF FGFLS
//
ID KDGB_HUMAN STANDARD; PRT; 804 AA.
AC Q9Y6T7; Q9UQ29;
DT 16-OCT-2001 (Rel. 40, Created)
DT 16-OCT-2001 (Rel. 40, Last sequence update)
DT 28-FEB-2003 (Rel. 41, Last annotation update)
DE Diacylglycerol kinase, beta (EC 2.7.1.107) (Diglyceride kinase) (DGK-
DE beta) (DAG kinase beta) (90 kDa diacylglycerol kinase).
GN DGKB OR DAGK2 OR KIAA0718.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE OF 1-49 FROM N.A.
RA Sun H., Bauer C., Sandberg B.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SEQUENCE OF 63-804 FROM N.A.
RC TISSUE=Brain;
RX MEDLINE=99087487; PubMed=9872452;
RA Nagase T., Ishikawa K.-I., Suyama M., Kikuno R., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [3]
RP SEQUENCE FROM N.A.
RA Caricasole A., Caldara F., Sala C.F.;
RT "Novel proteins.";
RL Patent number WO0047723, 17-AUG-2000.
CC -!- FUNCTION: Exhibit high phosphorylation activity for long-chain
CC diacylglycerols (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + 1,2-diacylglycerol = ADP + 1,2-
CC diacylglycerol 3-phosphate.
CC -!- ENZYME REGULATION: Stimulated by phosphatidylserine (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasmic (By similarity).
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase
CC family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AC006150; AAD28352.1; -.
DR EMBL; AB018261; BAA34438.1; -.
DR EMBL; AX032742; CAC09945.1; -.
DR HSSP; P02593; 1CTR.
DR Genew; HGNC:2850; DGKB.
DR MIM; 604070; -.
DR InterPro; IPR000756; DAGKa.
DR InterPro; IPR001206; DAGKc.
DR InterPro; IPR002219; DAG_PE-bind.
DR InterPro; IPR002048; EF-hand.
DR Pfam; PF00609; DAGKa; 1.
DR Pfam; PF00781; DAGKc; 1.
DR Pfam; PF00130; DAG_PE-bind; 2.
DR Pfam; PF00036; efhand; 2.
DR ProDom; PD002939; DAGKa; 1.
DR ProDom; PD005043; DAGKc; 1.
DR ProDom; PD000012; EF-hand; 1.
DR SMART; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SMART; SM00054; EFh; 2.
DR PROSITE; PS00479; DAG_PE_BIND_DOM_1; 2.
DR PROSITE; PS50081; DAG_PE_BIND_DOM_2; 2.
DR PROSITE; PS00018; EF_HAND; 2.
KW Transferase; Kinase; Calcium-binding; Phorbol-ester binding;
KW Repeat; Multigene family.
FT CA_BIND 162 173 EF-HAND 1 (POTENTIAL).
FT CA_BIND 207 218 EF-HAND 2 (POTENTIAL).
FT DOMAIN 245 294 PHORBOL-ESTER AND DAG BINDING 1.
FT DOMAIN 309 358 PHORBOL-ESTER AND DAG BINDING 2.
FT DOMAIN 436 562 CATALYTIC-A (POTENTIAL).
FT DOMAIN 582 762 CATALYTIC-B (POTENTIAL).
SQ SEQUENCE 804 AA; 90595 MW; CBCABD2339BFE176 CRC64;
MTNQEKWAHL SPSEFSQLQK YAEYSTKKLK DVLEEFHGNG VLAKYNPEGK QDILNQTIDF
EGFKLFMKTF LEAELPDDFT AHLFMSFSNK FPHSSPMVKS KPALLSGGLR MNKGAITPPR
TTSPANTCSP EVIHLKDIVC YLSLLERGRP EDKLEFMFRL YDTDGNGFLD SSELENIISQ
MMHVAEYLEW DVTELNPILH EMMEEIDYDH DGTVSLEEWI QGGMTTIPLL VLLGLENNVK
DDGQHVWRLK HFNKPAYCNL CLNMLIGVGK QGLCCSFCKY TVHERCVARA PPSCIKTYVK
SKRNTDVMHH YWVEGNCPTK CDKCHKTVKC YQGLTGLHCV WCQITLHNKC ASHLKPECDC
GPLKDHILPP TTICPVVLQT LPTSGVSVPE ERQSTVKKEK SGSQQPNKVI DKNKMQRANS
VTVDGQGLQV TPVPGTHPLL VFVNPKSGGK QGERIYRKFQ YLLNPRQVYS LSGNGPMPGL
NFFRDVPDFR VLACGGDGTV GWVLDCIEKA NVGKHPPVAI LPLGTGNDLA RCLRWGGGYE
GENLMKILKD IENSTEIMLD RWKFEVIPND KDEKGDPVPY SIINNYFSIG VDASIAHRFH
IMREKHPEKF NSRMKNKFWY FEFGTSETFS ATCKKLHESV EIECDGVQID LINISLEGIA
ILNIPSMHGG SNLWGESKKR RSHRRIEKKG SDKRTTVTDA KELKFASQDL SDQLLEVVGL
EGAMEMGQIY TGLKSAGRRL AQCSCVVIRT SKSLPMQIDG EPWMQTPCTI KITHKNQAPM
LMGPPPKTGL FCSLVKRTRN RSKE
//
ID KDGD_HUMAN STANDARD; PRT; 1195 AA.
AC Q16760; Q14158;
DT 01-NOV-1997 (Rel. 35, Created)
DT 16-OCT-2001 (Rel. 40, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Diacylglycerol kinase, delta (EC 2.7.1.107) (Diglyceride kinase)
DE (DGK-delta) (DAG kinase delta) (130 kDa diacylglycerol kinase)
DE (Fragment).
GN DGKD OR KIAA0145.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE OF 26-1195 FROM N.A.
RC TISSUE=Hepatoma, and Testis;
RX MEDLINE=96215245; PubMed=8626538;
RA Sakane F., Imai S., Kai M., Wada I., Kanoh H.;
RT "Molecular cloning of a novel diacylglycerol kinase isozyme with a
RT pleckstrin homology domain and a C-terminal tail similar to those of
RT the EPH family of protein-tyrosine kinases.";
RL J. Biol. Chem. 271:8394-8401(1996).
RN [2]
RP SEQUENCE FROM N.A.
RA Nomura N.;
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SEQUENCE OF 516-1195 FROM N.A.
RC TISSUE=Bone marrow;
RX MEDLINE=96127530; PubMed=8590280;
RA Nagase T., Seki N., Tanaka A., Ishikawa K.-I., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. IV.
RT The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by
RT analysis of cDNA clones from human cell line KG-1.";
RL DNA Res. 2:167-174(1995).
CC -!- CATALYTIC ACTIVITY: ATP + 1,2-diacylglycerol = ADP + 1,2-
CC diacylglycerol 3-phosphate.
CC -!- ENZYME REGULATION: Partially inhibited by phosphatidylserine.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic. Can be loosely bound to the
CC membranes.
CC -!- TISSUE SPECIFICITY: Most abundant in skeletal muscle. Detected to
CC a lesser extent in testis, colon, peripheral blood leukocytes, and
CC hepatoma cells. Undetectable in the brain, retina, or thymus.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase
CC family.
CC -!- SIMILARITY: Contains 2 zinc-dependent phorbol-ester and DAG
CC binding domains.
CC -!- SIMILARITY: Contains 1 PH domain.
CC -!- SIMILARITY: Contains 1 sterile alpha motif (SAM) domain.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; D73409; BAA11134.1; -.
DR EMBL; D63479; BAA09766.2; -.
DR Genew; HGNC:2851; DGKD.
DR MIM; 601826; -.
DR GO; GO:0004143; F:diacylglycerol kinase activity; TAS.
DR GO; GO:0007165; P:signal transduction; TAS.
DR InterPro; IPR002219; DAG_PE-bind.
DR InterPro; IPR000756; DAGKa.
DR InterPro; IPR001206; DAGKc.
DR InterPro; IPR001849; PH.
DR InterPro; IPR001660; SAM.
DR Pfam; PF00130; DAG_PE-bind; 2.
DR Pfam; PF00609; DAGKa; 1.
DR Pfam; PF00781; DAGKc; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00536; SAM; 1.
DR ProDom; PD002939; DAGKa; 1.
DR ProDom; PD005043; DAGKc; 1.
DR SMART; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00454; SAM; 1.
DR PROSITE; PS00479; DAG_PE_BIND_DOM_1; 2.
DR PROSITE; PS50081; DAG_PE_BIND_DOM_2; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
KW Transferase; Kinase; Phorbol-ester binding; Repeat; Multigene family.
FT NON_TER 1 1
FT DOMAIN 34 127 PH.
FT DOMAIN 145 194 PHORBOL-ESTER AND DAG BINDING 1.
FT DOMAIN 217 267 PHORBOL-ESTER AND DAG BINDING 2.
FT DOMAIN 300 427 CATALYTIC-A (POTENTIAL).
FT DOMAIN 744 901 CATALYTIC-B (POTENTIAL).
FT DOMAIN 1126 1189 SAM.
FT CONFLICT 26 33 TSGQIRQK -> MNMFLYFQ (in Ref. 1).
FT CONFLICT 492 492 V -> P (in Ref. 1).
FT CONFLICT 809 815 RPIPLPS -> DPSHSPV (in Ref. 1).
FT CONFLICT 941 941 L -> V (in Ref. 1).
FT CONFLICT 1037 1037 Missing (in Ref. 1).
SQ SEQUENCE 1195 AA; 132825 MW; 78C57125EDB41462 CRC64;
PPEESSDSEP EAEPGSPQKL IRKVSTSGQI RQKTIIKEGM LTKQNNSFQR SKRRYFKLRG
RTLYYAKTAK SIIFDEVDLT DASVAESSTK NVNNSFTVIT PCRKLILCAD NRKEMEDWIA
ALKTVQNREH FEPTQYSMDH FSGMHNWYAC SHARPTYCNV CREALSGVTS HGLSCEVCKF
KAHKRCAVRA TNNCKWTTLA SIGKDIIEDA DGIAMPHQWL EGNLPVSAKC TVCDKTCGSV
LRLQDWRCLW CKAMVHTSCK ESLLTKCPLG LCKVSVIPPT ALNSIDSDGF WKASCPPSCT
SPLLVFVNSK SGDNQGVKFL RRFKQLLNPA QVFDLMNGGP HLGLRLFQKF DTFRILVCGG
DGSVGWVLSE IDSLNLHKQC QLGVLPLGTG NDLARVLGWG SACDDDTQLP QILEKLERAS
TKMLDRWSVM AYEAKLPRQA SSSTVTEDFS EDSEVQQILF YEDSVAAHLS KILTSDQHSV
VISSAKVLCE TVKDFVARVG KAYEKTTESS EESEVMAKKC SVLKEKLDSL LKTLDDESQA
SSSLPNPPPT IAEEAEDGDG SGSICGSTGD RLVASACPAR PQIFRPREQL MLRANSLKKA
IRQIIEHTEK AVDEQNAQTQ EQEGFVLGLS ESEEKMDHRV CPPLSHSESF GVPKGRSQRK
VSKSPCEKLI SKGSLSLGSS ASLPPQPGSR DGLPALNTKI LYPNVRAGMS GSLPGGSVIS
RLLINADPFN SEPETLEYYT EKCVMNNYFG IGLDAKISLD FNNKRDEHPE KCRSRTKNMM
WYGVLGTKEL LHRTYKNLEQ KVLLECDGRP IPLPSLQGIA VLNIPSYAGG TNFWGGTKED
DTFAAPSFDD KILEVVAVFG SMQMAVSRVI RLQHHRIAQC RTVKISILGD EGVPVQVDGE
AWVQPPGYIR IVHKNRAQTL TRDRAFESTL KSWEDKQKCE LPRPPSCSLH PEMLSEEEAT
QMDQFGQAAG VLIHSIREIA QSHRDMEQEL AHAVNASSKS MDRVYGKPRT TEGLNCSFVL
EMVNNFRALR SETELLLSGK MALQLDPPQK EQLGSALAEM DRQLRRLADT PWLCQSAEPG
DEESVMLDLA KRSRSGKFRL VTKFKKEKNN KNKEAHSSLG APVHLWGTEE VAAWLEHLSL
CEYKDIFTRH DIRGSELLHL ERRDLKDLGV TKVGHMKRIL CGIKELSRSA PAVEA
//
ID KDGE_HUMAN STANDARD; PRT; 567 AA.
AC P52429; Q9UKQ3;
DT 01-OCT-1996 (Rel. 34, Created)
DT 01-OCT-1996 (Rel. 34, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Diacylglycerol kinase, epsilon (EC 2.7.1.107) (Diglyceride kinase)
DE (DGK-epsilon) (DAG kinase epsilon).
GN DGKE OR DAGK5.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RC TISSUE=Umbilical vein endothelial cells;
RX MEDLINE=96215320; PubMed=8626589;
RA Tang W., Bunting M., Zimmerman G.A., McIntyre T.M., Prescott S.M.;
RT "Molecular cloning of a novel human diacylglycerol kinase highly
RT selective for arachidonate-containing substrates.";
RL J. Biol. Chem. 271:10237-10241(1996).
RN [2]
RP SEQUENCE OF 1-154 FROM N.A.
RX MEDLINE=20035825; PubMed=10571048;
RA Tang W., Bardien S., Bhattacharya S.S., Prescott S.M.;
RT "Characterization of the human diacylglycerol kinase epsilon gene and
RT its assessment as a candidate for inherited retinitis pigmentosa.";
RL Gene 239:185-192(1999).
CC -!- FUNCTION: Highly selective for arachidonate-containing species of
CC diacylglycerol (DAG). May terminate signals transmitted through
CC arachidonoyl-DAG or may contribute to the synthesis of
CC phospholipids with defined fatty acid composition.
CC -!- CATALYTIC ACTIVITY: ATP + 1,2-diacylglycerol = ADP + 1,2-
CC diacylglycerol 3-phosphate.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in testis.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase
CC family.
CC -!- SIMILARITY: Contains 2 zinc-dependent phorbol-ester and DAG
CC binding domains.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; U49379; AAC50497.1; -.
DR EMBL; AF136745; AAD45666.1; -.
DR Genew; HGNC:2852; DGKE.
DR MIM; 601440; -.
DR GO; GO:0005524; F:ATP binding; TAS.
DR GO; GO:0004143; F:diacylglycerol kinase activity; TAS.
DR GO; GO:0008654; P:phospholipid biosynthesis; TAS.
DR InterPro; IPR000756; DAGKa.
DR InterPro; IPR001206; DAGKc.
DR InterPro; IPR002219; DAG_PE-bind.
DR Pfam; PF00609; DAGKa; 1.
DR Pfam; PF00781; DAGKc; 1.
DR Pfam; PF00130; DAG_PE-bind; 2.
DR ProDom; PD002939; DAGKa; 1.
DR ProDom; PD005043; DAGKc; 1.
DR SMART; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR PROSITE; PS00479; DAG_PE_BIND_DOM_1; 2.
DR PROSITE; PS50081; DAG_PE_BIND_DOM_2; 2.
KW Transferase; Kinase; Phorbol-ester binding; Multigene family;
KW Transmembrane; Repeat.
FT TRANSMEM 22 42 Potential.
FT TRANSMEM 436 456 Potential.
FT DOMAIN 60 108 PHORBOL-ESTER AND DAG BINDING 1.
FT DOMAIN 125 177 PHORBOL-ESTER AND DAG BINDING 2.
FT DOMAIN 217 350 CATALYTIC-A (POTENTIAL).
FT DOMAIN 369 524 CATALYTIC-B (POTENTIAL).
SQ SEQUENCE 567 AA; 63927 MW; BC334AD15FB4D0B4 CRC64;
MEAERRPAPG SPSEGLFADG HLILWTLCSV LLPVFITFWC SLQRSRRQLH RRDIFRKSKH
GWRDTDLFSQ PTYCCVCAQH ILQGAFCDCC GLRVDEGCLR KADKRFQCKE IMLKNDTKVL
DAMPHHWIRG NVPLCSYCMV CKQQCGCQPK LCDYRCIWCQ KTVHDECMKN SLKNEKCDFG
EFKNLIIPPS YLTSINQMRK DKKTDYEVLA SKLGKQWTPL IILANSRSGT NMGEGLLGEF
RILLNPVQVF DVTKTPPIKA LQLCTLLPYY SARVLVCGGD GTVGWVLDAV DDMKIKGQEK
YIPQVAVLPL GTGNDLSNTL GWGTGYAGEI PVAQVLRNVM EADGIKLDRW KVQVTNKGYY
NLRKPKEFTM NNYFSVGPDA LMALNFHAHR EKAPSLFSSR ILNKAVYLFY GTKDCLVQEC
KDLNKKVELE LDGERVALPS LEGIIVLNIG YWGGGCRLWE GMGDETYPLA RHDDGLLEVV
GVYGSFHCAQ IQVKLANPFR IGQAHTVRLI LKCSMMPMQV DGEPWAQGPC TVTITHKTHA
MMLYFSGEQT DDDISSTSDQ EDIKATE
//
ID KDGG_HUMAN STANDARD; PRT; 791 AA.
AC P49619;
DT 01-FEB-1996 (Rel. 33, Created)
DT 01-FEB-1996 (Rel. 33, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Diacylglycerol kinase, gamma (EC 2.7.1.107) (Diglyceride kinase) (DGK-
DE gamma) (DAG kinase gamma).
GN DGKG OR DAGK3.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RC TISSUE=Liver;
RX MEDLINE=94308084; PubMed=8034597;
RA Kai M., Sakane F., Imai S.-I., Wada I., Kanoh H.;
RT "Molecular cloning of a diacylglycerol kinase isozyme predominantly
RT expressed in human retina with a truncated and inactive enzyme
RT expression in most other human cells.";
RL J. Biol. Chem. 269:18492-18498(1994).
RN [2]
RP SEQUENCE FROM N.A.
RX MEDLINE=99168758; PubMed=10071200;
RA Stoehr H., Klein J., Gehrig A., Koehler M.R., Jurklies B., Kellner U.,
RA Leo-Kottler B., Schmid M., Weber B.H.F.;
RT "Mapping and genomic characterization of the gene encoding
RT diacylglycerol kinase gamma (DAGK3): assessment of its role in
RT dominant optic atrophy (OPA1).";
RL Hum. Genet. 104:99-105(1999).
CC -!- FUNCTION: Reverses the normal flow of glycerolipid biosynthesis by
CC phosphorylating diacylglycerol back to phosphatidic acid.
CC -!- CATALYTIC ACTIVITY: ATP + 1,2-diacylglycerol = ADP + 1,2-
CC diacylglycerol 3-phosphate.
CC -!- ENZYME REGULATION: Requires phosphatidylserine for maximal
CC activity.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic. Can be loosely bound to the
CC membranes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P49619-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P49619-2; Sequence=VSP_001267;
CC Note=May be inactive;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in retina and in a
CC much lesser extent in the brain. Other tissues contain extremely
CC low levels of DGK-gamma.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase
CC family.
CC -!- SIMILARITY: Contains 2 zinc-dependent phorbol-ester and DAG
CC binding domains.
CC -!- SIMILARITY: Contains 2 EF-hand calcium-binding domains.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; D26135; BAA05132.1; -.
DR EMBL; AF020945; AAC04686.1; -.
DR EMBL; AF020922; AAC04686.1; JOINED.
DR EMBL; AF020923; AAC04686.1; JOINED.
DR EMBL; AF020924; AAC04686.1; JOINED.
DR EMBL; AF020925; AAC04686.1; JOINED.
DR EMBL; AF020926; AAC04686.1; JOINED.
DR EMBL; AF020927; AAC04686.1; JOINED.
DR EMBL; AF020928; AAC04686.1; JOINED.
DR EMBL; AF020929; AAC04686.1; JOINED.
DR EMBL; AF020930; AAC04686.1; JOINED.
DR EMBL; AF020931; AAC04686.1; JOINED.
DR EMBL; AF020932; AAC04686.1; JOINED.
DR EMBL; AF020933; AAC04686.1; JOINED.
DR EMBL; AF020934; AAC04686.1; JOINED.
DR EMBL; AF020935; AAC04686.1; JOINED.
DR EMBL; AF020936; AAC04686.1; JOINED.
DR EMBL; AF020937; AAC04686.1; JOINED.
DR EMBL; AF020938; AAC04686.1; JOINED.
DR EMBL; AF020939; AAC04686.1; JOINED.
DR EMBL; AF020940; AAC04686.1; JOINED.
DR EMBL; AF020941; AAC04686.1; JOINED.
DR EMBL; AF020942; AAC04686.1; JOINED.
DR EMBL; AF020943; AAC04686.1; JOINED.
DR EMBL; AF020944; AAC04686.1; JOINED.
DR PIR; A53691; A53691.
DR Genew; HGNC:2853; DGKG.
DR MIM; 601854; -.
DR GO; GO:0004143; F:diacylglycerol kinase activity; TAS.
DR GO; GO:0007165; P:signal transduction; TAS.
DR InterPro; IPR000756; DAGKa.
DR InterPro; IPR001206; DAGKc.
DR InterPro; IPR002219; DAG_PE-bind.
DR InterPro; IPR002048; EF-hand.
DR Pfam; PF00609; DAGKa; 1.
DR Pfam; PF00781; DAGKc; 1.
DR Pfam; PF00130; DAG_PE-bind; 1.
DR Pfam; PF00036; efhand; 2.
DR ProDom; PD002939; DAGKa; 1.
DR ProDom; PD005043; DAGKc; 1.
DR ProDom; PD000012; EF-hand; 1.
DR SMART; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SMART; SM00054; EFh; 2.
DR PROSITE; PS00479; DAG_PE_BIND_DOM_1; 2.
DR PROSITE; PS50081; DAG_PE_BIND_DOM_2; 2.
DR PROSITE; PS00018; EF_HAND; 2.
KW Transferase; Kinase; Calcium-binding; Phorbol-ester binding;
KW Repeat; Multigene family; Alternative splicing.
FT DOMAIN 151 156 POLY-SER.
FT CA_BIND 188 199 EF-HAND 1 (POTENTIAL).
FT CA_BIND 233 244 EF-HAND 2 (POTENTIAL).
FT DOMAIN 272 321 PHORBOL-ESTER AND DAG BINDING 1.
FT DOMAIN 337 383 PHORBOL-ESTER AND DAG BINDING 2.
FT DOMAIN 432 558 CATALYTIC-A (POTENTIAL).
FT DOMAIN 578 752 CATALYTIC-B (POTENTIAL).
FT VARSPLIC 451 475 Missing (in isoform Short).
FT /FTId=VSP_001267.
SQ SEQUENCE 791 AA; 88996 MW; C7DD07F5B285FF62 CRC64;
MGEERWVSLT PEEFDQLQKY SEYSSKKIKD ALTEFNEGGS LKQYDPHEPI SYDVFKLFMR
AYLEVDLPQP LSTHLFLAFS QKPRHETSDH PTEGASNSEA NSADTNIQNA DNATKADEAC
APDTESNMAE KQAPAEDQVA ATPLEPPVPR SSSSESPVVY LKDVVCYLSL LETGRPQDKL
EFMFRLYDSD ENGLLDQAEM DCIVNQMLHI AQYLEWDPTE LRPILKEMLQ GMDYDRDGFV
SLQEWVHGGM TTIPLLVLLG MDDSGSKGDG GHAWTMKHFK KPTYCNFCHI MLMGVRKQGL
CCTYCKYTVH ERCVSKNIPG CVKTYSKAKR SGEVMQHAWV EGNSSVKCDR CHKSIKCYQS
VTARHCVWCR MTFHRKCELS TLCDGGELRD HILLPTSICP ITRDRPGEKS DGCVSAKGEL
VMQYKIIPTP GTHPLLVLVN PKSGGRQGER ILRKFHYLLN PKQVFNLDNG GPTPGLNFFR
DTPDFRVLAC GGDGTVGWIL DCIDKANFAK HPPVAVLPLG TGNDLARCLR WGGGYEGGSL
TKILKDIEQS PLVMLDRWHL EVIPREEVEN GDQVPYSIMN NYFSIGVDAS IAHRFHVMRE
KHPEKFNSRM KNKLWYFEFG TSETFAATCK KLHDHIELEC DGVGVDLSNI FLEGIAILNI
PSMYGGTNLW GENKKNRAVI RESRKGVTDP KELKFCVQDL SDQLLEVVGL EGAMEMGQIY
TGLKSAGRRL AQCASVTIRT NKLLPMQVDG EPWMQPCCTI KITHKNQAPM MMGPPQKSSF
FSLRRKSRSK D
//
ID KDGI_HUMAN STANDARD; PRT; 1065 AA.
AC O75912; Q9NZ49;
DT 16-OCT-2001 (Rel. 40, Created)
DT 16-OCT-2001 (Rel. 40, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE Diacylglycerol kinase, iota (EC 2.7.1.107) (Diglyceride kinase) (DGK-
DE iota) (DAG kinase iota).
GN DGKI.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RC TISSUE=Retina;
RX MEDLINE=99047655; PubMed=9830018;
RA Ding L., Traer E., McIntyre T.M., Zimmerman G.A., Prescott S.M.;
RT "The cloning and characterization of a novel human diacylglycerol
RT kinase, DGK-iota.";
RL J. Biol. Chem. 273:32746-32752(1998).
RN [2]
RP SEQUENCE OF 135-1065 FROM N.A., AND VARIANT PHE-153.
RX MEDLINE=20173854; PubMed=10706894;
RA Bowne S.J., Sullivan L.S., Ding L., Traer E., Prescott S.M.,
RA Birch D.G., Kennan A., Humphries P., Daiger S.P.;
RT "Evaluation of human diacylglycerol kinase iota, DGKI, a homolog of
RT Drosophila rdgA, in inherited retinopathy mapping to 7q.";
RL Mol. Vision 6:6-9(2000).
CC -!- CATALYTIC ACTIVITY: ATP + 1,2-diacylglycerol = ADP + 1,2-
CC diacylglycerol 3-phosphate.
CC -!- SUBCELLULAR LOCATION: Nuclear and cytoplasmic.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase
CC family.
CC -!- SIMILARITY: Contains 2 zinc-dependent phorbol-ester and DAG
CC binding domains.
CC -!- SIMILARITY: Contains 2 ANK repeats.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AF061936; AAC62010.1; -.
DR EMBL; AF219939; AAF43006.1; -.
DR EMBL; AF219907; AAF43006.1; JOINED.
DR EMBL; AF219908; AAF43006.1; JOINED.
DR EMBL; AF219909; AAF43006.1; JOINED.
DR EMBL; AF219910; AAF43006.1; JOINED.
DR EMBL; AF219911; AAF43006.1; JOINED.
DR EMBL; AF219912; AAF43006.1; JOINED.
DR EMBL; AF219913; AAF43006.1; JOINED.
DR EMBL; AF219914; AAF43006.1; JOINED.
DR EMBL; AF219915; AAF43006.1; JOINED.
DR EMBL; AF219916; AAF43006.1; JOINED.
DR EMBL; AF219917; AAF43006.1; JOINED.
DR EMBL; AF219918; AAF43006.1; JOINED.
DR EMBL; AF219919; AAF43006.1; JOINED.
DR EMBL; AF219920; AAF43006.1; JOINED.
DR EMBL; AF219921; AAF43006.1; JOINED.
DR EMBL; AF219922; AAF43006.1; JOINED.
DR EMBL; AF219923; AAF43006.1; JOINED.
DR EMBL; AF219924; AAF43006.1; JOINED.
DR EMBL; AF219925; AAF43006.1; JOINED.
DR EMBL; AF219926; AAF43006.1; JOINED.
DR EMBL; AF219927; AAF43006.1; JOINED.
DR EMBL; AF219928; AAF43006.1; JOINED.
DR EMBL; AF219929; AAF43006.1; JOINED.
DR EMBL; AF219930; AAF43006.1; JOINED.
DR EMBL; AF219931; AAF43006.1; JOINED.
DR EMBL; AF219932; AAF43006.1; JOINED.
DR EMBL; AF219933; AAF43006.1; JOINED.
DR EMBL; AF219934; AAF43006.1; JOINED.
DR EMBL; AF219935; AAF43006.1; JOINED.
DR EMBL; AF219936; AAF43006.1; JOINED.
DR EMBL; AF219937; AAF43006.1; JOINED.
DR EMBL; AF219938; AAF43006.1; JOINED.
DR Genew; HGNC:2855; DGKI.
DR MIM; 604072; -.
DR GO; GO:0005737; C:cytoplasm; TAS.
DR GO; GO:0005634; C:nucleus; TAS.
DR GO; GO:0004143; F:diacylglycerol kinase activity; TAS.
DR InterPro; IPR002110; ANK.
DR InterPro; IPR002219; DAG_PE-bind.
DR InterPro; IPR000756; DAGKa.
DR InterPro; IPR001206; DAGKc.
DR Pfam; PF00023; ank; 2.
DR Pfam; PF00609; DAGKa; 1.
DR Pfam; PF00781; DAGKc; 1.
DR ProDom; PD002939; DAGKa; 1.
DR ProDom; PD005043; DAGKc; 1.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS00479; DAG_PE_BIND_DOM_1; FALSE_NEG.
DR PROSITE; PS50081; DAG_PE_BIND_DOM_2; FALSE_NEG.
KW Transferase; Kinase; ANK repeat; Repeat; Nuclear protein;
KW Multigene family; Polymorphism.
FT DOMAIN 178 232 PHORBOL-ESTER AND DAG BINDING 1.
FT DOMAIN 251 309 PHORBOL-ESTER AND DAG BINDING 2.
FT DOMAIN 374 500 CATALYTIC-A (POTENTIAL).
FT DOMAIN 526 683 CATALYTIC-B (POTENTIAL).
FT REPEAT 958 990 ANK 1.
FT REPEAT 997 1026 ANK 2.
FT DOMAIN 20 31 POLY-ALA.
FT DOMAIN 69 74 POLY-SER.
FT DOMAIN 95 102 POLY-ALA.
FT VARIANT 153 153 L -> F.
FT /FTId=VAR_010190.
FT CONFLICT 160 160 A -> P (in Ref. 2).
SQ SEQUENCE 1065 AA; 116996 MW; B84971AA7630A799 CRC64;
MDAAGRGCHL LPLPAARGPA RAPAAAAAAA ASPPGPCSGA ACAPSAAAGA GAMNPSSSAG
EEKGATGGSS SSGSGAGSCC LGAEGGADPR GAGSAAAAGA AALDEPAAAG QKEKDEALEE
KLRNLTFRKQ VSYRKAISRA GLQHLAPAHP LSLPVANGPA KEPRATLDWS ENAVNGEHLW
LETNVSGDLC YLGEENCQVR FAKSALRRKC AVCKIVVHTA CIEQLEKINF RCKPTFREGG
SRSPRENFVR HHWVHRRRQE GKCKQCGKGF QQKFSFHSKE IVAISCSWCK QAFHNKVTCF
MLHHIEEPCS LGAHAAVIVP PTWIIKVKKP QNSLKASNRK KKRTSFKRKA SKRGMEQENK
GRPFVIKPIS SPLMKPLLVF VNPKSGGNQG TKVLQMFMWY LNPRQVFDLS QEGPKDALEL
YRKVPNLRIL ACGGDGTVGW ILSILDELQL SPQPPVGVLP LGTGNDLART LNWGGGYTDE
PVSKILCQVE DGTVVQLDRW NLHVERNPDL PPEELEDGVC KLPLNVFNNY FSLGFDAHVT
LEFHESREAN PEKFNSRFRN KMFYAGAAFS DFLQRSSRDL SKHVKVVCDG TDLTPKIQEL
KFQCIVFLNI PRYCAGTMPW GNPGDHHDFE PQRHDDGYIE VIGFTMASLA ALQVGGHGER
LHQCREVMLL TYKSIPMQVD GEPCRLAPAM IRISLRNQAN MVQKSKRRTS MPLLNDPQSV
PDRLRIRVNK ISLQDYEGFH YDKEKLREAS ISDWLRTIAG ELVQSFGAIP LGILVVRGDC
DLETCRMYID RLQEDLQSVS SGSQRVHYQD HETSFPRALS AQRLSPRWCF LDDRSQEHLH
FVMEISQDEI FILDPDMVVS QPAGTPPGMP DLVVEQASGI SDWWNPALRK RMLSDSGLGM
IAPYYEDSDL KDLSHSRVLQ SPVSSEDHAI LQAVIAGDLM KLIESYKNGG SLLIQGPDHC
SLLHYAAKTG NGEIVKYILD HGPSELLDMA DSETGETALH KAACQRNRAV CQLLVDAGAS
LRKTDSKGKT PQERAQQAGD PDLAAYLESR QNYKVIGHED LETAV
//
ID KDGT_HUMAN STANDARD; PRT; 942 AA.
AC P52824;
DT 01-OCT-1996 (Rel. 34, Created)
DT 01-OCT-1996 (Rel. 34, Last sequence update)
DT 28-FEB-2003 (Rel. 41, Last annotation update)
DE Diacylglycerol kinase, theta (EC 2.7.1.107) (Diglyceride kinase) (DGK-
DE theta) (DAG kinase theta).
GN DGKQ OR DAGK4.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RX MEDLINE=95331799; PubMed=7607687;
RA Pilz A., Schaap D., Hunt D., Fitzgibbon J.;
RT "Chromosomal localization of three mouse diacylglycerol kinase (DAGK)
RT genes: genes sharing sequence homology to the Drosophila retinal
RT degeneration A (rdgA) gene.";
RL Genomics 26:599-601(1995).
CC -!- CATALYTIC ACTIVITY: ATP + 1,2-diacylglycerol = ADP + 1,2-
CC diacylglycerol 3-phosphate.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase
CC family.
CC -!- SIMILARITY: Contains 3 zinc-dependent phorbol-ester and DAG
CC binding domains.
CC -!- SIMILARITY: Contains 1 Ras-associating domain.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; L38707; AAA98749.1; -.
DR HSSP; P04049; 1FAR.
DR Genew; HGNC:2856; DGKQ.
DR MIM; 601207; -.
DR GO; GO:0004143; F:diacylglycerol kinase activity; TAS.
DR InterPro; IPR000756; DAGKa.
DR InterPro; IPR001206; DAGKc.
DR InterPro; IPR002219; DAG_PE-bind.
DR InterPro; IPR000159; RA_domain.
DR Pfam; PF00609; DAGKa; 1.
DR Pfam; PF00781; DAGKc; 1.
DR Pfam; PF00130; DAG_PE-bind; 3.
DR Pfam; PF00788; RA; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR ProDom; PD002939; DAGKa; 1.
DR ProDom; PD005043; DAGKc; 1.
DR SMART; SM00109; C1; 3.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SMART; SM00314; RA; 1.
DR PROSITE; PS00479; DAG_PE_BIND_DOM_1; 3.
DR PROSITE; PS50081; DAG_PE_BIND_DOM_2; 3.
DR PROSITE; PS50200; RA; 1.
KW Transferase; Kinase; Phorbol-ester binding; Repeat; Multigene family.
FT DOMAIN 61 108 PHORBOL-ESTER AND DAG BINDING 1.
FT DOMAIN 122 168 PHORBOL-ESTER AND DAG BINDING 2.
FT DOMAIN 184 234 PHORBOL-ESTER AND DAG BINDING 3.
FT DOMAIN 395 494 RAS-ASSOCIATING.
FT DOMAIN 586 715 CATALYTIC-A (POTENTIAL).
FT DOMAIN 741 893 CATALYTIC-B (POTENTIAL).
SQ SEQUENCE 942 AA; 101403 MW; 26F8D135B248477E CRC64;
MAAAAEPGAR AWLGGGSPRP GSPACSPVLG SGGRARPGPG PGPGRDRAGG VRARARAAPG
HSFRKVTLTK PTFCHLCSDF IWGLAGFLCD VCNFMSHEKC LKHVRIPCTS VAPSLVRVPV
AHCFGPRGLH KRKFCAVCRK VLEAPALHCE VCELHLHPDC VPFACSDCRQ CHQDGHQDHD
THHHHWREGN LPSGARCEVC RKTCGSSDVL AGVRCEWCGV QAHSLCSAAL APECGFGRLR
SLVLPPACVR LLPGGFSKTQ SFRIVEAAEP GEGGDGADGS AAVGPGRETQ ATPESGKQTL
KIFDGDDAVR RSQFRLVTVS RLAGAEEVLE AALRAHHIPE DPGHLELCRL PPSSQACDAW
AGGKAGSAVI SEEGRSPGSG EATPEAWVIR ALPRAQEVLK IYPGWLKVGV AYVSVRVTPK
STARSVVLEV LPLLGRQAES PESFQLVEVA MGCRHVQRTM LMDEQPLLDR LQDIRQMSVR
QVSQTRFYVA ESRDVAPHVS LFVGGLPPGL SPEEYSSLLH EAGATKATVV SVSHIYSSQG
AVVLDVACFA EAERLYMLLK DMAVRGRLLT ALVLPDLLHA KLPPDSCPLL VFVNPKSGGL
KGRDLLCSFR KLLNPHQVFD LTNGGPLPGL HLFSQVPCFR VLVCGGDGTV GWVLGALEET
RYRLACPEPS VAILPLGTGN DLGRVLRWGA GYSGEDPFSV LLSVDEADAV LMDRWTILLD
AHEAGSAEND TADAEPPKIV QMSNYCGIGI DAELSLDFHQ AREEEPGKFT SRLHNKGVYV
RVGLQKISHS RSLHKQIRLQ VERQEVELPS IEGLIFINIP SWGSGADLWG SDSDTRFEKP
RMDDGLLEVV GVTGVVHMGQ VQGGLRSGIR IAQGSYFRVT LLKATPVQVD GEPWVQAPGH
MIISAAGPKV HMLRKAKQKP RRAGTTRDAR ADRAPAPESD PR
//
ID KDGZ_HUMAN STANDARD; PRT; 1117 AA.
AC Q13574; O00542;
DT 01-NOV-1997 (Rel. 35, Created)
DT 16-OCT-2001 (Rel. 40, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE Diacylglycerol kinase, zeta (EC 2.7.1.107) (Diglyceride kinase) (DGK-
DE zeta) (DAG kinase zeta).
GN DGKZ OR DAGK6.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A. (ISOFORM SHORT).
RC TISSUE=Endothelial cells;
RX MEDLINE=96215319; PubMed=8626588;
RA Bunting M., Tang W., Zimmerman G.A., McIntyre T.M., Prescott S.M.;
RT "Molecular cloning and characterization of a novel human
RT diacylglycerol kinase zeta.";
RL J. Biol. Chem. 271:10230-10236(1996).
RN [2]
RP SEQUENCE FROM N.A. (ISOFORM LONG).
RC TISSUE=Skeletal muscle;
RX MEDLINE=97303161; PubMed=9159104;
RA Ding L., Bunting M., Topham M.K., McIntyre T.M., Zimmerman G.A.,
RA Prescott S.M.;
RT "Alternative splicing of the human diacylglycerol kinase zeta gene in
RT muscle.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:5519-5524(1997).
RN [3]
RP PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX MEDLINE=98379993; PubMed=9716136;
RA Topham M.K., Bunting M., Zimmerman G.A., McIntyre T.M.,
RA Blackshear P.J., Prescott S.M.;
RT "Protein kinase C regulates the nuclear localization of diacylglycerol
RT kinase-zeta.";
RL Nature 394:697-700(1998).
RN [4]
RP INTERACTION WITH SNTG1, AND MUTAGENESIS OF 1115-THR-ALA-1116.
RX MEDLINE=21336641; PubMed=11352924;
RA Hogan A., Shepherd L., Chabot J., Quenneville S., Prescott S.M.,
RA Topham M.K., Gee S.H.;
RT "Interaction of gamma 1-syntrophin with diacylglycerol kinase-zeta.
RT Regulation of nuclear localization by PDZ interactions.";
RL J. Biol. Chem. 276:26526-26533(2001).
CC -!- FUNCTION: Displays a strong preference for 1,2-diacylglycerols
CC over 1,3-diacylglycerols, but lacks substrate specificity among
CC molecular species of long chain diacylglycerols.
CC -!- CATALYTIC ACTIVITY: ATP + 1,2-diacylglycerol = ADP + 1,2-
CC diacylglycerol 3-phosphate.
CC -!- SUBUNIT: Interacts with the PDZ domain of the syntrophin SNTG1.
CC -!- SUBCELLULAR LOCATION: Nuclear and cytoplasmic.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=Q13574-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q13574-2; Sequence=VSP_001268;
CC -!- TISSUE SPECIFICITY: Highest levels in brain, and substantial
CC levels in skeletal muscle, heart, and pancreas.
CC -!- PTM: Phosphorylation of the MARCKS homology domain by PKC reduces
CC nuclear accumulation of DGK-zeta.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase
CC family.
CC -!- SIMILARITY: Contains 2 zinc-dependent phorbol-ester and DAG
CC binding domains.
CC -!- SIMILARITY: Contains 2 ANK repeats.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; U51477; AAC50478.1; -.
DR EMBL; U94905; AAB60859.1; -.
DR Genew; HGNC:2857; DGKZ.
DR MIM; 601441; -.
DR GO; GO:0005634; C:nucleus; TAS.
DR GO; GO:0005524; F:ATP binding; TAS.
DR GO; GO:0004143; F:diacylglycerol kinase activity; TAS.
DR GO; GO:0007165; P:signal transduction; TAS.
DR InterPro; IPR002110; ANK.
DR InterPro; IPR002219; DAG_PE-bind.
DR InterPro; IPR000756; DAGKa.
DR InterPro; IPR001206; DAGKc.
DR Pfam; PF00023; ank; 2.
DR Pfam; PF00609; DAGKa; 1.
DR Pfam; PF00781; DAGKc; 1.
DR ProDom; PD002939; DAGKa; 1.
DR ProDom; PD005043; DAGKc; 1.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS00479; DAG_PE_BIND_DOM_1; FALSE_NEG.
DR PROSITE; PS50081; DAG_PE_BIND_DOM_2; FALSE_NEG.
KW Transferase; Kinase; Phorbol-ester binding; Repeat; ANK repeat;
KW Nuclear protein; Multigene family; Phosphorylation;
KW Alternative splicing.
FT DOMAIN 287 341 PHORBOL-ESTER AND DAG BINDING 1.
FT DOMAIN 361 419 PHORBOL-ESTER AND DAG BINDING 2.
FT DOMAIN 448 462 MARCKS HOMOLOGY.
FT DOMAIN 482 608 CATALYTIC-A (POTENTIAL).
FT DOMAIN 635 792 CATALYTIC-B (POTENTIAL).
FT REPEAT 1011 1041 ANK 1.
FT REPEAT 1046 1075 ANK 2.
FT DOMAIN 256 261 POLY-PRO.
FT DOMAIN 448 451 POLY-LYS.
FT DOMAIN 560 563 POLY-PRO.
FT VARSPLIC 1 243 METFFRRHFRGKVPGPGEGQRRPSSVGLPTGKARRRSPAGQ
FT ASSSLAQRRRSSAQLQGCLLSCGVRAQGSSRRRSSTVPPSC
FT NPRFIVDKVLTPQPTTVGAQLLGAPLLLTGLVGMNEEEGVQ
FT EDVVAEASSAIQPGTKTPGPPPPRGAQPLLPLPRYVRRASS
FT HCCPADAVYDHALWGLHGYYRRLSQRRPSGQHPGPGGRRAS
FT GTTAGTMLPTRVRPLSRRRQVALRRKAAGPQAWSALLA ->
FT MEPRDGSPEARSSDSESASASSSGSERDAGPEPDKAPRRLN
FT KRRFPGLRLFGHR (in isoform Short).
FT /FTId=VSP_001268.
FT MUTAGEN 1115 1116 TA->NS: LOSS OF INTERACTION WITH SNTG1.
SQ SEQUENCE 1117 AA; 124122 MW; 213BC8ADDB4E1402 CRC64;
METFFRRHFR GKVPGPGEGQ RRPSSVGLPT GKARRRSPAG QASSSLAQRR RSSAQLQGCL
LSCGVRAQGS SRRRSSTVPP SCNPRFIVDK VLTPQPTTVG AQLLGAPLLL TGLVGMNEEE
GVQEDVVAEA SSAIQPGTKT PGPPPPRGAQ PLLPLPRYVR RASSHCCPAD AVYDHALWGL
HGYYRRLSQR RPSGQHPGPG GRRASGTTAG TMLPTRVRPL SRRRQVALRR KAAGPQAWSA
LLAKAITKSG LQHLAPPPPT PGAPCSESER QIRSTVDWSE SATYGEHIWF ETNVSGDFCY
VGEQYCVARM LKSVSRRKCA ACKIVVHTPC IEQLEKINFR CKPSFRESGS RNVREPTFVR
HHWVHRRRQD GKCRHCGKGF QQKFTFHSKE IVAISCSWCK QAYHSKVSCF MLQQIEEPCS
LGVHAAVVIP PTWILRARRP QNTLKASKKK KRASFKRKSS KKGPEEGRWR PFIIRPTPSP
LMKPLLVFVN PKSGGNQGAK IIQSFLWYLN PRQVFDLSQG GPKEALEMYR KVHNLRILAC
GGDGTVGWIL STLDQLRLKP PPPVAILPLG TGNDLARTLN WGGGYTDEPV SKILSHVEEG
NVVQLDRWDL HAEPNPEAGP EDRDEGATDR LPLDVFNNYF SLGFDAHVTL EFHESREANP
EKFNSRFRNK MFYAGTAFSD FLMGSSKDLA KHIRVVCDGM DLTPKIQDLK PQCVVFLNIP
RYCAGTMPWG HPGEHHDFEP QRHDDGYLEV IGFTMTSLAA LQVGGHGERL TQCREVVLTT
SKAIPVQVDG EPCKLAASRI RIALRNQATM VQKAKRRSAA PLHSDQQPVP EQLRIQVSRV
SMHDYEALHY DKEQLKEASV PLGTVVVPGD SDLELCRAHI ERLQQEPDGA GAKSPTCQKL
SPKWCFLDAT TASRFYRIDR AQEHLNYVTE IAQDEIYILD PELLGASARP DLPTPTSPLP
TSPCSPTPRS LQGDAAPPQG EELIEAAKRN DFCKLQELHR AGGDLMHRDE QSRTLLHHAV
STGSKDVVRY LLDHAPPEIL DAVEENGETC LHQAAALGQR TICHYIVEAG ASLMKTDQQG
DTPRQRAEKA QDTELAAYLE NRQHYQMIQR EDQETAV
//
ID KGUA_HUMAN STANDARD; PRT; 196 AA.
AC Q16774;
DT 01-NOV-1997 (Rel. 35, Created)
DT 01-NOV-1997 (Rel. 35, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE Guanylate kinase (EC 2.7.4.8) (GMP kinase).
GN GUK1 OR GMK.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RC TISSUE=Retina;
RX MEDLINE=96213684; PubMed=8647247;
RA Fitzgibbon J., Katsanis N., Wells D., Delhanty J., Vallins W.,
RA Hunt D.M.;
RT "Human guanylate kinase (GUK1): cDNA sequence, expression and
RT chromosomal localisation.";
RL FEBS Lett. 385:185-188(1996).
RN [2]
RP SEQUENCE FROM N.A.
RX MEDLINE=96279248; PubMed=8663313;
RA Brady W.A., Kokoris M.S., Fitzgibbon M., Black M.E.;
RT "Cloning, characterization, and modeling of mouse and human guanylate
RT kinases.";
RL J. Biol. Chem. 271:16734-16740(1996).
RN [3]
RP SEQUENCE FROM N.A.
RC TISSUE=Lung;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC -!- FUNCTION: Essential for recycling GMP and indirectly, cGMP.
CC -!- CATALYTIC ACTIVITY: ATP + GMP = ADP + GDP.
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SIMILARITY: Belongs to the guanylate kinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; L76200; AAC37598.1; -.
DR EMBL; U66895; AAC50659.1; -.
DR EMBL; BC006249; AAH06249.1; -.
DR EMBL; BC009914; AAH09914.1; -.
DR PIR; S68864; S68864.
DR HSSP; P15454; 1GKY.
DR Genew; HGNC:4693; GUK1.
DR GK; Q16774; -.
DR MIM; 139270; -.
DR GO; GO:0004385; F:guanylate kinase activity; TAS.
DR GO; GO:0006183; P:GTP biosynthesis; TAS.
DR InterPro; IPR008144; Guanylate_kin.
DR InterPro; IPR008145; Guanylt/Ca.
DR Pfam; PF00625; Guanylate_kin; 1.
DR SMART; SM00072; GuKc; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
KW Transferase; Kinase; ATP-binding; Acetylation.
FT INIT_MET 0 0 By similarity.
FT NP_BIND 10 17 ATP (By similarity).
FT MOD_RES 1 1 ACETYLATION (BY SIMILARITY).
SQ SEQUENCE 196 AA; 21594 MW; C4727A7E2AA261B3 CRC64;
SGPRPVVLSG PSGAGKSTLL KRLLQEHSGI FGFSVSHTTR NPRPGEENGK DYYFVTREVM
QRDIAAGDFI EHAEFSGNLY GTSKVAVQAV QAMNRICVLD VDLQGVRNIK ATDLRPIYIS
VQPPSLHVLE QRLRQRNTET EESLVKRLAA AQADMESSKE PGLFDVVIIN DSLDQAYAEL
KEALSEEIKK AQRTGA
//
ID KHK_HUMAN STANDARD; PRT; 298 AA.
AC P50053; Q99532; Q9BRJ3; Q9UMN1;
DT 01-OCT-1996 (Rel. 34, Created)
DT 01-OCT-1996 (Rel. 34, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Ketohexokinase (EC 2.7.1.3) (Hepatic fructokinase).
GN KHK.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A., VARIANTS FRUCTOSURIA ARG-40 AND THR-43, AND
RP VARIANT ILE-49.
RX MEDLINE=95135420; PubMed=7833921;
RA Bonthron D.T., Brady N., Donaldson I.A., Steinmann B.;
RT "Molecular basis of essential fructosuria: molecular cloning and
RT mutational analysis of human ketohexokinase (fructokinase).";
RL Hum. Mol. Genet. 3:1627-1631(1994).
RN [2]
RP SEQUENCE FROM N.A.
RC TISSUE=Lung;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [3]
RP SEQUENCE OF 1-26 AND 71-298 FROM N.A., AND ALTERNATIVE SPLICING.
RX MEDLINE=99013450; PubMed=9799106;
RA Hayward B.E., Bonthron D.T.;
RT "Structure and alternative splicing of the ketohexokinase gene.";
RL Eur. J. Biochem. 257:85-91(1998).
CC -!- CATALYTIC ACTIVITY: ATP + D-fructose = ADP + D-fructose 1-
CC phosphate.
CC -!- ENZYME REGULATION: Requires potassium. Inhibition by ADP.
CC -!- PATHWAY: Primary metabolism of dietary fructose in mammals.
CC -!- SUBUNIT: DIMER OF A-A, A-C OR C-C (PROBABLE).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=P50053-1; Sequence=Displayed;
CC Name=C;
CC IsoId=P50053-2; Sequence=VSP_004669;
CC -!- TISSUE SPECIFICITY: Most abundant in liver, kidney, gut, spleen
CC and pancreas. Low levels also found in adrenal, muscle, brain and
CC eye.
CC -!- DISEASE: Defects in KHK are the cause of fructosuria [MIM:229800].
CC Fructosuria is a benign defect of intermediary metabolism.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase pfkB family.
CC -!- CAUTION: Form C has not yet been fully sequenced in its N-terminal
CC (from 1-69).
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; X78678; CAA55347.1; -.
DR EMBL; X78677; CAA55346.1; -.
DR EMBL; BC006233; AAH06233.1; -.
DR EMBL; Y09336; CAA70516.1; -.
DR EMBL; Y09341; CAA70522.1; -.
DR EMBL; Y09341; CAA70523.1; -.
DR EMBL; Y09340; CAA70521.1; -.
DR EMBL; AJ005168; CAA06409.1; -.
DR Genew; HGNC:6315; KHK.
DR GK; P50053; -.
DR MIM; 229800; -.
DR GO; GO:0004454; F:ketohexokinase activity; TAS.
DR InterPro; IPR002173; PfkB.
DR Pfam; PF00294; pfkB; 1.
DR PROSITE; PS00583; PFKB_KINASES_1; FALSE_NEG.
DR PROSITE; PS00584; PFKB_KINASES_2; FALSE_NEG.
KW Transferase; Kinase; Alternative splicing; Disease mutation;
KW Polymorphism.
FT VARSPLIC 72 115 VLDDLRRYSVDLRYTVFQTTGSVPIATVIINEASGSRTILY
FT YDR -> LVADFRRRGVDVSQVAWQSKGDTPSSCCIINNSN
FT GNRTIVLHDT (in isoform C).
FT /FTId=VSP_004669.
FT VARIANT 40 40 G -> R (in fructosuria).
FT /FTId=VAR_006072.
FT VARIANT 43 43 A -> T (in fructosuria).
FT /FTId=VAR_006073.
FT VARIANT 49 49 V -> I.
FT /FTId=VAR_006074.
FT VARIANT 159 159 R -> G (either a polymorphism or a
FT cloning artifact).
FT /FTId=VAR_006075.
SQ SEQUENCE 298 AA; 32730 MW; 1BA47BDC60C1B89F CRC64;
MEEKQILCVG LVVLDVISLV DKYPKEDSEI RCLSQRWQRG GNASNSCTVL SLLGAPCAFM
GSMAPGHVAD FVLDDLRRYS VDLRYTVFQT TGSVPIATVI INEASGSRTI LYYDRSLPDV
SATDFEKVDL TQFKWIHIEG RNASEQVKML QRIDAHNTRQ PPEQKIRVSV EVEKPREELF
QLFGYGDVVF VSKDVAKHLG FQSAEEALRG LYGRVRKGAV LVCAWAEEGA DALGPDGKLL
HSDAFPPPRV VDTLGAGDTF NASVIFSLSQ GRSVQEALRF GCQVAGKKCG LQGFDGIV
//
ID KICE_HUMAN STANDARD; PRT; 395 AA.
AC Q9Y259; Q13388;
DT 30-MAY-2000 (Rel. 39, Created)
DT 30-MAY-2000 (Rel. 39, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE Choline/ethanolamine kinase [Includes: Choline kinase (EC 2.7.1.32)
DE (CK); Ethanolamine kinase (EC 2.7.1.82) (EK)].
GN CHKL OR CHETK.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RA Yamazaki N.;
RT "Human gene for choline/ethanolamine kinase.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SEQUENCE FROM N.A.
RA Smink L.J., Huckle E.J.;
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SEQUENCE FROM N.A.
RA Adams M.D.;
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY: ATP + choline = ADP + O-phosphocholine.
CC -!- CATALYTIC ACTIVITY: ATP + ethanolamine = ADP + O-
CC phosphoethanolamine.
CC -!- SIMILARITY: Belongs to the choline/ethanolamine kinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AB029885; BAA82511.1; -.
DR EMBL; AB029886; BAA82512.1; -.
DR EMBL; AL096780; CAB46629.1; -.
DR EMBL; AL096781; CAB46630.1; -.
DR EMBL; U62317; AAB03342.2; -.
DR Genew; HGNC:1938; CHKL.
DR InterPro; IPR002573; Choline_kinase.
DR Pfam; PF01633; Choline_kinase; 1.
KW Transferase; Kinase.
FT ACT_SITE 240 240 By similarity.
SQ SEQUENCE 395 AA; 45271 MW; 18367468B22FB9CE CRC64;
MAAEATAVAG SGAVGGCLAK DGLQQSKCPD TTPKRRRASS LSRDAERRAY QWCREYLGGA
WRRVQPEELR VYPVSGGLSN LLFRCSLPDH LPSVGEEPRE VLLRLYGAIL QGVDSLVLES
VMFAILAERS LGPQLYGVFP EGRLEQYIPS RPLKTQELRE PVLSAAIATK MAQFHGMEMP
FTKEPHWLFG TMERYLKQIQ DLPPTGLPEM NLLEMYSLKD EMGNLRKLLE STPSPVVFCH
NDIQEGNILL LSEPENADSL MLVDFEYSSY NYRGFDIGNH FCEWVYDYTH EEWPFYKARP
TDYPTQEQQL HFIRHYLAEA KKGETLSQEE QRKLEEDLLV EVSRYALASH FFWGLWSILQ
ASMSTIEFGY LDYAQSRFQF YFQQKGQLTS VHSSS
//
ID KICH_HUMAN STANDARD; PRT; 456 AA.
AC P35790;
DT 01-JUN-1994 (Rel. 29, Created)
DT 01-JUN-1994 (Rel. 29, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Choline kinase (EC 2.7.1.32) (CK) (CHETK-alpha).
GN CHK OR CKI.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RX MEDLINE=92316236; PubMed=1618328;
RA Hosaka K., Tanaka S., Nikawa J.-I., Yamashita S.;
RT "Cloning of a human choline kinase cDNA by complementation of the
RT yeast cki mutation.";
RL FEBS Lett. 304:229-232(1992).
CC -!- FUNCTION: May have a regulatory role in phosphatidylcholine
CC synthesis.
CC -!- CATALYTIC ACTIVITY: ATP + choline = ADP + O-phosphocholine.
CC -!- PATHWAY: CDP-choline and CDP-ethanolamine pathways; initial step.
CC -!- SUBUNIT: Homotetramer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasmic.
CC -!- SIMILARITY: Belongs to the choline/ethanolamine kinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; D10704; BAA01547.1; -.
DR PIR; S23104; S23104.
DR Genew; HGNC:1937; CHK.
DR MIM; 118491; -.
DR GO; GO:0004103; F:choline kinase activity; TAS.
DR GO; GO:0004871; F:signal transducer activity; TAS.
DR GO; GO:0006629; P:lipid metabolism; TAS.
DR GO; GO:0006869; P:lipid transport; TAS.
DR InterPro; IPR002573; Choline_kinase.
DR Pfam; PF01633; Choline_kinase; 1.
KW Transferase; Kinase.
FT DOMAIN 50 84 PRO-RICH.
FT ACT_SITE 303 303 By similarity.
SQ SEQUENCE 456 AA; 52065 MW; BD8D13D102178E97 CRC64;
MKTKFCTGGE AEPSPLGLLL SCGSGSAAPA PGVGQQRDAA SDLESKQLAP TAALALPPPP
PLPLPLPLPQ PPPPQPPADE QPEPRARRRA YLWCKEFLPG AWRGLREDEF HISVIRGGLS
NMLFQCSLPD TTATLGDEPR KVLLRLYGAI LQMRSCNKEG SEQAQKENEF QGAEAMVLES
VMFAILAERS LGPKLYGIFP QGRLEQFIPS RRLDTEELSL PDISAEIAEK MATFHGMKMP
FNKEPKWLFG TMEKYLKEVL RIKFTEESRI KKLHKLLSYN LPLELENLRS LLESTPSPVV
FCHNDCQEGN ILLLEGRENS EKQKLMLIDF EYSSYNYRGF DIGNHFCEWM YDYSYEKYPF
FRANIRKYPT KKQQLHFISS YLPAFQNDFE NLSTEEKSII KEEMLLEVNR FALASHFLWG
LWSIVQAKIS SIEFGYMDYA QARFDAYFHQ KRKLGV
//
ID KIME_HUMAN STANDARD; PRT; 396 AA.
AC Q03426;
DT 01-OCT-1993 (Rel. 27, Created)
DT 01-OCT-1993 (Rel. 27, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Mevalonate kinase (EC 2.7.1.36) (MK).
GN MVK.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A., AND VARIANT THR-301.
RX MEDLINE=92317034; PubMed=1377680;
RA Schafer B.L., Bishop R.W., Kratunis V.J., Kalinowski S.S.,
RA Mosley S.T., Gibson K.M., Tanaka R.D.;
RT "Molecular cloning of human mevalonate kinase and identification of a
RT missense mutation in the genetic disease mevalonic aciduria.";
RL J. Biol. Chem. 267:13229-13238(1992).
RN [2]
RP SEQUENCE FROM N.A.
RC TISSUE=Hepatoma;
RX MEDLINE=94134441; PubMed=8302606;
RA Graef E., Caselmann W.H., Wells J., Koshy R.;
RT "Insertional activation of mevalonate kinase by hepatitis B virus DNA
RT in a human hepatoma cell line.";
RL Oncogene 9:81-87(1994).
RN [3]
RP SEQUENCE FROM N.A., VARIANTS HIDS PRO-20; PRO-39; LEU-135; THR-148;
RP THR-268 AND ILE-377, AND VARIANTS MEVALONICACIDURIA PRO-20; PHE-264;
RP THR-268; THR-334 AND MET-310.
RX MEDLINE=21214737; PubMed=11313768;
RA Houten S.M., Koster J., Romeijn G.-J., Frenkel J., Di Rocco M.,
RA Caruso U., Landrieu P., Kelley R.I., Kuis W., Poll-The B.T.,
RA Gibson K.M., Wanders R.J.A., Waterham H.R.;
RT "Organization of the mevalonate kinase (MVK) gene and identification
RT of novel mutations causing mevalonic aciduria and
RT hyperimmunoglobulinaemia D and periodic fever syndrome.";
RL Eur. J. Hum. Genet. 9:253-259(2001).
RN [4]
RP SEQUENCE FROM N.A.
RC TISSUE=Skin;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [5]
RP VARIANTS MEVALONICACIDURIA ILE-243; PHE-264; PRO-265 AND THR-268.
RX MEDLINE=99347937; PubMed=10417275;
RA Hinson D.D., Ross R.M., Krisans S., Shaw J.L., Kozich V.,
RA Rolland M.-O., Divry P., Mancini J., Hoffmann G.F., Gibson K.M.;
RT "Identification of a mutation cluster in mevalonate kinase deficiency,
RT including a new mutation in a patient of Mennonite ancestry.";
RL Am. J. Hum. Genet. 65:327-335(1999).
RN [6]
RP VARIANTS MEVALONICACIDURIA MET-310 AND THR-334.
RX MEDLINE=99330561; PubMed=10401001;
RA Houten S.M., Romeijn G.J., Koster J., Gray R.G.F., Darbyshire P.,
RA Smit G.P.A., de Klerk J.B.C., Duran R., Gibson K.M., Wanders R.J.A.,
RA Waterham H.R.;
RT "Identification and characterization of three novel missense mutations
RT in mevalonate kinase cDNA causing mevalonic aciduria, a disorder of
RT isoprene biosynthesis.";
RL Hum. Mol. Genet. 8:1523-1528(1999).
RN [7]
RP VARIANTS HIDS PRO-20; THR-268 AND ILE-377.
RX MEDLINE=99295935; PubMed=10369261;
RA Houten S.M., Kuis W., Duran M., de Koning T.J., van Royen-Kerkhof A.,
RA Romeijn G.J., Frenkel J., Dorland L., de Barse M.M.J.,
RA Huijbers W.A.R., Rijkers G.T., Waterham H.R., Wanders R.J.A.,
RA Poll-The B.T.;
RT "Mutations in MVK, encoding mevalonate kinase, cause
RT hyperimmunoglobulinaemia D and periodic fever syndrome.";
RL Nat. Genet. 22:175-177(1999).
RN [8]
RP VARIANTS HIDS LEU-167; THR-268 AND ILE-377.
RX MEDLINE=99295936; PubMed=10369262;
RA Drenth J.P.H., Cuisset L., Grateau G., Vasseur C.,
RA van der Velde-Visser S.D., de Jong J.G.N., Beckmann J.S.,
RA van der Meer J.W.M., Delpech M.;
RT "Mutations in the gene encoding mevalonate kinase cause hyper-IgD and
RT periodic fever syndrome.";
RL Nat. Genet. 22:178-181(1999).
RN [9]
RP VARIANTS HIDS ASN-20; PRO-20; PRO-39; LEU-150; LEU-167; ARG-202;
RP GLN-215; THR-268; SER-309; ARG-326 AND ILE-377, VARIANT
RP MEVALONICACIDURIA THR-334, AND VARIANT ASN-52.
RX MEDLINE=21214738; PubMed=11313769;
RA Cuisset L., Drenth J.P.H., Simon A., Vincent M.F.,
RA van der Velde-Visser S.D., van der Meer J.W.M., Grateau G.,
RA Delpech M.;
RT "Molecular analysis of MVK mutations and enzymatic activity in
RT hyper-IgD and periodic fever syndrome.";
RL Eur. J. Hum. Genet. 9:260-266(2001).
CC -!- FUNCTION: May be a regulatory site in cholesterol biosynthetic
CC pathway.
CC -!- CATALYTIC ACTIVITY: ATP + (R)-mevalonate = ADP + (R)-5-
CC phosphomevalonate.
CC -!- ENZYME REGULATION: Farnesyl- and geranyl-pyrophosphates are
CC competitive inhibitors.
CC -!- PATHWAY: Cholesterol biosynthesis, mevalonate catabolism.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic and peroxisomal.
CC -!- DISEASE: Defects in MVK are the cause of mevalonicaciduria
CC [MIM:251170]. It is an accumulation of mevalonic acid which cause
CC a variety of symptoms such as psychomotor retardation, dysmorphic
CC features, cataracts, hepatosplenomegaly, lymphadenopathy, anemia,
CC hypotonia, myopathy, and ataxia.
CC -!- DISEASE: Defects in MVK are the cause of hyperimmunoglobulinemia D
CC and periodic fever syndrome (HIDS) [MIM:260920]. HIDS is an
CC autosomal recessive disease characterized by recurrent epidoses of
CC unexplained high fever associated with skin rash, diarrhea,
CC adenopathy (swollen, tender lymph nodes), athralgias and/or
CC arthritis. Concentration of IgD, and often IgA, are above normal.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. Mevalonate kinase
CC subfamily.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; M88468; AAB59362.1; -.
DR EMBL; X75311; CAA53060.1; -.
DR EMBL; X75311; CAA53059.1; ALT_INIT.
DR EMBL; AF217535; AAF82407.1; -.
DR EMBL; AF217528; AAF82407.1; JOINED.
DR EMBL; AF217529; AAF82407.1; JOINED.
DR EMBL; AF217530; AAF82407.1; JOINED.
DR EMBL; AF217531; AAF82407.1; JOINED.
DR EMBL; AF217532; AAF82407.1; JOINED.
DR EMBL; AF217533; AAF82407.1; JOINED.
DR EMBL; AF217534; AAF82407.1; JOINED.
DR EMBL; BC016140; AAH16140.1; -.
DR PIR; A42919; A42919.
DR Genew; HGNC:7530; MVK.
DR MIM; 251170; -.
DR MIM; 260920; -.
DR GO; GO:0004496; F:mevalonate kinase activity; TAS.
DR GO; GO:0008299; P:isoprenoid biosynthesis; TAS.
DR InterPro; IPR001174; Galkinase.
DR InterPro; IPR006204; GHMP_kinase.
DR InterPro; IPR006203; GHMPknse_ATP.
DR InterPro; IPR006205; Mev_gal_kin.
DR InterPro; IPR006206; Mev_galkinase.
DR Pfam; PF00288; GHMP_kinases; 1.
DR PRINTS; PR00960; LMBPPROTEIN.
DR PRINTS; PR00959; MEVGALKINASE.
DR TIGRFAMs; TIGR00549; mevalon_kin; 1.
DR PROSITE; PS00627; GHMP_KINASES_ATP; 1.
KW Transferase; Kinase; Cholesterol biosynthesis; ATP-binding;
KW Peroxisome; Disease mutation; Polymorphism.
FT NP_BIND 138 148 ATP (By similarity).
FT VARIANT 20 20 H -> N (in HIDS).
FT /FTId=VAR_010956.
FT VARIANT 20 20 H -> P (in HIDS and mevalonicaciduria).
FT /FTId=VAR_004022.
FT VARIANT 39 39 L -> P (in HIDS).
FT /FTId=VAR_010957.
FT VARIANT 52 52 S -> N.
FT /FTId=VAR_010958.
FT VARIANT 135 135 S -> L (in HIDS).
FT /FTId=VAR_010959.
FT VARIANT 148 148 A -> T (in HIDS).
FT /FTId=VAR_010960.
FT VARIANT 150 150 S -> L (in HIDS).
FT /FTId=VAR_010961.
FT VARIANT 167 167 P -> L (in HIDS).
FT /FTId=VAR_004023.
FT VARIANT 202 202 G -> R (in HIDS).
FT /FTId=VAR_010962.
FT VARIANT 215 215 R -> Q (in HIDS).
FT /FTId=VAR_010963.
FT VARIANT 243 243 T -> I (in mevalonicaciduria).
FT /FTId=VAR_010964.
FT VARIANT 264 264 L -> F (in mevalonicaciduria).
FT /FTId=VAR_010965.
FT VARIANT 265 265 L -> P (in mevalonicaciduria).
FT /FTId=VAR_010966.
FT VARIANT 268 268 I -> T (in HIDS and mevalonicaciduria).
FT /FTId=VAR_004024.
FT VARIANT 301 301 N -> T (in mevalonicaciduria; diminished
FT activity).
FT /FTId=VAR_004025.
FT VARIANT 309 309 G -> S (in HIDS).
FT /FTId=VAR_010967.
FT VARIANT 310 310 V -> M (in mevalonicaciduria).
FT /FTId=VAR_009068.
FT VARIANT 326 326 G -> R (in HIDS).
FT /FTId=VAR_010968.
FT VARIANT 334 334 A -> T (in mevalonicaciduria).
FT /FTId=VAR_004026.
FT VARIANT 377 377 V -> I (in HIDS; most frequent mutation).
FT /FTId=VAR_004027.
SQ SEQUENCE 396 AA; 42451 MW; C8F6B629B58CD229 CRC64;
MLSEVLLVSA PGKVILHGEH AVVHGKVALA VSLNLRTFLR LQPHSNGKVD LSLPNIGIKR
AWDVARLQSL DTSFLEQGDV TTPTSEQVEK LKEVAGLPDD CAVTERLAVL AFLYLYLSIC
RKQRALPSLD IVVWSELPPG AGLGSSAAYS VCLAAALLTV CEEIPNPLKD GDCVNRWTKE
DLELINKWAF QGERMIHGNP SGVDNAVSTW GGALRYHQGK ISSLKRSPAL QILLTNTKVP
RNTRALVAGV RNRLLKFPEI VAPLLTSIDA ISLECERVLG EMGEAPAPEQ YLVLEELIDM
NQHHLNALGV GHASLDQLCQ VTRARGLHSK LTGAGGGGCG ITLLKPGLEQ PEVEATKQAL
TSCGFDCLET SIGAPGVSIH SATSLDSRVQ QALDGL
//
ID KITH_EBV STANDARD; PRT; 607 AA.
AC P03177;
DT 21-JUL-1986 (Rel. 01, Created)
DT 01-NOV-1995 (Rel. 32, Last sequence update)
DT 30-MAY-2000 (Rel. 39, Last annotation update)
DE Thymidine kinase (EC 2.7.1.21).
GN TK OR BXLF1.
OS Epstein-barr virus (strain B95-8) (Human herpesvirus 4).
OC Viruses; dsDNA viruses, no RNA stage; Herpesviridae;
OC Gammaherpesvirinae; Lymphocryptovirus.
OX NCBI_TaxID=10377;
RN [1]
RP SEQUENCE FROM N.A.
RX MEDLINE=85035713; PubMed=6092825;
RA Bankier A.T., Deininger P.L., Farrell P.J., Barrell B.G.;
RT "Sequence analysis of the 17,166 base-pair EcoRI fragment C of B95-8
RT Epstein-Barr virus.";
RL Mol. Biol. Med. 1:21-45(1983).
RN [2]
RP IDENTIFICATION OF PROTEIN.
RX MEDLINE=87004565; PubMed=3019675;
RA Littler E., Zeuthen J., McBride A.A., Soerensen E.T., Powell K.L.,
RA Walsh-Arrand J.E., Arrand J.R.;
RT "Identification of an Epstein-Barr virus-coded thymidine kinase.";
RL EMBO J. 5:1959-1966(1986).
CC -!- CATALYTIC ACTIVITY: ATP + thymidine = ADP + thymidine 5'-
CC phosphate.
CC -!- SIMILARITY: Belongs to the herpesviruses thymidine kinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; V01555; CAA24799.1; -.
DR PIR; A00615; KIBETE.
DR InterPro; IPR001889; TK_herpes.
DR Pfam; PF00693; TK_herpes; 1.
DR ProDom; PD001519; TK_herpes; 1.
KW Transferase; Kinase; DNA synthesis; Early protein; ATP-binding.
FT NP_BIND 291 298 ATP (Probable).
SQ SEQUENCE 607 AA; 67193 MW; 97A4CCDB598A09F1 CRC64;
MAGFPGKEAG PPGGWRKCQE DESPENERHE NFYAEIDDFA PSVLTPTGSD SGAGEEDDDG
LYQVPTHWPP LMAPTGLSGE RVPCRTQAAV TSNTGNSPGS RHTSCPFTLP RGAQPPAPAH
QKPTAPTPKP RSRECGPSKT PDPFSWFRKT SCTEGGADST SRSFMYQKGF EEGLAGLGLD
DKSDCESEDE SNFRRPSSHS ALKQKNGGKG KPSGLFEHLA AHGREFSKLS KHAAQLKRLS
GSVMNVLNLD DAQDTRQAKA QRKESMRVPI VTHLTNHVPV IKPACSLFLE GAPGVGKTTM
LNHLKAVFGD LTIVVPEPMR YWTHVYENAI KAMHKNVTRA RHGREDTSAE VLACQMKFTT
PFRVLASRKR SLLVTESGAR SVAPLDCWIL HDRHLLSASV VFPLMLLRSQ LLSYSDFIQV
LATFTADPGD TIVWMKLNVE ENMRRLKKRG RKHESGLDAG YLKSVNDAYH AVYCAWLLTQ
YFAPEDIVKV CAGLTTITTV CHQSHTPIIR SGVAEKLYKN SIFSVLKEVI QPFRADAVLL
EVCLAFTRTL AYLQFVLVDL SEFQDDLPGC WTEIYMQALK NPAIRSQFFD WAGLSKVISD
FERGNRD
//
ID KITH_HUMAN STANDARD; PRT; 234 AA.
AC P04183; Q969V0;
DT 20-MAR-1987 (Rel. 04, Created)
DT 28-FEB-2003 (Rel. 41, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Thymidine kinase, cytosolic (EC 2.7.1.21).
GN TK1.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RX MEDLINE=85085935; PubMed=6549046;
RA Bradshaw H.D. Jr., Deininger P.L.;
RT "Human thymidine kinase gene: molecular cloning and nucleotide
RT sequence of a cDNA expressible in mammalian cells.";
RL Mol. Cell. Biol. 4:2316-2320(1984).
RN [2]
RP SEQUENCE FROM N.A.
RX MEDLINE=87277399; PubMed=3301530;
RA Flemington E., Bradshaw H.D. Jr., Traina-Dorge V., Slagel V.,
RA Deininger P.L.;
RT "Sequence, structure and promoter characterization of the human
RT thymidine kinase gene.";
RL Gene 52:267-277(1987).
RN [3]
RP SEQUENCE FROM N.A.
RC TISSUE=Lymph, and Uterus;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [4]
RP PHOSPHORYLATION OF SER-13.
RX MEDLINE=98241568; PubMed=9575153;
RA Chang Z.F., Huang D.Y., Chi L.M.;
RT "Serine 13 is the site of mitotic phosphorylation of human thymidine
RT kinase.";
RL J. Biol. Chem. 273:12095-12100(1998).
CC -!- CATALYTIC ACTIVITY: ATP + thymidine = ADP + thymidine 5'-
CC phosphate.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic.
CC -!- PTM: Phosphorylated on Ser-13 in mitosis.
CC -!- MISCELLANEOUS: Two forms have been identified in animal cells, one
CC in cytosol and one in mitochondria. Activity of the cytosolic
CC enzyme is high in proliferating cells and peaks during the S-phase
CC of the cell cycle; it is very low in resting cells.
CC -!- SIMILARITY: Belongs to the thymidine kinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; K02581; AAA61187.1; -.
DR EMBL; M15205; AAA61191.1; -.
DR EMBL; BC007872; AAH07872.1; -.
DR EMBL; BC007986; AAH07986.1; -.
DR PIR; A27318; KIHUT.
DR Genew; HGNC:11830; TK1.
DR GK; P04183; -.
DR MIM; 188300; -.
DR GO; GO:0004797; F:thymidine kinase activity; TAS.
DR GO; GO:0006139; P:nucleobase, nucleoside, nucleotide and nucl...; TAS.
DR InterPro; IPR001267; TK_cell.
DR Pfam; PF00265; TK; 1.
DR PROSITE; PS00603; TK_CELLULAR_TYPE; 1.
KW Transferase; Kinase; DNA synthesis; ATP-binding; Phosphorylation.
FT NP_BIND 26 33 ATP (Probable).
FT MOD_RES 13 13 PHOSPHORYLATION.
FT CONFLICT 106 106 V -> M (in Ref. 1 and 2).
SQ SEQUENCE 234 AA; 25468 MW; 76901415C631EF21 CRC64;
MSCINLPTVL PGSPSKTRGQ IQVILGPMFS GKSTELMRRV RRFQIAQYKC LVIKYAKDTR
YSSSFCTHDR NTMEALPACL LRDVAQEALG VAVIGIDEGQ FFPDIVEFCE AMANAGKTVI
VAALDGTFQR KPFGAILNLV PLAESVVKLT AVCMECFREA AYTKRLGTEK EVEVIGGADK
YHSVCRLCYF KKASGQPAGP DNKENCPVPG KPGEAVAARK LFAPQQILQC SPAN
//
ID KITM_HUMAN STANDARD; PRT; 266 AA.
AC O00142; O15238;
DT 01-NOV-1997 (Rel. 35, Created)
DT 28-FEB-2003 (Rel. 41, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Thymidine kinase 2, mitochondrial precursor (EC 2.7.1.21) (Mt-TK).
GN TK2.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A. (ISOFORM SHORT).
RC TISSUE=Liver;
RX MEDLINE=97236800; PubMed=9079672;
RA Johansson M., Karlsson A.;
RT "Cloning of the cDNA and chromosome localization of the gene for
RT human thymidine kinase 2.";
RL J. Biol. Chem. 272:8454-8458(1997).
RN [2]
RP SEQUENCE FROM N.A. (ISOFORM LONG), AND REVISIONS TO 37 AND 240-241.
RA Wang L.;
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SEQUENCE OF 34-266 FROM N.A. (ISOFORM LONG), SEQUENCE OF 34-61
RP (ISOFORM LONG), AND CHARACTERIZATION.
RC TISSUE=Brain;
RX MEDLINE=99142705; PubMed=9989599;
RA Wang L., Munch-Petersen B., Herrstroem Sjoeberg A., Hellman U.,
RA Bergman T., Joernvall H., Eriksson S.;
RT "Human thymidine kinase 2: molecular cloning and characterisation of
RT the enzyme activity with antiviral and cytostatic nucleoside
RT substrates.";
RL FEBS Lett. 443:170-174(1999).
CC -!- FUNCTION: Deoxyribonucleoside kinase that phosphorylates
CC thymidine, deoxycytidine, and deoxyuridine. Also phosphorylates
CC anti-viral and anti-cancer nucleoside analogs.
CC -!- CATALYTIC ACTIVITY: ATP + thymidine = ADP + thymidine 5'-
CC phosphate.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Mitochondrial.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=O00142-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=O00142-2; Sequence=VSP_003028;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in liver, pancreas,
CC muscle, and brain.
CC -!- SIMILARITY: Belongs to the DCK/DGK family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; U77088; AAC51167.1; -.
DR EMBL; Y10498; CAA71523.3; -.
DR Genew; HGNC:11831; TK2.
DR MIM; 188250; -.
DR GO; GO:0004797; F:thymidine kinase activity; TAS.
DR GO; GO:0006139; P:nucleobase, nucleoside, nucleotide and nucl...; TAS.
DR InterPro; IPR002624; dNK.
DR Pfam; PF01712; dNK; 1.
KW Transferase; Kinase; DNA synthesis; ATP-binding; Mitochondrion;
KW Transit peptide; Alternative splicing.
FT TRANSIT 1 33 Mitochondrion.
FT CHAIN 34 266 THYMIDINE KINASE 2.
FT NP_BIND 57 64 ATP (Potential).
FT VARSPLIC 1 41 MLLWPLRGWAARALRCFGPGSRGSPASGPGPRRVQRRAWPP
FT -> MGAFCQRPSS (in isoform Short).
FT /FTId=VSP_003028.
FT CONFLICT 61 61 S -> G (in Ref. 1).
FT CONFLICT 241 241 Missing (in Ref. 1).
SQ SEQUENCE 266 AA; 31142 MW; 5387470F210F8695 CRC64;
MLLWPLRGWA ARALRCFGPG SRGSPASGPG PRRVQRRAWP PDKEQEKEKK SVICVEGNIA
SGKTTCLEFF SNATDVEVLT EPVSKWRNVR GHNPLGLMYH DASRWGLTLQ TYVQLTMLDR
HTRPQVSSVR LMERSIHSAR YIFVENLYRS GKMPEVDYVV LSEWFDWILR NMDVSVDLIV
YLRTNPETCY QRLKKRCREE EKVIPLEYLE AIHHLHEEWL IKGSLFPMAA PVLVIEADHH
HMERMLELFE QNRDRILTPE NRKHCP
//
ID KPR1_HUMAN STANDARD; PRT; 317 AA.
AC P09329;
DT 01-MAR-1989 (Rel. 10, Created)
DT 01-OCT-1989 (Rel. 12, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Ribose-phosphate pyrophosphokinase I (EC 2.7.6.1) (Phosphoribosyl
DE pyrophosphate synthetase I) (PPRibP) (PRS-I).
GN PRPS1.
OS Homo sapiens (Human), and
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606, 10116;
RN [1]
RP SEQUENCE FROM N.A.
RC SPECIES=Human; TISSUE=Lymphoblast;
RX MEDLINE=90174926; PubMed=2155397;
RA Roessler B.J., Bell G., Heidler S., Seino S., Becker M., Palella T.D.;
RT "Cloning of two distinct copies of human phosphoribosylpyrophosphate
RT synthetase cDNA.";
RL Nucleic Acids Res. 18:193-193(1990).
RN [2]
RP SEQUENCE FROM N.A.
RC SPECIES=Human;
RX MEDLINE=91324322; PubMed=1650777;
RA Sonoda T., Taira M., Ishijima S., Ishizuka T., Iizaka T., Tatibana M.;
RT "Complete nucleotide sequence of human phosphoribosyl pyrophosphate
RT synthetase subunit I (PRS I) cDNA and a comparison with human and rat
RT PRPS gene families.";
RL J. Biochem. 109:361-364(1991).
RN [3]
RP SEQUENCE FROM N.A.
RC SPECIES=Human; TISSUE=Lymph;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [4]
RP SEQUENCE FROM N.A.
RC SPECIES=Rat; TISSUE=Liver;
RX MEDLINE=88033052; PubMed=2822704;
RA Taira M., Ishijima S., Kita K., Yamada K., Iizasa T., Tatibana M.;
RT "Nucleotide and deduced amino acid sequences of two distinct cDNAs
RT for rat phosphoribosylpyrophosphate synthetase.";
RL J. Biol. Chem. 262:14867-14870(1987).
RN [5]
RP SEQUENCE FROM N.A.
RC SPECIES=Rat;
RX MEDLINE=90067855; PubMed=2555779;
RA Ishijima S., Taira M., Tatibana M.;
RT "Complete cDNA sequence of rat phosphoribosylpyrophosphate synthetase
RT subunit I (PRS I).";
RL Nucleic Acids Res. 17:8860-8860(1989).
RN [6]
RP SEQUENCE FROM N.A.
RC SPECIES=Rat;
RX MEDLINE=90154083; PubMed=2154494;
RA Shimada H., Taira M., Yamada K., Iizasa T., Tatibana M.;
RT "Structure of the rat PRPS1 gene encoding phosphoribosylpyrophosphate
RT synthetase subunit I.";
RL J. Biol. Chem. 265:3956-3960(1990).
RN [7]
RP VARIANTS PRPS-RELATED SER-113 AND HIS-182.
RC SPECIES=Human;
RA Roessler B.J., Palella T.D., Heidler S., Becker M.A.;
RT "Identification of distinct PRPS1 mutations in two patients with
RT X-linked phosphoribosylpyrophosphate synthetase superactivity.";
RL Clin. Res. 39:267A-267A(1991).
RN [8]
RP VARIANTS PRPS-RELATED HIS-51; SER-113; ILE-128; HIS-182; VAL-189 AND
RP GLN-192.
RC SPECIES=Human;
RX MEDLINE=96066677; PubMed=7593598;
RA Becker M.A., Smith P.R., Taylor W., Mustafi R., Switzer R.L.;
RT "The genetic and functional basis of purine nucleotide
RT feedback-resistant phosphoribosylpyrophosphate synthetase
RT superactivity.";
RL J. Clin. Invest. 96:2133-2141(1995).
CC -!- CATALYTIC ACTIVITY: ATP + D-ribose 5-phosphate = AMP + 5-phospho-
CC alpha-D-ribose 1-diphosphate.
CC -!- COFACTOR: Both inorganic phosphate and magnesium ion are required
CC for enzyme stability and activity.
CC -!- PATHWAY: Utilized by both the de novo and the salvage pathways by
CC which endogenously formed or exogenously added pyrimidine, purine,
CC or pyridine bases are converted to the corresponding
CC ribonucleoside monophosphates.
CC -!- DISEASE: Defects in PRPS1 are the cause of PRPS-related gout
CC [MIM:311850]; also known as gout due to PRPS1 superactivity. It is
CC a familial disorder characterized by excessive purine production,
CC gout and uric acid urolithiasis.
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase
CC family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; M29392; AAA41960.1; -.
DR EMBL; M31084; AAA41959.1; -.
DR EMBL; M31078; AAA41959.1; JOINED.
DR EMBL; M31079; AAA41959.1; JOINED.
DR EMBL; M31080; AAA41959.1; JOINED.
DR EMBL; M31082; AAA41959.1; JOINED.
DR EMBL; M31083; AAA41959.1; JOINED.
DR EMBL; X15331; CAA33386.1; -.
DR EMBL; BC001605; AAH01605.1; -.
DR EMBL; D00860; BAA00733.1; -.
DR EMBL; M17258; AAA41963.1; -.
DR EMBL; X16554; CAA34555.1; -.
DR PIR; A35465; KIRTR1.
DR PIR; JX0159; KIHUR1.
DR HSSP; P14193; 1DKU.
DR Genew; HGNC:9462; PRPS1.
DR GK; P09329; -.
DR MIM; 311850; -.
DR GO; GO:0004749; F:ribose-phosphate diphosphokinase activity; TAS.
DR GO; GO:0007399; P:neurogenesis; TAS.
DR GO; GO:0006144; P:purine base metabolism; TAS.
DR InterPro; IPR000842; PRPP_synthetase.
DR InterPro; IPR000836; PRTransferase.
DR InterPro; IPR005946; RibP_Ppkin.
DR Pfam; PF00156; Pribosyltran; 1.
DR TIGRFAMs; TIGR01251; ribP_PPkin; 1.
DR PROSITE; PS00114; PRPP_SYNTHETASE; 1.
KW Nucleotide biosynthesis; Transferase; Kinase; Magnesium;
KW Multigene family; Gout; Disease mutation.
FT INIT_MET 0 0
FT METAL 127 127 MAGNESIUM (POTENTIAL).
FT METAL 129 129 MAGNESIUM (POTENTIAL).
FT METAL 138 138 MAGNESIUM (POTENTIAL).
FT METAL 142 142 MAGNESIUM (POTENTIAL).
FT DOMAIN 211 226 BINDING OF PHOSPHORIBOSYLPYROPHOSPHATE
FT (POTENTIAL).
FT VARIANT 51 51 D -> H (in PRPS-related gout).
FT /FTId=VAR_016044.
FT VARIANT 113 113 N -> S (in PRPS-related gout).
FT /FTId=VAR_004163.
FT VARIANT 128 128 L -> I (in PRPS-related gout).
FT /FTId=VAR_016045.
FT VARIANT 182 182 D -> H (in PRPS-related gout).
FT /FTId=VAR_004164.
FT VARIANT 189 189 A -> V (in PRPS-related gout).
FT /FTId=VAR_016046.
FT VARIANT 192 192 H -> Q (in PRPS-related gout).
FT /FTId=VAR_016047.
SQ SEQUENCE 317 AA; 34703 MW; 5EB0961050726999 CRC64;
PNIKIFSGSS HQDLSQKIAD RLGLELGKVV TKKFSNQETC VEIGESVRGE DVYIVQSGCG
EINDNLMELL IMINACKIAS ASRVTAVIPC FPYARQDKKD KSRAPISAKL VANMLSVAGA
DHIITMDLHA SQIQGFFDIP VDNLYAEPAV LKWIRENISE WRNCTIVSPD AGGAKRVTSI
ADRLNVDFAL IHKERKKANE VDRMVLVGDV KDRVAILVDD MADTCGTICH AADKLLSAGA
TRVYAILTHG IFSGPAISRI NNACFEAVVV TNTIPQEDKM KHCSKIQVID ISMILAEAIR
RTHNGESVSY LFSHVPL
//
ID KPR2_HUMAN STANDARD; PRT; 317 AA.
AC P11908;
DT 01-OCT-1989 (Rel. 12, Created)
DT 01-OCT-1989 (Rel. 12, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Ribose-phosphate pyrophosphokinase II (EC 2.7.6.1) (Phosphoribosyl
DE pyrophosphate synthetase II) (PPRibP) (PRS-II).
GN PRPS2.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RC TISSUE=Testis;
RX MEDLINE=89171273; PubMed=2538352;
RA Iizasa T., Taira M., Shimada H., Ishijima S., Tatibana M.;
RT "Molecular cloning and sequencing of human cDNA for phosphoribosyl
RT pyrophosphate synthetase subunit II.";
RL FEBS Lett. 244:47-50(1989).
RN [2]
RP SEQUENCE FROM N.A.
RC TISSUE=Testis;
RX MEDLINE=90164248; PubMed=2560337;
RA Iizasa T., Taira M., Shimada H., Tatibana M.;
RT "Deduced amino acid sequence from human phosphoribosylpyrophosphate
RT synthetase subunit II cDNA.";
RL Adv. Exp. Med. Biol. 253A:519-523(1989).
RN [3]
RP SEQUENCE FROM N.A.
RC TISSUE=Testis;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC -!- CATALYTIC ACTIVITY: ATP + D-ribose 5-phosphate = AMP + 5-phospho-
CC alpha-D-ribose 1-diphosphate.
CC -!- COFACTOR: Both inorganic phosphate and magnesium ion are required
CC for enzyme stability and activity.
CC -!- ENZYME REGULATION: Activated by Mg(2+) and inorganic phosphate and
CC competitive or non-competitive inhibited by ADP,
CC 2,3-bisphosphoglyceride or GDP.
CC -!- PATHWAY: Utilized by both the de novo and the salvage pathways by
CC which endogenously formed or exogenously added pyrimidine, purine,
CC or pyridine bases are converted to the corresponding
CC ribonucleoside monophosphates.
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase
CC family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; Y00971; CAA68785.1; -.
DR EMBL; BC030019; AAH30019.1; -.
DR EMBL; BC040483; AAH40483.1; -.
DR PIR; S02778; KIHUR2.
DR HSSP; P14193; 1DKU.
DR Genew; HGNC:9465; PRPS2.
DR MIM; 311860; -.
DR GO; GO:0004749; F:ribose-phosphate diphosphokinase activity; TAS.
DR GO; GO:0006139; P:nucleobase, nucleoside, nucleotide and nucl...; TAS.
DR InterPro; IPR000842; PRPP_synthetase.
DR InterPro; IPR000836; PRTransferase.
DR InterPro; IPR005946; RibP_Ppkin.
DR Pfam; PF00156; Pribosyltran; 1.
DR TIGRFAMs; TIGR01251; ribP_PPkin; 1.
DR PROSITE; PS00114; PRPP_SYNTHETASE; 1.
KW Nucleotide biosynthesis; Transferase; Kinase; Magnesium;
KW Multigene family.
FT INIT_MET 0 0
FT METAL 127 127 MAGNESIUM (POTENTIAL).
FT METAL 129 129 MAGNESIUM (POTENTIAL).
FT METAL 138 138 MAGNESIUM (POTENTIAL).
FT METAL 142 142 MAGNESIUM (POTENTIAL).
FT DOMAIN 211 226 BINDING OF PHOSPHORIBOSYLPYROPHOSPHATE
FT (POTENTIAL).
SQ SEQUENCE 317 AA; 34638 MW; 6AC206CD31C7EE08 CRC64;
PNIVLFSGSS HQDLSQRVAD RLGLELGKVV TKKFSNQETS VEIGESVRGE DVYIIQSGCG
EINDNLMELL IMINACKIAS SSRVTAVIPC FPYARQDKKD KSRAPISAKL VANMLSVAGA
DHIITMDLHA SQIQGFFDIP VDNLYAEPAV LQWIRENIAE WKNCIIVSPD AGGAKRVTSI
ADRLNVEFAL IHKERKKANE VDRMVLVGDV KDRVAILVDD MADTCGTICH AADKLLSAGA
TKVYAILTHG IFSGPAISRI NNAAFEAVVV TNTIPQEDKM KHCTKIQVID ISMILAEAIR
RTHNGESVSY LFSHVPL
//
ID KPR3_HUMAN STANDARD; PRT; 317 AA.
AC P21108;
DT 01-FEB-1991 (Rel. 17, Created)
DT 01-FEB-1991 (Rel. 17, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Ribose-phosphate pyrophosphokinase III (EC 2.7.6.1) (Phosphoribosyl
DE pyrophosphate synthetase III) (PRS-III).
GN PRPS3.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A., AND SEQUENCE OF 1-10.
RC TISSUE=Testis;
RX MEDLINE=90375519; PubMed=2168892;
RA Taira M., Iizasa T., Shimada H., Kudoh J., Shimizu N., Tatibana M.;
RT "A human testis-specific mRNA for phosphoribosylpyrophosphate
RT synthetase that initiates from a non-AUG codon.";
RL J. Biol. Chem. 265:16491-16497(1990).
CC -!- CATALYTIC ACTIVITY: ATP + D-ribose 5-phosphate = AMP + 5-phospho-
CC alpha-D-ribose 1-diphosphate.
CC -!- COFACTOR: Both inorganic phosphate and magnesium ion are required
CC for enzyme stability and activity.
CC -!- PATHWAY: Utilized by both the de novo and the salvage pathways by
CC which endogenously formed or exogenously added pyrimidine, purine,
CC or pyridine bases are converted to the corresponding
CC ribonucleoside monophosphates.
CC -!- TISSUE SPECIFICITY: Testis.
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase
CC family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; M57423; AAB59463.1; -.
DR PIR; A37893; KIHUR3.
DR HSSP; P14193; 1DKR.
DR SWISS-2DPAGE; P21108; HUMAN.
DR GO; GO:0004749; F:ribose-phosphate diphosphokinase activity; NAS.
DR GO; GO:0009156; P:ribonucleoside monophosphate biosynthesis; NAS.
DR InterPro; IPR000842; PRPP_synthetase.
DR InterPro; IPR000836; PRTransferase.
DR InterPro; IPR005946; RibP_Ppkin.
DR Pfam; PF00156; Pribosyltran; 1.
DR TIGRFAMs; TIGR01251; ribP_PPkin; 1.
DR PROSITE; PS00114; PRPP_SYNTHETASE; 1.
KW Nucleotide biosynthesis; Transferase; Kinase; Magnesium.
FT INIT_MET 0 0
FT METAL 127 127 MAGNESIUM (POTENTIAL).
FT METAL 129 129 MAGNESIUM (POTENTIAL).
FT METAL 138 138 MAGNESIUM (POTENTIAL).
FT METAL 142 142 MAGNESIUM (POTENTIAL).
FT DOMAIN 211 226 BINDING OF PHOSPHORIBOSYLPYROPHOSPHATE
FT (POTENTIAL).
SQ SEQUENCE 317 AA; 34708 MW; 722E5D80B65150AF CRC64;
PNIKIFSGSS HQDLSQKIAD RLGLELGKVV TKKFSNQETC VEIDESVRGE DVYIVQSGCG
EINDSLMELL IMINACKIAS ASRVTAVIPC FPYARQDKKD KSRSPISAKL VANMLSIAGA
DHIITMDLHA SQIQGFFDIP VDNLYAEPTV LKWIRENIPE WKNCIIVSPD AGGAKRVTSI
ADQLNVDFAL IHKERKKANE VDCIVLVGDV NDRVAILVDD MADTCVTICL AADKLLSAGA
TRVYAILTHG IFSGPAISRI NTACFEAVVV TNTIPQDEKM KHCSKIRVID ISMILAEAIR
RTHNGESVSY LFSHVPL
//
ID KPY1_HUMAN STANDARD; PRT; 530 AA.
AC P14618; Q96E76; Q9BWB5;
DT 01-APR-1990 (Rel. 14, Created)
DT 28-FEB-2003 (Rel. 41, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE Pyruvate kinase, M1 isozyme (EC 2.7.1.40) (Pyruvate kinase muscle
DE isozyme) (Cytosolic thyroid hormone-binding protein) (CTHBP) (THBP1).
GN PKM2 OR PKM.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RX MEDLINE=90046696; PubMed=2813362;
RA Kato H., Fukuda T., Parkison C., McPhie P., Cheng S.-Y.;
RT "Cytosolic thyroid hormone-binding protein is a monomer of pyruvate
RT kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:7861-7865(1989).
RN [2]
RP SEQUENCE FROM N.A.
RX MEDLINE=91249787; PubMed=2040271;
RA Takenaka M., Noguchi T., Sadahiro S., Hirai H., Yamada K., Matsuda T.,
RA Imai E., Tanaka T.;
RT "Isolation and characterization of the human pyruvate kinase M gene.";
RL Eur. J. Biochem. 198:101-106(1991).
RN [3]
RP SEQUENCE FROM N.A.
RC TISSUE=Eye, Kidney, Lung, Muscle, and Ovary;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [4]
RP SEQUENCE OF 1-31.
RC TISSUE=Platelet;
RX MEDLINE=22608298; PubMed=12665801;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
CC -!- CATALYTIC ACTIVITY: ATP + pyruvate = ADP + phosphoenolpyruvate.
CC -!- COFACTOR: Requires magnesium and potassium.
CC -!- PATHWAY: Glycolysis; final step.
CC -!- SUBUNIT: Homotetramer.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=M1;
CC IsoId=P14618-1; Sequence=Displayed;
CC Name=M2;
CC IsoId=P14786-1; Sequence=External;
CC -!- MISCELLANEOUS: There are 4 isozymes of pyruvate kinase in mammals:
CC L, R, M1 and M2. L type is major isozyme in the liver, R is found
CC in red cells, M1 is the main form in muscle, heart and brain, and
CC M2 is found in early fetal tissues.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; X56494; CAA39849.1; -.
DR EMBL; M26252; AAA36672.1; -.
DR EMBL; BC000481; AAH00481.1; -.
DR EMBL; BC007640; AAH07640.1; -.
DR EMBL; BC007952; AAH07952.1; -.
DR EMBL; BC012811; AAH12811.1; -.
DR EMBL; BC035198; AAH35198.1; -.
DR PIR; S30038; S30038.
DR HSSP; P11974; 1PKN.
DR Genew; HGNC:9021; PKM2.
DR MIM; 179050; -.
DR GO; GO:0005829; C:cytosol; NAS.
DR GO; GO:0004743; F:pyruvate kinase activity; TAS.
DR GO; GO:0006096; P:glycolysis; NAS.
DR InterPro; IPR001697; Pyruvate_kinase.
DR Pfam; PF00224; PK; 1.
DR Pfam; PF02887; PK_C; 1.
DR PRINTS; PR01050; PYRUVTKNASE.
DR ProDom; PD001009; Pyruvate_kinase; 1.
DR TIGRFAMs; TIGR01064; pyruv_kin; 1.
DR PROSITE; PS00110; PYRUVATE_KINASE; 1.
KW Transferase; Kinase; Glycolysis; Multigene family; Magnesium;
KW Alternative splicing.
FT INIT_MET 0 0
FT ACT_SITE 269 269 By similarity.
FT METAL 271 271 MAGNESIUM (POTENTIAL).
FT METAL 292 292 MAGNESIUM (POTENTIAL).
FT METAL 293 293 MAGNESIUM (POTENTIAL).
FT CONFLICT 6 6 E -> Q (IN REF. 3; AAH12811).
FT CONFLICT 102 102 I -> Y (in Ref. 1).
FT CONFLICT 131 131 V -> L (in Ref. 1).
FT CONFLICT 203 203 G -> V (IN REF. 3; AAH35198).
FT CONFLICT 338 338 R -> P (in Ref. 2).
FT CONFLICT 506 506 D -> H (IN REF. 3; AAH12811).
SQ SEQUENCE 530 AA; 57805 MW; AA94C376A9DD8BAD CRC64;
SKPHSEAGTA FIQTQQLHAA MADTFLEHMC RLDIDSPPIT ARNTGIICTI GPASRSVETL
KEMIKSGMNV ARLNFSHGTH EYHAETIKNV RTATESFASD PILYRPVAVA LDTKGPEIRT
GLIKGSGTAE VELKKGATLK ITLDNAYMEK CDENILWLDY KNICKVVEVG SKIYVDDGLI
SLQVKQKGAD FLVTEVENGG SLGSKKGVNL PGAAVDLPAV SEKDIQDLKF GVEQDVDMVF
ASFIRKASDV HEVRKVLGEK GKNIKIISKI ENHEGVRRFD EILEASDGIM VARGDLGIEI
PAEKVFLAQK MMIGRCNRAG KPVICATQML ESMIKKPRPT RAEGSDVANA VLDGADCIML
SGETAKGDYP LEAVRMQHLI AREAEAAIYH LQLFEELRRL APITSDPTEA TAVGAVEASF
KCCSGAIIVL TKSGRSAHQV ARYRPRAPII AVTRNPQTAR QAHLYRGIFP VLCKDPVQEA
WAEDVDLRVN FAMNVGKARG FFKKGDVVIV LTGWRPGSGF TNTMRVVPVP
//
ID KPY2_HUMAN STANDARD; PRT; 530 AA.
AC P14786; Q9UPF2;
DT 01-APR-1990 (Rel. 14, Created)
DT 01-APR-1990 (Rel. 14, Last sequence update)
DT 28-FEB-2003 (Rel. 41, Last annotation update)
DE Pyruvate kinase, M2 isozyme (EC 2.7.1.40).
GN PKM2 OR PKM.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RX MEDLINE=89211988; PubMed=2854097;
RA Tani K., Yoshida M.C., Satoh H., Mitamura K., Noguchi T., Tanaka T.,
RA Fujii H., Miwa S.;
RT "Human M2-type pyruvate kinase: cDNA cloning, chromosomal assignment
RT and expression in hepatoma.";
RL Gene 73:509-516(1988).
RN [2]
RP SEQUENCE OF 367-530 FROM N.A.
RX MEDLINE=98125741; PubMed=9466265;
RA Williams J.M., Chen G.C., Zhu L., Rest R.F.;
RT "Using the yeast two-hybrid system to identify human epithelial cell
RT proteins that bind gonococcal Opa proteins: intracellular gonococci
RT bind pyruvate kinase via their Opa proteins and require host pyruvate
RT for growth.";
RL Mol. Microbiol. 27:171-186(1998).
CC -!- CATALYTIC ACTIVITY: ATP + pyruvate = ADP + phosphoenolpyruvate.
CC -!- COFACTOR: Requires magnesium and potassium.
CC -!- PATHWAY: Glycolysis; final step.
CC -!- SUBUNIT: Homotetramer.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=M2;
CC IsoId=P14786-1; Sequence=Displayed;
CC Name=M1;
CC IsoId=P14618-1; Sequence=External;
CC -!- MISCELLANEOUS: There are 4 isozymes of pyruvate kinase in mammals:
CC L, R, M1 and M2. L type is major isozyme in the liver, R is found
CC in red cells, M1 is the main form in muscle, heart and brain, and
CC M2 is found in early fetal tissues.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; M23725; AAA36449.1; -.
DR EMBL; AF025439; AAC39559.1; -.
DR PIR; S30038; S30038.
DR HSSP; P11974; 1PKN.
DR Aarhus/Ghent-2DPAGE; 3509; NEPHGE.
DR Genew; HGNC:9021; PKM2.
DR GK; P14786; -.
DR MIM; 179050; -.
DR GO; GO:0004743; F:pyruvate kinase activity; TAS.
DR GO; GO:0006096; P:glycolysis; NAS.
DR InterPro; IPR001697; Pyruvate_kinase.
DR Pfam; PF00224; PK; 1.
DR Pfam; PF02887; PK_C; 1.
DR PRINTS; PR01050; PYRUVTKNASE.
DR ProDom; PD001009; Pyruvate_kinase; 1.
DR TIGRFAMs; TIGR01064; pyruv_kin; 1.
DR PROSITE; PS00110; PYRUVATE_KINASE; 1.
KW Transferase; Kinase; Glycolysis; Multigene family; Magnesium;
KW Alternative splicing.
FT INIT_MET 0 0
FT ACT_SITE 269 269 By similarity.
FT METAL 271 271 MAGNESIUM (POTENTIAL).
FT METAL 292 292 MAGNESIUM (POTENTIAL).
FT METAL 293 293 MAGNESIUM (POTENTIAL).
FT DOMAIN 388 432 INTERSUBUNIT CONTACT.
FT CONFLICT 378 378 N -> H (in Ref. 2).
SQ SEQUENCE 530 AA; 57782 MW; F6AEFCB6CFDD8DCD CRC64;
SKPHSEAGTA FIQTQQLHAA MADTFLEHMC RLDIDSPPIT ARNTGIICTI GPASRSVETL
KEMIKSGMNV ARLNFSHGTH EYHAETIKNV RTATESFASD PILYRPVAVA LDTKGPEIRT
GLIKGSGTAE VELKKGATLK ITLDNAYMEK CDENILWLDY KNICKVVEVG SKIYVDDGLI
SLQVKQKGAD FLVTEVENGG SLGSKKGVNL PGAAVDLPAV SEKDIQDLKF GVEQDVDMVF
ASFIRKASDV HEVRKVLGEK GKNIKIISKI ENHEGVRRFD EILEASDGIM VARGDLGIEI
PAEKVFLAQK MMIGRCNRAG KPVICATQML ESMIKKPRPT RAEGSDVANA VLDGADCIML
SGETAKGDYP LEAVRMQNLI AREAEAAIYH LQLFEELRRL APITSDPTEA TAVGAVEASF
KCCSGAIIVL TKSGRSAHQV ARYRPRAPII AVTRNPQTAR QAHLYRGIFP VLCKDPVQEA
WAEDVDLRVN FAMNVGKARG FFKKGDVVIV LTGWRPGSGF TNTMRVVPVP
//
ID KPYR_HUMAN STANDARD; PRT; 574 AA.
AC P30613; P11973;
DT 01-APR-1993 (Rel. 25, Created)
DT 30-MAY-2000 (Rel. 39, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Pyruvate kinase, isozymes R/L (EC 2.7.1.40) (R-type/L-type pyruvate
DE kinase) (Red cell/liver pyruvate kinase).
GN PKLR OR PKL OR PK1.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A., AND VARIANT CNSHA TOKYO/BEIRUT MET-384.
RX MEDLINE=91376115; PubMed=1896471;
RA Kanno H., Fujii H., Hirono A., Miwa S.;
RT "cDNA cloning of human R-type pyruvate kinase and identification of a
RT single amino acid substitution (Thr384-->Met) affecting enzymatic
RT stability in a pyruvate kinase variant (PK Tokyo) associated with
RT hereditary hemolytic anemia.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:8218-8221(1991).
RN [2]
RP SEQUENCE FROM N.A.
RX MEDLINE=88158079; PubMed=3126495;
RA Tani K., Fujii H., Nagata S., Miwa S.;
RT "Human liver type pyruvate kinase: complete amino acid sequence and
RT the expression in mammalian cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:1792-1795(1988).
RN [3]
RP REVISIONS TO 130 AND 232.
RA Kanno H.;
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SEQUENCE FROM N.A. (ISOFORM R-TYPE).
RC TISSUE=Pancreas;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [5]
RP SEQUENCE OF 470-574 FROM N.A.
RX MEDLINE=87184521; PubMed=3566732;
RA Tani K., Fujii H., Tsutsumi H., Sukegawa J., Toyoshima K.,
RA Yoshida M.C., Noguchi T., Tanaka T., Miwa S.;
RT "Human liver type pyruvate kinase: cDNA cloning and chromosomal
RT assignment.";
RL Biochem. Biophys. Res. Commun. 143:431-438(1987).
RN [6]
RP SEQUENCE OF 365-431 FROM N.A., AND VARIANT CNSHA OSAKA PHE-368.
RX MEDLINE=93236593; PubMed=8476433;
RA Kanno H., Fujii H., Tsujino G., Miwa S.;
RT "Molecular basis of impaired pyruvate kinase isozyme conversion in
RT erythroid cells: a single amino acid substitution near the active
RT site and decreased mRNA content of the R-type PK.";
RL Biochem. Biophys. Res. Commun. 192:46-52(1993).
RN [7]
RP REVIEW ON VARIANTS.
RX MEDLINE=96263732; PubMed=8664896;
RA Beutler E., Baronciani L.;
RT "Mutations in pyruvate kinase.";
RL Hum. Mutat. 7:1-6(1996).
RN [8]
RP REVIEW ON VARIANTS.
RX MEDLINE=96400713; PubMed=8807089;
RA Baronciani L., Bianchi P., Zanella A.;
RT "Hematologically important mutations: red cell pyruvate kinase.";
RL Blood Cells Mol. Dis. 22:85-89(1996).
RN [9]
RP REVIEW ON VARIANTS.
RX MEDLINE=97230013; PubMed=9075576;
RA Baronciani L., Bianchi P., Zanella A.;
RT "Hematologically important mutations: red cell pyruvate kinase (1st
RT update).";
RL Blood Cells Mol. Dis. 22:259-264(1996).
RN [10]
RP REVIEW ON VARIANTS.
RX MEDLINE=99187977; PubMed=10087985;
RA Baronciani L., Bianchi P., Zanella A.;
RT "Hematologically important mutations: red cell pyruvate kinase (2nd
RT update).";
RL Blood Cells Mol. Dis. 24:273-279(1998).
RN [11]
RP REVIEW ON VARIANTS.
RX MEDLINE=20238076; PubMed=10772876;
RA Bianchi P., Zanella A.;
RT "Hematologically important mutations: red cell pyruvate kinase (third
RT update).";
RL Blood Cells Mol. Dis. 26:47-53(2000).
RN [12]
RP VARIANTS CNSHA LINZ CYS-163 AND TOKYO/BEIRUT MET-384.
RX MEDLINE=91208396; PubMed=2018831;
RA Neubauer B., Lakomek M., Winkler H., Parke M., Hofferbert S.,
RA Schroter W.;
RT "Point mutations in the L-type pyruvate kinase gene of two children
RT with hemolytic anemia caused by pyruvate kinase deficiency.";
RL Blood 77:1871-1875(1991).
RN [13]
RP VARIANT CNSHA FUKUSHIMA/MAEBASHI LYS-421.
RX MEDLINE=92163106; PubMed=1536957;
RA Kanno H., Fujii H., Hirono A., Omine M., Miwa S.;
RT "Identical point mutations of the R-type pyruvate kinase (PK) cDNA
RT found in unrelated PK variants associated with hereditary hemolytic
RT anemia.";
RL Blood 79:1347-1350(1992).
RN [14]
RP VARIANT CNSHA SAPPORO GLN-426.
RX MEDLINE=93244440; PubMed=8481523;
RA Kanno H., Fujii H., Miwa S.;
RT "Low substrate affinity of pyruvate kinase variant (PK Sapporo)
RT caused by a single amino acid substitution (426 Arg-->Gln) associated
RT with hereditary hemolytic anemia.";
RL Blood 81:2439-2441(1993).
RN [15]
RP VARIANTS CNSHA ASP-134; PRO-155; HIS-359; TRP-486; VAL-495 AND
RP GLN-510.
RX MEDLINE=93248282; PubMed=8483951;
RA Baronciani L., Beutler E.;
RT "Analysis of pyruvate kinase-deficiency mutations that produce
RT nonspherocytic hemolytic anemia.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:4324-4327(1993).
RN [16]
RP VARIANT CNSHA AMISH HIS-479.
RX MEDLINE=94214145; PubMed=8161798;
RA Kanno H., Ballas S.K., Miwa S., Fujii H., Bowman H.S.;
RT "Molecular abnormality of erythrocyte pyruvate kinase deficiency in
RT the Amish.";
RL Blood 83:2311-2316(1994).
RN [17]
RP VARIANTS CNSHA SER-332; SER-336; LYS-354 DEL; ASP-361; THR-392;
RP HIS-498; GLN-510 AND TRP-532.
RX MEDLINE=94235845; PubMed=8180378;
RA Lenzner C., Nuernberg P., Thiele B.-J., Reis A., Brabec V.,
RA Sakalova A., Jacobasch G.;
RT "Mutations in the pyruvate kinase L gene in patients with hereditary
RT hemolytic anemia.";
RL Blood 83:2817-2822(1994).
RN [18]
RP VARIANTS CNSHA GLU-331; ALA-341; LYS-393; SER-393; ASP-458; MET-460
RP AND HIS-498.
RX MEDLINE=95221622; PubMed=7706479;
RA Baronciani L., Beutler E.;
RT "Molecular study of pyruvate kinase deficient patients with
RT hereditary nonspherocytic hemolytic anemia.";
RL J. Clin. Invest. 95:1702-1709(1995).
RN [19]
RP VARIANTS CNSHA.
RA Baronciani L., Westwood B., Beutler E.;
RT "Study of the molecular defects in pyruvate kinase (PK) deficient
RT patients affected by hereditary nonspherocytic hemolytic anemia
RT (HNHA).";
RL J. Invest. Med. 43:341A-341A(1995).
RN [20]
RP VARIANT PYRUVATE KINASE HYPERACTIVITY GLU-37.
RX MEDLINE=97245895; PubMed=9090535;
RA Beutler E., Westwood B., van Zwieten R., Roos D.;
RT "G-to-T transition at cDNA nt 110 (K37Q) in the PKLR (pyruvate
RT kinase) gene is the molecular basis of a case of hereditary increase
RT of red blood cell ATP.";
RL Hum. Mutat. 9:282-285(1997).
RN [21]
RP VARIANTS CNSHA GLN-172; GLN-337; HIS-339; THR-357; ILE-408; THR-431;
RP TRP-486 AND GLN-532.
RX MEDLINE=99043610; PubMed=9827908;
RA Zarza R., Alvarez R., Pujades A., Nomdedeu B., Carrera A., Estella J.,
RA Remacha A., Sanchez J.M., Morey M., Cortes T., Perez Lungmus G.,
RA Bureo E., Vives Corrons J.L.;
RT "Molecular characterization of the PK-LR gene in pyruvate kinase
RT deficient Spanish patients.";
RL Br. J. Haematol. 103:377-382(1998).
RN [22]
RP VARIANT CNSHA CONAKRY TYR-130.
RX MEDLINE=99101396; PubMed=9886305;
RA Cohen-Solal M., Prehu C., Wajcman H., Poyart C.,
RA Bardakdjian-Michau J., Kister J., Prome D., Valentin C., Bachir D.,
RA Galacteros F.;
RT "A new sickle cell disease phenotype associating Hb S trait, severe
RT pyruvate kinase deficiency (PK Conakry), and an alpha-2 globin gene
RT variant (Hb Conakry).";
RL Br. J. Haematol. 103:950-956(1998).
RN [23]
RP VARIANTS CNSHA SER-332; PRO-337; TRP-486; CYS-498 AND GLN-510.
RX MEDLINE=98141680; PubMed=9482576;
RA Pastore L., della Morte R., Frisso G., Alfinito F., Vitale D.,
RA Calise R.M., Ferraro F., Zagari A., Rotoli B., Salvatore F.;
RT "Novel mutations and structural implications in R-type pyruvate
RT kinase-deficient patients from Southern Italy.";
RL Hum. Mutat. 11:127-134(1998).
RN [24]
RP VARIANTS CNSHA MET-335; LYS-338 DEL; GLY-387; ASP-394 AND VAL-394.
RX MEDLINE=21226334; PubMed=11328279;
RA Zanella A., Bianchi P., Fermo E., Iurlo A., Zappa M., Vercellati C.,
RA Boschetti C., Baronciani L., Cotton F.;
RT "Molecular characterization of the PK-LR gene in sixteen pyruvate
RT kinase-deficient patients.";
RL Br. J. Haematol. 113:43-48(2001).
CC -!- CATALYTIC ACTIVITY: ATP + pyruvate = ADP + phosphoenolpyruvate.
CC -!- COFACTOR: Requires magnesium and potassium.
CC -!- PATHWAY: Glycolysis; final step.
CC -!- SUBUNIT: Homotetramer.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=R-type;
CC IsoId=P30613-1; Sequence=Displayed;
CC Name=L-type;
CC IsoId=P30613-2; Sequence=VSP_002883;
CC -!- DISEASE: Defects in PKLR are the cause of pyruvate kinase
CC hyperactivity [MIM:102900]; also known as high red cell ATP
CC syndrome. This autosomal dominant phenotype is characterized by
CC increase of red blood cell ATP.
CC -!- DISEASE: Defects in PKLR are a cause of chronic nonspherocytic
CC hemolytic anemia (CNSHA) [MIM:266200]; also called hereditary
CC nonspherocytic hemolytic anemia (HNSHA).
CC -!- MISCELLANEOUS: There are 4 isozymes of pyruvate kinase in mammals:
CC L, R, M1 and M2. L type is major isozyme in the liver, R is found
CC in red cells, M1 is the main form in muscle, heart and brain, and
CC M2 is found in early fetal tissues.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AB015983; BAA31706.1; -.
DR EMBL; M15465; AAA60104.1; -.
DR EMBL; BC025737; AAH25737.1; -.
DR EMBL; S60712; AAB26262.1; -.
DR PIR; I52269; KIHUPL.
DR PIR; I52269; KIHUPR.
DR PDB; 1LIU; 11-SEP-02.
DR PDB; 1LIW; 11-SEP-02.
DR SWISS-2DPAGE; P30613; HUMAN.
DR Genew; HGNC:9020; PKLR.
DR GK; P30613; -.
DR MIM; 266200; -.
DR MIM; 102900; -.
DR GO; GO:0004743; F:pyruvate kinase activity; TAS.
DR InterPro; IPR001697; Pyruvate_kinase.
DR Pfam; PF00224; PK; 1.
DR Pfam; PF02887; PK_C; 1.
DR PRINTS; PR01050; PYRUVTKNASE.
DR ProDom; PD001009; Pyruvate_kinase; 1.
DR TIGRFAMs; TIGR01064; pyruv_kin; 1.
DR PROSITE; PS00110; PYRUVATE_KINASE; 1.
KW Transferase; Kinase; Glycolysis; Multigene family; Phosphorylation;
KW Magnesium; Alternative splicing; Disease mutation; 3D-structure.
FT MOD_RES 43 43 PHOSPHORYLATION (BY PKA).
FT ACT_SITE 313 313 By similarity.
FT METAL 315 315 MAGNESIUM (POTENTIAL).
FT METAL 336 336 MAGNESIUM (POTENTIAL).
FT METAL 337 337 MAGNESIUM (POTENTIAL).
FT VARSPLIC 1 33 MSIQENISSLQLRSWVSKSQRDLAKSILIGAPG -> ME
FT (in isoform L-type).
FT /FTId=VSP_002883.
FT VARIANT 37 37 G -> E (in pyruvate kinase
FT hyperactivity).
FT /FTId=VAR_011435.
FT VARIANT 80 80 S -> P (in CNSHA).
FT /FTId=VAR_011436.
FT VARIANT 86 86 R -> P (in CNSHA).
FT /FTId=VAR_011437.
FT VARIANT 90 90 I -> N (in CNSHA).
FT /FTId=VAR_011438.
FT VARIANT 95 95 G -> R (in CNSHA).
FT /FTId=VAR_011439.
FT VARIANT 107 107 M -> T (in CNSHA).
FT /FTId=VAR_004028.
FT VARIANT 111 111 G -> R (in CNSHA).
FT /FTId=VAR_011440.
FT VARIANT 115 115 A -> P (in CNSHA; Val de Marne).
FT /FTId=VAR_011441.
FT VARIANT 120 120 S -> F (in CNSHA; Beaujon).
FT /FTId=VAR_011442.
FT VARIANT 130 130 S -> Y (in CNSHA; Conakry).
FT /FTId=VAR_011443.
FT VARIANT 131 131 Missing (in CNSHA).
FT /FTId=VAR_004029.
FT VARIANT 134 134 V -> D (in CNSHA).
FT /FTId=VAR_004030.
FT VARIANT 153 153 I -> T (in CNSHA).
FT /FTId=VAR_011474.
FT VARIANT 155 155 L -> P (in CNSHA).
FT /FTId=VAR_004031.
FT VARIANT 159 159 G -> V (in CNSHA).
FT /FTId=VAR_011444.
FT VARIANT 163 163 R -> C (in CNSHA; Linz).
FT /FTId=VAR_004033.
FT VARIANT 172 172 E -> Q (in CNSHA; Sassari).
FT /FTId=VAR_004032.
FT VARIANT 219 219 I -> T (in CNSHA).
FT /FTId=VAR_011475.
FT VARIANT 221 221 D -> DD (in CNSHA).
FT /FTId=VAR_004034.
FT VARIANT 222 222 G -> A (in CNSHA; Katsushika).
FT /FTId=VAR_011445.
FT VARIANT 263 263 G -> R (in CNSHA).
FT /FTId=VAR_011447.
FT VARIANT 263 263 G -> W (in CNSHA).
FT /FTId=VAR_011448.
FT VARIANT 275 275 G -> R (in CNSHA).
FT /FTId=VAR_004035.
FT VARIANT 281 281 D -> N (in CNSHA).
FT /FTId=VAR_004036.
FT VARIANT 287 287 F -> V (in CNSHA).
FT /FTId=VAR_004037.
FT VARIANT 288 288 V -> L (in CNSHA; Moriguchi).
FT /FTId=VAR_011449.
FT VARIANT 293 293 D -> N (in CNSHA).
FT /FTId=VAR_011446.
FT VARIANT 295 295 A -> V (in CNSHA).
FT /FTId=VAR_011450.
FT VARIANT 310 310 I -> N (in CNSHA; Dordrecht).
FT /FTId=VAR_011451.
FT VARIANT 314 314 I -> T (in CNSHA; Hong Kong).
FT /FTId=VAR_004038.
FT VARIANT 315 315 E -> K (in CNSHA).
FT /FTId=VAR_011452.
FT VARIANT 331 331 D -> E (in CNSHA; Parma).
FT /FTId=VAR_004039.
FT VARIANT 331 331 D -> N (in CNSHA).
FT /FTId=VAR_011453.
FT VARIANT 332 332 G -> S (in CNSHA).
FT /FTId=VAR_004040.
FT VARIANT 335 335 V -> M (in CNSHA).
FT /FTId=VAR_011476.
FT VARIANT 336 336 A -> S (in CNSHA).
FT /FTId=VAR_004041.
FT VARIANT 337 337 R -> P (in CNSHA).
FT /FTId=VAR_004042.
FT VARIANT 337 337 R -> Q (in CNSHA).
FT /FTId=VAR_004043.
FT VARIANT 339 339 D -> H (in CNSHA).
FT /FTId=VAR_004044.
FT VARIANT 341 341 G -> A (in CNSHA).
FT /FTId=VAR_004045.
FT VARIANT 341 341 G -> D (in CNSHA).
FT /FTId=VAR_011454.
FT VARIANT 342 342 I -> F (in CNSHA).
FT /FTId=VAR_011455.
FT VARIANT 348 348 K -> N (in CNSHA; Kamata).
FT /FTId=VAR_011456.
FT VARIANT 348 348 Missing (in CNSHA; Brescia).
FT /FTId=VAR_011457.
FT VARIANT 352 352 A -> D (in CNSHA).
FT /FTId=VAR_011477.
FT VARIANT 354 354 Missing (in CNSHA).
FT /FTId=VAR_004046.
FT VARIANT 357 357 I -> T (in CNSHA).
FT /FTId=VAR_004047.
FT VARIANT 359 359 R -> C (in CNSHA; Aomori).
FT /FTId=VAR_004048.
FT VARIANT 359 359 R -> H (in CNSHA).
FT /FTId=VAR_004049.
FT VARIANT 361 361 N -> D (in CNSHA).
FT /FTId=VAR_004050.
FT VARIANT 364 364 G -> D (in CNSHA; Tjaereborg).
FT /FTId=VAR_011458.
FT VARIANT 368 368 V -> F (in CNSHA; Osaka).
FT /FTId=VAR_004051.
FT VARIANT 376 376 S -> I (in CNSHA).
FT /FTId=VAR_011459.
FT VARIANT 384 384 T -> M (in CNSHA; Tokyo/Beirut; most
FT common mutation in Japanese population).
FT /FTId=VAR_004052.
FT VARIANT 385 385 R -> W (in CNSHA).
FT /FTId=VAR_011478.
FT VARIANT 387 387 E -> G (in CNSHA).
FT /FTId=VAR_011460.
FT VARIANT 390 390 D -> N (in CNSHA; Mantova).
FT /FTId=VAR_011461.
FT VARIANT 392 392 A -> T (in CNSHA).
FT /FTId=VAR_004053.
FT VARIANT 393 393 N -> K (in CNSHA).
FT /FTId=VAR_004054.
FT VARIANT 393 393 N -> S (in CNSHA; Paris).
FT /FTId=VAR_004055.
FT VARIANT 394 394 A -> D (in CNSHA).
FT /FTId=VAR_011462.
FT VARIANT 394 394 A -> V (in CNSHA).
FT /FTId=VAR_011463.
FT VARIANT 401 401 C -> CS (in CNSHA).
FT /FTId=VAR_004056.
FT VARIANT 408 408 T -> A (in CNSHA; Hirosaki).
FT /FTId=VAR_011464.
FT VARIANT 408 408 T -> I (in CNSHA).
FT /FTId=VAR_004057.
FT VARIANT 421 421 Q -> K (in CNSHA;
FT Fukushima/Maebashi/Sendai).
FT /FTId=VAR_004058.
FT VARIANT 426 426 R -> Q (in CNSHA; Sapporo).
FT /FTId=VAR_004059.
FT VARIANT 426 426 R -> W (in CNSHA; Naniwa).
FT /FTId=VAR_004060.
FT VARIANT 427 427 E -> A (in CNSHA).
FT /FTId=VAR_011465.
FT VARIANT 427 427 E -> D (in CNSHA).
FT /FTId=VAR_011466.
FT VARIANT 431 431 A -> T (in CNSHA).
FT /FTId=VAR_004061.
FT VARIANT 458 458 G -> D (in CNSHA).
FT /FTId=VAR_004062.
FT VARIANT 459 459 A -> V (in CNSHA).
FT /FTId=VAR_004063.
FT VARIANT 460 460 V -> M (in CNSHA).
FT /FTId=VAR_004064.
FT VARIANT 468 468 A -> G (in CNSHA).
FT /FTId=VAR_011479.
FT VARIANT 468 468 A -> V (in CNSHA; Hadano).
FT /FTId=VAR_004065.
FT VARIANT 477 477 T -> A (in CNSHA).
FT /FTId=VAR_011467.
FT VARIANT 479 479 R -> H (in CNSHA; Amish).
FT /FTId=VAR_011480.
FT VARIANT 485 485 S -> F (in CNSHA).
FT /FTId=VAR_011468.
FT VARIANT 486 486 R -> W (in CNSHA; frequent mutation).
FT /FTId=VAR_004066.
FT VARIANT 488 488 R -> Q (in CNSHA).
FT /FTId=VAR_011469.
FT VARIANT 490 490 R -> W (in CNSHA).
FT /FTId=VAR_004067.
FT VARIANT 495 495 A -> T (in CNSHA).
FT /FTId=VAR_011470.
FT VARIANT 495 495 A -> V (in CNSHA).
FT /FTId=VAR_004068.
FT VARIANT 498 498 R -> C (in CNSHA).
FT /FTId=VAR_004069.
FT VARIANT 498 498 R -> H (in CNSHA).
FT /FTId=VAR_004070.
FT VARIANT 504 504 R -> L (in CNSHA).
FT /FTId=VAR_011471.
FT VARIANT 510 510 R -> Q (in CNSHA; the most common
FT mutation in European population).
FT /FTId=VAR_004071.
FT VARIANT 511 511 G -> R (in CNSHA).
FT /FTId=VAR_011472.
FT VARIANT 531 531 R -> C (in CNSHA).
FT /FTId=VAR_011473.
FT VARIANT 532 532 R -> Q (in CNSHA).
FT /FTId=VAR_004072.
FT VARIANT 532 532 R -> W (in CNSHA).
FT /FTId=VAR_004073.
FT VARIANT 552 552 V -> M (in CNSHA).
FT /FTId=VAR_004074.
FT VARIANT 557 557 G -> A (in CNSHA).
FT /FTId=VAR_011481.
FT VARIANT 559 559 R -> G (in CNSHA).
FT /FTId=VAR_004075.
FT VARIANT 566 566 N -> K (in CNSHA).
FT /FTId=VAR_004076.
FT VARIANT 569 569 R -> Q (in CNSHA).
FT /FTId=VAR_011482.
FT CONFLICT 423 423 A -> R (in Ref. 2).
FT TURN 59 60
FT HELIX 61 64
FT TURN 65 65
FT HELIX 69 73
FT TURN 74 75
FT TURN 78 79
FT STRAND 89 93
FT HELIX 96 98
FT HELIX 101 110
FT TURN 111 111
FT STRAND 112 118
FT TURN 119 120
FT HELIX 124 139
FT TURN 140 143
FT TURN 145 147
FT STRAND 152 156
FT STRAND 163 164
FT STRAND 176 177
FT TURN 179 180
FT STRAND 182 185
FT STRAND 199 200
FT STRAND 202 202
FT TURN 205 206
FT HELIX 207 210
FT TURN 213 214
FT STRAND 216 219
FT TURN 220 223
FT STRAND 224 227
FT STRAND 238 242
FT STRAND 244 245
FT STRAND 251 253
FT TURN 255 256
FT HELIX 266 277
FT TURN 278 279
FT STRAND 282 285
FT TURN 286 287
FT HELIX 291 301
FT HELIX 303 305
FT STRAND 309 314
FT HELIX 317 321
FT TURN 322 322
FT HELIX 323 329
FT STRAND 332 336
FT HELIX 337 343
FT HELIX 346 348
FT HELIX 349 363
FT TURN 364 364
FT STRAND 367 370
FT TURN 373 374
FT HELIX 375 378
FT TURN 379 379
FT HELIX 385 397
FT TURN 398 398
FT STRAND 401 404
FT HELIX 406 409
FT TURN 410 410
FT HELIX 414 431
FT HELIX 434 444
FT HELIX 451 466
FT TURN 467 467
FT STRAND 470 474
FT HELIX 479 486
FT TURN 487 487
FT STRAND 492 497
FT HELIX 500 505
FT HELIX 506 508
FT TURN 510 511
FT STRAND 512 516
FT HELIX 525 543
FT TURN 544 544
FT TURN 548 549
FT STRAND 551 557
FT STRAND 565 572
SQ SEQUENCE 574 AA; 61830 MW; 3B430896832032F5 CRC64;
MSIQENISSL QLRSWVSKSQ RDLAKSILIG APGGPAGYLR RASVAQLTQE LGTAFFQQQQ
LPAAMADTFL EHLCLLDIDS EPVAARSTSI IATIGPASRS VERLKEMIKA GMNIARLNFS
HGSHEYHAES IANVREAVES FAGSPLSYRP VAIALDTKGP EIRTGILQGG PESEVELVKG
SQVLVTVDPA FRTRGNANTV WVDYPNIVRV VPVGGRIYID DGLISLVVQK IGPEGLVTQV
ENGGVLGSRK GVNLPGAQVD LPGLSEQDVR DLRFGVEHGV DIVFASFVRK ASDVAAVRAA
LGPEGHGIKI ISKIENHEGV KRFDEILEVS DGIMVARGDL GIEIPAEKVF LAQKMMIGRC
NLAGKPVVCA TQMLESMITK PRPTRAETSD VANAVLDGAD CIMLSGETAK GNFPVEAVKM
QHAIAREAEA AVYHRQLFEE LRRAAPLSRD PTEVTAIGAV EAAFKCCAAA IIVLTTTGRS
AQLLSRYRPR AAVIAVTRSA QAARQVHLCR GVFPLLYREP PEAIWADDVD RRVQFGIESG
KLRGFLRVGD LVIVVTGWRP GSGYTNIMRV LSIS
//
ID KTHY_HUMAN STANDARD; PRT; 212 AA.
AC P23919; Q9BUX4;
DT 01-MAR-1992 (Rel. 21, Created)
DT 28-FEB-2003 (Rel. 41, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Thymidylate kinase (EC 2.7.4.9) (dTMP kinase).
GN DTYMK OR TYMK OR TMPK OR CDC8.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RX MEDLINE=91204436; PubMed=2017365;
RA Su J.Y., Sclafani R.A.;
RT "Molecular cloning and expression of the human deoxythymidylate kinase
RT gene in yeast.";
RL Nucleic Acids Res. 19:823-827(1991).
RN [2]
RP SEQUENCE FROM N.A.
RX MEDLINE=94296549; PubMed=8024690;
RA Huang S.H., Tang A., Drisco B., Zhang S.Q., Seeger R., Li C.,
RA Jong A.;
RT "Human dTMP kinase: gene expression and enzymatic activity coinciding
RT with cell cycle progression and cell growth.";
RL DNA Cell Biol. 13:461-471(1994).
RN [3]
RP SEQUENCE FROM N.A.
RC TISSUE=Muscle;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC -!- FUNCTION: Catalyzes the conversion of dTMP to dTDP.
CC -!- CATALYTIC ACTIVITY: ATP + thymidine 5'-phosphate = ADP + thymidine
CC 5'-diphosphate.
CC -!- PATHWAY: Biosynthesis of dTTP from dTMP.
CC -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; X54729; CAA38528.1; -.
DR EMBL; L16991; AAA21719.1; -.
DR EMBL; BC001827; AAH01827.1; -.
DR PIR; S26845; S26845.
DR PDB; 1E2D; 21-FEB-02.
DR PDB; 1E2E; 21-FEB-02.
DR PDB; 1E2F; 24-JUN-03.
DR PDB; 1E2G; 21-FEB-02.
DR PDB; 1E2Q; 24-JUN-03.
DR PDB; 1E98; 18-JUL-03.
DR PDB; 1E99; 18-JUL-03.
DR PDB; 1E9A; 18-JUL-03.
DR PDB; 1E9B; 01-AUG-03.
DR PDB; 1E9C; 18-JUL-03.
DR PDB; 1E9D; 18-JUL-03.
DR PDB; 1E9E; 18-JUL-03.
DR PDB; 1E9F; 18-JUL-03.
DR PDB; 1NMX; 18-MAR-03.
DR PDB; 1NMY; 18-MAR-03.
DR PDB; 1NMZ; 18-MAR-03.
DR PDB; 1NN0; 18-MAR-03.
DR PDB; 1NN5; 18-MAR-03.
DR Genew; HGNC:3061; DTYMK.
DR GK; P23919; -.
DR MIM; 188345; -.
DR GO; GO:0004798; F:thymidylate kinase activity; TAS.
DR GO; GO:0007049; P:cell cycle; TAS.
DR InterPro; IPR000062; Thymidylate_kin.
DR Pfam; PF02223; Thymidylate_kin; 1.
DR TIGRFAMs; TIGR00041; DTMP_kinase; 1.
DR PROSITE; PS01331; THYMIDYLATE_KINASE; 1.
KW Transferase; Kinase; Nucleotide biosynthesis; ATP-binding;
KW 3D-structure.
FT NP_BIND 13 20 ATP (Probable).
FT CONFLICT 31 37 CAAGHRA -> SRGPPP (in Ref. 1).
FT CONFLICT 58 58 Q -> K (in Ref. 2).
FT CONFLICT 183 184 SI -> RL (in Ref. 1).
FT CONFLICT 190 191 EL -> DI (in Ref. 3).
FT STRAND 8 12
FT TURN 15 16
FT HELIX 19 32
FT TURN 33 34
FT STRAND 37 41
FT TURN 45 46
FT HELIX 48 57
FT TURN 58 59
FT HELIX 65 77
FT TURN 78 79
FT HELIX 80 88
FT TURN 89 90
FT STRAND 92 96
FT HELIX 99 106
FT TURN 107 108
FT TURN 110 111
FT HELIX 114 118
FT HELIX 119 121
FT TURN 122 123
FT STRAND 125 125
FT STRAND 129 134
FT HELIX 137 140
FT TURN 141 142
FT TURN 150 151
FT HELIX 154 167
FT TURN 168 169
FT TURN 171 172
FT STRAND 175 179
FT TURN 180 181
FT HELIX 184 202
FT TURN 203 204
FT STRAND 209 209
FT TURN 210 212
SQ SEQUENCE 212 AA; 23833 MW; E42876625B3096DA CRC64;
MAARRGALIV LEGVDRAGKS TQSRKLVEAL CAAGHRAELL RFPERSTEIG KLLSSYLQKK
SDVEDHSVHL LFSANRWEQV PLIKEKLSQG VTLVVDRYAF SGVAFTGAKE NFSLDWCKQP
DVGLPKPDLV LFLQLQLADA AKRGAFGHER YENGAFQERA LRCFHQLMKD TTLNWKMVDA
SKSIEAVHEE LRVLSEDAIR TATEKPLGEL WK
//
ID M4K1_HUMAN STANDARD; PRT; 833 AA.
AC Q92918;
DT 10-OCT-2003 (Rel. 42, Created)
DT 10-OCT-2003 (Rel. 42, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE Mitogen-activated protein kinase kinase kinase kinase 1 (EC 2.7.1.37)
DE (MAPK/ERK kinase kinase kinase 1) (MEK kinase kinase 1) (MEKKK 1)
DE (Hematopoietic progenitor kinase).
GN MAP4K1 OR HPK1.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A., FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH
RP MAP3K1.
RC TISSUE=Fetal liver;
RX MEDLINE=96421968; PubMed=8824585;
RA Hu M.C.-T., Qiu W.R., Wang X., Meyer C.F., Tan T.-H.;
RT "Human HPK1, a novel human hematopoietic progenitor kinase that
RT activates the JNK/SAPK kinase cascade.";
RL Genes Dev. 10:2251-2264(1996).
CC -!- FUNCTION: May play a role in the response to environmental stress.
CC Appears to act upstream of the c-jun N-terminal pathway.
CC -!- FUNCTION: May play a role in hematopoietic lineage decisions and
CC growth regulation (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC -!- COFACTOR: Magnesium.
CC -!- SUBUNIT: Interacts with MAP3K1.
CC -!- TISSUE SPECIFICITY: Expressed primarily in hematopoietic organs,
CC including bone marrow, spleen and thymus. Also expressed at very
CC low levels in lung, kidney, mammary glands and small
CC intestine.
CC -!- SIMILARITY: Belongs to the Ser/Thr protein kinase family. STE20
CC subfamily.
CC -!- SIMILARITY: Contains 1 CNH domain.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; U66464; AAB97983.1; -.
DR HSSP; Q63450; 1A06.
DR Genew; HGNC:6863; MAP4K1.
DR MIM; 601983; -.
DR GO; GO:0005524; F:ATP binding; IDA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA.
DR GO; GO:0007257; P:activation of JUNK; TAS.
DR GO; GO:0006468; P:protein amino acid phosphorylation; IDA.
DR GO; GO:0007243; P:protein kinase cascade; IDA.
DR GO; GO:0045610; P:regulation of hemocyte differentiation; ISS.
DR GO; GO:0006950; P:response to stress; IDA.
DR InterPro; IPR001180; Citron.
DR InterPro; IPR000719; Prot_kinase.
DR InterPro; IPR002290; Ser_thr_pkinase.
DR InterPro; IPR008271; Ser_thr_pkin_AS.
DR InterPro; IPR001245; Tyr_pkinase.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00069; pkinase; 1.
DR PRINTS; PR00109; TYRKINASE.
DR ProDom; PD000001; Prot_kinase; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00220; S_TKc; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; FALSE_NEG.
KW ATP-binding; Transferase; Kinase; Serine/threonine-protein kinase.
FT DOMAIN 17 274 PROTEIN KINASE.
FT DOMAIN 501 807 CNH.
FT NP_BIND 23 31 ATP (By similarity).
FT BINDING 46 46 ATP (By similarity).
FT ACT_SITE 137 137 By similarity.
SQ SEQUENCE 833 AA; 91296 MW; 3C98CF01BE42E151 CRC64;
MDVVDPDIFN RDPRDHYDLL QRLGGGTYGE VFKARDKVSG DLVALKMVKM EPDDDVSTLQ
KEILILKTCR HANIVAYHGS YLWLQKLWIC MEFCGAGSLQ DIYQVTGSLS ELQISYVCRE
VLQGLAYLHS QKKIHRDIKG ANILINDAGE VRLADFGISA QIGATLARRL SFIGTPYWMA
PEVAAVALKG GYNELCDIWS LGITAIELAE LQPPLFDVHP LRVLFLMTKS GYQPPRLKEK
GKWSAAFHNF IKVTLTKSPK KRPSATKMLS HQLVSQPGLN RGLILDLLDK LKNPGKGPSI
GDIEDEEPEL PPAIPRRIRS THRSSSLGIP DADCCRRHME FRKLRGMETR PPANTARLQP
PRDLRSSSPR KQLSESSDDD YDDVDIPTPA EDTPPPLPPK PKFRSPSDEG PGSMGDDGQL
SPGVLVRCAS GPPPNSPRPG PPPSTSSPHL TAHSEPSLWN PPSRELDKPP LLPPKKEKMK
RKGCALLVKL FNGCPLRIHS TAAWTHPSTK DQHLLLGAEE GIFILNRNDQ EATLEMLFPS
RTTWVYSINN VLMSLSGKTP HLYSHSILGL LERKETRAGN PIAHISPHRL LARKNMVSTK
IQDTKGCRAC CVAEGASSGG PFLCGALETS VVLLQWYQPM NKFLLVRQVL FPLPTPLSVF
ALLTGPGSEL PAVCIGVSPG RPGKSVLFHT VRFGALSCWL GEMSTEHRGP VQVTQVEEDM
VMVLMDGSVK LVTPEGSPVR GLRTPEIPMT EAVEAVAMVG GQLQAFWKHG VQVWALGSDQ
LLQELRDPTL TFRLLGSPRL ECSGTISPHC NLLLPGSSNS PASASRVAGI TGL
//
ID NAGK_HUMAN STANDARD; PRT; 344 AA.
AC Q9UJ70; Q9BS29; Q9BVP0;
DT 28-FEB-2003 (Rel. 41, Created)
DT 28-FEB-2003 (Rel. 41, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE N-acetylglucosamine kinase (EC 2.7.1.59) (GlcNAc kinase).
GN NAGK.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A., AND TISSUE SPECIFICITY.
RX MEDLINE=20285356; PubMed=10824116;
RA Hinderlich S., Berger M., Schwarzkopf M., Effertz K., Reutter W.;
RT "Molecular cloning and characterization of murine and human N-
RT acetylglucosamine kinase.";
RL Eur. J. Biochem. 267:3301-3308(2000).
RN [2]
RP SEQUENCE FROM N.A.
RC TISSUE=Kidney, and Skin;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [3]
RP PHOSPHORYLATION OF TYR-205.
RX MEDLINE=22107313; PubMed=12112843;
RA Maguire P.B., Wynne K.J., Harney D.F., O'Donoghue N.M., Stephens G.,
RA Fitzgerald D.J.;
RT "Identification of the phosphotyrosine proteome from thrombin
RT activated platelets.";
RL Proteomics 2:642-648(2002).
CC -!- FUNCTION: Converts endogenous N-acetylglucosamine (GlcNAc), a
CC major component of complex carbohydrates, from lysosomal
CC degradation or nutritional sources into GlcNAc 6-phosphate. Also
CC has ManNAc kinase activity (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + N-acetyl-D-glucosamine = ADP + N-acetyl-
CC D-glucosamine 6-phosphate.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AJ242910; CAB61848.1; -.
DR EMBL; BC001029; AAH01029.1; -.
DR EMBL; BC005371; AAH05371.1; -.
DR Genew; HGNC:17174; NAGK.
DR MIM; 606828; -.
DR GO; GO:0006044; P:N-acetylglucosamine metabolism; TAS.
DR GO; GO:0006051; P:N-acetylmannosamine metabolism; TAS.
DR InterPro; IPR002731; ATPase_BadF.
DR Pfam; PF01869; BcrAD_BadFG; 1.
KW Kinase; Transferase; ATP-binding; Phosphorylation.
FT MOD_RES 205 205 PHOSPHORYLATION.
FT CONFLICT 38 38 W -> R (IN REF. 2; AAH05371).
FT CONFLICT 60 60 A -> V (IN REF. 2; AAH05371).
FT CONFLICT 70 70 S -> I (in Ref. 1).
FT CONFLICT 121 121 V -> I (in Ref. 1).
SQ SEQUENCE 344 AA; 37375 MW; FCBB6B328EF4D515 CRC64;
MAAIYGGVEG GGTRSEVLLV SEDGKILAEA DGLSTNHWLI GTDKCVERIN EMVNRAKRKA
GVDPLVPLRS LGLSLSGGDQ EDAGRILIEE LRDRFPYLSE SYLITTDAAG SIATATPDGG
VVLISGTGSN CRLINPDGSE SGCGGWGHMM GDEGSAYWIA HQAVKIVFDS IDNLEAAPHD
IGYVKQAMFH YFQVPDRLGI LTHLYRDFDK CRFAGFCRKI AEGAQQGDPL SRYIFRKAGE
MLGRHIVAVL PEIDPVLFQG KIGLPILCVG SVWKSWELLK EGFLLALTQG REIQAQNFFS
SFTLMKLRHS SALGGASLGA RHIGHLLPMD YSANAIAFYS YTFS
//
ID NDK3_HUMAN STANDARD; PRT; 169 AA.
AC Q13232; Q9BWH4;
DT 15-DEC-1998 (Rel. 37, Created)
DT 28-FEB-2003 (Rel. 41, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Nucleoside diphosphate kinase 3 (EC 2.7.4.6) (NDK 3) (NDP kinase 3)
DE (nm23-H3) (DR-nm23).
GN NME3.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RX MEDLINE=95365382; PubMed=7638209;
RA Venturelli D., Martinez R., Melotti P., Casella I., Peschle C.,
RA Cucco C., Spampinato G., Darzynkiewicz Z., Calabretta B.;
RT "Overexpression of DR-nm23, a protein encoded by a member of the nm23
RT gene family, inhibits granulocyte differentiation and induces
RT apoptosis in 32Dc13 myeloid cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:7435-7439(1995).
RN [2]
RP SEQUENCE FROM N.A.
RX MEDLINE=21096910; PubMed=11157797;
RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K.,
RA Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J.,
RA Higgs D.R.;
RT "Sequence, structure and pathology of the fully annotated terminal 2
RT Mb of the short arm of human chromosome 16.";
RL Hum. Mol. Genet. 10:339-352(2001).
RN [3]
RP SEQUENCE FROM N.A.
RC TISSUE=Eye;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC -!- FUNCTION: Major role in the synthesis of nucleoside triphosphates
CC other than ATP (By similarity). Has probably a role for in normal
CC hematopoiesis inhibits granulocyte differentiation and induces
CC apoptosis.
CC -!- CATALYTIC ACTIVITY: ATP + nucleoside diphosphate = ADP +
CC nucleoside triphosphate.
CC -!- DEVELOPMENTAL STAGE: Preferentially expressed at early stages of
CC myeloid differentiation of highly purified CD34+ cells.
CC -!- SIMILARITY: Belongs to the NDK family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; U29656; AAA85097.1; -.
DR EMBL; AE006639; AAK61291.1; -.
DR EMBL; BC000250; AAH00250.1; -.
DR PIR; I39074; I39074.
DR HSSP; P08879; 1NSQ.
DR Genew; HGNC:7851; NME3.
DR MIM; 601817; -.
DR GO; GO:0006917; P:induction of apoptosis; TAS.
DR InterPro; IPR001564; NDK.
DR Pfam; PF00334; NDK; 1.
DR PRINTS; PR01243; NUCDPKINASE.
DR ProDom; PD001018; NDK; 1.
DR SMART; SM00562; NDK; 1.
DR PROSITE; PS00469; NDP_KINASES; 1.
KW Transferase; Kinase; ATP-binding.
FT ACT_SITE 135 135 By similarity.
FT CONFLICT 60 60 A -> S (in Ref. 1).
FT CONFLICT 131 131 Missing (in Ref. 1).
SQ SEQUENCE 169 AA; 19015 MW; CCA41A122A37202D CRC64;
MICLVLTIFA NLFPAACTGA HERTFLAVKP DGVQRRLVGE IVRRFERKGF KLVALKLVQA
SEELLREHYA ELRERPFYGR LVKYMASGPV VAMVWQGLDV VRTSRALIGA TNPADAPPGT
IRGDFCIEVG KNLIHGSDSV ESARREIALW FRADELLCWE DSAGHWLYE
//
ID NDK6_HUMAN STANDARD; PRT; 186 AA.
AC O75414; Q96E73; Q9BQ63;
DT 16-OCT-2001 (Rel. 40, Created)
DT 16-OCT-2001 (Rel. 40, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Nucleoside diphosphate kinase 6 (EC 2.7.4.6) (NDK 6) (NDP kinase 6)
DE (nm23-H6) (Inhibitor of p53-induced apoptosis-alpha) (IPIA-alpha).
GN NME6.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RC TISSUE=Liver;
RX MEDLINE=99381535; PubMed=10453732;
RA Mehus J.G., Deloukas P., Lambeth D.O.;
RT "NME6: a new member of the nm23/nucleoside diphosphate kinase gene
RT family located on human chromosome 3p21.3.";
RL Hum. Genet. 104:454-459(1999).
RN [2]
RP SEQUENCE FROM N.A.
RA Nakamura H., Tsuiki H., Honda Y., Sasaki J., Masuko N., Akagi K.,
RA Saya H.;
RT "Identification of a gene that inhibits p53-induced apoptosis.";
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SEQUENCE FROM N.A.
RC TISSUE=Lymph;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC -!- FUNCTION: Major role in the synthesis of nucleoside triphosphates
CC other than ATP (By similarity). Inhibitor of p53-induced
CC apoptosis.
CC -!- CATALYTIC ACTIVITY: ATP + nucleoside diphosphate = ADP +
CC nucleoside triphosphate.
CC -!- TISSUE SPECIFICITY: Expressed at a moderately low level in many
CC tissues. Most abundant in kidney, prostate, ovary, intestine, and
CC spleen.
CC -!- SIMILARITY: Belongs to the NDK family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AF051941; AAC78463.1; -.
DR EMBL; U90449; AAC69439.1; ALT_INIT.
DR EMBL; BC001808; AAH01808.1; ALT_INIT.
DR EMBL; BC012828; AAH12828.1; ALT_INIT.
DR Genew; HGNC:20567; NME6.
DR MIM; 608294; -.
DR GO; GO:0008189; F:apoptosis inhibitor activity; NAS.
DR GO; GO:0005524; F:ATP binding; NAS.
DR GO; GO:0004550; F:nucleoside-diphosphate kinase activity; TAS.
DR GO; GO:0009142; P:nucleoside triphosphate biosynthesis; NAS.
DR InterPro; IPR001564; NDK.
DR Pfam; PF00334; NDK; 1.
DR PRINTS; PR01243; NUCDPKINASE.
DR ProDom; PD001018; NDK; 1.
DR SMART; SM00562; NDK; 1.
DR PROSITE; PS00469; NDP_KINASES; 1.
KW Transferase; Kinase; ATP-binding; Apoptosis.
FT ACT_SITE 129 129 By similarity.
SQ SEQUENCE 186 AA; 21142 MW; DB8C5E046FACD143 CRC64;
MASILRSPQA LQLTLALIKP DAVAHPLILE AVHQQILSNK FLIVRMRELL WRKEDCQRFY
REHEGRFFYQ RLVEFMASGP IRAYILAHKD AIQLWRTLMG PTRVFRARHV APDSIRGSFG
LTDTRNTTHG SDSVVSASRE IAAFFPDFSE QRWYEEEEPQ LRCGPVCYSP EGGVHYVAGT
GGLGPA
//
ID NDK7_HUMAN STANDARD; PRT; 376 AA.
AC Q9Y5B8;
DT 16-OCT-2001 (Rel. 40, Created)
DT 16-OCT-2001 (Rel. 40, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE Nucleoside diphosphate kinase 7 (EC 2.7.4.6) (NDK 7) (NDP kinase 7)
DE (nm23-H7).
GN NME7.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RA Mehus J.G., Lambeth D.O.;
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SEQUENCE FROM N.A.
RC TISSUE=Urinary bladder;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC -!- CATALYTIC ACTIVITY: ATP + nucleoside diphosphate = ADP +
CC nucleoside triphosphate.
CC -!- SIMILARITY: Belongs to the NDK family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AF153191; AAD34622.1; -.
DR EMBL; BC006983; AAH06983.1; -.
DR HSSP; P22887; 1LEO.
DR Genew; HGNC:20461; NME7.
DR InterPro; IPR006602; DUF_DM10.
DR InterPro; IPR001564; NDK.
DR Pfam; PF00334; NDK; 2.
DR PRINTS; PR01243; NUCDPKINASE.
DR ProDom; PD001018; NDK; 2.
DR SMART; SM00676; DM10; 1.
DR SMART; SM00562; NDK; 2.
DR PROSITE; PS00469; NDP_KINASES; FALSE_NEG.
KW Transferase; Kinase; ATP-binding.
FT ACT_SITE 206 206 By similarity.
SQ SEQUENCE 376 AA; 42491 MW; 67C121D6C36E7012 CRC64;
MNHSERFVFI AEWYDPNASL LRRYELLFYP GDGSVEMHDV KNHRTFLKRT KYDNLHLEDL
FIGNKVNVFS RQLVLIDYGD QYTARQLGSR KEKTLALIKP DAISKAGEII EIINKAGFTI
TKLKMMMLSR KEALDFHVDH QSRPFFNELI QFITTGPIIA MEILRDDAIC EWKRLLGPAN
SGVARTDASE SIRALFGTDG IRNAAHGPDS FASAAREMEL FFPSSGGCGP ANTAKFTNCT
CCIVKPHAVS EGLLGKILMA IRDAGFEISA MQMFNMDRVN VEEFYEVYKG VVTEYHDMVT
EMYSGPCVAM EIQQNNATKT FREFCGPADP EIARHLRPGT LRAIFGKTKI QNAVHCTDLP
EDGLLEVQYF FKILDN
//
ID NDK8_HUMAN STANDARD; PRT; 137 AA.
AC O60361;
DT 15-DEC-1998 (Rel. 37, Created)
DT 15-DEC-1998 (Rel. 37, Last sequence update)
DT 16-OCT-2001 (Rel. 40, Last annotation update)
DE Putative nucleoside diphosphate kinase (EC 2.7.4.6) (NDK) (NDP
DE kinase).
GN H_278C19.3.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RA Bradshaw H., Ozersky P.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Major role in the synthesis of nucleoside triphosphates
CC other than ATP (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + nucleoside diphosphate = ADP +
CC nucleoside triphosphate.
CC -!- SIMILARITY: Belongs to the NDK family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AC004263; AAC05177.1; -.
DR HSSP; P22392; 1NUE.
DR InterPro; IPR001564; NDK.
DR Pfam; PF00334; NDK; 1.
DR PRINTS; PR01243; NUCDPKINASE.
DR ProDom; PD001018; NDK; 1.
DR SMART; SM00562; NDK; 1.
DR PROSITE; PS00469; NDP_KINASES; 1.
KW Transferase; Kinase; ATP-binding.
FT ACT_SITE 103 103 By similarity.
SQ SEQUENCE 137 AA; 15529 MW; 92671EB92FE23167 CRC64;
MQCGLVGKII KRFEQKGFRL VAMKFLPASE EHLKQHYIDL KDRPFFPGLV KYMNSGPVVA
MVWEGLNVVK TGRVMLGETN PADSKPGTIR GDFCIQVGRN IIHGSDSVKS AEKEISLRFK
PEELVDYKSC AHDWVYE
//
ID NDKA_HUMAN STANDARD; PRT; 152 AA.
AC P15531;
DT 01-APR-1990 (Rel. 14, Created)
DT 01-APR-1990 (Rel. 14, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Nucleoside diphosphate kinase A (EC 2.7.4.6) (NDK A) (NDP kinase A)
DE (Tumor metastatic process-associated protein) (Metastasis inhibition
DE factor nm23) (nm23-H1).
GN NME1 OR NDPKA OR NM23.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RX MEDLINE=90044071; PubMed=2509941;
RA Rosengard A.M., Krutzsch H.C., Shearn A., Biggs J.R., Barker E.,
RA Margulies I.M.K., King C.R., Liotta L.A., Steeg P.S.;
RT "Reduced Nm23/Awd protein in tumour metastasis and aberrant
RT Drosophila development.";
RL Nature 342:177-180(1989).
RN [2]
RP SEQUENCE FROM N.A.
RX MEDLINE=94095204; PubMed=8270257;
RA Dooley S., Seib T., Engel M., Theisinger B., Janz H., Piontek K.,
RA Zang K.D., Welter C.;
RT "Isolation and characterization of the human genomic locus coding for
RT the putative metastasis control gene nm23-H1.";
RL Hum. Genet. 93:63-66(1994).
RN [3]
RP SEQUENCE FROM N.A.
RX MEDLINE=93153759; PubMed=7916650;
RA Wang L., Patel U., Ghosh L., Chen H.C., Banerjee S.;
RT "Mutation in the nm23 gene is associated with metastasis in
RT colorectal cancer.";
RL Cancer Res. 53:717-720(1993).
RN [4]
RP SEQUENCE FROM N.A.
RC TISSUE=Brain, and Lung;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [5]
RP SEQUENCE, SUBUNITS, AND ACTIVE SITE.
RX MEDLINE=91224972; PubMed=1851158;
RA Gilles A.-M., Presecan E., Vonica A., Lascu I.;
RT "Nucleoside diphosphate kinase from human erythrocytes. Structural
RT characterization of the two polypeptide chains responsible for
RT heterogeneity of the hexameric enzyme.";
RL J. Biol. Chem. 266:8784-8789(1991).
RN [6]
RP VARIANT NEUROBLASTOMA GLY-120.
RX MEDLINE=94322908; PubMed=8047138;
RA Chang C.L., Zhu X.-X., Thoraval D.H., Ungar D., Rawwas J., Hora N.,
RA Strahler J.R., Hanash S.M.;
RT "Nm23-H1 mutation in neuroblastoma.";
RL Nature 370:335-336(1994).
CC -!- FUNCTION: Major role in the synthesis of nucleoside triphosphates
CC other than ATP.
CC -!- CATALYTIC ACTIVITY: ATP + nucleoside diphosphate = ADP +
CC nucleoside triphosphate.
CC -!- SUBUNIT: Hexamer of two different chains: A and B (A6, A5B, A4B2,
CC A3B3, A2B4, AB5, B6).
CC -!- SUBCELLULAR LOCATION: Nuclear and cytoplasmic.
CC -!- PTM: The N-terminus is blocked.
CC -!- DISEASE: This protein is found in reduced amount in tumor cells
CC of high metastasic potential. Somatic mutations of NME1 are found
CC in neuroblastoma.
CC -!- SIMILARITY: Belongs to the NDK family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; X17620; CAA35621.1; ALT_INIT.
DR EMBL; X75598; CAA53270.1; -.
DR EMBL; X73066; CAA51527.1; -.
DR EMBL; BC000293; AAH00293.1; -.
DR EMBL; BC018994; AAH18994.1; -.
DR PIR; A33386; A33386.
DR PDB; 1JXV; 18-DEC-02.
DR Aarhus/Ghent-2DPAGE; 4115; IEF.
DR Aarhus/Ghent-2DPAGE; 5112; IEF.
DR PMMA-2DPAGE; P15531; -.
DR Genew; HGNC:7849; NME1.
DR GK; P15531; -.
DR MIM; 156490; -.
DR GO; GO:0005634; C:nucleus; NAS.
DR GO; GO:0005524; F:ATP binding; NAS.
DR GO; GO:0004550; F:nucleoside-diphosphate kinase activity; NAS.
DR GO; GO:0008285; P:negative regulation of cell proliferation; TAS.
DR GO; GO:0009142; P:nucleoside triphosphate biosynthesis; NAS.
DR InterPro; IPR001564; NDK.
DR Pfam; PF00334; NDK; 1.
DR PRINTS; PR01243; NUCDPKINASE.
DR ProDom; PD001018; NDK; 1.
DR SMART; SM00562; NDK; 1.
DR PROSITE; PS00469; NDP_KINASES; 1.
KW Transferase; Kinase; ATP-binding; Nuclear protein; Anti-oncogene;
KW Disease mutation; 3D-structure.
FT ACT_SITE 118 118
FT VARIANT 120 120 S -> G (in neuroblastoma).
FT /FTId=VAR_004625.
FT STRAND 6 11
FT HELIX 13 17
FT TURN 18 19
FT HELIX 21 31
FT TURN 32 32
FT STRAND 34 41
FT HELIX 45 51
FT TURN 52 52
FT HELIX 53 55
FT TURN 56 57
FT TURN 60 60
FT HELIX 61 69
FT STRAND 73 79
FT TURN 81 82
FT HELIX 83 91
FT HELIX 96 98
FT TURN 101 102
FT HELIX 104 108
FT STRAND 111 111
FT TURN 112 113
FT STRAND 114 114
FT STRAND 117 119
FT HELIX 123 133
FT HELIX 136 138
FT TURN 145 146
FT HELIX 147 150
SQ SEQUENCE 152 AA; 17149 MW; AAE9C0DF63CB70A1 CRC64;
MANCERTFIA IKPDGVQRGL VGEIIKRFEQ KGFRLVGLKF MQASEDLLKE HYVDLKDRPF
FAGLVKYMHS GPVVAMVWEG LNVVKTGRVM LGETNPADSK PGTIRGDFCI QVGRNIIHGS
DSVESAEKEI GLWFHPEELV DYTSCAQNWI YE
//
ID NDKB_HUMAN STANDARD; PRT; 152 AA.
AC P22392;
DT 01-AUG-1991 (Rel. 19, Created)
DT 01-AUG-1991 (Rel. 19, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Nucleoside diphosphate kinase B (EC 2.7.4.6) (NDK B) (NDP kinase B)
DE (nm23-H2) (C-myc purine-binding transcription factor PUF).
GN NME2 OR NM23B.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE, SUBUNITS, AND ACTIVE SITE.
RX MEDLINE=91224972; PubMed=1851158;
RA Gilles A.-M., Presecan E., Vonica A., Lascu I.;
RT "Nucleoside diphosphate kinase from human erythrocytes. Structural
RT characterization of the two polypeptide chains responsible for
RT heterogeneity of the hexameric enzyme.";
RL J. Biol. Chem. 266:8784-8789(1991).
RN [2]
RP SEQUENCE FROM N.A.
RX MEDLINE=91105674; PubMed=1988104;
RA Stahl J.A., Leone A., Rosengard A.M., Porter L., Liotta L.A.,
RA Steeg P.S., King C.R.;
RT "Identification of a second human nm23 gene, nm23-H2.";
RL Cancer Res. 51:445-449(1991).
RN [3]
RP SEQUENCE FROM N.A.
RX MEDLINE=93324921; PubMed=8392752;
RA Postel E.H., Berberich S.J., Flint S.J., Ferrone C.A.;
RT "Human c-myc transcription factor PuF identified as nm23-H2
RT nucleoside diphosphate kinase, a candidate suppressor of tumor
RT metastasis.";
RL Science 261:478-480(1993).
RN [4]
RP SEQUENCE FROM N.A.
RC TISSUE=Eye;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX MEDLINE=95387396; PubMed=7658474;
RA Webb P.A., Perisic O., Mendola C.E., Backer J.M., Williams R.L.;
RT "The crystal structure of a human nucleoside diphosphate kinase,
RT NM23-H2.";
RL J. Mol. Biol. 251:574-587(1995).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2 ANGSTROMS).
RX MEDLINE=96363668; PubMed=8747457;
RA Morera S., Lacombe M.-L., Xu Y., Lebras G., Janin J.;
RT "X-ray structure of human nucleoside diphosphate kinase B complexed
RT with GDP at 2-A resolution.";
RL Structure 3:1307-1314(1995).
CC -!- FUNCTION: Major role in the synthesis of nucleoside triphosphates
CC other than ATP.
CC -!- FUNCTION: Acts as a transcriptional activator of the c-Myc gene;
CC binds DNA nonspecifically (according to Ref.3).
CC -!- CATALYTIC ACTIVITY: ATP + nucleoside diphosphate = ADP +
CC nucleoside triphosphate.
CC -!- SUBUNIT: Hexamer of two different chains: A and B (A6, A5B, A4B2,
CC A3B3, A2B4, AB5, B6).
CC -!- SUBCELLULAR LOCATION: Nuclear and cytoplasmic.
CC -!- PTM: The N-terminus is blocked.
CC -!- DISEASE: This protein is found in reduced amount in tumor cells of
CC high metastasic potential.
CC -!- SIMILARITY: Belongs to the NDK family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; X58965; CAB37870.1; -.
DR EMBL; M36981; AAA36369.1; -.
DR EMBL; L16785; AAA60228.1; -.
DR EMBL; BC002476; AAH02476.1; -.
DR PIR; A49798; A49798.
DR PDB; 1NSK; 15-OCT-95.
DR PDB; 1NUE; 03-APR-96.
DR TRANSFAC; T00706; -.
DR Genew; HGNC:7850; NME2.
DR GK; P22392; -.
DR MIM; 156491; -.
DR GO; GO:0005634; C:nucleus; NAS.
DR GO; GO:0005524; F:ATP binding; NAS.
DR GO; GO:0004550; F:nucleoside-diphosphate kinase activity; TAS.
DR GO; GO:0003700; F:transcription factor activity; TAS.
DR GO; GO:0008285; P:negative regulation of cell proliferation; TAS.
DR GO; GO:0009142; P:nucleoside triphosphate biosynthesis; NAS.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; TAS.
DR InterPro; IPR001564; NDK.
DR Pfam; PF00334; NDK; 1.
DR PRINTS; PR01243; NUCDPKINASE.
DR ProDom; PD001018; NDK; 1.
DR SMART; SM00562; NDK; 1.
DR PROSITE; PS00469; NDP_KINASES; 1.
KW Transferase; Kinase; ATP-binding; Nuclear protein; Anti-oncogene;
KW DNA-binding; Transcription regulation; Activator; 3D-structure.
FT ACT_SITE 118 118
FT STRAND 6 11
FT HELIX 13 17
FT TURN 18 19
FT HELIX 21 31
FT TURN 32 32
FT STRAND 34 41
FT HELIX 45 51
FT TURN 52 52
FT HELIX 53 55
FT TURN 56 57
FT TURN 59 60
FT HELIX 61 69
FT STRAND 73 79
FT TURN 81 82
FT HELIX 83 91
FT HELIX 96 98
FT TURN 101 102
FT HELIX 104 108
FT HELIX 112 114
FT STRAND 117 119
FT HELIX 123 133
FT HELIX 136 138
FT TURN 145 146
FT HELIX 147 150
SQ SEQUENCE 152 AA; 17298 MW; 1A5C3F84D7AD272C CRC64;
MANLERTFIA IKPDGVQRGL VGEIIKRFEQ KGFRLVAMKF LRASEEHLKQ HYIDLKDRPF
FPGLVKYMNS GPVVAMVWEG LNVVKTGRVM LGETNPADSK PGTIRGDFCI QVGRNIIHGS
DSVKSAEKEI SLWFKPEELV DYKSCAHDWV YE
//
ID NDKM_HUMAN STANDARD; PRT; 187 AA.
AC O00746;
DT 01-NOV-1997 (Rel. 35, Created)
DT 01-NOV-1997 (Rel. 35, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Nucleoside diphosphate kinase, mitochondrial precursor (EC 2.7.4.6)
DE (NDP kinase, mitochondrial) (NDK) (nm23-H4).
GN NME4 OR NM23D.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE.
RC TISSUE=Stomach;
RX MEDLINE=97254440; PubMed=9099850;
RA Milon L., Rousseau-Merck M.-F., Munier A., Erent M., Lascu I.,
RA Capeau J., Lacombe M.-L.;
RT "nm23-H4, a new member of the family of human nm23/nucleoside
RT diphosphate kinase genes localised on chromosome 16p13.";
RL Hum. Genet. 99:550-557(1997).
RN [2]
RP SEQUENCE FROM N.A.
RX MEDLINE=21096910; PubMed=11157797;
RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K.,
RA Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J.,
RA Higgs D.R.;
RT "Sequence, structure and pathology of the fully annotated terminal 2
RT Mb of the short arm of human chromosome 16.";
RL Hum. Mol. Genet. 10:339-352(2001).
RN [3]
RP SEQUENCE FROM N.A.
RA Wallis J.;
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SEQUENCE FROM N.A.
RC TISSUE=Skin, and Uterus;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [5]
RP CHARACTERIZATION, AND X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX MEDLINE=20261549; PubMed=10799505;
RA Milon L., Meyer P., Chiadmi M., Munier A., Johansson M., Karlsson A.,
RA Lascu I., Capeau J., Janin J., Lacombe M.-L.;
RT "The human nm23-H4 gene product is a mitochondrial nucleoside
RT diphosphate kinase.";
RL J. Biol. Chem. 275:14264-14272(2000).
CC -!- FUNCTION: Major role in the synthesis of nucleoside triphosphates
CC other than ATP (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + nucleoside diphosphate = ADP +
CC nucleoside triphosphate.
CC -!- SUBUNIT: Homohexamer.
CC -!- SUBCELLULAR LOCATION: Mitochondrial intermembrane space.
CC -!- TISSUE SPECIFICITY: Widely distributed. Found at very high levels
CC in prostate, heart, liver, small intestine, and skeletal muscle
CC tissues, and in low amounts in the brain and in blood leukocytes.
CC -!- SIMILARITY: Belongs to the NDK family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; Y07604; CAA68877.1; -.
DR EMBL; AE006463; AAK61230.1; -.
DR EMBL; Z97634; CAC37288.1; -.
DR EMBL; BC004880; AAH04880.1; -.
DR EMBL; BC017067; AAH17067.1; -.
DR PDB; 1EHW; 17-MAY-00.
DR Genew; HGNC:7852; NME4.
DR MIM; 601818; -.
DR GO; GO:0005739; C:mitochondrion; TAS.
DR GO; GO:0004550; F:nucleoside-diphosphate kinase activity; TAS.
DR GO; GO:0009116; P:nucleoside metabolism; TAS.
DR InterPro; IPR001564; NDK.
DR Pfam; PF00334; NDK; 1.
DR PRINTS; PR01243; NUCDPKINASE.
DR ProDom; PD001018; NDK; 1.
DR SMART; SM00562; NDK; 1.
DR PROSITE; PS00469; NDP_KINASES; 1.
KW Transferase; Kinase; ATP-binding; Mitochondrion; Transit peptide;
KW 3D-structure.
FT TRANSIT 1 33 Mitochondrion (Potential).
FT CHAIN 34 187 NUCLEOSIDE DIPHOSPHATE KINASE.
FT ACT_SITE 151 151 By similarity.
FT TURN 36 37
FT STRAND 39 44
FT HELIX 46 50
FT TURN 51 52
FT HELIX 54 64
FT TURN 65 65
FT STRAND 67 74
FT HELIX 78 84
FT TURN 85 85
FT HELIX 86 88
FT TURN 89 90
FT TURN 92 93
FT HELIX 94 101
FT TURN 102 102
FT STRAND 106 112
FT TURN 114 115
FT HELIX 116 124
FT HELIX 129 131
FT TURN 134 135
FT HELIX 137 141
FT STRAND 150 152
FT HELIX 156 166
FT HELIX 169 171
SQ SEQUENCE 187 AA; 20658 MW; A56FEF18A7D712D4 CRC64;
MGGLFWRSAL RGLRCGPRAP GPSLLVRHGS GGPSWTRERT LVAVKPDGVQ RRLVGDVIQR
FERRGFTLVG MKMLQAPESV LAEHYQDLRR KPFYPALIRY MSSGPVVAMV WEGYNVVRAS
RAMIGHTDSA EAAPGTIRGD FSVHISRNVI HASDSVEGAQ REIQLWFQSS ELVSWADGGQ
HSSIHPA
//
ID P11A_HUMAN STANDARD; PRT; 1068 AA.
AC P42336; Q99762;
DT 01-NOV-1995 (Rel. 32, Created)
DT 01-NOV-1995 (Rel. 32, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit,
DE alpha isoform (EC 2.7.1.153) (PI3-kinase p110 subunit alpha) (PtdIns-
DE 3-kinase p110) (PI3K).
GN PIK3CA.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RX MEDLINE=95229146; PubMed=7713498;
RA Volinia S., Hiles I., Ormondroyd E., Nizetic D., Antonacci R.,
RA Rocchi M., Waterfield M.;
RT "Molecular cloning, cDNA sequence, and chromosomal localization of
RT the human phosphatidylinositol 3-kinase p110 alpha (PIK3CA) gene.";
RL Genomics 24:472-477(1994).
RN [2]
RP SEQUENCE FROM N.A.
RX MEDLINE=97196568; PubMed=9043658;
RA Stirdivant S.M., Ahern J., Conroy R.R., Barnett S.F., Ledder L.M.,
RA Oliff A., Heimbrook D.C.;
RT "Cloning and mutagenesis of the p110 alpha subunit of human
RT phosphoinositide 3'-hydroxykinase.";
RL Bioorg. Med. Chem. 5:65-74(1997).
CC -!- FUNCTION: PHOSPHORYLATES PTDINS, PTDINS4P AND PTDINS(4,5)P2 WITH A
CC PREFERENCE FOR PTDINS(4,5)P2.
CC -!- CATALYTIC ACTIVITY: ATP + 1-phosphatidyl-1D-myo-inositol 4,5-
CC bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-
CC trisphosphate.
CC -!- SUBUNIT: HETERODIMER OF A P110 (CATALYTIC) AND A P85 (REGULATORY)
CC SUBUNIT.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC -!- SIMILARITY: Contains 1 C2 domain.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; Z29090; CAA82333.1; -.
DR EMBL; U79143; AAB39753.1; -.
DR PIR; I38110; I38110.
DR Genew; HGNC:8975; PIK3CA.
DR GK; P42336; -.
DR MIM; 171834; -.
DR InterPro; IPR008938; ARM.
DR InterPro; IPR000008; C2.
DR InterPro; IPR008973; C2_CaLB.
DR InterPro; IPR000403; PI3_PI4_kinase.
DR InterPro; IPR002420; PI3K_C2.
DR InterPro; IPR003113; PI3K_p85B.
DR InterPro; IPR000341; PI3K_ras_bind.
DR InterPro; IPR001263; PI3Ka.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF02192; PI3K_p85B; 1.
DR Pfam; PF00794; PI3K_rbd; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00142; PI3K_C2; 1.
DR SMART; SM00143; PI3K_p85B; 1.
DR SMART; SM00144; PI3K_rbd; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR PROSITE; PS00499; C2_DOMAIN_1; FALSE_NEG.
DR PROSITE; PS50004; C2_DOMAIN_2; FALSE_NEG.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
KW Transferase; Kinase; Multigene family.
FT DOMAIN 319 428 C2 DOMAIN.
FT DOMAIN 797 1068 PI3K/PI4K.
FT CONFLICT 43 43 V -> I (in Ref. 2).
FT CONFLICT 170 170 H -> N (in Ref. 2).
FT CONFLICT 187 187 R -> K (in Ref. 2).
FT CONFLICT 286 287 KM -> ML (in Ref. 2).
FT CONFLICT 332 332 R -> S (in Ref. 2).
FT CONFLICT 346 346 L -> V (in Ref. 2).
FT CONFLICT 723 723 R -> K (in Ref. 2).
FT CONFLICT 751 751 L -> F (in Ref. 2).
FT CONFLICT 767 767 K -> E (in Ref. 2).
SQ SEQUENCE 1068 AA; 124412 MW; 9E16BA7401A87B57 CRC64;
MPPRPSSGEL WGIHLMPPRI LVECLLPNGM IVTLECLREA TLVTIKHELF KEARKYPLHQ
LLQDESSYIF VSVTQEAERE EFFDETRRLC DLRLFQPFLK VIEPVGNREE KILNREIGFA
IGMPVCEFDM VKDPEVQDFR RNILNVCKEA VDLRDLNSPH SRAMYVYPPH VESSPELPKH
IYNKLDRGQI IVVIWVIVSP NNDKQKYTLK INHDCVPEQV IAEAIRKKTR SMLLSSEQLK
LCVLEYQGKY ILKVCGCDEY FLEKYPLSQY KYIRSCIMLG RMPNLKMMAK ESLYSQLPMD
CFTMPSYSRR ISTATPYMNG ETSTKSLWVI NRALRIKILC ATYVNLNIRD IDKIYVRTGI
YHGGEPLCDN VNTQRVPCSN PRWNEWLNYD IYIPDLPRAA RLCLSICSVK GRKGAKEEHC
PLAWGNINLF DYTDTLVSGK MALNLWPVPH GLEDLLNPIG VTGSNPNKET PCLELEFDWF
SSVVKFPDMS VIEEHANWSV SREAGFSYSH AGLSNRLARD NELRENDKEQ LKAISTRDPL
SEITEQEKDF LWSHRHYCVT IPEILPKLLL SVKWNSRDEV AQMYCLVKDW PPIKPEQAME
LLDCNYPDPM VRGFAVRCLE KYLTDDKLSQ YLIQLVQVLK YEQYLDNLLV RFLLKKALTN
QRIGHFFFWH LKSEMHNKTV SQRFGLLLES YCRACGMYLK HLNRQVEAME KLINLTDILK
QERKDETQKV QMKFLVEQMR RPDFMDALQG LLSPLNPAHQ LGNLRLKECR IMSSAKRPLW
LNWENPDIMS ELLFQNNEII FKNGDDLRQD MLTLQIIRIM ENIWQNQGLD LRMLPYGCLS
IGDCVGLIEV VRNSHTIMQI QCKGGLKGAL QFNSHTLHQW LKDKNKGEIY DAAIDLFTRS
CAGYCVATFI LGIGDRHNSN IMVKDDGQLF HIDFGHFLDH KKKKFGYKRE RVPFVLTQDF
LIVISKGAQE CTKTREFERF QEMCYKAYLA IRQHANLFIN LFSMMLGSGM PELQSFDDIA
YIRKTLALDK TEQEALEYFM KQMNDAHHGG WTTKMDWIFH TIKQHALN
//
ID P11B_HUMAN STANDARD; PRT; 1070 AA.
AC P42338;
DT 01-NOV-1995 (Rel. 32, Created)
DT 01-NOV-1995 (Rel. 32, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit, beta
DE isoform (EC 2.7.1.153) (PI3-kinase p110 subunit beta) (PtdIns-3-kinase
DE p110) (PI3K) (PI3Kbeta).
GN PIK3CB.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RX MEDLINE=94067128; PubMed=8246984;
RA Hu P., Mondino A., Skolnik E.Y., Schlessinger J.;
RT "Cloning of a novel, ubiquitously expressed human
RT phosphatidylinositol 3-kinase and identification of its binding site
RT on p85.";
RL Mol. Cell. Biol. 13:7677-7688(1993).
RN [2]
RP SEQUENCE FROM N.A.
RA Kossila M., Sinkovic M., Karkkainen P., Laukkanen M.O., Miettinen R.,
RA Rissanen J., Kekalainen P., Kuusisto J., Yla-Herttuala S., Laakso M.;
RT "Gene encoding the catalytic subunit p110beta of human
RT phosphatidylinositol 3-kinase: cloning, genomic structure and
RT screening for variants in patients with type 2 diabetes.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: PHOSPHORYLATES PTDINS, PTDINS4P AND PTDINS(4,5)P2 WITH A
CC PREFERENCE FOR PTDINS(4,5)P2.
CC -!- CATALYTIC ACTIVITY: ATP + 1-phosphatidyl-1D-myo-inositol 4,5-
CC bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-
CC trisphosphate.
CC -!- PATHWAY: Signaling pathways regulating cell growth.
CC -!- SUBUNIT: HETERODIMER OF A P110 (CATALYTIC) AND A P85 (REGULATORY)
CC SUBUNIT.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; S67334; AAB29081.1; -.
DR EMBL; AJ297549; CAC21449.1; -.
DR EMBL; AJ297550; CAC21449.1; JOINED.
DR EMBL; AJ297551; CAC21449.1; JOINED.
DR EMBL; AJ297552; CAC21449.1; JOINED.
DR EMBL; AJ297553; CAC21449.1; JOINED.
DR EMBL; AJ297554; CAC21449.1; JOINED.
DR EMBL; AJ297555; CAC21449.1; JOINED.
DR EMBL; AJ297556; CAC21449.1; JOINED.
DR EMBL; AJ297557; CAC21449.1; JOINED.
DR EMBL; AJ297558; CAC21449.1; JOINED.
DR EMBL; AJ297559; CAC21449.1; JOINED.
DR EMBL; AJ297560; CAC21449.1; JOINED.
DR PIR; A54600; A54600.
DR Genew; HGNC:8976; PIK3CB.
DR GK; P42338; -.
DR MIM; 602925; -.
DR GO; GO:0016303; F:phosphatidylinositol 3-kinase activity; TAS.
DR GO; GO:0000187; P:activation of MAPK; TAS.
DR GO; GO:0006935; P:chemotaxis; TAS.
DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; TAS.
DR GO; GO:0000074; P:regulation of cell cycle; TAS.
DR InterPro; IPR008938; ARM.
DR InterPro; IPR008973; C2_CaLB.
DR InterPro; IPR000403; PI3_PI4_kinase.
DR InterPro; IPR002420; PI3K_C2.
DR InterPro; IPR003113; PI3K_p85B.
DR InterPro; IPR000341; PI3K_ras_bind.
DR InterPro; IPR001263; PI3Ka.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF02192; PI3K_p85B; 1.
DR Pfam; PF00794; PI3K_rbd; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR SMART; SM00142; PI3K_C2; 1.
DR SMART; SM00143; PI3K_p85B; 1.
DR SMART; SM00144; PI3K_rbd; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
KW Transferase; Kinase; Multigene family.
FT DOMAIN 800 1050 PI3K/PI4K.
SQ SEQUENCE 1070 AA; 122762 MW; 81135FE93452C00E CRC64;
MCFSFIMPPA MADILDIWAV DSQIASDGSI PVDFLLPTGI YIQLEVPREA TISYIKQMLW
KQVHNYPMFN LLMDIDSYMF ACVNQTAVYE ELEDETRRLC DVRPFLPVLK LVTRSCDPGE
KLDSKIGVLI GKGLHEFDSL KDPEVNEFRR KMRKFSEEKI LSLVGLSWMD WLKQTYPPEH
EPSIPENLED KLYGGKLIVA VHFENCQDVF SFQVSPNMNP IKVNELAIQK RLTIHGKEDE
VSPYDYVLQV SGRVEYVFGD HPLIQFQYIR NCVMNRALPH FILVECCKIK KMYEQEMIAI
EAAINRNSSN LPLPLPPKKT RIISHVWENN NPFQIVLVKG NKLNTEETVK VHVRAGLFHG
TELLCKTIVS SEVSGKNDHI WNEPLEFDIN ICDLPRMARL CFAVYAVLDK VKTKKSTKTI
NPSKYQTIRK AGKVHYPVAW VNTMVFDFKG QLRTGDIILH SWSSFPDELE EMLNPMGTVQ
TNPYTENATA LHVKFPENKK QPYYYPPFDK IIEKAAEIAS SDSANVSSRG GKKFLPVLKE
ILDRDPLSQL CENEMDLIWT LRQDCREIFP QSLPKLLLSI KWNKLEDVAQ LQALLQIWPK
LPPREALELL DFNYPDQYVR EYAVGCLRQM SDEELSQYLL QLVQVLKYEP FLDCALSRFL
LERALGNRRI GQFLFWHLRS EVHIPAVSVQ FGVILEAYCR GSVGHMKVLS KQVEALNKLK
TLNSLIKLNA VKLNRAKGKE AMHTCLKQSA YREALSDLQS PLNPCVILSE LYVEKCKYMD
SKMKPLWLVY NNKVFGEDSV GVIFKNGDDL RQDMLTLQML RLMDLLWKEA GLDLRMLPYG
CLATGDRSGL IEVVSTSETI ADIQLNSSNV AAAAAFNKDA LLNWLKEYNS GDDLDRAIEE
FTLSCAGYCV ASYVLGIGDR HSDNIMVKKT GQLFHIDFGH ILGNFKSKFG IKRERVPFIL
TYDFIHVIQQ GKTGNTEKFG RFRQCCEDAY LILRRHGNLF ITLFALMLTA GLPELTSVKD
IQYLKDSLAL GKSEEEALKQ FKQKFDEALR ESWTTKVNWM AHTVRKDYRS
//
ID P11D_HUMAN STANDARD; PRT; 1044 AA.
AC O00329; O15445;
DT 15-JUL-1998 (Rel. 36, Created)
DT 15-JUL-1998 (Rel. 36, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit,
DE delta isoform (EC 2.7.1.153) (PI3-kinase p110 subunit delta) (PtdIns-
DE 3-kinase p110) (PI3K) (p110delta).
GN PIK3CD.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RX MEDLINE=97272223; PubMed=9113989;
RA Vanhaesebroeck B.A.M., Welham M.J., Kotani K., Stein R., Warne P.H.,
RA Zvelebil M.J., Higashi K., Volinia S., Downward J., Waterfield M.D.;
RT "P110delta, a novel phosphoinositide 3-kinase in leukocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:4330-4335(1997).
RN [2]
RP SEQUENCE FROM N.A.
RX MEDLINE=97382246; PubMed=9235916;
RA Chantry D., Vojytek A., Kashishian A., Holtzman D.A., Wood C.,
RA Gray P.W., Cooper J.A., Hoekstra M.F.;
RT "p110delta, a novel phosphatidylinositol 3-kinase catalytic subunit
RT that associates with p85 and is expressed predominantly in
RT leukocytes.";
RL J. Biol. Chem. 272:19236-19241(1997).
CC -!- CATALYTIC ACTIVITY: ATP + 1-phosphatidyl-1D-myo-inositol 4,5-
CC bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-
CC trisphosphate.
CC -!- PATHWAY: Signaling pathways regulating cell growth.
CC -!- SUBUNIT: HETERODIMER OF A P110 (CATALYTIC) AND A P85 (REGULATORY)
CC SUBUNIT.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in leukocytes.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; Y10055; CAA71149.1; -.
DR EMBL; U86453; AAC25677.1; -.
DR Genew; HGNC:8977; PIK3CD.
DR MIM; 602839; -.
DR GO; GO:0005942; C:phosphoinositide 3-kinase complex; NAS.
DR GO; GO:0016303; F:phosphatidylinositol 3-kinase activity; NAS.
DR GO; GO:0006468; P:protein amino acid phosphorylation; NAS.
DR GO; GO:0007165; P:signal transduction; NAS.
DR InterPro; IPR008938; ARM.
DR InterPro; IPR008973; C2_CaLB.
DR InterPro; IPR000403; PI3_PI4_kinase.
DR InterPro; IPR002420; PI3K_C2.
DR InterPro; IPR003113; PI3K_p85B.
DR InterPro; IPR000341; PI3K_ras_bind.
DR InterPro; IPR001263; PI3Ka.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF02192; PI3K_p85B; 1.
DR Pfam; PF00794; PI3K_rbd; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR SMART; SM00142; PI3K_C2; 1.
DR SMART; SM00143; PI3K_p85B; 1.
DR SMART; SM00144; PI3K_rbd; 1.
DR SMART; SM00146; PI3Kc; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
KW Transferase; Kinase; Multigene family.
FT DOMAIN 776 1029 PI3K/PI4K.
FT CONFLICT 253 253 S -> N (in Ref. 2).
FT CONFLICT 675 675 R -> S (in Ref. 2).
SQ SEQUENCE 1044 AA; 119548 MW; B68B6F06A65AB97A CRC64;
MPPGVDCPME FWTKEENQSV VVDFLLPTGV YLNFPVSRNA NLSTIKQLLW HRAQYEPLFH
MLSGPEAYVF TCINQTAEQQ ELEDEQRRLC DVQPFLPVLR LVAREGDRVK KLINSQISLL
IGKGLHEFDS LCDPEVNDFR AKMCQFCEEA AARRQQLGWE AWLQYSFPLQ LEPSAQTWGP
GTLRLPNRAL LVNVKFEGSE ESFTFQVSTK DVPLALMACA LRKKATVFRQ PLVEQPEDYT
LQVNGRHEYL YGSYPLCQFQ YICSCLHSGL TPHLTMVHSS SILAMRDEQS NPAPQVQKPR
AKPPPIPAKK PSSVSLWSLE QPFRIELIQG SKVNADERMK LVVQAGLFHG NEMLCKTVSS
SEVSVCSEPV WKQRLEFDIN ICDLPRMARL CFALYAVIEK AKKARSTKKK SKKADCPIAW
ANLMLFDYKD QLKTGERCLY MWPSVPDEKG ELLNPTGTVR SNPNTDSAAA LLICLPEVAP
HPVYYPALEK ILELGRHSEC VHVTEEEQLQ LREILERRGS GELYEHEKDL VWKLRHEVQE
HFPEALARLL LVTKWNKHED VAQMLYLLCS WPELPVLSAL ELLDFSFPDC HVGSFAIKSL
RKLTDDELFQ YLLQLVQVLK YESYLDCELT KFLLDRALAN RKIGHFLFWH LRSEMHVPSV
ALRFGLILEA YCRGRTHHMK VLMKQGEALS KLKALNDFVK LSSQKTPKPQ TKELMHLCMR
QEAYLEALSH LQSPLDPSTL LAEVCVEQCT FMDSKMKPLW IMYSNEEAGS GGSVGIIFKN
GDDLRQDMLT LQMIQLMDVL WKQEGLDLRM TPYGCLPTGD RTGLIEVVLR SDTIANIQLN
KSNMAATAAF NKDALLNWLK SKNPGEALDR AIEEFTLSCA GYCVATYVLG IGDRHSDNIM
IRESGQLFHI DFGHFLGNFK TKFGINRERV PFILTYDFVH VIQQGKTNNS EKFERFRGYC
ERAYTILRRH GLLFLHLFAL MRAAGLPELS CSKDIQYLKD SLALGKTEEE ALKHFRVKFN
EALRESWKTK VNWLAHNVSK DNRQ
//
ID P11G_HUMAN STANDARD; PRT; 1101 AA.
AC P48736;
DT 01-FEB-1996 (Rel. 33, Created)
DT 01-OCT-1996 (Rel. 34, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit,
DE gamma isoform (EC 2.7.1.153) (PI3-kinase p110 subunit gamma) (PtdIns-
DE 3-kinase p110) (PI3K) (PI3Kgamma).
GN PIK3CG.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RX MEDLINE=95350661; PubMed=7624799;
RA Stoyanov B., Volinia S., Hanck T., Rubio I., Loubtchenkov M.,
RA Malek D., Stoyanova S., Vanhaesebroeck B., Dhand R., Nuernberg B.,
RA Gierschik P., Seedorf K., Hsuan J.J., Waterfield M.D., Wetzker R.;
RT "Cloning and characterization of a G protein-activated human
RT phosphoinositide-3 kinase.";
RL Science 269:690-693(1995).
RN [2]
RP REVISIONS.
RA Waterfield M.D.;
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: 3-PHOSPHORYLATES THE CELLULAR PHOSPHOINOSITIDE
CC PTDINS-4,5-BIPHOSPHATE (PTDINS(4,5)P2).
CC -!- CATALYTIC ACTIVITY: ATP + 1-phosphatidyl-1D-myo-inositol 4,5-
CC bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-
CC trisphosphate.
CC -!- ENZYME REGULATION: Activated by both the alpha and the beta-gamma
CC G proteins.
CC -!- PATHWAY: Signaling pathways regulating cell growth.
CC -!- SUBUNIT: Heterodimer of a 101 kDa subunit and a 120 kDa catalytic
CC subunit (By similarity).
CC -!- TISSUE SPECIFICITY: Pancreas, skeletal muscle, liver and heart.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; X83368; CAA58284.1; -.
DR PDB; 1E8Y; 17-NOV-00.
DR PDB; 1E8Z; 17-NOV-00.
DR PDB; 1HE8; 08-JAN-01.
DR Genew; HGNC:8978; PIK3CG.
DR MIM; 601232; -.
DR GO; GO:0016303; F:phosphatidylinositol 3-kinase activity; TAS.
DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; TAS.
DR InterPro; IPR008938; ARM.
DR InterPro; IPR008973; C2_CaLB.
DR InterPro; IPR000403; PI3_PI4_kinase.
DR InterPro; IPR002420; PI3K_C2.
DR InterPro; IPR000341; PI3K_ras_bind.
DR InterPro; IPR001263; PI3Ka.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF00794; PI3K_rbd; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR SMART; SM00142; PI3K_C2; 1.
DR SMART; SM00144; PI3K_rbd; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
KW Transferase; Kinase; Multigene family; 3D-structure.
FT DOMAIN 18 22 POLY-ARG.
FT DOMAIN 827 1072 PI3K/PI4K.
FT HELIX 144 157
FT TURN 158 158
FT TURN 161 162
FT TURN 165 166
FT HELIX 171 178
FT TURN 179 179
FT HELIX 180 189
FT HELIX 192 197
FT STRAND 201 201
FT HELIX 208 211
FT TURN 212 213
FT STRAND 219 225
FT TURN 226 227
FT STRAND 228 229
FT STRAND 233 234
FT TURN 236 237
FT HELIX 240 242
FT TURN 243 243
FT HELIX 245 251
FT STRAND 270 273
FT TURN 274 275
FT STRAND 279 280
FT HELIX 286 288
FT STRAND 289 289
FT HELIX 290 297
FT TURN 298 299
FT STRAND 302 307
FT HELIX 312 315
FT STRAND 359 368
FT STRAND 379 387
FT STRAND 392 397
FT STRAND 401 402
FT STRAND 406 418
FT HELIX 419 421
FT TURN 424 425
FT STRAND 427 433
FT STRAND 461 466
FT STRAND 468 468
FT TURN 470 471
FT STRAND 474 474
FT STRAND 477 482
FT STRAND 484 485
FT HELIX 498 501
FT STRAND 514 519
FT HELIX 548 559
FT TURN 562 563
FT HELIX 568 576
FT TURN 577 577
FT HELIX 578 581
FT TURN 582 583
FT HELIX 585 587
FT HELIX 588 592
FT TURN 593 594
FT TURN 597 598
FT HELIX 600 611
FT HELIX 614 617
FT TURN 618 618
FT HELIX 623 629
FT TURN 630 630
FT TURN 632 633
FT HELIX 637 647
FT TURN 648 649
FT HELIX 652 665
FT HELIX 666 668
FT HELIX 675 686
FT HELIX 688 704
FT TURN 706 708
FT HELIX 709 720
FT TURN 721 722
FT HELIX 725 750
FT TURN 751 751
FT HELIX 760 773
FT TURN 774 777
FT STRAND 782 784
FT TURN 785 786
FT STRAND 787 795
FT HELIX 797 799
FT STRAND 801 802
FT STRAND 810 816
FT TURN 819 820
FT STRAND 827 833
FT HELIX 837 855
FT TURN 856 858
FT STRAND 868 872
FT TURN 873 874
FT STRAND 875 879
FT TURN 882 883
FT STRAND 884 886
FT HELIX 887 894
FT TURN 903 904
FT HELIX 905 913
FT HELIX 917 940
FT TURN 941 942
FT HELIX 948 950
FT STRAND 951 954
FT TURN 955 956
FT STRAND 959 961
FT HELIX 988 993
FT TURN 994 995
FT HELIX 1003 1020
FT TURN 1021 1022
FT HELIX 1023 1037
FT TURN 1043 1044
FT HELIX 1045 1053
FT TURN 1054 1057
FT HELIX 1060 1077
FT TURN 1078 1079
FT HELIX 1080 1084
FT TURN 1085 1086
SQ SEQUENCE 1101 AA; 126410 MW; 266BAA6495C8AE9E CRC64;
MELENYKQPV VLREDNCRRR RRMKPRSAAS LSSMELIPIE FVLPTSQRKC KSPETALLHV
AGHGNVEQMK AQVWLRALET SVAADFYHRL GPHHFLLLYQ KKGQWYEIYD KYQVVQTLDC
LRYWKATHRS PGQIHLVQRH PPSEESQAFQ RQLTALIGYD VTDVSNVHDD ELEFTRRGLV
TPRMAEVASR DPKLYAMHPW VTSKPLPEYL WKKIANNCIF IVIHRSTTSQ TIKVSPDDTP
GAILQSFFTK MAKKKSLMDI PESQSEQDFV LRVCGRDEYL VGETPIKNFQ WVRHCLKNGE
EIHVVLDTPP DPALDEVRKE EWPLVDDCTG VTGYHEQLTI HGKDHESVFT VSLWDCDRKF
RVKIRGIDIP VLPRNTDLTV FVEANIQHGQ QVLCQRRTSP KPFTEEVLWN VWLEFSIKIK
DLPKGALLNL QIYCGKAPAL SSKASAESPS SESKGKVRLL YYVNLLLIDH RFLLRRGEYV
LHMWQISGKG EDQGSFNADK LTSATNPDKE NSMSISILLD NYCHPIALPK HQPTPDPEGD
RVRAEMPNQL RKQLEAIIAT DPLNPLTAED KELLWHFRYE SLKHPKAYPK LFSSVKWGQQ
EIVAKTYQLL ARREVWDQSA LDVGLTMQLL DCNFSDENVR AIAVQKLESL EDDDVLHYLL
QLVQAVKFEP YHDSALARFL LKRGLRNKRI GHFLFWFLRS EIAQSRHYQQ RFAVILEAYL
RGCGTAMLHD FTQQVQVIEM LQKVTLDIKS LSAEKYDVSS QVISQLKQKL ENLQNSQLPE
SFRVPYDPGL KAGALAIEKC KVMASKKKPL WLEFKCADPT ALSNETIGII FKHGDDLRQD
MLILQILRIM ESIWETESLD LCLLPYGCIS TGDKIGMIEI VKDATTIAKI QQSTVGNTGA
FKDEVLNHWL KEKSPTEEKF QAAVERFVYS CAGYCVATFV LGIGDRHNDN IMITETGNLF
HIDFGHILGN YKSFLGINKE RVPFVLTPDF LFVMGTSGKK TSPHFQKFQD ICVKAYLALR
HHTNLLIILF SMMLMTGMPQ LTSKEDIEYI RDALTVGKNE EDAKKYFLDQ IEVCRDKGWT
VQFNWFLHLV LGIKQGEKHS A
//
ID P4KB_HUMAN STANDARD; PRT; 816 AA.
AC Q9UBF8; O15096; P78405; Q9BWR6;
DT 15-MAR-2004 (Rel. 43, Created)
DT 15-MAR-2004 (Rel. 43, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Phosphatidylinositol 4-kinase beta (EC 2.7.1.67) (PtdIns 4-kinase)
DE (PI4Kbeta) (PI4K-beta) (NPIK) (PI4K92).
GN PIK4CB OR PI4KB.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RX MEDLINE=98069009; PubMed=9405935;
RA Suzuki K., Hirano H., Okutomi K., Suzuki M., Kuga Y., Fujiwara T.,
RA Kanemoto N., Isono K., Horie M.;
RT "Identification and characterization of a novel human
RT phosphatidylinositol 4-kinase.";
RL DNA Res. 4:273-280(1997).
RN [2]
RP SEQUENCE FROM N.A., AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX MEDLINE=98069012; PubMed=9405938;
RA Saito T., Seki N., Ishii H., Ohira M., Hayashi A., Kozuma S.,
RA Hori T.-A.;
RT "Complementary DNA cloning and chromosomal mapping of a novel
RT phosphatidylinositol kinase gene.";
RL DNA Res. 4:301-305(1997).
RN [3]
RP SEQUENCE FROM N.A. (ISOFORM 2), ENZYME REGULATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Heart, and Placenta;
RX MEDLINE=97172516; PubMed=9020160;
RA Meyers R., Cantley L.C.;
RT "Cloning and characterization of a wortmannin-sensitive human
RT phosphatidylinositol 4-kinase.";
RL J. Biol. Chem. 272:4384-4390(1997).
RN [4]
RP SEQUENCE FROM N.A. (ISOFORM 2).
RC TISSUE=Brain, and Testis;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length human
RT and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [5]
RP SUBCELLULAR LOCATION.
RX MEDLINE=97294736; PubMed=9148941;
RA Wong K., Meyers R., Cantley L.C.;
RT "Subcellular locations of phosphatidylinositol 4-kinase isoforms.";
RL J. Biol. Chem. 272:13236-13241(1997).
RN [6]
RP FUNCTION.
RX MEDLINE=20032720; PubMed=10559940;
RA Godi A., Pertile P., Meyers R., Marra P., Di Tullio G., Iurisci C.,
RA Luini A., Corda D., De Matteis M.A.;
RT "ARF mediates recruitment of PtdIns-4-OH kinase-beta and stimulates
RT synthesis of PtdIns(4,5)P2 on the Golgi complex.";
RL Nat. Cell Biol. 1:280-287(1999).
RN [7]
RP FUNCTION.
RX MEDLINE=22634631; PubMed=12749687;
RA Heilmeyer L.M.G. Jr., Vereb G. Jr., Vereb G., Kakuk A., Szivak I.;
RT "Mammalian phosphatidylinositol 4-kinases.";
RL IUBMB Life 55:59-65(2003).
RN [8]
RP PHOSPHORYLATION.
RX MEDLINE=21175828; PubMed=11277933;
RA Suer S., Sickmann A., Meyer H.E., Herberg F.W., Heilmeyer L.M.G. Jr.;
RT "Human phosphatidylinositol 4-kinase isoform PI4K92. Expression of the
RT recombinant enzyme and determination of multiple phosphorylation
RT sites.";
RL Eur. J. Biochem. 268:2099-2106(2001).
CC -!- FUNCTION: Phosphorylates phosphatidylinositol (PI) in the first
CC committed step in the production of the second messenger
CC inositol-1,4,5,-trisphosphate (PIP). May regulate Golgi
CC disintegration/reorganization during mitosis, possibly via its
CC phosphorylation.
CC -!- CATALYTIC ACTIVITY: ATP + 1-phosphatidyl-1D-myo-inositol = ADP +
CC 1-phosphatidyl-1D-myo-inositol 4-phosphate.
CC -!- ENZYME REGULATION: Inhibited by wortmannin.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic. Found in the outer membrane of
CC mitochondria and membranes of the rough endoplasmic reticulum.
CC Recruited to the Golgi complex by the small GTPase ARF to
CC stimulate the synthesis of phosphatidylinositol 4,5-biphosphate
CC (PIP2) on the Golgi complex.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=NPIK-B;
CC IsoId=Q9UBF8-1; Sequence=Displayed;
CC Name=2; Synonyms=NPIK-C;
CC IsoId=Q9UBF8-2; Sequence=VSP_050627;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in heart,
CC skeletal muscle, pancreas, testis and ovary. Weakly expressed in
CC liver.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AJ011121; CAA09495.1; -.
DR EMBL; AJ011122; -; NOT_ANNOTATED_CDS.
DR EMBL; AJ011123; CAA09496.1; -.
DR EMBL; AB005910; BAA21661.1; ALT_INIT.
DR EMBL; U81802; AAC51156.1; -.
DR EMBL; BC000029; AAH00029.1; -.
DR EMBL; BC040300; AAH40300.1; -.
DR PIR; JC5706; JC5706.
DR Genew; HGNC:8984; PIK4CB.
DR MIM; 602758; -.
DR InterPro; IPR008938; ARM.
DR InterPro; IPR000403; PI3_PI4_kinase.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM00146; PI3Kc; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
KW Transferase; Kinase; Golgi stack; Phosphorylation;
KW Alternative splicing.
FT DOMAIN 558 765 PI3K/PI4K.
FT MOD_RES 258 258 PHOSPHORYLATION.
FT MOD_RES 263 263 PHOSPHORYLATION.
FT MOD_RES 266 266 PHOSPHORYLATION.
FT MOD_RES 277 277 PHOSPHORYLATION.
FT MOD_RES 294 294 PHOSPHORYLATION.
FT MOD_RES 438 438 PHOSPHORYLATION.
FT MOD_RES 511 511 PHOSPHORYLATION.
FT MOD_RES 519 519 PHOSPHORYLATION.
FT VARSPLIC 304 318 Missing (in isoform 2).
FT /FTId=VSP_050627.
FT CONFLICT 216 216 L -> V (in Ref. 3).
FT CONFLICT 339 340 LA -> VV (in Ref. 3).
FT CONFLICT 370 370 P -> S (in Ref. 3).
SQ SEQUENCE 816 AA; 91378 MW; CAD8791729BB4308 CRC64;
MGDTVVEPAP LKPTSEPTSG PPGNNGGSLL SVITEGVGEL SVIDPEVAQK ACQEVLEKVK
LLHGGVAVSS RGTPLELVNG DGVDSEIRCL DDPPAQIREE EDEMGAAVAS GTAKGARRRR
QNNSAKQSWL LRLFESKLFD ISMAISYLYN SKEPGVQAYI GNRLFCFRNE DVDFYLPQLL
NMYIHMDEDV GDAIKPYIVH RCRQSINFSL QCALLLGAYS SDMHISTQRH SRGTKLRKLI
LSDELKPAHR KRELPSLSPA PDTGLSPSKR THQRSKSDAT ASISLSSNLK RTASNPKVEN
EDEELSSSTE SIDNSFSSPV RLAPEREFIK SLMAIGKRLA TLPTKEQKTQ RLISELSLLN
HKLPARVWLP TAGFDHHVVR VPHTQAVVLN SKDKAPYLIY VEVLECENFD TTSVPARIPE
NRIRSTRSVE NLPECGITHE QRAGSFSTVP NYDNDDEAWS VDDIGELQVE LPEVHTNSCD
NISQFSVDSI TSQESKEPVF IAAGDIRRRL SEQLAHTPTA FKRDPEDPSA VALKEPWQEK
VRRIREGSPY GHLPNWRLLS VIVKCGDDLR QELLAFQVLK QLQSIWEQER VPLWIKPYKI
LVISADSGMI EPVVNAVSIH QVKKQSQLSL LDYFLQEHGS YTTEAFLSAQ RNFVQSCAGY
CLVCYLLQVK DRHNGNILLD AEGHIIHIDF GFILSSSPRN LGFETSAFKL TTEFVDVMGG
LDGDMFNYYK MLMLQGLIAA RKHMDKVVQI VEIMQQGSQL PCFHGSSTIR NLKERFHMSM
TEEQLQLLVE QMVDGSMRSI TTKLYDGFQY LTNGIM
//
ID P5CS_HUMAN STANDARD; PRT; 795 AA.
AC P54886; O95952; Q9UM72;
DT 01-OCT-1996 (Rel. 34, Created)
DT 30-MAY-2000 (Rel. 39, Last sequence update)
DT 28-FEB-2003 (Rel. 41, Last annotation update)
DE Delta 1-pyrroline-5-carboxylate synthetase (P5CS) [Includes: Glutamate
DE 5-kinase (EC 2.7.2.11) (Gamma-glutamyl kinase) (GK); Gamma-glutamyl
DE phosphate reductase (GPR) (EC 1.2.1.41) (Glutamate-5-semialdehyde
DE dehydrogenase) (Glutamyl-gamma-semialdehyde dehydrogenase)].
GN PYCS OR P5CS.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RC TISSUE=Kidney;
RX MEDLINE=96340872; PubMed=8761662;
RA Aral B., Schlenzig J.S., Liu G., Kamoun P.;
RT "Database cloning human delta 1-pyrroline-5-carboxylate synthetase
RT (P5CS) cDNA: a bifunctional enzyme catalyzing the first 2 steps in
RT proline biosynthesis.";
RL C. R. Acad. Sci., III, Sci. Vie 319:171-178(1996).
RN [2]
RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING.
RC TISSUE=Small intestine;
RX MEDLINE=99156965; PubMed=10037775;
RA Hu C.A., Lin W.-W., Obie C., Valle D.;
RT "Molecular enzymology of mammalian delta1-pyrroline-5-carboxylate
RT synthase. Alternative splice donor utilization generates isoforms
RT with different sensitivity to ornithine inhibition.";
RL J. Biol. Chem. 274:6754-6762(1999).
CC -!- CATALYTIC ACTIVITY: ATP + L-glutamate = ADP + L-glutamate 5-
CC phosphate.
CC -!- CATALYTIC ACTIVITY: L-glutamate 5-semialdehyde + phosphate +
CC NADP(+) = L-gamma-glutamyl 5-phosphate + NADPH.
CC -!- ENZYME REGULATION: The short isoform is inhibited by L-ornithine
CC with a Ki of approximately 0.25 mm. The long isoform is
CC insensitive to ornithine inhibition. Thus, the two amino acid
CC insert in the long isoform abolishes feedback inhibition of P5CS
CC activity by L-ornithine.
CC -!- PATHWAY: Proline biosynthesis; first step.
CC -!- PATHWAY: Proline biosynthesis; second step.
CC -!- SUBCELLULAR LOCATION: Mitochondrial inner membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P54886-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P54886-2; Sequence=VSP_005215;
CC -!- SIMILARITY: In the N-terminal section; belongs to the glutamate 5-
CC kinase family.
CC -!- SIMILARITY: In the C-terminal section; belongs to the gamma-
CC glutamyl phosphate reductase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; X94453; CAA64224.1; -.
DR EMBL; U76542; AAD17454.1; -.
DR EMBL; U68758; AAD00169.1; -.
DR Genew; HGNC:9722; PYCS.
DR MIM; 138250; -.
DR GO; GO:0006561; P:proline biosynthesis; TAS.
DR InterPro; IPR001048; Aa_kinase.
DR InterPro; IPR000965; Gglut_pp_reduct.
DR InterPro; IPR001057; Glu_5kinase.
DR InterPro; IPR005766; P5_carboxy_syn.
DR Pfam; PF00696; aakinase; 1.
DR PRINTS; PR00474; GLU5KINASE.
DR TIGRFAMs; TIGR01092; P5CS; 1.
DR TIGRFAMs; TIGR00407; proA; 1.
DR PROSITE; PS00902; GLUTAMATE_5_KINASE; 1.
DR PROSITE; PS01223; PROA; 1.
KW Proline biosynthesis; Multifunctional enzyme; Oxidoreductase; NADP;
KW Transferase; Kinase; Mitochondrion; Inner membrane;
KW Alternative splicing.
FT DOMAIN 1 361 GLUTAMATE 5-KINASE.
FT DOMAIN 362 795 GAMMA-GLUTAMYL PHOSPHATE REDUCTASE.
FT VARSPLIC 239 240 Missing (in isoform Short).
FT /FTId=VSP_005215.
FT CONFLICT 126 126 R -> T (in Ref. 1).
FT CONFLICT 266 266 S -> P (in Ref. 1).
FT CONFLICT 299 299 T -> P (in Ref. 1).
FT CONFLICT 305 307 MGG -> NGC (in Ref. 1).
FT CONFLICT 314 315 AA -> ST (in Ref. 1).
FT CONFLICT 487 493 LPQVAAL -> PTPGGSF (in Ref. 1).
SQ SEQUENCE 795 AA; 87302 MW; 8BF27EF2A8FB2D79 CRC64;
MLSQVYRCGF QPFNQHLLPW VKCTTVFRSH CIQPSVIRHV RSWSNIPFIT VPLSRTHGKS
FAHRSELKHA KRIVVKLGSA VVTRGDECGL ALGRLASIVE QVSVLQNQGR EMMLVTSGAV
AFGKQRLRHE ILLSQSVRQA LHSGQNQLKE MAIPVLEARA CAAAGQSGLM ALYEAMFTQY
SICAAQILVT NLDFHDEQKR RNLNGTLHEL LRMNIVPIVN TNDAVVPPAE PNSDLQGVNV
ISVKDNDSLA ARLAVEMKTD LLIVLSDVEG LFDSPPGSDD AKLIDIFYPG DQQSVTFGTK
SRVGMGGMEA KVKAALWALQ GGTSVVIANG THPKVSGHVI TDIVEGKKVG TFFSEVKPAG
PTVEQQGEMA RSGGRMLATL EPEQRAEIIH HLADLLTDQR DEILLANKKD LEEAEGRLAA
PLLKRLSLST SKLNSLAIGL RQIAASSQDS VGRVLRRTRI AKNLELEQVT VPIGVLLVIF
ESRPDCLPQV AALAIASGNG LLLKGGKEAA HSNRILHLLT QEALSIHGVK EAVQLVNTRE
EVEDLCRLDK MIDLIIPRGS SQLVRDIQKA AKGIPVMGHS EGICHMYVDS EASVDKVTRL
VRDSKCEYPA ACNALETLLI HRDLLRTPLF DQIIDMLRVE QVKIHAGPKF ASYLTFSPSE
VKSLRTEYGD LELCIEVVDN VQDAIDHIHK YGSSHTDVIV TEDENTAEFF LQHVDSACVF
WNASTRFSDG YRFGLGAEVG ISTSRIHARG PVGLEGLLTT KWLLRGKDHV VSDFSEHGSL
KYLHENLPIP QRNTN
//
ID PDK1_HUMAN STANDARD; PRT; 436 AA.
AC Q15118;
DT 15-JUL-1998 (Rel. 36, Created)
DT 15-JUL-1998 (Rel. 36, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 1, mitochondrial
DE precursor (EC 2.7.1.99) (Pyruvate dehydrogenase kinase isoform 1).
GN PDK1.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RC TISSUE=Liver;
RX MEDLINE=96081973; PubMed=7499431;
RA Gudi R., Bowker-Kinley M.M., Kedishvili N.Y., Zhao Y., Popov K.M.;
RT "Diversity of the pyruvate dehydrogenase kinase gene family in
RT humans.";
RL J. Biol. Chem. 270:28989-28994(1995).
RN [2]
RP SEQUENCE FROM N.A.
RC TISSUE=Skin;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC -!- FUNCTION: Inhibits the mitochondrial pyruvate dehydrogenase
CC complex by phosphorylation of the E1 alpha subunit, thus
CC contributing to the regulation of glucose metabolism.
CC -!- CATALYTIC ACTIVITY: ATP + [pyruvate dehydrogenase (lipoamide)] =
CC ADP + [pyruvate dehydrogenase (lipoamide)] phosphate.
CC -!- SUBCELLULAR LOCATION: Mitochondrial matrix.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the heart.
CC -!- SIMILARITY: Belongs to the PDK/BCKDK protein kinase family.
CC -!- SIMILARITY: Contains 1 histidine kinase domain.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; L42450; AAC42009.1; -.
DR EMBL; BC039158; AAH39158.1; -.
DR PIR; I55465; I55465.
DR Genew; HGNC:8809; PDK1.
DR MIM; 602524; -.
DR GO; GO:0005739; C:mitochondrion; TAS.
DR GO; GO:0004672; F:protein kinase activity; TAS.
DR GO; GO:0004740; F:[pyruvate dehydrogenase (lipoamide)] kinase...; TAS.
DR GO; GO:0006006; P:glucose metabolism; TAS.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; TAS.
DR InterPro; IPR003594; ATPbind_ATPase.
DR InterPro; IPR005467; His_kinase.
DR Pfam; PF02518; HATPase_c; 1.
DR SMART; SM00387; HATPase_c; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
KW Kinase; Transferase; Transit peptide; Mitochondrion; Multigene family.
FT TRANSIT 1 28 Mitochondrion (Potential).
FT CHAIN 29 436 [PYRUVATE DEHYDROGENASE [LIPOAMIDE]]
FT KINASE ISOZYME 1.
FT DOMAIN 163 393 HISTIDINE KINASE.
SQ SEQUENCE 436 AA; 49244 MW; D14CD594E0EA45A2 CRC64;
MRLARLLRGA ALAGPGPGLR AAGFSRSFSS DSGSSPASER GVPGQVDFYA RFSPSPLSMK
QFLDFGSVNA CEKTSFMFLR QELPVRLANI MKEISLLPDN LLRTPSVQLV QSWYIQSLQE
LLDFKDKSAE DAKAIYDFTD TVIRIRNRHN DVIPTMAQGV IEYKESFGVD PVTSQNVQYF
LDRFYMSRIS IRMLLNQHSL LFGGKGKGSP SHRKHIGSIN PNCNVLEVIK DGYENARRLC
DLYYINSPEL ELEELNAKSP GQPIQVVYVP SHLYHMVFEL FKNAMRATME HHANRGVYPP
IQVHVTLGNE DLTVKMSDRG GGVPLRKIDR LFNYMYSTAP RPRVETSRAV PLAGFGYGLP
ISRLYAQYFQ GDLKLYSLEG YGTDAVIYIK ALSTDSIERL PVYNKAAWKH YNTNHEADDW
CVPSREPKDM TTFRSA
//
ID PDK2_HUMAN STANDARD; PRT; 407 AA.
AC Q15119; Q9BS05;
DT 15-JUL-1998 (Rel. 36, Created)
DT 28-FEB-2003 (Rel. 41, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 2, mitochondrial
DE precursor (EC 2.7.1.99) (Pyruvate dehydrogenase kinase isoform 2).
GN PDK2.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RC TISSUE=Liver;
RX MEDLINE=96081973; PubMed=7499431;
RA Gudi R., Bowker-Kinley M.M., Kedishvili N.Y., Zhao Y., Popov K.M.;
RT "Diversity of the pyruvate dehydrogenase kinase gene family in
RT humans.";
RL J. Biol. Chem. 270:28989-28994(1995).
RN [2]
RP SEQUENCE FROM N.A.
RC TISSUE=Lung, and Skin;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC -!- FUNCTION: Inhibits the mitochondrial pyruvate dehydrogenase
CC complex by phosphorylation of the E1 alpha subunit, thus
CC contributing to the regulation of glucose metabolism.
CC -!- CATALYTIC ACTIVITY: ATP + [pyruvate dehydrogenase (lipoamide)] =
CC ADP + [pyruvate dehydrogenase (lipoamide)] phosphate.
CC -!- SUBCELLULAR LOCATION: Mitochondrial matrix.
CC -!- TISSUE SPECIFICITY: EXPRESSED IN MANY TISSUES, WITH THE HIGHEST
CC LEVEL IN HEART AND SKELETAL MUSCLE, INTERMEDIATE LEVELS IN BRAIN,
CC KIDNEY, PANCREAS AND LIVER, AND LOW LEVELS IN PLACENTA AND LUNG.
CC -!- SIMILARITY: Belongs to the PDK/BCKDK protein kinase family.
CC -!- SIMILARITY: Contains 1 histidine kinase domain.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; L42451; AAC42010.1; -.
DR EMBL; BC005811; AAH05811.1; -.
DR EMBL; BC040478; AAH40478.1; -.
DR PIR; I70159; I70159.
DR Genew; HGNC:8810; PDK2.
DR MIM; 602525; -.
DR GO; GO:0004672; F:protein kinase activity; TAS.
DR GO; GO:0004740; F:[pyruvate dehydrogenase (lipoamide)] kinase...; TAS.
DR GO; GO:0006006; P:glucose metabolism; TAS.
DR InterPro; IPR003594; ATPbind_ATPase.
DR InterPro; IPR005467; His_kinase.
DR Pfam; PF02518; HATPase_c; 1.
DR SMART; SM00387; HATPase_c; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
KW Kinase; Transferase; Transit peptide; Mitochondrion; Multigene family.
FT TRANSIT 1 ? Mitochondrion (Potential).
FT CHAIN ? 407 [PYRUVATE DEHYDROGENASE [LIPOAMIDE]]
FT KINASE ISOZYME 2.
FT DOMAIN 135 364 HISTIDINE KINASE.
FT CONFLICT 80 80 S -> T (in Ref. 1).
FT CONFLICT 407 407 S -> T (in Ref. 1).
SQ SEQUENCE 407 AA; 46153 MW; 77DBA03EF922EF03 CRC64;
MRWVWALLKN ASLAGAPKYI EHFSKFSPSP LSMKQFLDFG SSNACEKTSF TFLRQELPVR
LANIMKEINL LPDRVLSTPS VQLVQSWYVQ SLLDIMEFLD KDPEDHRTLS QFTDALVTIR
NRHNDVVPTM AQGVLEYKDT YGDDPVSNQN IQYFLDRFYL SRISIRMLIN QHTLIFDGST
NPAHPKHIGS IDPNCNVSEV VKDAYDMAKL LCDKYYMASP DLEIQEINAA NSKQPIHMVY
VPSHLYHMLF ELFKNAMRAT VESHESSLIL PPIKVMVALG EEDLSIKMSD RGGGVPLRKI
ERLFSYMYST APTPQPGTGG TPLAGFGYGL PISRLYAKYF QGDLQLFSME GFGTDAVIYL
KALSTDSVER LPVYNKSAWR HYQTIQEAGD WCVPSTEPKN TSTYRVS
//
ID PDK3_HUMAN STANDARD; PRT; 406 AA.
AC Q15120;
DT 15-JUL-1998 (Rel. 36, Created)
DT 15-JUL-1998 (Rel. 36, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 3, mitochondrial
DE precursor (EC 2.7.1.99) (Pyruvate dehydrogenase kinase isoform 3).
GN PDK3.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RC TISSUE=Liver;
RX MEDLINE=96081973; PubMed=7499431;
RA Gudi R., Bowker-Kinley M.M., Kedishvili N.Y., Zhao Y., Popov K.M.;
RT "Diversity of the pyruvate dehydrogenase kinase gene family in
RT humans.";
RL J. Biol. Chem. 270:28989-28994(1995).
RN [2]
RP SEQUENCE FROM N.A.
RC TISSUE=Skin;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC -!- FUNCTION: Inhibits the mitochondrial pyruvate dehydrogenase
CC complex by phosphorylation of the E1 alpha subunit, thus
CC contributing to the regulation of glucose metabolism.
CC -!- CATALYTIC ACTIVITY: ATP + [pyruvate dehydrogenase (lipoamide)] =
CC ADP + [pyruvate dehydrogenase (lipoamide)] phosphate.
CC -!- SUBCELLULAR LOCATION: Mitochondrial matrix.
CC -!- TISSUE SPECIFICITY: FOUND ALMOST EXCLUSIVELY IN HEART AND SKELETAL
CC MUSCLE.
CC -!- SIMILARITY: Belongs to the PDK/BCKDK protein kinase family.
CC -!- SIMILARITY: Contains 1 histidine kinase domain.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; L42452; AAC42011.1; -.
DR EMBL; BC015948; AAH15948.1; -.
DR PIR; I70160; I70160.
DR Genew; HGNC:8811; PDK3.
DR MIM; 602526; -.
DR GO; GO:0005739; C:mitochondrion; TAS.
DR GO; GO:0004672; F:protein kinase activity; TAS.
DR GO; GO:0004740; F:[pyruvate dehydrogenase (lipoamide)] kinase...; TAS.
DR GO; GO:0006006; P:glucose metabolism; TAS.
DR InterPro; IPR003594; ATPbind_ATPase.
DR InterPro; IPR005467; His_kinase.
DR Pfam; PF02518; HATPase_c; 1.
DR SMART; SM00387; HATPase_c; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
KW Kinase; Transferase; Transit peptide; Mitochondrion; Multigene family.
FT TRANSIT 1 ? Mitochondrion (Potential).
FT CHAIN ? 406 [PYRUVATE DEHYDROGENASE [LIPOAMIDE]]
FT KINASE ISOZYME 3.
FT DOMAIN 131 362 HISTIDINE KINASE.
SQ SEQUENCE 406 AA; 46939 MW; EF2415D3F9D8D61E CRC64;
MRLFRWLLKQ PVPKQIERYS RFSPSPLSIK QFLDFGRDNA CEKTSYMFLR KELPVRLANT
MREVNLLPDN LLNRPSVGLV QSWYMQSFLE LLEYENKSPE DPQVLDNFLQ VLIKVRNRHN
DVVPTMAQGV IEYKEKFGFD PFISTNIQYF LDRFYTNRIS FRMLINQHTL LFGGDTNPVH
PKHIGSIDPT CNVADVVKDA YETAKMLCEQ YYLVAPELEV EEFNAKAPDK PIQVVYVPSH
LFHMLFELFK NSMRATVELY EDRKEGYPAV KTLVTLGKED LSIKISDLGG GVPLRKIDRL
FNYMYSTAPR PSLEPTRAAP LAGFGYGLPI SRLYARYFQG DLKLYSMEGV GTDAVIYLKA
LSSESFERLP VFNKSAWRHY KTTPEADDWS NPSSEPRDAS KYKAKQ
//
ID PDK4_HUMAN STANDARD; PRT; 411 AA.
AC Q16654;
DT 15-JUL-1998 (Rel. 36, Created)
DT 15-JUL-1998 (Rel. 36, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 4, mitochondrial
DE precursor (EC 2.7.1.99) (Pyruvate dehydrogenase kinase isoform 4).
GN PDK4.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RX MEDLINE=96394293; PubMed=8798399;
RA Rowles J., Scherer S.W., Xi T., Majer M., Nickle D.C., Rommens J.M.,
RA Popov K.M., Harris R.A., Riebow N.L., Xia J., Tsui L.-C., Bogardus C.,
RA Prochazka M.;
RT "Cloning and characterization of PDK4 on 7q21.3 encoding a fourth
RT pyruvate dehydrogenase kinase isoenzyme in human.";
RL J. Biol. Chem. 271:22376-22382(1996).
RN [2]
RP SEQUENCE FROM N.A.
RA Kramer J., Miller N., Gibson A.;
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SEQUENCE FROM N.A.
RC TISSUE=Cervix;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC -!- FUNCTION: Inhibits the mitochondrial pyruvate dehydrogenase
CC complex by phosphorylation of the E1 alpha subunit, thus
CC contributing to the regulation of glucose metabolism.
CC -!- CATALYTIC ACTIVITY: ATP + [pyruvate dehydrogenase (lipoamide)] =
CC ADP + [pyruvate dehydrogenase (lipoamide)] phosphate.
CC -!- SUBCELLULAR LOCATION: Mitochondrial matrix.
CC -!- TISSUE SPECIFICITY: Ubiquitous; highest levels of expression in
CC heart and skeletal muscle.
CC -!- SIMILARITY: Belongs to the PDK/BCKDK protein kinase family.
CC -!- SIMILARITY: Contains 1 histidine kinase domain.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; U54628; AAC50670.1; -.
DR EMBL; U54618; AAC50670.1; JOINED.
DR EMBL; U54619; AAC50670.1; JOINED.
DR EMBL; U54620; AAC50670.1; JOINED.
DR EMBL; U54621; AAC50670.1; JOINED.
DR EMBL; U54622; AAC50670.1; JOINED.
DR EMBL; U54623; AAC50670.1; JOINED.
DR EMBL; U54624; AAC50670.1; JOINED.
DR EMBL; U54625; AAC50670.1; JOINED.
DR EMBL; U54626; AAC50670.1; JOINED.
DR EMBL; U54627; AAC50670.1; JOINED.
DR EMBL; U54617; AAC50669.1; -.
DR EMBL; AC002451; AAB67048.1; -.
DR EMBL; BC040239; AAH40239.1; -.
DR Genew; HGNC:8812; PDK4.
DR MIM; 602527; -.
DR GO; GO:0005739; C:mitochondrion; TAS.
DR GO; GO:0004672; F:protein kinase activity; TAS.
DR GO; GO:0004740; F:[pyruvate dehydrogenase (lipoamide)] kinase...; TAS.
DR GO; GO:0006006; P:glucose metabolism; TAS.
DR InterPro; IPR003594; ATPbind_ATPase.
DR InterPro; IPR005467; His_kinase.
DR Pfam; PF02518; HATPase_c; 1.
DR SMART; SM00387; HATPase_c; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
KW Kinase; Transferase; Transit peptide; Mitochondrion; Multigene family;
KW Phosphorylation.
FT TRANSIT 1 ? Mitochondrion (Potential).
FT CHAIN ? 411 [PYRUVATE DEHYDROGENASE [LIPOAMIDE]]
FT KINASE ISOZYME 4.
FT DOMAIN 138 368 HISTIDINE KINASE.
FT MOD_RES 127 127 PHOSPHORYLATION (AUTO-) (BY SIMILARITY).
SQ SEQUENCE 411 AA; 46469 MW; C17B78B6057000E9 CRC64;
MKAARFVLRS AGSLNGAGLV PREVEHFSRY SPSPLSMKQL LDFGSENACE RTSFAFLRQE
LPVRLANILK EIDILPTQLV NTSSVQLVKS WYIQSLMDLV EFHEKSPDDQ KALSDFVDTL
IKVRNRHHNV VPTMAQGIIE YKDACTVDPV TNQNLQYFLD RFYMNRISTR MLMNQHILIF
SDSQTGNPSH IGSIDPNCDV VAVVQDAFEC SRMLCDQYYL SSPELKLTQV NGKFPDQPIH
IVYVPSHLHH MLFELFKNAM RATVEHQENQ PSLTPIEVIV VLGKEDLTIK ISDRGGGVPL
RIIDRLFSYT YSTAPTPVMD NSRNAPLAGF GYGLPISRLY AKYFQGDLNL YSLSGYGTDA
IIYLKALSSE SIEKLPVFNK SAFKHYQMSS EADDWCIPSR EPKNLAKEVA M
//
ID PDXK_HUMAN STANDARD; PRT; 312 AA.
AC O00764; Q9BS02;
DT 01-NOV-1997 (Rel. 35, Created)
DT 01-NOV-1997 (Rel. 35, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE Pyridoxal kinase (EC 2.7.1.35) (Pyridoxine kinase).
GN PDXK OR PKH OR PNK.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A. (ISOFORM 1).
RX MEDLINE=97256798; PubMed=9099727;
RA Hanna M.C., Turner A.J., Kirkness E.F.;
RT "Human pyridoxal kinase. cDNA cloning, expression, and modulation by
RT ligands of the benzodiazepine receptor.";
RL J. Biol. Chem. 272:10756-10760(1997).
RN [2]
RP SEQUENCE FROM N.A.
RX MEDLINE=20289799; PubMed=10830953;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T.,
RA Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y.,
RA Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K.,
RA Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D.,
RA Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W.,
RA Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S.,
RA Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E.,
RA Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P.,
RA Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H.,
RA Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E.,
RA Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F.,
RA Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [3]
RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 2).
RC TISSUE=Eye, and Ovary;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC -!- FUNCTION: Required for synthesis of pyridoxal-5-phosphate from
CC vitamin B6.
CC -!- CATALYTIC ACTIVITY: ATP + pyridoxal = ADP + pyridoxal 5'-
CC phosphate.
CC -!- SUBUNIT: Homodimer (Probable).
CC -!- SUBCELLULAR LOCATION: Cytoplasmic.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O00764-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O00764-2; Sequence=VSP_004653;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the pyridoxine kinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; U89606; AAC51233.1; -.
DR EMBL; AP001752; BAA95540.1; -.
DR EMBL; BC000123; AAH00123.1; -.
DR EMBL; BC005825; AAH05825.1; -.
DR Genew; HGNC:8819; PDXK.
DR MIM; 179020; -.
DR GO; GO:0008478; F:pyridoxal kinase activity; TAS.
DR InterPro; IPR002173; PfkB.
DR InterPro; IPR004625; Pyridox_kin.
DR Pfam; PF00294; pfkB; 1.
DR TIGRFAMs; TIGR00687; pyridox_kin; 1.
KW Transferase; Kinase; Alternative splicing.
FT VARSPLIC 83 110 Missing (in isoform 2).
FT /FTId=VSP_004653.
SQ SEQUENCE 312 AA; 35102 MW; 2DBDCAB5D8640569 CRC64;
MEEECRVLSI QSHVIRGYVG NRAATFPLQV LGFEIDAVNS VQFSNHTGYA HWKGQVLNSD
ELQELYEGLR LNNMNKYDYV LTGYTRDKSF LAMVVDIVQE LKQQNPRLVY VCDPVLGDKW
DGEGSMYVPE DLLPVYKEKV VPLADIITPN QFEAELLSGR KIHSQEEALR VMDMLHSMGP
DTVVITSSDL PSPQGSNYLI VLGSQRRRNP AGSVVMERIR MDIRKVDAVF VGTGDLFAAM
LLAWTHKHPN NLKVACEKTV STLHHVLQRT IQCAKAQAGE GVRPSPMQLE LRMVQSKRDI
EDPEIVVQAT VL
//
ID PGK1_HUMAN STANDARD; PRT; 417 AA.
AC P00558;
DT 21-JUL-1986 (Rel. 01, Created)
DT 21-JUL-1986 (Rel. 01, Last sequence update)
DT 28-FEB-2003 (Rel. 41, Last annotation update)
DE Phosphoglycerate kinase 1 (EC 2.7.2.3) (Primer recognition protein 2)
DE (PRP 2).
GN PGK1 OR PGKA.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RC TISSUE=Liver;
RX MEDLINE=83169680; PubMed=6188151;
RA Michelson A.M., Markham A.F., Orkin S.H.;
RT "Isolation and DNA sequence of a full-length cDNA clone for human X
RT chromosome-encoded phosphoglycerate kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:472-476(1983).
RN [2]
RP SEQUENCE OF 1-416 FROM N.A.
RX MEDLINE=86016816; PubMed=2995995;
RA Michelson A.M., Blake C.C., Evans S.T., Orkin S.H.;
RT "Structure of the human phosphoglycerate kinase gene and the intron-
RT mediated evolution and dispersal of the nucleotide-binding domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:6965-6969(1985).
RN [3]
RP SEQUENCE.
RC TISSUE=Erythrocyte;
RX MEDLINE=80227775; PubMed=7391027;
RA Huang I.-Y., Welch C.D., Yoshida A.;
RT "Complete amino acid sequence of human phosphoglycerate kinase.
RT Cyanogen bromide peptides and complete amino acid sequence.";
RL J. Biol. Chem. 255:6412-6420(1980).
RN [4]
RP PARTIAL SEQUENCE.
RC TISSUE=Placenta;
RX MEDLINE=90216667; PubMed=2324090;
RA Jindal H.K., Vishwanatha J.K.;
RT "Functional identity of a primer recognition protein as
RT phosphoglycerate kinase.";
RL J. Biol. Chem. 265:6540-6543(1990).
RN [5]
RP SEQUENCE OF 1-20 FROM N.A.
RX MEDLINE=85155507; PubMed=6099325;
RA Singer-Sam J., Keith D.H., Tani K., Simmer R.L., Shively L.,
RA Lindsay S., Yoshida A., Riggs A.D.;
RT "Sequence of the promoter region of the gene for human X-linked 3-
RT phosphoglycerate kinase].";
RL Gene 32:409-417(1984).
RN [6]
RP SEQUENCE OF 1-13 FROM N.A.
RX MEDLINE=90049205; PubMed=2814502;
RA Pfeifer G.P., Steigerwald S.D., Mueller P.R., Wold B., Riggs A.D.;
RT "Genomic sequencing and methylation analysis by ligation mediated
RT PCR.";
RL Science 246:810-813(1989).
RN [7]
RP REVIEW ON VARIANTS.
RX MEDLINE=97230014; PubMed=9075577;
RA Yoshida A.;
RT "Hematologically important mutations: molecular abnormalities of
RT phosphoglycerate kinase.";
RL Blood Cells Mol. Dis. 22:265-267(1996).
RN [8]
RP VARIANT CHRONIC HEMOLYTIC ANEMIA LYS-190 DEL.
RX MEDLINE=96230923; PubMed=8673469;
RA Yoshida A., Twele T.W., Dave V., Beutler E.;
RT "Molecular abnormality of a phosphoglycerate kinase variant
RT (PGK-Alabama).";
RL Blood Cells Mol. Dis. 21:179-181(1995).
RN [9]
RP VARIANT CHRONIC HEMOLYTIC ANEMIA/MENTAL RETARDATION VAL-163, AND
RP VARIANT RHABDOMYOLYSIS ASN-314.
RX MEDLINE=94318968; PubMed=8043870;
RA Cohen-Solal M., Valentin C., Plassa F., Guillemin G., Danze F.,
RA Jaisson F., Rosa R.;
RT "Identification of new mutations in two phosphoglycerate kinase (PGK)
RT variants expressing different clinical syndromes: PGK Creteil and PGK
RT Amiens.";
RL Blood 84:898-903(1994).
RN [10]
RP VARIANT CHRONIC HEMOLYTIC ANEMIA ALA-251.
RX MEDLINE=96201344; PubMed=8615693;
RA Ookawara T., Dave V., Willems P., Martin J.J., de Barsy T.,
RA Matthys E., Yoshida A.;
RT "Retarded and aberrant splicings caused by single exon mutation in a
RT phosphoglycerate kinase variant.";
RL Arch. Biochem. Biophys. 327:35-40(1996).
RN [11]
RP VARIANT CHRONIC HEMOLYTIC ANEMIA VAL-284.
RX MEDLINE=98415729; PubMed=9744480;
RA Valentin C., Birgens H., Craescu C.T., Broedum-Nielsen K.,
RA Cohen-Solal M.;
RT "A phosphoglycerate kinase mutant (PGK Herlev; D285V) in a Danish
RT patient with isolated chronic hemolytic anemia: mechanism of mutation
RT and structure-function relationships.";
RL Hum. Mutat. 12:280-287(1998).
RN [12]
RP VARIANT CONGENITAL NONSPHEROCYTIC ANEMIA PRO-87.
RX MEDLINE=91159642; PubMed=2001457;
RA Maeda M., Yoshida A.;
RT "Molecular defect of a phosphoglycerate kinase variant (PGK-Matsue)
RT associated with hemolytic anemia: Leu-->Pro substitution caused by
RT T/A-->C/G transition in exon 3.";
RL Blood 77:1348-1352(1991).
RN [13]
RP VARIANT CHRONIC HEMOLYTIC ANEMIA ARG-315.
RX MEDLINE=92265933; PubMed=1586722;
RA Maeda M., Bawle E.V., Kulkarni R., Beutler E., Yoshida A.;
RT "Molecular abnormalities of a phosphoglycerate kinase variant
RT generated by spontaneous mutation.";
RL Blood 79:2759-2762(1992).
RN [14]
RP VARIANT MUNCHEN ASN-267.
RX MEDLINE=80227776; PubMed=7391028;
RA Fujii H., Krietsch W.K.G., Yoshida A.;
RT "A single amino acid substitution (Asp leads to Asn) in a
RT phosphoglycerate kinase variant (PGK Munchen) associated with enzyme
RT deficiency.";
RL J. Biol. Chem. 255:6421-6423(1980).
RN [15]
RP VARIANT MUNCHEN ASN-267, AND VARIANT ASN-351.
RX MEDLINE=81069227; PubMed=7440217;
RA Huang I.-Y., Fujii H., Yoshida A.;
RT "Structure and function of normal and variant human phosphoglycerate
RT kinase.";
RL Hemoglobin 4:601-609(1980).
RN [16]
RP VARIANT CHRONIC HEMOLYTIC ANEMIA VAL-157.
RX MEDLINE=92190498; PubMed=1547346;
RA Fujii H., Kanno H., Hirono A., Shiomura T., Miwa S.;
RT "A single amino acid substitution (157 Gly-->Val) in a
RT phosphoglycerate kinase variant (PGK Shizuoka) associated with
RT chronic hemolysis and myoglobinuria.";
RL Blood 79:1582-1585(1992).
RN [17]
RP VARIANT CHRONIC NONSPHEROCYTIC HEMOLYTIC ANEMIA MET-265.
RX MEDLINE=81223926; PubMed=6941312;
RA Fujii H., Chen S.-H., Akatsuka J., Miwa S., Yoshida A.;
RT "Use of cultured lymphoblastoid cells for the study of abnormal
RT enzymes: molecular abnormality of a phosphoglycerate kinase variant
RT associated with hemolytic anemia.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:2587-2590(1981).
RN [18]
RP VARIANT CHRONIC HEMOLYTIC ANEMIA PRO-205.
RX MEDLINE=81054987; PubMed=6933565;
RA Fujii H., Yoshida A.;
RT "Molecular abnormality of phosphoglycerate kinase-Uppsala associated
RT with chronic nonspherocytic hemolytic anemia.";
RL Proc. Natl. Acad. Sci. U.S.A. 77:5461-5465(1980).
CC -!- FUNCTION: In addition to its role as a glycolytic enzyme, it
CC seems that PGK-1 acts as a polymerase alpha cofactor protein
CC (primer recognition protein).
CC -!- CATALYTIC ACTIVITY: ATP + 3-phospho-D-glycerate = ADP + 3-
CC phospho-D-glyceroyl phosphate.
CC -!- PATHWAY: Second phase of glycolysis; second step.
CC -!- SUBUNIT: Monomer.
CC -!- DISEASE: Defects in PGK1 are generally associated with chronic
CC hemolytic anemia [MIM:311800]; although it can be accompanied by
CC either mental retardation or muscular disease (rhabdomyolysis).
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; V00572; CAA23835.1; -.
DR EMBL; M11968; AAA60079.1; -.
DR EMBL; M11958; AAA60079.1; JOINED.
DR EMBL; M11959; AAA60079.1; JOINED.
DR EMBL; M11960; AAA60079.1; JOINED.
DR EMBL; M11961; AAA60079.1; JOINED.
DR EMBL; M11962; AAA60079.1; JOINED.
DR EMBL; M11963; AAA60079.1; JOINED.
DR EMBL; M11964; AAA60079.1; JOINED.
DR EMBL; M11965; AAA60079.1; JOINED.
DR EMBL; M11966; AAA60079.1; JOINED.
DR EMBL; M11967; AAA60079.1; JOINED.
DR EMBL; L00160; AAA60078.1; -.
DR EMBL; M34017; AAA60103.1; -.
DR HSSP; P00560; 1QPG.
DR Aarhus/Ghent-2DPAGE; 3308; NEPHGE.
DR Genew; HGNC:8896; PGK1.
DR GK; P00558; -.
DR MIM; 311800; -.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; TAS.
DR InterPro; IPR001576; PGK.
DR Pfam; PF00162; PGK; 1.
DR PRINTS; PR00477; PHGLYCKINASE.
DR PROSITE; PS00111; PGLYCERATE_KINASE; 1.
KW Transferase; Kinase; Multigene family; Glycolysis; Acetylation;
KW Disease mutation; Polymorphism; Hereditary hemolytic anemia.
FT INIT_MET 0 0
FT MOD_RES 1 1 ACETYLATION.
FT VARIANT 87 87 L -> P (in congenital nonspherocytic
FT anemia; variant Matsue).
FT /FTId=VAR_006076.
FT VARIANT 157 157 G -> V (in chronic hemolytic anemia;
FT variant Shizuoka).
FT /FTId=VAR_006077.
FT VARIANT 163 163 D -> V (in chronic hemolytic anemia and
FT mental retardation; variant Amiens).
FT /FTId=VAR_006078.
FT VARIANT 190 190 Missing (in chronic hemolytic anemia;
FT variant Alabama).
FT /FTId=VAR_006079.
FT VARIANT 205 205 R -> P (in chronic hemolytic anemia;
FT variant Uppsala).
FT /FTId=VAR_006080.
FT VARIANT 251 251 E -> A (in chronic hemolytic anemia;
FT variant Antwerp).
FT /FTId=VAR_006081.
FT VARIANT 265 265 V -> M (in chronic nonspherocytic
FT hemolytic anemia; variant Tokyo).
FT /FTId=VAR_006082.
FT VARIANT 267 267 D -> N (in Munchen; 21% of activity).
FT /FTId=VAR_006083.
FT VARIANT 284 284 D -> V (in chronic hemolytic anemia;
FT variant Herlev; 50% of activity).
FT /FTId=VAR_006084.
FT VARIANT 314 314 D -> N (in rhabdomyolysis; variant
FT Creteil).
FT /FTId=VAR_006085.
FT VARIANT 315 315 C -> R (in chronic hemolytic anemia;
FT variant Michigan).
FT /FTId=VAR_006086.
FT VARIANT 351 351 T -> N.
FT /FTId=VAR_006087.
FT CONFLICT 38 38 Missing (in Ref. 3).
SQ SEQUENCE 417 AA; 44596 MW; 9940760355AB9CEA CRC64;
SLSNKLTLDK LDVKGKRVVM RVDFNVPMKN NQITNNQRIK AAVPSIKFCL DNGAKSVVLM
SHLGRPDGVP MPDKYSLEPV AVELKSLLGK DVLFLKDCVG PEVEKACANP AAGSVILLEN
LRFHVEEEGK GKDASGNKVK AEPAKIEAFR ASLSKLGDVY VNDAFGTAHR AHSSMVGVNL
PQKAGGFLMK KELNYFAKAL ESPERPFLAI LGGAKVADKI QLINNMLDKV NEMIIGGGMA
FTFLKVLNNM EIGTSLFDEE GAKIVKDLMS KAEKNGVKIT LPVDFVTADK FDENAKTGQA
TVASGIPAGW MGLDCGPESS KKYAEAVTRA KQIVWNGPVG VFEWEAFARG TKALMDEVVK
ATSRGCITII GGGDTATCCA KWNTEDKVSH VSTGGGASLE LLEGKVLPGV DALSNIL
//
ID PGK2_HUMAN STANDARD; PRT; 416 AA.
AC P07205; Q9H107;
DT 01-APR-1988 (Rel. 07, Created)
DT 28-FEB-2003 (Rel. 41, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE Phosphoglycerate kinase, testis specific (EC 2.7.2.3).
GN PGK2 OR PGKB.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RX MEDLINE=87173013; PubMed=3453121;
RA McCarrey J.R., Thomas K.;
RT "Human testis-specific PGK gene lacks introns and possesses
RT characteristics of a processed gene.";
RL Nature 326:501-504(1987).
RN [2]
RP SEQUENCE FROM N.A.
RA Phillimore B.;
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SEQUENCE FROM N.A.
RC TISSUE=Brain;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC -!- CATALYTIC ACTIVITY: ATP + 3-phospho-D-glycerate = ADP + 3-
CC phospho-D-glyceroyl phosphate.
CC -!- PATHWAY: Second phase of glycolysis; second step.
CC -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; X05246; CAA28872.1; -.
DR EMBL; AL121974; CAC19655.1; -.
DR EMBL; BC038843; AAH38843.1; -.
DR PIR; A27816; A27816.
DR HSSP; P00560; 1QPG.
DR Genew; HGNC:8898; PGK2.
DR MIM; 172270; -.
DR GO; GO:0005829; C:cytosol; NAS.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; NAS.
DR GO; GO:0006096; P:glycolysis; NAS.
DR InterPro; IPR001576; PGK.
DR Pfam; PF00162; PGK; 1.
DR PRINTS; PR00477; PHGLYCKINASE.
DR PROSITE; PS00111; PGLYCERATE_KINASE; 1.
KW Transferase; Kinase; Multigene family; Glycolysis.
FT INIT_MET 0 0
FT CONFLICT 395 395 G -> R (in Ref. 1).
SQ SEQUENCE 416 AA; 44665 MW; F97C03FC7CA70EB2 CRC64;
SLSKKLTLDK LDVRGKRVIM RVDFNVPMKK NQITNNQRIK ASIPSIKYCL DNGAKAVVLM
SHLGRPDGVP MPDKYSLAPV AVELKSLLGK DVLFLKDCVG AEVEKACANP APGSVILLEN
LRFHVEEEGK GQDPSGKKIK AEPDKIEAFR ASLSKLGDVY VNDAFGTAHR AHSSMVGVNL
PHKASGFLMK KELDYFAKAL ENPVRPFLAI LGGAKVADKI QLIKNMLDKV NEMIIGGGMA
YTFLKVLNNM EIGASLFDEE GAKIVKDIMA KAQKNGVRIT FPVDFVTGDK FDENAQVGKA
TVASGISPGW MGLDCGPESN KNHAQVVAQA RLIVWNGPLG VFEWDAFAKG TKALMDEIVK
ATSKGCITVI GGGDTATCCA KWNTEDKVSH VSTGGGASLE LLEGKILPGV EALSNM
//
ID PI4K_HUMAN STANDARD; PRT; 2044 AA.
AC P42356; Q7Z625; Q9UPG2;
DT 01-NOV-1995 (Rel. 32, Created)
DT 15-MAR-2004 (Rel. 43, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Phosphatidylinositol 4-kinase alpha (EC 2.7.1.67) (PI4-kinase)
DE (PtdIns-4-kinase) (PI4K-alpha).
GN PIK4CA OR PIK4.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A. (ISOFORM 1), AND TISSUE SPECIFICITY.
RX MEDLINE=99203157; PubMed=10101268;
RA Gehrmann T., Guelkan H., Suer S., Herberg F.W., Balla A., Vereb G.,
RA Mayr G.W., Heilmeyer L.M.G. Jr.;
RT "Functional expression and characterisation of a new human
RT phosphatidylinositol 4-kinase PI4K230.";
RL Biochim. Biophys. Acta 1437:341-356(1999).
RN [2]
RP SEQUENCE FROM N.A. (ISOFORM 2), AND TISSUE SPECIFICITY.
RX MEDLINE=95050701; PubMed=7961848;
RA Wong K., Cantley L.C.;
RT "Cloning and characterization of a human phosphatidylinositol
RT 4-kinase.";
RL J. Biol. Chem. 269:28878-28884(1994).
RN [3]
RP SEQUENCE OF 1142-2044 FROM N.A. (ISOFORM 1).
RC TISSUE=Uterus;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC -!- FUNCTION: Acts on phosphatidylinositol (PtdIns) in the first
CC committed step in the production of the second messenger
CC inositol-1,4,5,-trisphosphate.
CC -!- CATALYTIC ACTIVITY: ATP + 1-phosphatidyl-1D-myo-inositol = ADP +
CC 1-phosphatidyl-1D-myo-inositol 4-phosphate.
CC -!- ENZYME REGULATION: THIS IS A TYPE II PTDINS-4-KINASE ACTIVATED BY
CC DETERGENTS SUCH AS TRITON AND INHIBITED BY ADENOSINE.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=PI4K230;
CC IsoId=P42356-1; Sequence=Displayed;
CC Name=2; Synonyms=PI4K97;
CC IsoId=P42356-2; Sequence=VSP_008805;
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously. Highest levels in
CC placenta and brain. Little or no expression in lung, liver,
CC pancreas, testis or leukocytes.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AF012872; AAD13352.1; -.
DR EMBL; L36151; AAA56839.1; -.
DR EMBL; BC018120; AAH18120.2; -.
DR EMBL; BC053654; AAH53654.1; -.
DR PIR; A55404; A55404.
DR Genew; HGNC:8983; PIK4CA.
DR MIM; 600286; -.
DR GO; GO:0005798; C:Golgi vesicle; TAS.
DR GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; TAS.
DR GO; GO:0006661; P:phosphatidylinositol biosynthesis; TAS.
DR GO; GO:0007268; P:synaptic transmission; TAS.
DR InterPro; IPR008938; ARM.
DR InterPro; IPR001263; PI3Ka.
DR InterPro; IPR000403; PI3_PI4_kinase.
DR Pfam; PF00613; PI3Ka; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
KW Transferase; Kinase; Alternative splicing.
FT DOMAIN 1788 2021 PI3K/PI4K.
FT VARSPLIC 1 1190 Missing (in isoform 2).
FT /FTId=VSP_008805.
SQ SEQUENCE 2044 AA; 231290 MW; EE189E8B0A91355D CRC64;
MCPVDFHGIF QLDERRRDAV IALGIFLIES DLQHKDCVVP YLLRLLKGLP KVYWVEESTA
RKGRGALPVA ESFSFCLVTL LSDVAYRDPS LRDEILEVLL QVLHVLLGMC QALEIQDKEY
LCKYAIPCLI GISRAFGRYS NMEESLLSKL FPKIPPHSLR VLEELEGVRR RSFNDFRSIL
PSNLLTVCQE GTLKRKTSSV SSISQVSPER GMPPPSSPGG SAFHYFEASC LPDGTALEPE
YYFSTISSSF SVSPLFNGVT YKEFNIPLEM LRELLNLVKK IVEEAVLKSL DAIVASVMEA
NPSADLYYTS FSDPLYLTMF KMLRDTLYYM KDLPTSFVKE IHDFVLEQFN TSQGELQKIL
HDADRIHNEL SPLKLRCQAS AACVDLMVWA VKDEQGAENL CIKLSEKLQS KTSSKVIIAH
LPLLICCLQG LGRLCERFPV VVHSVTPSLR DFLVIPSPVL VKLYKYHSQY HTVAGNDIKI
SVTNEHSEST LNVMSGKKSQ PSMYEQLRDI AIDNICRCLK AGLTVDPVIV EAFLASLSNR
LYISQESDKD AHLIPDHTIR ALGHIAVALR DTPKVMEPIL QILQQKFCQP PSPLDVLIID
QLGCLVITGN QYIYQEVWNL FQQISVKASS VVYSATKDYK DHGYRHCSLA VINALANIAA
NIQDEHLVDE LLMNLLELFV QLGLEGKRAS ERASEKGPAL KASSSAGNLG VLIPVIAVLT
RRLPPIKEAK PRLQKLFRDF WLYSVLMGFA VEGSGLWPEE WYEGVCEIAT KSPLLTFPSK
EPLRSVLQYN SAMKNDTVTP AELSELRSTI INLLDPPPEV SALINKLDFA MSTYLLSVYR
LEYMRVLRST DPDRFQVMFC YFEDKAIQKD KSGMMQCVIA VADKVFDAFL NMMADKAKTK
ENEEELERHA QFLLVNFNHI HKRIRRVADK YLSGLVDKFP HLLWSGTVLK TMLDILQTLS
LSLSADIHKD QPYYDIPDAP YRITVPDTYE ARESIVKDFA ARCGMILQEA MKWAPTVTKS
HLQEYLNKHQ NWVSGLSQHT GLAMATESIL HFAGYNKQNT TLGATQLSER PACVKKDYSN
FMASLNLRNR YAGEVYGMIR FSGTTGQMSD LNKMMVQDLH SALDRSHPQH YTQAMFKLTA
MLISSKDCDP QLLHHLCWGP LRMFNEHGME TALACWEWLL AGKDGVEVPF MREMAGAWHM
TVEQKFGLFS AEIKEADPLA ASEASQPKPC PPEVTPHYIW IDFLVQRFEI AKYCSSDQVE
IFSSLLQRSM SLNIGGAKGS MNRHVAAIGP RFKLLTLGLS LLHADVVPNA TIRNVLREKI
YSTAFDYFSC PPKFPTQGEK RLREDISIMI KFWTAMFSDK KYLTASQLVP PDNQDTRSNL
DITVGSRQQA TQGWINTYPL SSGMSTISKK SGMSKKTNRG SQLHKYYMKR RTLLLSLLAT
EIERLITWYN PLSAPELELD QAGENSVANW RSKYISLSEK QWKDNVNLAW SISPYLAVQL
PARFKNTEAI GNEVTRLVRL DPGAVSDVPE AIKFLVTWHT IDADAPELSH VLCWAPTDPP
TGLSYFSSMY PPHPLTAQYG VKVLRSFPPD AILFYIPQIV QALRYDKMGY VREYILWAAS
KSQLLAHQFI WNMKTNIYLD EEGHQKDPDI GDLLDQLVEE ITGSLSGPAK DFYQREFDFF
NKITNVSAII KPYPKGDERK KACLSALSEV KVQPGCYLPS NPEAIVLDID YKSGTPMQSA
AKAPYLAKFK VKRCGVSELE KEGLRCRSDS EDECSTQEAD GQKISWQAAI FKVGDDCRQD
MLALQIIDLF KNIFQLVGLD LFVFPYRVVA TAPGCGVIEC IPDCTSRDQL GRQTDFGMYD
YFTRQYGDES TLAFQQARYN FIRSMAAYSL LLFLLQIKDR HNGNIMLDKK GHIIHIDFGF
MFESSPGGNL GWEPDIKLTD EMVMIMGGKM EATPFKWFME MCVRGYLAVR PYMDAVVSLV
TLMLDTGLPC FRGQTIKLLK HRFSPNMTER EAANFIMKVI QSCFLSNRSR TYDMIQYYQN
DIPY
//
ID PI52_HUMAN STANDARD; PRT; 406 AA.
AC P48426;
DT 01-FEB-1996 (Rel. 33, Created)
DT 16-OCT-2001 (Rel. 40, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE Phosphatidylinositol-4-phosphate 5-kinase type II alpha (EC 2.7.1.149)
DE (PIP5KII-alpha) (1-phosphatidylinositol-4-phosphate 5-kinase)
DE (PtdIns(4)P-5-kinase B isoform) (Diphosphoinositide kinase).
GN PIP5K2A OR PIP5K2.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE.
RC TISSUE=Placenta;
RX MEDLINE=95155363; PubMed=7852364;
RA Boronenkov I.V., Anderson R.A.;
RT "The sequence of phosphatidylinositol-4-phosphate 5-kinase defines a
RT novel family of lipid kinases.";
RL J. Biol. Chem. 270:2881-2884(1995).
RN [2]
RP REVISIONS TO 298-310 AND 381-382.
RA Boronenkov I.V.;
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SEQUENCE FROM N.A.
RC TISSUE=Hippocampus;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC -!- FUNCTION: Catalyzes the phosphorylation of phosphatidylinositol-4-
CC phosphate on the fifth hydroxyl of the myo-inositol ring, to form
CC phosphatidylinositol-4,5-biphosphate.
CC -!- CATALYTIC ACTIVITY: ATP + 1-phosphatidyl-1D-myo-inositol 4-
CC monophosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-
CC bisphosphate.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- TISSUE SPECIFICITY: EXPRESSED UBIQUITOUSLY, WITH HIGH LEVELS IN
CC THE BRAIN.
CC -!- SIMILARITY: Belongs to the PtdIns(4)P-5-kinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; U14957; AAA64835.2; -.
DR EMBL; BC018034; AAH18034.1; -.
DR Genew; HGNC:8997; PIP5K2A.
DR MIM; 603140; -.
DR InterPro; IPR002498; PIP5K.
DR Pfam; PF01504; PIP5K; 1.
KW Transferase; Kinase.
SQ SEQUENCE 406 AA; 46224 MW; 5BAF0A27CC9EF376 CRC64;
MATPGNLGSS VLASKTKTKK KHFVAQKVKL FRASDPLLSV LMWGVNHSIN ELSHVQIPVM
LMPDDFKAYS KIKVDNHLFN KENMPSHFKF KEYCPMVFRN LRERFGIDDQ DFQNSLTRSA
PLPNDSQARS GARFHTSYDK RYIIKTITSE DVAEMHNILK KYHQYIVECH GITLLPQFLG
MYRLNVDGVE IYVIVTRNVF SHRLSVYRKY DLKGSTVARE ASDKEKAKEL PTLKDNDFIN
EGQKIYIDDN NKKVFLEKLK KDVEFLAQLK LMDYSLLVGI HDVERAEQEE VECEENDGEE
EGESDGTHPV GTPPDSPGNT LNSSPPLAPG EFDPNIDVYG IKCHENSPRK EVYFMAIIDI
LTHYDAKKKA AHAAKTVKHG AGAEISTVNP EQYSKRFLDF IGHILT
//
ID PI53_HUMAN STANDARD; PRT; 406 AA.
AC P53807;
DT 01-OCT-1996 (Rel. 34, Created)
DT 01-OCT-1996 (Rel. 34, Last sequence update)
DT 28-FEB-2003 (Rel. 41, Last annotation update)
DE Phosphatidylinositol-4-phosphate 5-kinase type III (EC 2.7.1.149) (1-
DE phosphatidylinositol-4-phosphate kinase) (PIP5KIII) (PtdIns(4)P-5-
DE kinase C isoform) (Diphosphoinositide kinase).
GN PIP5K3.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RC TISSUE=Leukocyte;
RX MEDLINE=95366942; PubMed=7639683;
RA Divecha N., Truong O., Hsuan J.J., Hinchliffe K.A., Irvine R.F.;
RT "The cloning and sequence of the C isoform of PtdIns4P 5-kinase.";
RL Biochem. J. 309:715-719(1995).
CC -!- FUNCTION: Catalyzes the phosphorylation of phosphatidylinositol-4-
CC phosphate on the fifth hydroxyl of the myo-inositol ring, to form
CC phosphatidylinositol-4,5-biphosphate.
CC -!- CATALYTIC ACTIVITY: ATP + 1-phosphatidyl-1D-myo-inositol 5-
CC phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.
CC -!- TISSUE SPECIFICITY: Particularly abundant in platelets and in
CC brain. Present in most tissues, except notably skeletal muscle and
CC small intestine.
CC -!- SIMILARITY: Belongs to the PtdIns(4)P-5-kinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; S78798; AAB35041.1; -.
DR PIR; S57217; S57217.
DR GO; GO:0016308; F:1-phosphatidylinositol-4-phosphate 5-kinase...; NAS.
DR GO; GO:0016310; P:phosphorylation; NAS.
DR InterPro; IPR002498; PIP5K.
DR Pfam; PF01504; PIP5K; 1.
DR SMART; SM00330; PIPKc; 1.
KW Transferase; Kinase.
SQ SEQUENCE 406 AA; 46078 MW; E8DDFAF61A17534B CRC64;
MATPGNLGSS VLASKTKTKK KHFVAQKVKL FRASDPLLSV LMWGVNHSIN ELSHVQIPVM
LMPDDFKAYS KIKVDNHLFN KENMPSHFKF KEYCPMVFRN CGKRFGIDVQ DFQNSLTRSA
PLPNDSQARS GARFHTSYDK RYMIKTITSE DVAEMHNILK KYHQYIVECH GITLLPHLLG
MYRLNVDGVE IYVIVTRNVF SHRLSVYRKY DLKGSTVARE ASDKEKAKEL PTLKDNDFIN
EGQKIYIDDN SKKVFLEKLK KDVEFLAQLK LMDYSLLVGI HDVERAEQEE VECEENDGEE
EGESDGTHPV GTPPDSPGNT LNSSPPLAPG EFEPNIDVYG IKCHENSPRK EVYFMAIIDI
LTHYDAKKKA AHAAKTVKHG AGAEISTVNP EQYSKRFLDF IGHILT
//
ID PK3B_HUMAN STANDARD; PRT; 1634 AA.
AC O00750; O95666;
DT 16-OCT-2001 (Rel. 40, Created)
DT 16-OCT-2001 (Rel. 40, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing beta
DE polypeptide (EC 2.7.1.154) (Phosphoinositide 3-Kinase-C2-beta)
DE (PtdIns-3-kinase C2 beta) (PI3K-C2beta) (C2-PI3K).
GN PIK3C2B.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A., AND TISSUE SPECIFICITY.
RC TISSUE=Breast;
RX MEDLINE=97289668; PubMed=9144573;
RA Brown R.A., Ho L.K.F., Weber-Hall S.J., Shipley J.M., Fry M.J.;
RT "Identification and cDNA cloning of a novel mammalian C2 domain-
RT containing phosphoinositide 3-kinase, HsC2-PI3K.";
RL Biochem. Biophys. Res. Commun. 233:537-544(1997).
RN [2]
RP SEQUENCE OF 26-1634 FROM N.A., AND CHARACTERIZATION.
RC TISSUE=Monocytes;
RX MEDLINE=99047700; PubMed=9830063;
RA Arcaro A., Volinia S., Zvelebil M.J., Stein R., Watton S.J.,
RA Layton M.J., Gout I., Ahmadi K., Downward J., Waterfield M.D.;
RT "Human phosphoinositide 3-kinase C2beta, the role of calcium and the
RT C2 domain in enzyme activity.";
RL J. Biol. Chem. 273:33082-33090(1998).
CC -!- FUNCTION: PHOSPHORYLATES PTDINS AND PTDINS4P WITH A PREFERENCE FOR
CC PTDINS. DOES NOT PHOSPHORYLATE PTDINS(4,5)P2.
CC -!- CATALYTIC ACTIVITY: ATP + 1-phosphatidyl-1D-myo-inositol 4-
CC phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate.
CC -!- SUBCELLULAR LOCATION: Found mostly in the microsome, but also in
CC the plasma membrane and cytosol.
CC -!- TISSUE SPECIFICITY: Widely expressed, but levels are highest in
CC thymus and placenta and lowest in peripheral blood, skeletal
CC muscle and kidney.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC -!- SIMILARITY: Contains 1 C2 domain.
CC -!- SIMILARITY: Contains 1 phox homology (PX) domain.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-26 is the initiator.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; Y11312; CAA72168.1; -.
DR EMBL; Y13892; CAA74194.1; -.
DR PIR; JC5500; JC5500.
DR HSSP; P21707; 1RSY.
DR Genew; HGNC:8972; PIK3C2B.
DR MIM; 602838; -.
DR GO; GO:0005829; C:cytosol; NAS.
DR GO; GO:0005792; C:microsome; NAS.
DR GO; GO:0005886; C:plasma membrane; NAS.
DR GO; GO:0035005; F:phosphatidylinositol-4-phosphate 3-kinase a...; NAS.
DR InterPro; IPR008938; ARM.
DR InterPro; IPR000008; C2.
DR InterPro; IPR008973; C2_CaLB.
DR InterPro; IPR000403; PI3_PI4_kinase.
DR InterPro; IPR002420; PI3K_C2.
DR InterPro; IPR000341; PI3K_ras_bind.
DR InterPro; IPR001263; PI3Ka.
DR InterPro; IPR001683; PX.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF00794; PI3K_rbd; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00142; PI3K_C2; 1.
DR SMART; SM00144; PI3K_rbd; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM00312; PX; 1.
DR PROSITE; PS00499; C2_DOMAIN_1; FALSE_NEG.
DR PROSITE; PS50004; C2_DOMAIN_2; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS50195; PX; 1.
KW Transferase; Kinase; Multigene family.
FT DOMAIN 1365 1481 PX.
FT DOMAIN 156 162 PRO-RICH.
FT DOMAIN 169 174 PRO-RICH.
FT DOMAIN 1079 1343 PI3K/PI4K.
FT DOMAIN 1517 1608 C2 DOMAIN.
FT CONFLICT 63 63 P -> S (in Ref. 2).
FT CONFLICT 75 75 R -> W (in Ref. 2).
FT CONFLICT 99 99 Q -> L (in Ref. 2).
FT CONFLICT 246 246 V -> A (in Ref. 2).
FT CONFLICT 278 278 K -> E (in Ref. 2).
FT CONFLICT 567 567 P -> S (in Ref. 2).
FT CONFLICT 664 665 DM -> EL (in Ref. 2).
SQ SEQUENCE 1634 AA; 184856 MW; C0B5DF63C668B824 CRC64;
MSSTQDNGEH WKSLESVGIS RKELAMAEAL QMEYDALSRL RHDKEENRAK QNADPSLISW
DEPGVDFYSK PAGRRTDLKL LRGLSGSDPT LNYNSLSPQE GPPNHSTSQG PQPGSDPWPK
GSLSGDYLYI FDGSDGGVSS SPGPGDIEGS CKKLSPPPLP PRASIWDTPP LPPRKGSPSS
SKISQPSDIN TFSLVEQLPG KLLEHRILEE EEVLGGGGQG RLLGSVDYDG INDAITRLNL
KSTYDVEMLR DATRGWKEGR GPLDFSKDTS GKPVARSKTM PPQVPPRTYA SRYGNRKNAT
PGKNRRISAA PVGSRPHTVA NGHELFEVSE ERDEEVAAFC HMLDILRSGS DIQDYFLTGY
VWSAVTPSPE HLGDEVNLKV TVLCDRLQEA LTFTCNCSST VDLLIYQTLC YTHDDLRNVD
VGDFVLKPCG LEEFLQNKHA LGSHEYIQYC RKFDIDIRLQ LMEQKVVRSD LARTVNDDQS
PSTLNYLVHL QERPVKQTIS RQALSLLFDT YHNEVDAFLL ADGDFPLKAD RVVQSVKAIC
NALAAVETPE ITSALNQLPP CPSRMQPKIQ KDPSVLAVRE NREKVVEALT AAILDLVELY
CNTFNADFQT AVPGSRKHDL VQEACHFARS LAFTVYATHR IPIIWATSYE DFYLSCSLSH
GGKDMCSPLQ TRRAHFSKYL FHLIVWDQQI CFPVQVNRLP RETLLCATLY ALPIPPPGSS
SEANKQRRVP EALGWVTTPL FNFRQVLTCG RKLLGLWPAT QENPSARWSA PNFHQPDSVI
LQIDFPTSAF DIKFTSPPGD KFSPRYEFGS LREEDQRKLK DIMQKESLYW LTDADKKRLW
EKRYYCHSEV SSLPLVLASA PSWEWACLPD IYVLLKQWTH MNHQDALGLL HATFPDQEVR
RMAVQWIGSL SDAELLDYLP QLVQALKYEC YLDSPLVRFL LKRAVSDLRV THYFFWLLKD
GLKDSQFSIR YQYLLAALLC CCGKGLREEF NRQCWLVNAL AKLAQQVREA APSARQGILR
TGLEEVKQFF ALNGSCRLPL SPSLLVKGIV PRDCSYFNSN AVPLKLSFQN VDPLGENIRV
IFKCGDDLRQ DMLTLQMIRI MSKIWVQEGL DMRMVIFRCF STGRGRGMVE MIPNAETLRK
IQVEHGVTGS FKDRPLADWL QKHNPGEDEY EKAVENFIYS CAGCCVATYV LGICDRHNDN
IMLKTTGHMF HIDFGRFLGH AQMFGNIKRD RAPFVFTSDM AYVINGGDKP SSRFHDFVDL
CCQAYNLIRK HTHLFLNLLG LMLSCGIPEL SDLEDLKYVY DALRPQDTEA NATTYFTRLI
ESSLGSVATK LNFFIHNLAQ MKFTGSDDRL TLSFASRTHT LKSSGRISDV FLCRHEKIFH
PNKGYIYVVK VMRENTHEAT YIQRTFEEFQ ELHNKLRLLF PSSHLPSFPS RFVIGRSRGE
AVAERRREEL NGYIWHLIHA PPEVAECDLV YTFFHPLPRD EKAMGTSPAP KSSDGTWARP
VGKVGGEVKL SISYKNNKLF IMVMHIRGLQ LLQDGNDPDP YVKIYLLPDP QKTTKRKTKV
ARKTCNPTYN EMLVYDGIPK GDLQQRELQL SVLSEQGFWE NVLLGEVNIR LRELDLAQEK
TGWFALGSRS HGTL
//
ID PK3G_HUMAN STANDARD; PRT; 1448 AA.
AC O75747;
DT 16-OCT-2001 (Rel. 40, Created)
DT 16-OCT-2001 (Rel. 40, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing gamma
DE polypeptide (EC 2.7.1.154) (Phosphoinositide 3-Kinase-C2-gamma)
DE (PtdIns-3-kinase C2 gamma) (PI3K-C2gamma).
GN PIK3C2G.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A., AND TISSUE SPECIFICITY.
RC TISSUE=Breast, Liver, Mammary gland, and Prostate;
RX MEDLINE=99097359; PubMed=9878262;
RA Rozycka M., Lu Y.-J., Brown R.A., Lau M.R., Shipley J.M., Fry M.J.;
RT "cDNA cloning of a third human C2-domain-containing class II
RT phosphoinositide 3-kinase, PI3K-C2gamma, and chromosomal assignment
RT of this gene (PIK3C2G) to 12p12.";
RL Genomics 54:569-574(1998).
CC -!- FUNCTION: IN VITRO, PHOSPHORYLATES PTDINS AND PTDINS4P BUT NOT
CC PTDINS(4,5)P2 (BY SIMILARITY).
CC -!- CATALYTIC ACTIVITY: ATP + 1-phosphatidyl-1D-myo-inositol 4-
CC phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate.
CC -!- SUBCELLULAR LOCATION: Membrane-associated (By similarity).
CC -!- TISSUE SPECIFICITY: Highly expressed in liver, prostate and
CC testis. Lower levels in small intestine, kidney and pancreas.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC -!- SIMILARITY: Contains 1 C2 domain.
CC -!- SIMILARITY: Contains 1 phox homology (PX) domain.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AJ000008; CAA03853.1; -.
DR Genew; HGNC:8973; PIK3C2G.
DR GO; GO:0005624; C:membrane fraction; ISS.
DR GO; GO:0016303; F:phosphatidylinositol 3-kinase activity; NAS.
DR GO; GO:0016307; F:phosphatidylinositol phosphate kinase activity; NAS.
DR InterPro; IPR008938; ARM.
DR InterPro; IPR000008; C2.
DR InterPro; IPR008973; C2_CaLB.
DR InterPro; IPR000403; PI3_PI4_kinase.
DR InterPro; IPR002420; PI3K_C2.
DR InterPro; IPR000341; PI3K_ras_bind.
DR InterPro; IPR001263; PI3Ka.
DR InterPro; IPR001683; PX.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF00794; PI3K_rbd; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00142; PI3K_C2; 1.
DR SMART; SM00144; PI3K_rbd; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM00312; PX; 1.
DR PROSITE; PS00499; C2_DOMAIN_1; FALSE_NEG.
DR PROSITE; PS50004; C2_DOMAIN_2; FALSE_NEG.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS50195; PX; 1.
KW Transferase; Kinase; Membrane; Multigene family.
FT DOMAIN 916 1180 PI3K/PI4K.
FT DOMAIN 1198 1310 PX.
FT DOMAIN 1341 1438 C2 DOMAIN.
SQ SEQUENCE 1448 AA; 166094 MW; FFA6C6EA2ACD11B7 CRC64;
MAYSWQTDPN PNESHEKQYE HQEFLFVNQP HSSSQVSLGF DQIVDEISGK IPHYESEIDE
NTFFVPTAPK WDSTGHSLNE AHQISLNEFT SKSRELSWHQ VSKAPAIGFS PSVLPKPQNT
NKECSWGSPI GKHHGADDSR FSILAPSFTS LDKINLEKEL ENENHNYHIG FESSIPPTNS
SFSSDFMPKE ENKRSGHVNI VEPSLMLLKG SLQPGMWEST WQKNIESIGC SIQLVEVPQS
SNTSLASFCN KVKKIRERYH AADVNFNSGK IWSTTTAFPY QLFSKTKFNI HIFIDNSTQP
LHFMPCANYL VKDLIAEILH FCTNDQLLPK DHILSVCGSE EFLQNDHCLG SHKMFQKDKS
VIQLHLQKSR EAPGKLSRKH EEDHSQFYLN QLLEFMHIWK VSRQCLLTLI RKYDFHLKYL
LKTQENVYNI IEEVKKICSV LGCVETKQIT DAVNELSLIL QRKGENFYQS SETSAKGLIE
KVTTELSTSI YQLINVYCNS FYADFQPVNV PRCTSYLNPG LPSHLSFTVY AAHNIPETWV
HRINFPLEIK SLPRESMLTV KLFGIACATN NANLLAWTCL PLFPKEKSIL GSMLFSMTLQ
SEPPVEMITP GVWDVSQPSP VTLQIDFPAT GWEYMKPDSE ENRSNLEEPL KECIKHIARL
SQKQTPLLLS EEKKRYLWFY RFYCNNENCS LPLVLGSAPG WDERTVSEMH TILRRWTFSQ
PLEALGLLTS SFPDQEIRKV AVQQLDNLLN DELLEYLPQL VQAVKFEWNL ESPLVQLLLH
RSLQSIQVAH RLYWLLKNAE NEAYFKSWYQ KLLAALQFCA GKALNDEFSK EQKLIKILGD
IGERVKSASD HQRQEVLKKE IGRLEEFFQD VNTCHLPLNP ALCIKGIDHD ACSYFTSNAL
PLKITFINAN LMGKNISIIF KAGDDLRQDM LVLQLIQVMD NIWLQEGLDM QMIIYRCLST
GKDQRLVQMV PDAVTLAKIH RHSGLIGPLK ENTIKKWFSQ HNHLKADYEK ALRNFFYSCA
GWCVVTFILG VCDRHNDNIM LTKSGHMFHI DFGKFLGHAQ TFGGIKRDRA PFIFTSEMEY
FITEGGKNPQ HFQDFVELCC RAYNIIRKHS QLLLNLLEMM LYAGLPELSG IQDLKYVYNN
LRPQDTDLEA TSHFTKKIKE SLECFPVKLN NLIHTLAQMS AISPAKSTSQ TFPQESCLLS
TTRSIERAIL GFSKKSSNLY LIQVTHSNNE TSLTEKSFEQ FSKLHSQLQK QFASLTLPEF
PHWWHLPFTN SDHRRFRDLN HYMEQILNVS HEVTNSDCVL SFFLSEAVQQ TVESSPVYLG
EKKFPDKKPK VQLVISYEDV KLTILVKHMK NIHLPDGSAP SAHVEFYLLP YPSEVLRRKT
KSVPKCTDPT YNEIVVYDEV TELQGHVLML IVKSKTVFVG AINIRLCSVP LDKEKWYPLG
NSIISPLL
//
ID PMVK_HUMAN STANDARD; PRT; 191 AA.
AC Q15126;
DT 15-JUL-1998 (Rel. 36, Created)
DT 15-DEC-1998 (Rel. 37, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE Phosphomevalonate kinase (EC 2.7.4.2) (PMKase).
GN PMVK OR PMKI.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RC TISSUE=Liver;
RX MEDLINE=96291886; PubMed=8663599;
RA Chambliss K.L., Slaughter C.A., Schreiner R., Hoffmann G.F.,
RA Gibson K.M.;
RT "Molecular cloning of human phosphomevalonate kinase and
RT identification of a consensus peroxisomal targeting sequence.";
RL J. Biol. Chem. 271:17330-17334(1996).
RN [2]
RP SEQUENCE FROM N.A.
RC TISSUE=Skin, and Uterus;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [3]
RP SEQUENCE OF 32-191 FROM N.A.
RX MEDLINE=99208737; PubMed=10191291;
RA Olivier L.M., Chambliss K.L., Gibson K.M., Krisans S.K.;
RT "Characterization of phosphomevalonate kinase: chromosomal
RT localization, regulation, and subcellular targeting.";
RL J. Lipid Res. 40:672-679(1999).
CC -!- CATALYTIC ACTIVITY: ATP + (R)-5-phosphomevalonate = ADP + (R)-5-
CC diphosphomevalonate.
CC -!- PATHWAY: Cholesterol biosynthesis.
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SUBCELLULAR LOCATION: Peroxisomal.
CC -!- TISSUE SPECIFICITY: Heart, liver, skeletal muscle, kidney, and
CC pancreas. Lower level in brain, placenta, and lung.
CC -!- INDUCTION: By sterol.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; L77213; AAC37593.1; -.
DR EMBL; BC006089; AAH06089.1; -.
DR EMBL; BC007694; AAH07694.1; -.
DR EMBL; AF026069; AAC60791.1; -.
DR Genew; HGNC:9141; PMVK.
DR MIM; 607622; -.
DR GO; GO:0005777; C:peroxisome; TAS.
DR GO; GO:0004631; F:phosphomevalonate kinase activity; TAS.
DR GO; GO:0006629; P:lipid metabolism; TAS.
DR GO; GO:0006468; P:protein amino acid phosphorylation; TAS.
DR InterPro; IPR005919; Pmev_kin_anim.
DR Pfam; PF04275; P-mevalo_kinase; 1.
DR TIGRFAMs; TIGR01223; Pmev_kin_anim; 1.
KW Transferase; Kinase; Sterol biosynthesis; Cholesterol biosynthesis;
KW Peroxisome.
FT INIT_MET 0 0 By similarity.
FT SITE 189 191 MICROBODY TARGETING SIGNAL (POTENTIAL).
SQ SEQUENCE 191 AA; 21864 MW; 282EB6D0723CC492 CRC64;
APLGGAPRLV LLFSGKRKSG KDFVTEALQS RLGADVCAVL RLSGPLKEQY AQEHGLNFQR
LLDTSTYKEA FRKDMIRWGE EKRQADPGFF CRKIVEGISQ PIWLVSDTRR VSDIQWFREA
YGAVTQTVRV VALEQSRQQR GWVFTPGVDD AESECGLDNF GDFDWVIENH GVEQRLEEQL
ENLIEFIRSR L
//
ID PNK1_HUMAN STANDARD; PRT; 598 AA.
AC Q8TE04; Q8TBQ8;
DT 28-FEB-2003 (Rel. 41, Created)
DT 28-FEB-2003 (Rel. 41, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Pantothenate kinase 1 (EC 2.7.1.33) (Pantothenic acid kinase 1)
DE (hPanK1) (hPanK).
GN PANK1 OR PANK.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A. (ISOFORM 3).
RC TISSUE=Fetal brain;
RX MEDLINE=21668246; PubMed=11809413;
RA Ni X., Ma Y., Cheng H., Jiang M., Ying K., Xie Y., Mao Y.;
RT "Cloning and characterization of a novel human pantothenate kinase
RT gene.";
RL Int. J. Biochem. Cell Biol. 34:109-115(2002).
RN [2]
RP SEQUENCE FROM N.A.
RA Heath P.;
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SEQUENCE OF 460-598 FROM N.A. (ISOFORM 2).
RC TISSUE=Skeletal muscle;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [4]
RP IDENTIFICATION OF ISOFORM 1.
RA Zhou B., Westaway S.K., Levinson B., Johnson M.A., Gitschier J.,
RA Hayflick S.J.;
RL Unpublished observations (JUL-2001).
CC -!- FUNCTION: Plays a role in the physiological regulation of the
CC intracellular CoA concentration (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + (R)-pantothenate = ADP + (R)-4'-
CC phosphopantothenate.
CC -!- ENZYME REGULATION: Regulated by feedback inhibition by CoA and its
CC thioesters. Strongly inhibited by acetyl-CoA and by manyl-CoA and
CC also inhibited by high concentration of non-esterified CoA (CoASH)
CC (By similarity).
CC -!- PATHWAY: Coenzyme A (CoA) biosynthesis; first step.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic (Probable).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=PanK1-alpha;
CC IsoId=Q8TE04-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TE04-2; Sequence=VSP_004520;
CC Name=3;
CC IsoId=Q8TE04-3; Sequence=VSP_004520, VSP_004521;
CC -!- TISSUE SPECIFICITY: Expressed in liver and kidney.
CC -!- DOMAIN: The N-terminal extension, present in isoform 1 may be the
CC regulatory domain.
CC -!- SIMILARITY: Belongs to the eukaryotic pantothenate kinase family.
CC -!- CAUTION: Isoform 2, although confirmed in the murine ortholog, is
CC only partially cloned and needs a further complete identification.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AF355198; AAL86371.1; -.
DR EMBL; AL157400; -; NOT_ANNOTATED_CDS.
DR EMBL; BC026296; AAH26296.1; ALT_INIT.
DR EMBL; BK000008; DAA00002.1; -.
DR Genew; HGNC:8598; PANK1.
DR MIM; 606160; -.
DR InterPro; IPR004567; PanK_eukar.
DR Pfam; PF03630; Fumble; 1.
KW Transferase; Kinase; ATP-binding; Coenzyme A biosynthesis;
KW Alternative splicing.
FT VARSPLIC 1 235 MLKLVGGGGGQDWACSVAGTSLGGEEAAFEVARPGDQGKAG
FT GGSPGWGCAGIPDSAPGAGVLQAGAVGPARGGQGAEEVGES
FT AGGGEERRVRHPQAPALRLLNRKPQGGSGEIKTPENDLQRG
FT RLSRGPRTAPPAPGMGDRSGQQERSVPHSPGAPVGTSAAAV
FT NGLLHNGFHPPPVQPPHVCSRGPVGGSDAAPQRLPLLPELQ
FT PQPLLPQHDSPAKKCRLRRRMDSGRKNRPP -> MKLINGK
FT KQT (in isoform 2 and isoform 3).
FT /FTId=VSP_004520.
FT VARSPLIC 438 496 Missing (in isoform 3).
FT /FTId=VSP_004521.
FT CONFLICT 306 306 N -> D (in Ref. 1).
SQ SEQUENCE 598 AA; 64339 MW; 0A92115D5BEDFC4C CRC64;
MLKLVGGGGG QDWACSVAGT SLGGEEAAFE VARPGDQGKA GGGSPGWGCA GIPDSAPGAG
VLQAGAVGPA RGGQGAEEVG ESAGGGEERR VRHPQAPALR LLNRKPQGGS GEIKTPENDL
QRGRLSRGPR TAPPAPGMGD RSGQQERSVP HSPGAPVGTS AAAVNGLLHN GFHPPPVQPP
HVCSRGPVGG SDAAPQRLPL LPELQPQPLL PQHDSPAKKC RLRRRMDSGR KNRPPFPWFG
MDIGGTLVKL VYFEPKDITA EEEQEEVENL KSIRKYLTSN TAYGKTGIRD VHLELKNLTM
CGRKGNLHFI RFPSCAMHRF IQMGSEKNFS SLHTTLCATG GGAFKFEEDF RMIADLQLHK
LDELDCLIQG LLYVDSVGFN GKPECYYFEN PTNPELCQKK PYCLDNPYPM LLVNMGSGVS
ILAVYSKDNY KRVTGTSLGG GTFLGLCCLL TGCETFEEAL EMAAKGDSTN VDKLVKDIYG
GDYERFGLQG SAVASSFGNM MSKEKRDSIS KEDLARATLV TITNNIGSIA RMCALNENID
RVVFVGNFLR INMVSMKLLA YAMDFWSKGQ LKALFLEHEG YFGAVGALLE LFKMTDDK
//
ID PNK2_HUMAN STANDARD; PRT; 570 AA.
AC Q9BZ23; Q8N7Q4; Q8TCR5; Q9BYW5; Q9HAF2;
DT 28-FEB-2003 (Rel. 41, Created)
DT 28-FEB-2003 (Rel. 41, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Pantothenate kinase 2, mitochondrial precursor (EC 2.7.1.33)
DE (Pantothenic acid kinase 2) (hPANK2).
GN PANK2 OR C20ORF48.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A. (ISOFORM 1), AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX MEDLINE=22442039; PubMed=12554685;
RA Hoertnagel K., Prokisch H., Meitinger T.;
RT "An isoform of hPANK2, deficient in pantothenate kinase-associated
RT neurodegeneration, localizes to mitochondria.";
RL Hum. Mol. Genet. 12:321-327(2003).
RN [2]
RP SEQUENCE FROM N.A.
RX MEDLINE=21638749; PubMed=11780052;
RA Deloukas P., Matthews L.H., Ashurst J., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
RP SEQUENCE FROM N.A. (ISOFORM 3), AND VARIANT GLY-126.
RC TISSUE=Testis;
RA Suzuki O., Sasaki N., Aotsuka S., Shoji T., Ichihara T., Shiohata N.,
RA Matsumoto K., Hirano M., Sano S., Nomura R., Yoshikawa Y.,
RA Matsumura Y., Moriya S., Chiba E., Momiyama H., Onogawa S.,
RA Kaeriyama S., Satoh N., Matsunawa H., Takahashi E., Kataoka R.,
RA Kuga N., Kuroda A., Satoh I., Kamata K., Takami S., Terashima Y.,
RA Watanabe M., Sugiyama T., Irie R., Otsuki T., Sato H., Wakamatsu A.,
RA Ishii S., Yamamoto J., Isono Y., Kawai-Hio Y., Saito K., Nishikawa T.,
RA Kimura K., Yamashita H., Matsuo K., Nakamura Y., Sekine M.,
RA Kikuchi H., Kanda K., Wagatsuma M., Murakawa K., Kanehori K.,
RA Takahashi-Fujii A., Oshima A., Sugiyama A., Kawakami B., Suzuki Y.,
RA Sugano S., Nagahari K., Masuho Y., Nagai K., Isogai T., Ota T.,
RA Hayashi K., Hara H., Tanase T., Nomura Y., Togiya S., Komai F.,
RA Hara R., Takeuchi K., Arita M., Nabekura T., Kawai Y.;
RT "NEDO human cDNA sequencing project.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SEQUENCE OF 406-570 FROM N.A.
RC TISSUE=Brain;
RA Koehrer K., Beyer A., Mewes H.-W., Weil B., Wiemann S.;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP DISEASE.
RX MEDLINE=22053542; PubMed=12058097;
RA Ching K.H.L., Westaway S.K., Gitschier J., Higgins J.J.,
RA Hayflick S.J.;
RT "HARP syndrome is allelic with pantothenate kinase-associated
RT neurodegeneration.";
RL Neurology 58:1673-1674(2002).
RN [6]
RP VARIANTS GLN-111 AND GLY-126, VARIANTS PKAN VAL-219; ALA-234; TRP-264;
RP CYS-278; VAL-282; CYS-286; ILE-327; PRO-351; SER-355; ILE-404;
RP PRO-413; ASN-471; THR-497; ILE-500; ARG-521 AND MET-528, AND TISSUE
RP SPECIFICITY.
RX MEDLINE=21372465; PubMed=11479594;
RA Zhou B., Westaway S.K., Levinson B., Johnson M.A., Gitschier J.,
RA Hayflick S.J.;
RT "A novel pantothenate kinase gene (PANK2) is defective in
RT Hallervorden-Spatz syndrome.";
RL Nat. Genet. 28:345-349(2001).
CC -!- FUNCTION: Maybe the master regulator of the CoA biosynthesis (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: ATP + (R)-pantothenate = ADP + (R)-4'-
CC phosphopantothenate.
CC -!- ENZYME REGULATION: Regulated by feedback inhibition by CoA and its
CC thioesters.
CC -!- PATHWAY: Coenzyme A (CoA) biosynthesis; first step.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic and mitochondrial.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BZ23-1; Sequence=Displayed;
CC Note=Mitochondrial isoform;
CC Name=3;
CC IsoId=Q9BZ23-2; Sequence=VSP_007424;
CC Event=Alternative initiation;
CC Comment=2 isoforms, 1 (shown here) and 2, are produced by
CC alternative initiation;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DISEASE: Defects in PANK2 are the cause of pantothenate kinase-
CC associated neurodegeneration (PKAN) [MIM:234200], formerly known
CC as Hallervorden-Spatz syndrome (HSS). PKAN is an autosomal
CC recessive neurodegenerative disorder associated with iron
CC accumulation in the brain. Clinical features include
CC extrapyramidal dysfunction, and a relentlessly progressive course.
CC Atypical PKAN is diagnosed in individuals who may not fit with the
CC diagnostic criteria of PKAN yet have radiographic or pathologic
CC evidence of increased basal ganglia iron.
CC -!- DISEASE: Defects in PANK2 are the cause of
CC hypoprebetalipoproteinemia, acanthocytosis, retinitis pigmentosa,
CC and pallidal degeneration (HARP) [MIM:607236]. HARP is a rare
CC syndrome with many clinical similarities to PKAN.
CC -!- MISCELLANEOUS: The HSS syndrome has been proposed to be renamed to
CC PKAN because of the unethical activities of Julius Hallervorden
CC and Hugo Spatz during World War II.
CC -!- SIMILARITY: Belongs to the eukaryotic pantothenate kinase family.
CC -!- CAUTION: Ref.2 sequence differs from that shown due to erroneous
CC gene model prediction.
CC -!- CAUTION: In addition to the presence of a second start site in
CC position 124, it is not excluded that the Leu-111 may
CC exceptionally also serve as an alternative initiation codon.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AF494409; AAN32907.1; -.
DR EMBL; AL353194; CAC15924.2; ALT_SEQ.
DR EMBL; AL031670; CAC32829.1; -.
DR EMBL; AK021791; BAB13897.1; -.
DR EMBL; AK097796; BAC05173.1; ALT_INIT.
DR EMBL; AL713654; CAD28463.1; -.
DR Genew; HGNC:15894; PANK2.
DR MIM; 606157; -.
DR MIM; 234200; -.
DR MIM; 607236; -.
DR InterPro; IPR004567; PanK_eukar.
DR Pfam; PF03630; Fumble; 1.
KW Transferase; Kinase; ATP-binding; Coenzyme A biosynthesis;
KW Alternative splicing; Alternative initiation; Transit peptide;
KW Disease mutation; Polymorphism.
FT TRANSIT 1 46 Mitochondrion (Potential).
FT CHAIN 47 570 PANTOTHENATE KINASE 2, ISOFORM 1.
FT CHAIN 124 570 PANTOTHENATE KINASE 2, ISOFORM 2.
FT INIT_MET 124 124 For isoform 2.
FT DOMAIN 236 243 POLY-GLU.
FT VARSPLIC 1 291 Missing (in isoform 3).
FT /FTId=VSP_007424.
FT VARIANT 111 111 L -> Q.
FT /FTId=VAR_015152.
FT VARIANT 126 126 A -> G.
FT /FTId=VAR_015153.
FT VARIANT 219 219 G -> V (in PKAN; atypical).
FT /FTId=VAR_015154.
FT VARIANT 234 234 T -> A (in PKAN; atypical).
FT /FTId=VAR_015155.
FT VARIANT 264 264 R -> W (in PKAN).
FT /FTId=VAR_015156.
FT VARIANT 278 278 R -> C (in PKAN; atypical).
FT /FTId=VAR_015157.
FT VARIANT 282 282 L -> V (in PKAN).
FT /FTId=VAR_015158.
FT VARIANT 286 286 R -> C (in PKAN).
FT /FTId=VAR_015159.
FT VARIANT 327 327 T -> I (in PKAN).
FT /FTId=VAR_015160.
FT VARIANT 351 351 S -> P (in PKAN; atypical).
FT /FTId=VAR_015161.
FT VARIANT 355 355 N -> S (in PKAN; atypical).
FT /FTId=VAR_015162.
FT VARIANT 404 404 N -> I (in PKAN; atypical).
FT /FTId=VAR_015163.
FT VARIANT 413 413 L -> P (in PKAN).
FT /FTId=VAR_015164.
FT VARIANT 471 471 S -> N (in PKAN).
FT /FTId=VAR_015165.
FT VARIANT 497 497 I -> T (in PKAN).
FT /FTId=VAR_015166.
FT VARIANT 500 500 N -> I (in PKAN).
FT /FTId=VAR_015167.
FT VARIANT 521 521 G -> R (in PKAN).
FT /FTId=VAR_015168.
FT VARIANT 528 528 T -> M (in PKAN).
FT /FTId=VAR_015169.
FT CONFLICT 210 210 L -> V (IN REF. 3; BAB13897).
FT CONFLICT 281 281 N -> K (IN REF. 3; BAB13897).
FT CONFLICT 460 460 R -> G (IN REF. 3; BAB13897).
FT CONFLICT 475 475 M -> K (IN REF. 3; BAB13897).
SQ SEQUENCE 570 AA; 62694 MW; CCDA845473349B5D CRC64;
MRRLGPFHPR VHWAAPPSLS SGLHRLLFLR GTRIPSSTTL SPPRHDSLSL DGGTVNPPRV
REPTGREAFG PSPASSDWLP ARWRNGRGGR PRARLCSGWT AAEEARRNPT LGGLLGRQRL
LLRMGAGRLG APMERHGRAS ATSVSSAGEQ AAGDPEGRRQ EPLRRRASSA SVPAVGASAE
GTRRDRLGSY SGPTSVSRQR VESLRKKRPL FPWFGLDIGG TLVKLVYFEP KDITAEEEEE
EVESLKSIRK YLTSNVAYGS TGIRDVHLEL KDLTLCGRKG NLHFIRFPTH DMPAFIQMGR
DKNFSSLHTV FCATGGGAYK FEQDFLTIGD LQLCKLDELD CLIKGILYID SVGFNGRSQC
YYFENPADSE KCQKLPFDLK NPYPLLLVNI GSGVSILAVY SKDNYKRVTG TSLGGGTFFG
LCCLLTGCTT FEEALEMASR GDSTKVDKLV RDIYGGDYER FGLPGWAVAS SFGNMMSKEK
REAVSKEDLA RATLITITNN IGSIARMCAL NENINQVVFV GNFLRINTIA MRLLAYALDY
WSKGQLKALF SEHEGYFGAV GALLELLKIP
//
ID PNK3_HUMAN STANDARD; PRT; 370 AA.
AC Q9H999;
DT 28-FEB-2003 (Rel. 41, Created)
DT 28-FEB-2003 (Rel. 41, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Pantothenate kinase 3 (EC 2.7.1.33) (Pantothenic acid kinase 3)
DE (hPanK3).
GN PANK3.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RA Isogai T., Ota T., Hayashi K., Sugiyama T., Otsuki T., Suzuki Y.,
RA Nishikawa T., Nagai K., Sugano S., Takahashi-Fujii A., Hara H.,
RA Tanase T., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Nabekura T., Ishii S., Kawai Y., Saito K., Yamamoto J.,
RA Wakamatsu A., Nakamura Y., Nagahari K., Masuho Y., Oshima A.;
RT "NEDO human cDNA sequencing project.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SEQUENCE FROM N.A.
RC TISSUE=Lymph;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [3]
RP TISSUE SPECIFICITY.
RX MEDLINE=21372465; PubMed=11479594;
RA Zhou B., Westaway S.K., Levinson B., Johnson M.A., Gitschier J.,
RA Hayflick S.J.;
RT "A novel pantothenate kinase gene (PANK2) is defective in
RT Hallervorden-Spatz syndrome.";
RL Nat. Genet. 28:345-349(2001).
CC -!- FUNCTION: Plays a role in the physiological regulation of the
CC intracellular CoA concentration (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + (R)-pantothenate = ADP + (R)-4'-
CC phosphopantothenate.
CC -!- ENZYME REGULATION: Regulated by feedback inhibition by CoA and its
CC thioesters (By similarity).
CC -!- PATHWAY: Coenzyme A (CoA) biosynthesis; first step.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic (Probable).
CC -!- TISSUE SPECIFICITY: Highly expressed in the liver.
CC -!- SIMILARITY: Belongs to the eukaryotic pantothenate kinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AK022961; BAB14333.1; -.
DR EMBL; BC013705; AAH13705.1; -.
DR Genew; HGNC:19365; PANK3.
DR MIM; 606161; -.
DR InterPro; IPR004567; PanK_eukar.
DR Pfam; PF03630; Fumble; 1.
KW Transferase; Kinase; ATP-binding; Coenzyme A biosynthesis.
SQ SEQUENCE 370 AA; 41094 MW; 71EEFA56079F352D CRC64;
MKIKDAKKPS FPWFGMDIGG TLVKLSYFEP IDITAEEEQE EVESLKSIRK YLTSNVAYGS
TGIRDVHLEL KDLTLFGRRG NLHFIRFPTQ DLPTFIQMGR DKNFSTLQTV LCATGGGAYK
FEKDFRTIGN LHLHKLDELD CLVKGLLYID SVSFNGQAEC YYFANASEPE RCQKMPFNLD
DPYPLLVVNI GSGVSILAVH SKDNYKRVTG TSLGGGTFLG LCSLLTGCES FEEALEMASK
GDSTQADKLV RDIYGGDYER FGLPGWAVAS SFGNMIYKEK RESVSKEDLA RATLVTITNN
IGSVARMCAV NEKINRVVFV GNFLRVNTLS MKLLAYALDY WSKGQLKALF LEHEGYFGAV
GALLGLPNFS
//
ID PNK4_HUMAN STANDARD; PRT; 773 AA.
AC Q9NVE7; Q9H3X5;
DT 28-FEB-2003 (Rel. 41, Created)
DT 28-FEB-2003 (Rel. 41, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Pantothenate kinase 4 (EC 2.7.1.33) (Pantothenic acid kinase 4)
DE (hPanK4).
GN PANK4.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RA Isogai T., Ota T., Hayashi K., Sugiyama T., Otsuki T., Suzuki Y.,
RA Nishikawa T., Nagai K., Sugano S., Aotsuka S., Yoshikawa Y.,
RA Matsunawa H., Ishii S., Kawai Y., Saito K., Yamamoto J., Wakamatsu A.,
RA Nakamura Y., Nagahari K., Masuho Y., Sasaki N.;
RT "NEDO human cDNA sequencing project.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SEQUENCE FROM N.A.
RC TISSUE=Brain;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [3]
RP SEQUENCE OF 6-773 FROM N.A.
RC TISSUE=Brain;
RA Wambutt R., Heubner D., Mewes H.-W., Weil B., Wiemann S.;
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP TISSUE SPECIFICITY.
RX MEDLINE=21372465; PubMed=11479594;
RA Zhou B., Westaway S.K., Levinson B., Johnson M.A., Gitschier J.,
RA Hayflick S.J.;
RT "A novel pantothenate kinase gene (PANK2) is defective in
RT Hallervorden-Spatz syndrome.";
RL Nat. Genet. 28:345-349(2001).
CC -!- FUNCTION: Plays a role in the physiological regulation of the
CC intracellular CoA concentration (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + (R)-pantothenate = ADP + (R)-4'-
CC phosphopantothenate.
CC -!- ENZYME REGULATION: Regulated by feedback inhibition by CoA and its
CC thioesters (By similarity).
CC -!- PATHWAY: Coenzyme A (CoA) biosynthesis; first step.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic (Probable).
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with higher expression
CC in the muscle.
CC -!- SIMILARITY: Belongs to the eukaryotic pantothenate kinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AK001644; BAA91805.1; -.
DR EMBL; BC043496; AAH43496.1; -.
DR EMBL; AL442072; CAC09438.1; -.
DR Genew; HGNC:19366; PANK4.
DR MIM; 606162; -.
DR InterPro; IPR002791; DUF89.
DR InterPro; IPR004567; PanK_eukar.
DR Pfam; PF01937; DUF89; 1.
DR Pfam; PF03630; Fumble; 1.
DR TIGRFAMs; TIGR00555; panK_eukar; 1.
KW Transferase; Kinase; ATP-binding; Coenzyme A biosynthesis;
KW Polymorphism.
FT VARIANT 684 684 Q -> R (in dbSNP:2494620).
FT /FTId=VAR_015170.
FT CONFLICT 547 547 A -> V (in Ref. 3).
SQ SEQUENCE 773 AA; 85990 MW; D55027171A85E8B6 CRC64;
MAECGASGSG SSGDSLDKSI TLPPDEIFRN LENAKRFAID IGGSLTKLAY YSTVQHKVAK
VRSFDHSGKD TEREHEPPYE ISVQEEITAR LHFIKFENTY IEACLDFIKD HLVNTETKVI
QATGGGAYKF KDLIEEKLRL KVDKEDVMTC LIKGCNFVLK NIPHEAFVYQ KDSDPEFRFQ
TNHPHIFPYL LVNIGSGVSI VKVETEDRFE WVGGSSIGGG TFWGLGALLT KTKKFDELLH
LASRGQHSNV DMLVRDVYGG AHQTLGLSGN LIASSFGKSA TADQEFSKED MAKSLLHMIS
NDIGQLACLH ARLHSLDRVY FGGFFIRGHP VTMRTITYSI NFFSKGEVQA LFLRHEGYLG
AIGAFLKGAE QDNPNQYSWG ENYAGSSGLM SASPELGPAQ RARSGTFDLL EMDRLERPLV
DLPLLLDPPS YVPDTVDLTD DALARKYWLT CFEEALDGVV KRAVASQPDS VDAAERAEKF
RQKYWNKLQT LRQQPFAYGT LTVRSLLDTR EHCLNEFNFP DPYSKVKQRE NGVALRCFPG
VVRSLDALGW EERQLALVKG LLAGNVFDWG AKAVSAVLES DPYFGFEEAK RKLQERPWLV
DSYSEWLQRL KGPPHKCALI FADNSGIDII LGVFPFVREL LLRGTEVILA CNSGPALNDV
THSESLIVAE RIAGMDPVVH SALQEERLLL VQTGSSSPCL DLSRLDKGLA ALVRERGADL
VVIEGMGRAV HTNYHAALRC ESLKLAVIKN AWLAERLGGR LFSVIFKYEV PAE
//
ID PPNK_HUMAN STANDARD; PRT; 446 AA.
AC O95544; Q9H931;
DT 30-MAY-2000 (Rel. 39, Created)
DT 30-MAY-2000 (Rel. 39, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE Putative inorganic polyphosphate/ATP-NAD kinase (EC 2.7.1.23)
DE (Poly(P)/ATP NAD kinase).
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RX MEDLINE=21478959; PubMed=11594753;
RA Lerner F., Niere M., Ludwig A., Ziegler M.;
RT "Structural and functional characterization of human NAD kinase.";
RL Biochem. Biophys. Res. Commun. 288:69-74(2001).
RN [2]
RP SEQUENCE FROM N.A.
RA Pearce A.;
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SEQUENCE FROM N.A.
RA Isogai T., Ota T., Hayashi K., Sugiyama T., Otsuki T., Suzuki Y.,
RA Nishikawa T., Nagai K., Sugano S., Shiratori A., Sudo H.,
RA Wagatsuma M., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Chiba Y., Ishida S., Murakawa K., Ono Y., Takiguchi S.,
RA Watanabe S., Kimura K., Murakami K., Ishii S., Kawai Y., Saito K.,
RA Yamamoto J., Wakamatsu A., Nakamura Y., Nagahari K., Masuho Y.,
RA Ninomiya K., Iwayanagi T.;
RT "NEDO human cDNA sequencing project.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SEQUENCE FROM N.A.
RC TISSUE=Lymph;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC -!- CATALYTIC ACTIVITY: ATP + NAD(+) = ADP + NADP(+).
CC -!- SIMILARITY: Belongs to the NAD kinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AY090771; AAM01195.1; -.
DR EMBL; AL031282; CAA20354.1; -.
DR EMBL; AK023114; BAB14412.1; -.
DR EMBL; BC001709; AAH01709.1; -.
DR GO; GO:0005829; C:cytosol; IEP.
DR GO; GO:0003951; F:NAD kinase activity; IDA.
DR GO; GO:0046034; P:ATP metabolism; NAS.
DR GO; GO:0016310; P:phosphorylation; NAS.
DR InterPro; IPR002504; ATP_NADK.
DR Pfam; PF01513; NAD_kinase; 1.
KW Hypothetical protein; Transferase; Kinase; NAD; NADP.
FT DOMAIN 326 333 POLY-ALA.
FT DOMAIN 437 445 POLY-GLU.
FT CONFLICT 262 262 N -> K (in Ref. 1 and 4).
FT CONFLICT 445 445 E -> EE (in Ref. 3).
SQ SEQUENCE 446 AA; 49228 MW; 48CE7AF05EDD7E8B CRC64;
MEMEQEKMTM NKELSPDAAA YCCSACHGDE TWSYNHPIRG RAKSRSLSAS PALGSTKEFR
RTRSLHGPCP VTTFGPKACV LQNPQTIMHI QDPASQRLTW NKSPKSVLVI KKMRDASLLQ
PFKELCTHLM EENMIVYVEK KVLEDPAIAS DESFGAVKKK FCTFREDYDD ISNQIDFIIC
LGGDGTLLYA SSLFQGSVPP VMAFHLGSLG FLTPFSFENF QSQVTQVIEG NAAVVLRSRL
KVRVVKELRG KKTAVHNGLG ENGSQAAGLD MDVGKQAMQY QVLNEVVIDR GPSSYLSNVD
VYLDGHLITT VQGDGVIVST PTGSTAYAAA AGASMIHPNV PAIMITPICP HSLSFRPIVV
PAGVELKIML SPEARNTAWV SFDGRKRQEI RHGDSISITT SCYPLPSICV RDPVSDWFES
LAQCLHWNVR KKQAHFEEEE EEEEEG
//
ID PPS1_HUMAN STANDARD; PRT; 624 AA.
AC O43252; O43841; O75332; Q96FB1; Q96TF4; Q9P1P9; Q9UE98;
DT 30-MAY-2000 (Rel. 39, Created)
DT 28-FEB-2003 (Rel. 41, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthethase 1 (PAPS
DE synthethase 1) (PAPSS 1) (Sulfurylase kinase 1) (SK1) (SK 1)
DE [Includes: Sulfate adenylyltransferase (EC 2.7.7.4) (Sulfate adenylate
DE transferase) (SAT) (ATP-sulfurylase); Adenylylsulfate kinase
DE (EC 2.7.1.25) (Adenylylsulfate 3'-phosphotransferase) (APS kinase)
DE (Adenosine-5'-phosphosulfate 3'-phosphotransferase) (3'-
DE phosphoadenosine-5'-phosphosulfate synthetase)].
GN PAPSS1 OR PAPSS OR ATPSK1.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RC TISSUE=Tonsil;
RX MEDLINE=98236023; PubMed=9576487;
RA Girard J.-P., Baekkevold E.S., Amalric F.;
RT "Sulfation in high endothelial venules: cloning and expression of the
RT human PAPS synthetase.";
RL FASEB J. 12:603-612(1998).
RN [2]
RP SEQUENCE FROM N.A., AND VARIANTS PHE-270 AND LEU-587.
RC TISSUE=Fetal brain;
RX MEDLINE=98334672; PubMed=9668121;
RA Venkatachalam K.V., Akita H., Strott C.A.;
RT "Molecular cloning, expression, and characterization of human
RT bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase and its
RT functional domains.";
RL J. Biol. Chem. 273:19311-19320(1998).
RN [3]
RP SEQUENCE FROM N.A.
RC TISSUE=Brain;
RX MEDLINE=98312048; PubMed=9648242;
RA Yanagisawa K., Sakakibara Y., Suiko M., Takami Y., Nakayama T.,
RA Nakajima H., Takayanagi K., Natori Y., Liu M.-C.;
RT "cDNA cloning, expression, and characterization of the human
RT bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase
RT enzyme.";
RL Biosci. Biotechnol. Biochem. 62:1037-1040(1998).
RN [4]
RP SEQUENCE FROM N.A., AND VARIANT LEU-587.
RA Deyrup A.T.;
RT "Human ATP sulfurylase/APS kinase.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SEQUENCE FROM N.A., AND VARIANT LEU-587.
RC TISSUE=Brain;
RX MEDLINE=20145452; PubMed=10679223;
RA Xu Z.-H., Otterness D.M., Freimuth R.R., Carlini E.J., Wood T.C.,
RA Mitchell S., Moon E., Kim U.-J., Xu J.-P., Siciliano M.J.,
RA Weinshilboum R.M.;
RT "Human 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 (PAPSS1) and
RT PAPSS2: gene cloning, characterization and chromosomal
RT localization.";
RL Biochem. Biophys. Res. Commun. 268:437-444(2000).
RN [6]
RP SEQUENCE FROM N.A.
RC TISSUE=Eye, and Uterus;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [7]
RP MUTAGENESIS OF HIS-425; ASN-426; GLY-427 AND HIS-428.
RX MEDLINE=99115594; PubMed=9915785;
RA Venkatachalam K.V., Fuda H., Koonin E.V., Strott C.A.;
RT "Site-selected mutagenesis of a conserved nucleotide binding HXGH
RT motif located in the ATP sulfurylase domain of human bifunctional
RT 3'-phosphoadenosine 5'-phosphosulfate synthase.";
RL J. Biol. Chem. 274:2601-2604(1999).
CC -!- FUNCTION: Bifunctional enzyme with both ATP sulfurylase and APS
CC kinase activity, which mediates two steps in the sulfate
CC activation pathway. The first step is the transfer of a sulfate
CC group to ATP to yield adenosine 5'-phosphosulfate (APS), and the
CC second step is the transfer of a phosphate group from ATP to APS
CC yielding 3'-phosphoadenylylsulfate (PAPS: activated sulfate donor
CC used by sulfotransferase). In mammals, PAPS is the sole source of
CC sulfate; APS appears to be only an intermediate in the sulfate-
CC activation pathway. Also involved in the biosynthesis of sulfated
CC L-selectin ligands in endothelial cells.
CC -!- CATALYTIC ACTIVITY: ATP + sulfate = diphosphate + adenylylsulfate.
CC -!- CATALYTIC ACTIVITY: ATP + adenylylsulfate = ADP + 3'-
CC phosphoadenylylsulfate.
CC -!- ENZYME REGULATION: Inhibited by chlorate.
CC -!- PATHWAY: Belongs to the sulfate assimilation pathway that leads to
CC the biosynthesis of cysteine and methionine, and to the sulfation
CC of proteins, carbohydrates, lipids, drugs and xenobiotics.
CC -!- TISSUE SPECIFICITY: Expressed in testis, pancreas, kidney, thymus,
CC prostate, ovary, small intestine, colon, leukocytes and liver.
CC Also expressed in high endothelial venules (HEV) cells and in
CC cartilage.
CC -!- SIMILARITY: In the N-terminal section; belongs to the APS kinase
CC family.
CC -!- SIMILARITY: In the C-terminal section; belongs to the sulfate
CC adenylyltransferase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; Y10387; CAA71413.1; -.
DR EMBL; U53447; AAC39894.1; -.
DR EMBL; AF033026; AAC28429.1; -.
DR EMBL; AF016496; AAD09325.1; -.
DR EMBL; AF105227; AAF40236.1; -.
DR EMBL; AF097721; AAF40235.1; -.
DR EMBL; AF097710; AAF40235.1; JOINED.
DR EMBL; AF097711; AAF40235.1; JOINED.
DR EMBL; AF097712; AAF40235.1; JOINED.
DR EMBL; AF097713; AAF40235.1; JOINED.
DR EMBL; AF097714; AAF40235.1; JOINED.
DR EMBL; AF097715; AAF40235.1; JOINED.
DR EMBL; AF097716; AAF40235.1; JOINED.
DR EMBL; AF097717; AAF40235.1; JOINED.
DR EMBL; AF097718; AAF40235.1; JOINED.
DR EMBL; AF097719; AAF40235.1; JOINED.
DR EMBL; AF097720; AAF40235.1; JOINED.
DR EMBL; BC011392; AAH11392.1; -.
DR EMBL; BC050627; AAH50627.1; -.
DR PIR; JW0087; JW0087.
DR Genew; HGNC:8603; PAPSS1.
DR MIM; 603262; -.
DR GO; GO:0001501; P:skeletal development; TAS.
DR InterPro; IPR002891; APS_kinase.
DR InterPro; IPR002650; ATP-sulfurylase.
DR Pfam; PF01583; APS_kinase; 1.
DR Pfam; PF01747; ATP-sulfurylase; 1.
DR ProDom; PD002350; APS_kinase; 1.
DR ProDom; PD002381; ATP-sulfurylase; 1.
DR TIGRFAMs; TIGR00455; apsK; 1.
KW Transferase; Nucleotidyltransferase; Kinase; Multifunctional enzyme;
KW ATP-binding; Multigene family; Polymorphism.
FT DOMAIN 1 ?220 ADENYLYLSULFATE KINASE.
FT DOMAIN ?221 624 SULFATE ADENYLYLTRANSFERASE.
FT NP_BIND 59 66 ATP (Potential).
FT ACT_SITE 133 133 PHOSPHOSERINE INTERMEDIATE
FT (BY SIMILARITY).
FT SITE 521 525 PP-MOTIF (BY SIMILARITY).
FT VARIANT 270 270 L -> F (in dbSNP:1127008).
FT /FTId=VAR_014065.
FT VARIANT 587 587 S -> L.
FT /FTId=VAR_014064.
FT MUTAGEN 425 425 H->A: LOSS OF ACTIVITY.
FT MUTAGEN 426 426 N->K: INCREASED ACTIVITY.
FT MUTAGEN 427 427 G->A: 30% DECREASE IN ACTIVITY.
FT MUTAGEN 428 428 H->A: LOSS OF ACTIVITY.
FT MUTAGEN 427 428 GH->AA: LOSS OF ACTIVITY.
FT CONFLICT 456 456 G -> A (in Ref. 1).
FT CONFLICT 456 456 Missing (in Ref. 2 and 3).
FT CONFLICT 519 520 IV -> MC (in Ref. 4).
SQ SEQUENCE 624 AA; 70833 MW; A3DC9B943E68CDD6 CRC64;
MEIPGSLCKK VKLSNNAQNW GMQRATNVTY QAHHVSRNKR GQVVGTRGGF RGCTVWLTGL
SGAGKTTVSM ALEEYLVCHG IPCYTLDGDN IRQGLNKNLG FSPEDREENV RRIAEVAKLF
ADAGLVCITS FISPYTQDRN NARQIHEGAS LPFFEVFVDA PLHVCEQRDV KGLYKKARAG
EIKGFTGIDS EYEKPEAPEL VLKTDSCDVN DCVQQVVELL QERDIVPVDA SYEVKELYVP
ENKLHLAKTD AETLPALKIN KVDMQWVQVL AEGWATPLNG FMREREYLQC LHFDCLLDGG
VINLSVPIVL TATHEDKERL DGCTAFALMY EGRRVAILRN PEFFEHRKEE RCARQWGTTC
KNHPYIKMVM EQGDWLIGGD LQVLDRVYWN DGLDQYRLTP TELKQKFKDM NADAVFAFQL
RNPVHNGHAL LMQDTHKQLL ERGYRRPVLL LHPLGGWTKD DDVPLMWRMK QHAAVLEEGV
LNPETTVVAI FPSPMMYAGP TEVQWHCRAR MVAGANFYIV GRDPAGMPHP ETGKDLYEPS
HGAKVLTMAP GLITLEIVPF RVAAYNKKKK RMDYYDSEHH EDFEFISGTR MRKLAREGQK
PPEGFMAPKA WTVLTEYYKS LEKA
//
ID PPS2_HUMAN STANDARD; PRT; 614 AA.
AC O95340; Q9BZL2; Q9P0G6; Q9UHM1; Q9UKD3; Q9UP30;
DT 30-MAY-2000 (Rel. 39, Created)
DT 28-FEB-2003 (Rel. 41, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthethase 2 (PAPS
DE synthethase 2) (PAPSS 2) (Sulfurylase kinase 2) (SK2) (SK 2)
DE [Includes: Sulfate adenylyltransferase (EC 2.7.7.4) (Sulfate adenylate
DE transferase) (SAT) (ATP-sulfurylase); Adenylylsulfate kinase
DE (EC 2.7.1.25) (Adenylylsulfate 3'-phosphotransferase) (APS kinase)
DE (Adenosine-5'-phosphosulfate 3'-phosphotransferase) (3'-
DE phosphoadenosine-5'-phosphosulfate synthetase)].
GN PAPSS2 OR ATPSK2.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A. (ISOFORM A).
RC TISSUE=Fetal cartilage;
RX MEDLINE=98442651; PubMed=9771708;
RA Ul Haque M.F., King L.M., Krakow D., Cantor R.M., Rusiniak M.E.,
RA Swank R.T., Superti-Furga A., Haque S., Abbas H., Ahmad W., Ahmad M.,
RA Cohn D.H.;
RT "Mutations in orthologous genes in human spondyloepimetaphyseal
RT dysplasia and the brachymorphic mouse.";
RL Nat. Genet. 20:157-162(1998).
RN [2]
RP SEQUENCE FROM N.A. (ISOFORM A).
RA Franzon V.L., Gibson M.A., Hatzinikolas G., Cleary E.G., Woolatt E.,
RA Sutherland G.R.;
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SEQUENCE FROM N.A. (ISOFORM A).
RA Fuda H., Shimizu C., Strott C.A.;
RT "Human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase:
RT differential expression of isoforms and effect of polymorphisms on
RT activity.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SEQUENCE FROM N.A. (ISOFORM A).
RX MEDLINE=20145452; PubMed=10679223;
RA Xu Z.-H., Otterness D.M., Freimuth R.R., Carlini E.J., Wood T.C.,
RA Mitchell S., Moon E., Kim U.-J., Xu J.-P., Siciliano M.J.,
RA Weinshilboum R.M.;
RT "Human 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 (PAPSS1) and
RT PAPSS2: gene cloning, characterization and chromosomal localization.";
RL Biochem. Biophys. Res. Commun. 268:437-444(2000).
RN [5]
RP SEQUENCE FROM N.A. (ISOFORM B).
RC TISSUE=Liver;
RX MEDLINE=20026854; PubMed=10559207;
RA Kurima K., Singh B., Schwartz N.B.;
RT "Genomic organization of the mouse and human genes encoding the ATP
RT sulfurylase/adenosine 5'-phosphosulfate kinase isoform SK2.";
RL J. Biol. Chem. 274:33306-33312(1999).
RN [6]
RP SEQUENCE FROM N.A. (ISOFORM B).
RA Venkatachalam K.V., Fuda H., Strott C.A.;
RT "3'-phosphoadenosine 5'-phosphosulfate synthase 2b isoform.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP SEQUENCE FROM N.A. (ISOFORM A).
RC TISSUE=Colon;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [8]
RP INVOLVEMENT IN SEMD.
RX MEDLINE=98377817; PubMed=9714015;
RA Ahmad M., Haque M.F., Ahmad W., Abbas H., Haque S., Krakow D.,
RA Rimoin D.L., Lachman R.S., Cohn D.H.;
RT "Distinct, autosomal recessive form of spondyloepimetaphyseal
RT dysplasia segregating in an inbred Pakistani kindred.";
RL Am. J. Med. Genet. 78:468-473(1998).
CC -!- FUNCTION: Bifunctional enzyme with both ATP sulfurylase and APS
CC kinase activity, which mediates two steps in the sulfate
CC activation pathway. The first step is the transfer of a sulfate
CC group to ATP to yield adenosine 5'-phosphosulfate (APS), and the
CC second step is the transfer of a phosphate group from ATP to APS
CC yielding 3'-phosphoadenylylsulfate (PAPS: activated sulfate donor
CC used by sulfotransferase). In mammals, PAPS is the sole source of
CC sulfate; APS appears to be only an intermediate in the sulfate-
CC activation pathway. May have a important role in skeletogenesis
CC during postnatal growth (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + sulfate = diphosphate + adenylylsulfate.
CC -!- CATALYTIC ACTIVITY: ATP + adenylylsulfate = ADP + 3'-
CC phosphoadenylylsulfate.
CC -!- PATHWAY: Belongs to the sulfate assimilation pathway that leads to
CC the biosynthesis of cysteine and methionine, and to the sulfation
CC of proteins, carbohydrates, lipids, drugs and xenobiotics.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=O95340-1; Sequence=Displayed;
CC Name=B;
CC IsoId=O95340-2; Sequence=VSP_001259;
CC -!- TISSUE SPECIFICITY: Expressed in cartilage.
CC -!- DISEASE: Defects in PAPSS2 are the cause of spondyloepimetaphyseal
CC dysplasia pakistani type (SEMD) [MIM:603005]. This autosomal
CC recessive form of SEMD is characterized by a dysplasia that is
CC primarily epiphyseal with only mild metaphyseal abnormalities,
CC leading to short, bowed lower limbs, enlarged knee joints,
CC kyphoscoliosis and a mild generalized brachydactyly.
CC -!- SIMILARITY: In the N-terminal section; belongs to the APS kinase
CC family.
CC -!- SIMILARITY: In the C-terminal section; belongs to the sulfate
CC adenylyltransferase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AF091242; AAC64583.1; -.
DR EMBL; AF074331; AAD38423.1; -.
DR EMBL; AF313907; AAK00296.1; -.
DR EMBL; AF160509; AAF40307.2; -.
DR EMBL; AF160503; AAF40307.2; JOINED.
DR EMBL; AF160504; AAF40307.2; JOINED.
DR EMBL; AF160505; AAF40307.2; JOINED.
DR EMBL; AF160506; AAF40307.2; JOINED.
DR EMBL; AF160507; AAF40307.2; JOINED.
DR EMBL; AF160508; AAF40307.2; JOINED.
DR EMBL; AF173365; AAF12761.1; -.
DR EMBL; AF150754; AAF20366.2; -.
DR EMBL; BC009894; AAH09894.1; -.
DR Genew; HGNC:8604; PAPSS2.
DR MIM; 603005; -.
DR GO; GO:0001501; P:skeletal development; TAS.
DR InterPro; IPR002891; APS_kinase.
DR InterPro; IPR002650; ATP-sulfurylase.
DR Pfam; PF01583; APS_kinase; 1.
DR Pfam; PF01747; ATP-sulfurylase; 1.
DR ProDom; PD002350; APS_kinase; 1.
DR ProDom; PD002381; ATP-sulfurylase; 1.
DR TIGRFAMs; TIGR00455; apsK; 1.
KW Transferase; Nucleotidyltransferase; Kinase; Multifunctional enzyme;
KW ATP-binding; Multigene family; Alternative splicing.
FT DOMAIN 1 ?210 ADENYLYLSULFATE KINASE.
FT DOMAIN ?211 614 SULFATE ADENYLYLTRANSFERASE.
FT NP_BIND 49 56 ATP (Potential).
FT ACT_SITE 123 123 PHOSPHOSERINE INTERMEDIATE
FT (BY SIMILARITY).
FT SITE 511 515 PP-MOTIF (BY SIMILARITY).
FT VARSPLIC 288 288 D -> DGMALP (in isoform B).
FT /FTId=VSP_001259.
FT CONFLICT 166 166 R -> K (in Ref. 2).
FT CONFLICT 361 361 E -> G (in Ref. 3).
FT CONFLICT 426 426 R -> C (in Ref. 1).
FT CONFLICT 567 567 P -> L (in Ref. 2).
SQ SEQUENCE 614 AA; 69500 MW; 52F4B6D972DDA91E CRC64;
MSGIKKQKTE NQQKSTNVVY QAHHVSRNKR GQVVGTRGGF RGCTVWLTGL SGAGKTTISF
ALEEYLVSHA IPCYSLDGDN VRHGLNRNLG FSPGDREENI RRIAEVAKLF ADAGLVCITS
FISPFAKDRE NARKIHESAG LPFFEIFVDA PLNICESRDV KGLYKRARAG EIKGFTGIDS
DYEKPETPER VLKTNLSTVS DCVHQVVELL QEQNIVPYTI IKDIHELFVP ENKLDHVRAE
AETLPSLSIT KLDLQWVQVL SEGWATPLKG FMREKEYLQV MHFDTLLDDG VINMSIPIVL
PVSAEDKTRL EGCSKFVLAH GGRRVAILRD AEFYEHRKEE RCSRVWGTTC TKHPHIKMVM
ESGDWLVGGD LQVLEKIRWN DGLDQYRLTP LELKQKCKEM NADAVFAFQL RNPVHNGHAL
LMQDTRRRLL ERGYKHPVLL LHPLGGWTKD DDVPLDWRMK QHAAVLEEGV LDPKSTIVAI
FPSPMLYAGP TEVQWHCRSR MIAGANFYIV GRDPAGMPHP ETKKDLYEPT HGGKVLSMAP
GLTSVEIIPF RVAAYNKAKK AMDFYDPARH NEFDFISGTR MRKLAREGEN PPDGFMAPKA
WKVLTDYYRS LEKN
//
ID RBSK_HUMAN STANDARD; PRT; 322 AA.
AC Q9H477;
DT 28-FEB-2003 (Rel. 41, Created)
DT 28-FEB-2003 (Rel. 41, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE Ribokinase (EC 2.7.1.15).
GN RBSK.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RA Wightman P.J.;
RL Thesis (2000), University of Edinburgh, U.K.
RN [2]
RP SEQUENCE FROM N.A.
RC TISSUE=Lung;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC -!- CATALYTIC ACTIVITY: ATP + D-ribose = ADP + D-ribose 5-phosphate.
CC -!- PATHWAY: Ribose metabolism; first step.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase pfkB family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AJ404857; CAC12877.1; -.
DR EMBL; BC017425; AAH17425.1; -.
DR HSSP; P05054; 1RK2.
DR InterPro; IPR002173; PfkB.
DR InterPro; IPR002139; Ribokinase.
DR Pfam; PF00294; pfkB; 1.
DR PRINTS; PR00990; RIBOKINASE.
DR PROSITE; PS00583; PFKB_KINASES_1; FALSE_NEG.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
KW Transferase; Kinase.
SQ SEQUENCE 322 AA; 34143 MW; 50D0E7161F33E94B CRC64;
MAASGEPQRQ WQEEVAAVVV VGSCMTDLVS LTSRLPKTGE TIHGHKFFIG FGGKGANQCV
QAARLGAMTS MVCKVGKDSF GNDYIENLKQ NDISTEFTYQ TKDAATGTAS IIVNNEGQNI
IVIVAGANLL LNTEDLRAAA NVISRAKVMV CQLEITPATS LEALTMARRS GVKTLFNPAP
AIADLDPQFY TLSDVFCCNE SEAEILTGLT VGSAADAGEA ALVLLKRGCQ VVIITLGAEG
CVVLSQTEPE PKHIPTEKVK AVDTTGAGDS FVGALAFYLA YYPNLSLEDM LNRSNFIAAV
SVQAAGTQSS YPYKKDLPLT LF
//
ID RIFK_HUMAN STANDARD; PRT; 162 AA.
AC Q969G6; Q9NUT7;
DT 10-OCT-2003 (Rel. 42, Created)
DT 10-OCT-2003 (Rel. 42, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE Riboflavin kinase (EC 2.7.1.26) (ATP:riboflavin 5'-phosphotransferase)
DE (Flavokinase).
GN RFK.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RC TISSUE=Placenta;
RA Isogai T., Ota T., Hayashi K., Sugiyama T., Otsuki T., Suzuki Y.,
RA Nishikawa T., Nagai K., Sugano S., Ishibashi T., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Ishii S., Kawai Y.,
RA Saito K., Yamamoto J., Wakamatsu A., Nakamura Y., Nagahari K.,
RA Masuho Y., Kanehori K.;
RT "NEDO human cDNA sequencing project.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SEQUENCE FROM N.A.
RC TISSUE=Urinary bladder;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 9-155 IN COMPLEX WITH MG-ADP
RP AND RIBOFLAVIN NUCLEOTIDE.
RX MEDLINE=22511990; PubMed=12623014;
RA Karthikeyan S., Zhou Q., Mseeh F., Grishin N.V., Osterman A.L.,
RA Zhang H.;
RT "Crystal structure of human riboflavin kinase reveals a beta barrel
RT fold and a novel active site arch.";
RL Structure 11:265-273(2003).
CC -!- FUNCTION: Catalyzes the phosphorylation of riboflavin (vitamin B2)
CC to form flavin-mononucleotide (FMN).
CC -!- CATALYTIC ACTIVITY: ATP + riboflavin = ADP + FMN.
CC -!- COFACTOR: Needs Zn(2+) or Mg(2+) for activity.
CC -!- PATHWAY: FMN biosynthesis; last step.
CC -!- PATHWAY: FAD biosynthesis.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic (By similarity).
CC -!- TISSUE SPECIFICITY: Detected in brain, placenta and urinary
CC bladder.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AK002011; BAA92033.1; -.
DR EMBL; BC007069; AAH07069.1; -.
DR PDB; 1NB9; 11-MAR-03.
DR InterPro; IPR002606; FAD_Synth.
DR Pfam; PF01687; FAD_Synth; 1.
DR ProDom; PD003662; FAD_Synth; 1.
KW Transferase; Kinase; FMN; Metal-binding; Magnesium; Zinc;
KW 3D-structure.
FT BINDING 22 22 ADP (VIA AMIDE NITROGEN).
FT BINDING 28 28 ADP (VIA AMIDE NITROGEN).
FT BINDING 34 34 ADP (VIA AMIDE NITROGEN).
FT METAL 34 34 MAGNESIUM.
FT BINDING 36 36 ADP.
FT BINDING 89 89 ADP (VIA AMIDE NITROGEN AND CARBONYL
FT OXYGEN).
FT BINDING 91 91 ADP (VIA CARBONYL OXYGEN).
FT BINDING 98 98 ADP.
FT BINDING 111 111 FMN (NON COVALENT).
FT BINDING 114 114 FMN (NON COVALENT) (VIA AMIDE NITROGEN
FT AND CARBONYL OXYGEN).
FT BINDING 116 116 FMN (NON COVALENT) (VIA AMIDE NITROGEN).
FT CONFLICT 103 103 N -> S (in Ref. 1).
SQ SEQUENCE 162 AA; 18410 MW; E80042E7E5C38ACD CRC64;
MPRADCIMRH LPYFCRGQVV RGFGRGSKQL GIPTANFPEQ VVDNLPADIS TGIYYGWASV
GSGDVHKMVV SIGWNPYYKN TKKSMETHIM HTFKEDFYGE ILNVAIVGYL RPEKNFDSLE
SLISAIQGDI EEAKKRLELP EHLKIKEDNF FQVSKSKIMN GH
//
ID SPH1_HUMAN STANDARD; PRT; 384 AA.
AC Q9NYA1; Q9HD92; Q9NY70; Q9NYL3;
DT 28-FEB-2003 (Rel. 41, Created)
DT 28-FEB-2003 (Rel. 41, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE Sphingosine kinase 1 (EC 2.7.1.-) (SK 1) (SPK 1).
GN SPHK1 OR SPHK OR SPK.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RX MEDLINE=20323213; PubMed=10863092;
RA Melendez A.J., Carlos-Dias E., Gosink M., Allen J.M., Takacs L.;
RT "Human sphingosine kinase: molecular cloning, functional
RT characterization and tissue distribution.";
RL Gene 251:19-26(2000).
RN [2]
RP SEQUENCE FROM N.A., AND CHARACTERIZATION.
RX MEDLINE=20263733; PubMed=10802064;
RA Nava V.E., Lacana' E., Poulton S., Liu H., Sugiura M., Kono K.,
RA Milstien S., Kohama T., Spiegel S.;
RT "Functional characterization of human sphingosine kinase-1.";
RL FEBS Lett. 473:81-84(2000).
RN [3]
RP SEQUENCE FROM N.A., AND CHARACTERIZATION.
RX MEDLINE=20407120; PubMed=10947957;
RA Pitson S.M., D'Andrea R.J., Vandeleur L., Moretti P.A.B., Xia P.,
RA Gamble J.R., Vadas M.A., Wattenberg B.W.;
RT "Human sphingosine kinase: purification, molecular cloning and
RT characterization of the native and recombinant enzymes.";
RL Biochem. J. 350:429-441(2000).
RN [4]
RP SEQUENCE FROM N.A.
RA Van Veldhoven P.P., Gijsbers S.;
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SEQUENCE FROM N.A.
RC TISSUE=Mammary gland, and Ovary;
RA Isogai T., Ota T., Hayashi K., Sugiyama T., Otsuki T., Suzuki Y.,
RA Nishikawa T., Nagai K., Sugano S., Shiratori A., Sudo H.,
RA Wagatsuma M., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Chiba Y., Ishida S., Murakawa K., Ono Y., Takiguchi S.,
RA Watanabe S., Kimura K., Murakami K., Ishii S., Kawai Y., Saito K.,
RA Yamamoto J., Wakamatsu A., Nakamura Y., Nagahari K., Masuho Y.,
RA Ninomiya K., Iwayanagi T.;
RT "NEDO human cDNA sequencing project.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phosphorylation of sphingosine to form
CC sphingosine 1-phosphate (SPP), a lipid mediator with both intra-
CC and extracellular functions. Also acts on D-erythro-sphingosine
CC and to a lesser extent sphinganine, but not other lipids, such as
CC D,L-threo-dihydrosphingosine, N,N-dimethylsphingosine,
CC diacylglycerol, ceramide, or phosphatidylinositol.
CC -!- CATALYTIC ACTIVITY: Sphingosine + ATP = sphingosine 1-phosphate +
CC ADP.
CC -!- SUBUNIT: Binds to calmodulin.
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in adult
CC liver, kidney, heart and skeletal muscle.
CC -!- SIMILARITY: Contains 1 DAGKc domain.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AF266756; AAF73470.1; -.
DR EMBL; AF238083; AAF73423.1; -.
DR EMBL; AF200328; AAG01980.1; -.
DR EMBL; AK023393; BAB14558.1; -.
DR EMBL; AK022402; BAB14028.1; -.
DR EMBL; AJ245504; CAB92131.1; -.
DR Genew; HGNC:11240; SPHK1.
DR MIM; 603730; -.
DR GO; GO:0005829; C:cytosol; TAS.
DR GO; GO:0005624; C:membrane fraction; TAS.
DR GO; GO:0005524; F:ATP binding; IDA.
DR GO; GO:0005516; F:calmodulin binding; IDA.
DR GO; GO:0017050; F:D-erythro-sphingosine kinase activity; IDA.
DR GO; GO:0000287; F:magnesium ion binding; IDA.
DR GO; GO:0006916; P:anti-apoptosis; TAS.
DR GO; GO:0019722; P:calcium-mediated signaling; IDA.
DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; TAS.
DR GO; GO:0007242; P:intracellular signaling cascade; TAS.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IDA.
DR GO; GO:0030307; P:positive regulation of cell growth; IDA.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; IDA.
DR GO; GO:0045987; P:positive regulation of smooth muscle contra...; IDA.
DR GO; GO:0046521; P:sphingoid catabolism; NAS.
DR InterPro; IPR001206; DAGKc.
DR Pfam; PF00781; DAGKc; 1.
DR ProDom; PD005043; DAGKc; 1.
DR SMART; SM00046; DAGKc; 1.
KW Transferase; Kinase; ATP-binding; Calmodulin-binding.
FT CONFLICT 6 6 Missing (in Ref. 4).
FT CONFLICT 11 15 LPRPC -> ARL (in Ref. 4).
FT CONFLICT 114 115 NA -> KP (in Ref. 4).
FT CONFLICT 251 251 V -> M (in Ref. 2).
FT CONFLICT 260 260 V -> I (in Ref. 2).
FT CONFLICT 302 302 L -> F (in Ref. 2).
FT CONFLICT 325 325 V -> G (in Ref. 4).
FT CONFLICT 337 337 V -> M (in Ref. 3).
SQ SEQUENCE 384 AA; 42517 MW; EB04A7F2034C2DB0 CRC64;
MDPAGGPRGV LPRPCRVLVL LNPRGGKGKA LQLFRSHVQP LLAEAEISFT LMLTERRNHA
RELVRSEELG RWDALVVMSG DGLMHEVVNG LMERPDWETA IQKPLCSLPA GSGNALAASL
NHYAGYEQVT NEDLLTNCTL LLCRRLLSPM NLLSLHTASG LRLFSVLSLA WGFIADVDLE
SEKYRRLGEM RFTLGTFLRL AALRTYRGRL AYLPVGRVGS KTPASPVVVQ QGPVDAHLVP
LEEPVPSHWT VVPDEDFVLV LALLHSHLGS EMFAAPMGRC AAGVMHLFYV RAGVSRAMLL
RLFLAMEKGR HMEYECPYLV YVPVVAFRLE PKDGKGVFAV DGELMVSEAV QGQVHPNYFW
MVSGCVEPPP SWKPQQMPPP EEPL
//
ID SPH2_HUMAN STANDARD; PRT; 654 AA.
AC Q9NRA0; Q9BRN1; Q9H0Q2; Q9NWU7;
DT 28-FEB-2003 (Rel. 41, Created)
DT 28-FEB-2003 (Rel. 41, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE Sphingosine kinase 2 (EC 2.7.1.-) (SK 2) (SPK 2).
GN SPHK2.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A. (ISOFORM 2), AND CHARACTERIZATION.
RX MEDLINE=20347850; PubMed=10751414;
RA Liu H., Sugiura M., Nava V.E., Edsall L.C., Kono K., Poulton S.,
RA Milstien S., Kohama T., Spiegel S.;
RT "Molecular cloning and functional characterization of a novel
RT mammalian sphingosine kinase type 2 isoform.";
RL J. Biol. Chem. 275:19513-19520(2000).
RN [2]
RP SEQUENCE FROM N.A. (ISOFORM 2).
RC TISSUE=Brain;
RX MEDLINE=21154917; PubMed=11230166;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 2).
RC TISSUE=Eye, and Lymph;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [4]
RP SEQUENCE OF 1-354 FROM N.A. (ISOFORM 3).
RC TISSUE=Carcinoma;
RA Watanabe K., Kumagai A., Itakura S., Yamazaki M., Tashiro H., Ota T.,
RA Suzuki Y., Obayashi M., Nishi T., Shibahara T., Tanaka T.,
RA Nakamura Y., Isogai T., Sugano S.;
RT "NEDO human cDNA sequencing project.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phosphorylation of sphingosine to form
CC sphingosine 1-phosphate (SPP), a lipid mediator with both intra-
CC and extracellular functions. Also acts on D-erythro-
CC dihydrosphingosine, D-erythro-sphingosine and L-threo-
CC dihydrosphingosine.
CC -!- CATALYTIC ACTIVITY: Sphingosine + ATP = sphingosine 1-phosphate +
CC ADP.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Experimental confirmation may be lacking for some
CC isoforms;
CC Name=1;
CC IsoId=Q9NRA0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NRA0-2; Sequence=VSP_006217;
CC Name=3;
CC IsoId=Q9NRA0-3; Sequence=VSP_006217, VSP_006218;
CC -!- SIMILARITY: Contains 1 DAGKc domain.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AF245447; AAF74124.1; -.
DR EMBL; AL136701; CAB66636.1; -.
DR EMBL; BC006161; AAH06161.1; -.
DR EMBL; BC010671; AAH10671.1; -.
DR EMBL; AK000599; BAA91280.1; -.
DR Genew; HGNC:18859; SPHK2.
DR MIM; 607092; -.
DR GO; GO:0005829; C:cytosol; IEP.
DR GO; GO:0005624; C:membrane fraction; IEP.
DR GO; GO:0008189; F:apoptosis inhibitor activity; NAS.
DR GO; GO:0005515; F:protein binding; IPI.
DR GO; GO:0017016; F:Ras interactor activity; NAS.
DR GO; GO:0008481; F:sphinganine kinase activity; NAS.
DR GO; GO:0006916; P:anti-apoptosis; NAS.
DR GO; GO:0008283; P:cell proliferation; NAS.
DR GO; GO:0006669; P:sphinganine-1-phosphate biosynthesis; NAS.
DR InterPro; IPR001206; DAGKc.
DR InterPro; IPR007110; Ig-like.
DR Pfam; PF00781; DAGKc; 1.
DR ProDom; PD005043; DAGKc; 1.
DR SMART; SM00046; DAGKc; 1.
KW Transferase; Kinase; ATP-binding; Alternative splicing.
FT VARSPLIC 1 36 Missing (in isoform 2 and isoform 3).
FT /FTId=VSP_006217.
FT VARSPLIC 292 390 FEPALGLDLLLNCSLLLCRGGGHPLDLLSVTLASGSRCFSF
FT LSVAWGFVSDVDIQSERFRALGSARFTLGTVLGLATLHTYR
FT GRLSYLPATVEPASPTP -> PREDSDSSTSSSACPLWTTA
FT RSCPRAAASMPGSCPLLPQQLALGFSRFIQDRVNGGGGRIG
FT SLTCRGHTQRTLPAPAREGGGSLFLKNINVFICKKKKK
FT (in isoform 3).
FT /FTId=VSP_006218.
FT CONFLICT 49 49 P -> S (in Ref. 2).
SQ SEQUENCE 654 AA; 69217 MW; F73FFCEC930DA50F CRC64;
MNGHLEAEEQ QDQRPDQELT GSWGHGPRST LVRAKAMAPP PPPLAASTPL LHGEFGSYPA
RGPRFALTLT SQALHIQRLR PKPEARPRGG LVPLAEVSGC CTLRSRSPSD SAAYFCIYTY
PRGRRGARRR ATRTFRADGA ATYEENRAEA QRWATALTCL LRGLPLPGDG EITPDLLPRP
PRLLLLVNPF GGRGLAWQWC KNHVLPMISE AGLSFNLIQT ERQNHARELV QGLSLSEWDG
IVTVSGDGLL HEVLNGLLDR PDWEEAVKMP VGILPCGSGN ALAGAVNQHG GFEPALGLDL
LLNCSLLLCR GGGHPLDLLS VTLASGSRCF SFLSVAWGFV SDVDIQSERF RALGSARFTL
GTVLGLATLH TYRGRLSYLP ATVEPASPTP AHSLPRAKSE LTLTPDPAPP MAHSPLHRSV
SDLPLPLPQP ALASPGSPEP LPILSLNGGG PELAGDWGGA GDAPLSPDPL LSSPPGSPKA
ALHSPVSEGA PVIPPSSGLP LPTPDARVGA STCGPPDHLL PPLGTPLPPD WVTLEGDFVL
MLAISPSHLG ADLVAAPHAR FDDGLVHLCW VRSGISRAAL LRLFLAMERG SHFSLGCPQL
GYAAARAFRL EPLTPRGVLT VDGEQVEYGP LQAQMHPGIG TLLTGPPGCP GREP
//
ID UCK1_HUMAN STANDARD; PRT; 277 AA.
AC Q9HA47;
DT 28-FEB-2003 (Rel. 41, Created)
DT 28-FEB-2003 (Rel. 41, Last sequence update)
DT 28-FEB-2003 (Rel. 41, Last annotation update)
DE Uridine-cytidine kinase 1 (EC 2.7.1.48) (UCK 1) (Uridine
DE monophosphokinase 1) (Cytidine monophosphokinase 1).
GN UCK1.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A., AND CHARACTERIZATION.
RX MEDLINE=21203813; PubMed=11306702;
RA Van Rompay A.R., Norda A., Linden K., Johansson M., Karlsson A.;
RT "Phosphorylation of uridine and cytidine nucleoside analogs by two
RT human uridine-cytidine kinases.";
RL Mol. Pharmacol. 59:1181-1186(2001).
RN [2]
RP SEQUENCE FROM N.A.
RA Ho Y.S., Johnson R.K.;
RT "Human uridine kinase from prostate cancer cell line (LNCap).";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SEQUENCE FROM N.A.
RC TISSUE=Mammary gland;
RA Isogai T., Ota T., Hayashi K., Sugiyama T., Otsuki T., Suzuki Y.,
RA Nishikawa T., Nagai K., Sugano S., Shiratori A., Sudo H.,
RA Wagatsuma M., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Chiba Y., Ishida S., Murakawa K., Ono Y., Takiguchi S.,
RA Watanabe S., Kimura K., Murakami K., Ishii S., Kawai Y., Saito K.,
RA Yamamoto J., Wakamatsu A., Nakamura Y., Nagahari K., Masuho Y.,
RA Ninomiya K., Iwayanagi T.;
RT "NEDO human cDNA sequencing project.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SEQUENCE FROM N.A.
RA Xin Y.R., Yu L., Zhao S.Y.;
RT "Cloning of a new human cDNA similar to Mus musculus uridine kinase
RT mRNA.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phosphorylates uridine and cytidine to uridine
CC monophosphate and cytidine monophosphate. Does not phosphorylate
CC deoxyribonucleosides or purine ribonucleosides. Can use ATP or GTP
CC as a phosphate donor. Can also phosphorylate cytidine and uridine
CC nucleoside analogs such as 6-azauridine, 5-fluorouridine, 4-
CC thiouridine, 5-bromouridine, N(4)-acetylcytidine, N(4)-
CC benzoylcytidine, 5-fluorocytidine, 2-thiocytidine, 5-
CC methylcytidine, and N(4)-anisoylcytidine.
CC -!- CATALYTIC ACTIVITY: ATP + uridine = ADP + UMP.
CC -!- CATALYTIC ACTIVITY: ATP + cytidine = ADP + CMP.
CC -!- PATHWAY: Pyrimidine salvage pathway.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the uridine kinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AF237290; AAK28324.1; -.
DR EMBL; AF254133; AAK49122.1; -.
DR EMBL; AK022317; BAB14010.1; -.
DR EMBL; AF125106; AAL75943.1; -.
DR GK; Q9HA47; -.
DR InterPro; IPR006083; PRK_URK.
DR InterPro; IPR000764; Uridine_kin.
DR Pfam; PF00485; PRK; 1.
DR PRINTS; PR00988; URIDINKINASE.
DR TIGRFAMs; TIGR00235; udk; 1.
KW Transferase; Kinase; ATP-binding.
FT NP_BIND 30 37 ATP (Potential).
FT CONFLICT 8 17 DCESPAPEAD -> GARARAGAN (in Ref. 4).
FT CONFLICT 56 57 QR -> HG (in Ref. 4).
FT CONFLICT 247 247 S -> T (in Ref. 4).
SQ SEQUENCE 277 AA; 31434 MW; AFD9ED92780CD502 CRC64;
MASAGGEDCE SPAPEADRPH QRPFLIGVSG GTASGKSTVC EKIMELLGQN EVEQRQRKVV
ILSQDRFYKV LTAEQKAKAL KGQYNFDHPD AFDNDLMHRT LKNIVEGKTV EVPTYDFVTH
SRLPETTVVY PADVVLFEGI LVFYSQEIRD MFHLRLFVDT DSDVRLSRRV LRDVRRGRDL
EQILTQYTTF VKPAFEEFCL PTKKYADVII PRGVDNMVAI NLIVQHIQDI LNGDICKWHR
GGSNGRSYKR TFSEPGDHPG MLTSGKRSHL ESSSRPH
//
ID UCK2_HUMAN STANDARD; PRT; 261 AA.
AC Q9BZX2; Q96KG5;
DT 28-FEB-2003 (Rel. 41, Created)
DT 28-FEB-2003 (Rel. 41, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE Uridine-cytidine kinase 2 (EC 2.7.1.48) (UCK 2) (Uridine
DE monophosphokinase 2) (Cytidine monophosphokinase 2).
GN UCK2 OR UMPK.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A., AND CHARACTERIZATION.
RX MEDLINE=21203813; PubMed=11306702;
RA Van Rompay A.R., Norda A., Linden K., Johansson M., Karlsson A.;
RT "Phosphorylation of uridine and cytidine nucleoside analogs by two
RT human uridine-cytidine kinases.";
RL Mol. Pharmacol. 59:1181-1186(2001).
RN [2]
RP SEQUENCE FROM N.A.
RC TISSUE=Lung;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [3]
RP SEQUENCE OF 15-261 FROM N.A.
RC TISSUE=Fibrosarcoma;
RX MEDLINE=21385121; PubMed=11494055;
RA Koizumi K., Shimamoto Y., Azuma A., Wataya Y., Matsuda A., Sasaki T.,
RA Fukushima M.;
RT "Cloning and expression of uridine/cytidine kinase cDNA from human
RT fibrosarcoma cells.";
RL Int. J. Mol. Med. 8:273-278(2001).
CC -!- FUNCTION: Phosphorylates uridine and cytidine to uridine
CC monophosphate and cytidine monophosphate. Does not phosphorylate
CC deoxyribonucleosides or purine ribonucleosides. Can use ATP or GTP
CC as a phosphate donor. Can also phosphorylate cytidine and uridine
CC nucleoside analogs such as 6-azauridine, 5-fluorouridine, 4-
CC thiouridine, 5-bromouridine, N(4)-acetylcytidine, N(4)-
CC benzoylcytidine, 5-fluorocytidine, 2-thiocytidine, 5-
CC methylcytidine, and N(4)-anisoylcytidine.
CC -!- CATALYTIC ACTIVITY: ATP + uridine = ADP + UMP.
CC -!- CATALYTIC ACTIVITY: ATP + cytidine = ADP + CMP.
CC -!- PATHWAY: Pyrimidine salvage pathway.
CC -!- TISSUE SPECIFICITY: Expressed in placenta.
CC -!- SIMILARITY: Belongs to the uridine kinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AF236637; AAK14053.1; -.
DR EMBL; BC002906; AAH02906.2; -.
DR EMBL; AB062451; BAB56162.1; -.
DR Genew; HGNC:12562; UMPK.
DR InterPro; IPR006082; PRK.
DR InterPro; IPR006083; PRK_URK.
DR InterPro; IPR000764; Uridine_kin.
DR Pfam; PF00485; PRK; 1.
DR PRINTS; PR00478; PHRIBLKINASE.
DR PRINTS; PR00988; URIDINKINASE.
DR TIGRFAMs; TIGR00235; udk; 1.
KW Transferase; Kinase; ATP-binding.
FT NP_BIND 27 34 ATP (Potential).
SQ SEQUENCE 261 AA; 29299 MW; 71791346F091EBFD CRC64;
MAGDSEQTLQ NHQQPNGGEP FLIGVSGGTA SGKSSVCAKI VQLLGQNEVD YRQKQVVILS
QDSFYRVLTS EQKAKALKGQ FNFDHPDAFD NELILKTLKE ITEGKTVQIP VYDFVSHSRK
EETVTVYPAD VVLFEGILAF YSQEVRDLFQ MKLFVDTDAD TRLSRRVLRD ISERGRDLEQ
ILSQYITFVK PAFEEFCLPT KKYADVIIPR GADNLVAINL IVQHIQDILN GGPSKRQTNG
CLNGYTPSRK RQASESSSRP H
//
ID UDP1_HUMAN STANDARD; PRT; 507 AA.
AC Q07131;
DT 01-FEB-1995 (Rel. 31, Created)
DT 01-FEB-1995 (Rel. 31, Last sequence update)
DT 15-JUL-1999 (Rel. 38, Last annotation update)
DE UTP--glucose-1-phosphate uridylyltransferase 1 (EC 2.7.7.9) (UDP-
DE glucose pyrophosphorylase 1) (UDPGP 1) (UGPase 1).
GN UGP1.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RC TISSUE=Liver;
RX MEDLINE=93359039; PubMed=8354390;
RA Peng H.-L., Chang H.-Y.;
RT "Cloning of a human liver UDP-glucose pyrophosphorylase cDNA by
RT complementation of the bacterial galU mutation.";
RL FEBS Lett. 329:153-158(1993).
RN [2]
RP MUTAGENESIS.
RX MEDLINE=96195686; PubMed=8612650;
RA Chang H.-Y., Peng H.-L., Chao Y.C., Duggleby R.G.;
RT "The importance of conserved residues in human liver UDPglucose
RT pyrophosphorylase.";
RL Eur. J. Biochem. 236:723-728(1996).
CC -!- FUNCTION: Plays a central role as a glucosyl donor in cellular
CC metabolic pathways.
CC -!- CATALYTIC ACTIVITY: UTP + alpha-D-glucose 1-phosphate =
CC diphosphate + UDP-glucose.
CC -!- SUBUNIT: Homooctamer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasmic.
CC -!- SIMILARITY: Belongs to the eukaryotic UDPGP family.
DR PIR; S35692; S35692.
DR Genew; HGNC:12526; UGP1.
DR GK; Q07131; -.
DR MIM; 191750; -.
DR GO; GO:0005737; C:cytoplasm; NAS.
DR GO; GO:0003983; F:UTP-glucose-1-phosphate uridylyltransferase...; TAS.
DR GO; GO:0016310; P:phosphorylation; NAS.
DR InterPro; IPR002618; UDPGP.
DR Pfam; PF01704; UDPGP; 1.
KW Transferase; Kinase; Nucleotidyltransferase; Multigene family.
FT INIT_MET 0 0 By similarity.
FT MOD_RES 1 1 BLOCKED (BY SIMILARITY).
FT MUTAGEN 122 122 C->S: NO SIGNIFICANT LOSS OF ACTIVITY.
FT MUTAGEN 217 217 W->S: NO SIGNIFICANT LOSS OF ACTIVITY.
FT MUTAGEN 265 265 H->R: NO SIGNIFICANT LOSS OF ACTIVITY.
FT MUTAGEN 332 332 W->S: LOSS OF ACTIVITY; PROBABLE FOLDING
FT DEFECT.
FT MUTAGEN 388 388 R->H: NO SIGNIFICANT LOSS OF ACTIVITY.
FT MUTAGEN 390 390 R->H: LOSS OF ACTIVITY; PROBABLE FOLDING
FT DEFECT.
FT MUTAGEN 421 421 R->H: NO SIGNIFICANT LOSS OF ACTIVITY.
FT MUTAGEN 444 444 R->H: NO SIGNIFICANT LOSS OF ACTIVITY.
SQ SEQUENCE 507 AA; 56818 MW; E3177B3CA23D1C80 CRC64;
SRFVQDLSKA MSQDGASQFQ EVILQELELS VKKELEKILT TATSHEYEHT KKDLDGFRKL
YHRFLQEKGP SVDWGKIQRP PEDSIQPYEK IKARGLPDNI SSVLNKLVVV KLNGGLGTSM
GCKGPKSLIG VRNENTFLDL TVQQIEHLNK SYNTDVPLVL MNSFNTDEDT KKILQKYNHC
RVKIYTFNQS RYPRINKESL RPVAKDVSSS GESTEAWYPP GHGDIYASFY NSGLLDTFLE
EGKEYIFVSN IDNLGATVDL YILNHLINPP NGKRCEFVME VTNKTRADVK GGTLTQYEGK
LRLVEIAQVP KAHVDEFKSV SKFKIFNTNN LWISLAAVKR LQEQNAIDME IIVNPKTLDG
GLNVIQLETA VGAAIKSFEN SLGINVPRSR FLPVKTTSDL LLVMSNLYSL NAGSLTMSEK
REFPTVPLVK LGSSFTKVQD YLRRFESIPD MLELDHLTVS GDVTFGKNVS LKGTVIIIAN
HGDRIDIPPG AVLENKIVSG NLRILDH
//
ID UDP2_HUMAN STANDARD; PRT; 497 AA.
AC Q16851; Q9BU15;
DT 15-JUL-1999 (Rel. 38, Created)
DT 28-FEB-2003 (Rel. 41, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE UTP--glucose-1-phosphate uridylyltransferase 2 (EC 2.7.7.9) (UDP-
DE glucose pyrophosphorylase 2) (UDPGP 2) (UGPase 2).
GN UGP2.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RC TISSUE=Skeletal muscle;
RX MEDLINE=96202932; PubMed=8631325;
RA Duggleby R.G., Chao Y.C., Huang J.G., Peng H.-L., Chang H.-Y.;
RT "Sequence differences between human muscle and liver cDNAs for
RT UDPglucose pyrophosphorylase and kinetic properties of the recombinant
RT enzymes expressed in Escherichia coli.";
RL Eur. J. Biochem. 235:173-179(1996).
RN [2]
RP SEQUENCE FROM N.A.
RC TISSUE=Lymph;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC -!- FUNCTION: Plays a central role as a glucosyl donor in cellular
CC metabolic pathways.
CC -!- CATALYTIC ACTIVITY: UTP + alpha-D-glucose 1-phosphate =
CC diphosphate + UDP-glucose.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic (By similarity).
CC -!- SIMILARITY: Belongs to the eukaryotic UDPGP family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; U27460; AAB05640.1; -.
DR EMBL; BC002954; AAH02954.1; -.
DR Genew; HGNC:12527; UGP2.
DR GK; Q16851; -.
DR MIM; 191751; -.
DR GO; GO:0003983; F:UTP-glucose-1-phosphate uridylyltransferase...; TAS.
DR GO; GO:0006011; P:UDP-glucose metabolism; TAS.
DR InterPro; IPR002618; UDPGP.
DR Pfam; PF01704; UDPGP; 1.
KW Transferase; Kinase; Nucleotidyltransferase; Multigene family.
FT CONFLICT 191 191 L -> R (in Ref. 1).
FT CONFLICT 257 257 M -> I (in Ref. 1).
SQ SEQUENCE 497 AA; 55676 MW; 2B3FD9731E371E47 CRC64;
MSQDGASQFQ EVIRQELELS VKKELEKILT TASSHEFEHT KKDLDGFRKL FHRFLQEKGP
SVDWGKIQRP PEDSIQPYEK IKARGLPDNI SSVLNKLVVV KLNGGLGTSM GCKGPKSLIG
VRNENTFLDL TVQQIEHLNK TYNTDVPLVL MNSFNTDEDT KKILQKYNHC RVKIYTFNQS
RYPRINKESL LPVAKDVSYS GENTEAWYPP GHGDIYASFY NSGLLDTFIG EGKEYIFVSN
IDNLGATVDL YILNHLMNPP NGKRCEFVME VTNKTRADVK GGTLTQYEGK LRLVEIAQVP
KAHVDEFKSV SKFKIFNTNN LWISLAAVKR LQEQNAIDME IIVNAKTLDG GLNVIQLETA
VGAAIKSFEN SLGINVPRSR FLPVKTTSDL LLVMSNLYSL NAGSLTMSEK REFPTVPLVK
LGSSFTKVQD YLRRFESIPD MLELDHLTVS GDVTFGKNVS LKGTVIIIAN HGDRIDIPPG
AVLENKIVSG NLRILDH
//
ID URL1_HUMAN STANDARD; PRT; 548 AA.
AC Q9NWZ5; Q9H3Z2;
DT 28-FEB-2003 (Rel. 41, Created)
DT 28-FEB-2003 (Rel. 41, Last sequence update)
DT 28-FEB-2003 (Rel. 41, Last annotation update)
DE Uridine kinase-like 1.
GN URKL1.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A.
RA Watanabe K., Kumagai A., Itakura S., Yamazaki M., Tashiro H., Ota T.,
RA Suzuki Y., Obayashi M., Nishi T., Shibahara T., Tanaka T.,
RA Nakamura Y., Isogai T., Sugano S.;
RT "NEDO human cDNA sequencing project.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SEQUENCE FROM N.A.
RX MEDLINE=21638749; PubMed=11780052;
RA Deloukas P., Matthews L.H., Ashurst J., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
CC -!- SIMILARITY: Belongs to the uridine kinase family.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; AK000524; BAA91230.1; -.
DR EMBL; AL118506; CAC15497.1; -.
DR HSSP; Q26998; 1BD3.
DR Genew; HGNC:15938; URKL1.
DR InterPro; IPR006082; PRK.
DR InterPro; IPR006083; PRK_URK.
DR InterPro; IPR000764; Uridine_kin.
DR Pfam; PF00485; PRK; 1.
DR PRINTS; PR00478; PHRIBLKINASE.
DR PRINTS; PR00988; URIDINKINASE.
DR TIGRFAMs; TIGR00235; udk; 1.
KW Transferase; Kinase; ATP-binding.
FT NP_BIND 105 112 ATP (Potential).
FT CONFLICT 219 228 Missing (in Ref. 2).
FT CONFLICT 290 290 N -> D (in Ref. 2).
SQ SEQUENCE 548 AA; 61139 MW; 0CD03697E02FE7DB CRC64;
MAAPPARADA DPSPTSPPTA RDTPGRQAEK SETACEDRSN AESLDRLLPP VGTGRSPRKR
TTSQCKSEPP LLRTSKRTIY TAGRPPWYNE HGTQSKEAFA IGLGGGSASG KTTVARMIIE
ALDVPWVVLL SMDSFYKVLT EQQQEQAAHN NFNFDHPDAF DFDLIISTLK KLKQGKSVKV
PIYDFTTHSR KKDWKTLYGA NVIIFEGIMA FADKTLLELL DMKIFVDTDS DIRLVRRLRR
DISERGRDIE GVIKQYNKFV KPSFDQYIQP TMRLADIVVP RGSGNTVAIN LIVQHVHSQL
EERELSVRAA LASAHQCHPL PRTLSVLKST PQVRGMHTII RDKETSRDEF IFYSKRLMRL
LIEHALSFLP FQDCVVQTPQ GQDYAGKCYA GKQITGVSIL RAGETMEPAL RAVCKDVRIG
TILIQTNQLT GEPELHYLRL PKDISDDHVI LMDCTVSTGA AAMMAVRVLL DHDVPEDKIF
LLSLLMAEMG VHSVAYAFPR VRIITTAVDK RVNDLFRIIP GIGNFGDRYF GTDAVPDGSD
EEEVAYTG
//
ID VGR1_HUMAN STANDARD; PRT; 1338 AA.
AC P17948; O60722; P16057; Q12954;
DT 01-NOV-1990 (Rel. 16, Created)
DT 01-NOV-1990 (Rel. 16, Last sequence update)
DT 15-MAR-2004 (Rel. 43, Last annotation update)
DE Vascular endothelial growth factor receptor 1 precursor (EC 2.7.1.112)
DE (VEGFR-1) (Vascular permeability factor receptor) (Tyrosine-protein
DE kinase receptor FLT) (Flt-1) (Tyrosine-protein kinase FRT) (Fms-like
DE tyrosine kinase 1).
GN FLT1 OR FLT OR FRT.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE FROM N.A. (ISOFORM FLT1).
RC TISSUE=Placenta;
RX MEDLINE=90221591; PubMed=2158038;
RA Shibuya M., Yamaguchi S., Yamane A., Ikeda T., Tojo A.,
RA Matsushime H., Sato M.;
RT "Nucleotide sequence and expression of a novel human receptor-type
RT tyrosine kinase gene (flt) closely related to the fms family.";
RL Oncogene 5:519-524(1990).
RN [2]
RP SEQUENCE FROM N.A. (ISOFORM FLT1).
RC TISSUE=Umbilical vein;
RA Yu Y., Whitney R.G., Sato J.D.;
RT "Coding region for human VEGF receptor FLT1 (VEGFR-1).";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SEQUENCE FROM N.A. (ISOFORM SFLT1), AND SEQUENCE OF N-TERMINUS.
RC TISSUE=Umbilical vein;
RX MEDLINE=94068470; PubMed=8248162;
RA Kendall R.L., Thomas K.A.;
RT "Inhibition of vascular endothelial cell growth factor activity by an
RT endogenously encoded soluble receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:10705-10709(1993).
RN [4]
RP SEQUENCE FROM N.A. (ISOFORM SFLT1).
RC TISSUE=Ovary;
RX MEDLINE=22388257; PubMed=12477932;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length
RT human and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [5]
RP SEQUENCE OF 1018-1058 FROM N.A. (ISOFORM FLT1).
RX MEDLINE=87307638; PubMed=3040650;
RA Matsushime H., Yoshida M.C., Sasaki M., Shibuya M.;
RT "A possible new member of tyrosine kinase family, human frt sequence,
RT is highly conserved in vertebrates and located on human chromosome
RT 13.";
RL Jpn. J. Cancer Res. 78:655-661(1987).
RN [6]
RP PARTIAL SEQUENCE, PHOSPHORYLATION SITES, AND MUTAGENESIS OF TYR-914;
RP TYR-1213; TYR-1242; TYR-1327 AND TYR-1333.
RX MEDLINE=98389777; PubMed=9722576;
RA Ito N., Wernstedt C., Engstrom U., Claesson-Welsh L.;
RT "Identification of vascular endothelial growth factor receptor-1
RT tyrosine phosphorylation sites and binding of SH2 domain-containing
RT molecules.";
RL J. Biol. Chem. 273:23410-23418(1998).
RN [7]
RP STRUCTURE BY NMR OF 129-229.
RX MEDLINE=20013066; PubMed=10543948;
RA Starovasnik M.A., Christinger H.W., Wiesmann C., Champe M.A.,
RA de Vos A.M., Skelton N.J.;
RT "Solution structure of the VEGF-binding domain of Flt-1: comparison
RT of its free and bound states.";
RL J. Mol. Biol. 293:531-544(1999).
CC -!- FUNCTION: Receptor for VEGF, VEGFB and PGF. Has a tyrosine-protein
CC kinase activity. The VEGF-kinase ligand/receptor signaling system
CC plays a key role in vascular development and regulation of
CC vascular permeability. Isoform SFlt1 may have an inhibitory role
CC in angiogenesis.
CC -!- CATALYTIC ACTIVITY: ATP + a protein tyrosine = ADP + protein
CC tyrosine phosphate.
CC -!- SUBUNIT: Interacts in vitro with various phosphotyrosine-binding
CC proteins, including PLC-gammas, PTPN11, GRB2, CRK and NCK1.
CC -!- SUBCELLULAR LOCATION: Type I membrane protein (Flt1) and soluble
CC (SFlt1).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist;
CC Name=Flt1;
CC IsoId=P17948-1; Sequence=Displayed;
CC Name=sFlt1;
CC IsoId=P17948-2; Sequence=VSP_002955, VSP_002956;
CC -!- TISSUE SPECIFICITY: Mostly in normal lung, but also in placenta,
CC liver, kidney, heart and brain tissues. Specifically expressed in
CC most of the vascular endothelial cells, and also expressed in
CC peripheral blood monocytes. It is not expressed in tumor cell
CC lines. Isoform sFlt1 is strongly expressed in placenta.
CC -!- SIMILARITY: Belongs to the Tyr family of protein kinases.
CC CSF-1/PDGF receptor subfamily.
CC -!- SIMILARITY: Contains 7 immunoglobulin-like C2-type domains.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; X51602; CAA35946.1; -.
DR EMBL; AF063657; AAC16449.1; -.
DR EMBL; U01134; AAC50060.1; -.
DR EMBL; BC039007; AAH39007.1; -.
DR EMBL; D00133; BAA00080.1; -.
DR PIR; A49636; A49636.
DR PIR; S09982; S09982.
DR PDB; 1QSV; 10-NOV-99.
DR PDB; 1QSZ; 10-NOV-99.
DR PDB; 1FLT; 13-JAN-99.
DR PDB; 1QTY; 19-APR-00.
DR Genew; HGNC:3763; FLT1.
DR MIM; 165070; -.
DR GO; GO:0005615; C:extracellular space; TAS.
DR GO; GO:0005887; C:integral to plasma membrane; TAS.
DR GO; GO:0004872; F:receptor activity; TAS.
DR GO; GO:0005021; F:vascular endothelial growth factor receptor...; TAS.
DR GO; GO:0008284; P:positive regulation of cell proliferation; TAS.
DR GO; GO:0007565; P:pregnancy; TAS.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kin...; TAS.
DR InterPro; IPR007110; Ig-like.
DR InterPro; IPR003598; Ig_c2.
DR InterPro; IPR000719; Prot_kinase.
DR InterPro; IPR001824; RecepttyrkinsIII.
DR InterPro; IPR001245; Tyr_pkinase.
DR InterPro; IPR008266; Tyr_pkinase_AS.
DR Pfam; PF00047; ig; 7.
DR Pfam; PF00069; pkinase; 1.
DR ProDom; PD000001; Prot_kinase; 2.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00219; TyrKc; 1.
DR PROSITE; PS50835; IG_LIKE; 6.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
KW Angiogenesis; Transferase; Kinase; Tyrosine-protein kinase; Receptor;
KW ATP-binding; Transmembrane; Signal; Immunoglobulin domain; Repeat;
KW Phosphorylation; Glycoprotein; Alternative splicing; 3D-structure.
FT SIGNAL 1 26
FT CHAIN 27 1338 VASCULAR ENDOTHELIAL GROWTH FACTOR
FT RECEPTOR 1.
FT DOMAIN 27 758 Extracellular (Potential).
FT TRANSMEM 759 780 Potential.
FT DOMAIN 781 1338 Cytoplasmic (Potential).
FT DOMAIN 32 123 IG-LIKE C2-TYPE 1.
FT DOMAIN 151 214 IG-LIKE C2-TYPE 2.
FT DOMAIN 230 327 IG-LIKE C2-TYPE 3.
FT DOMAIN 335 421 IG-LIKE C2-TYPE 4.
FT DOMAIN 428 553 IG-LIKE C2-TYPE 5.
FT DOMAIN 556 654 IG-LIKE C2-TYPE 6.
FT DOMAIN 661 747 IG-LIKE C2-TYPE 7.
FT DOMAIN 827 1158 PROTEIN KINASE.
FT NP_BIND 833 841 ATP (By similarity).
FT BINDING 861 861 ATP (By similarity).
FT ACT_SITE 1022 1022 By similarity.
FT MOD_RES 1053 1053 PHOSPHORYLATION (AUTO-) (BY SIMILARITY).
FT MOD_RES 1169 1169 PHOSPHORYLATION (AUTO-) (BY SIMILARITY).
FT MOD_RES 1213 1213 PHOSPHORYLATION (AUTO-).
FT MOD_RES 1242 1242 PHOSPHORYLATION (AUTO-).
FT MOD_RES 1327 1327 PHOSPHORYLATION (AUTO-) (PARTIAL).
FT MOD_RES 1333 1333 PHOSPHORYLATION (AUTO-) (PARTIAL).
FT DISULFID 53 107 Potential.
FT DISULFID 158 207
FT DISULFID 252 311 Potential.
FT DISULFID 454 535 Potential.
FT DISULFID 577 636 Potential.
FT DISULFID 682 731 Potential.
FT CARBOHYD 100 100 N-LINKED (GLCNAC...) (POTENTIAL).
FT CARBOHYD 164 164 N-LINKED (GLCNAC...) (POTENTIAL).
FT CARBOHYD 196 196 N-LINKED (GLCNAC...) (POTENTIAL).
FT CARBOHYD 251 251 N-LINKED (GLCNAC...) (POTENTIAL).
FT CARBOHYD 323 323 N-LINKED (GLCNAC...) (POTENTIAL).
FT CARBOHYD 402 402 N-LINKED (GLCNAC...) (POTENTIAL).
FT CARBOHYD 417 417 N-LINKED (GLCNAC...) (POTENTIAL).
FT CARBOHYD 474 474 N-LINKED (GLCNAC...) (POTENTIAL).
FT CARBOHYD 547 547 N-LINKED (GLCNAC...) (POTENTIAL).
FT CARBOHYD 597 597 N-LINKED (GLCNAC...) (POTENTIAL).
FT CARBOHYD 620 620 N-LINKED (GLCNAC...) (POTENTIAL).
FT CARBOHYD 625 625 N-LINKED (GLCNAC...) (POTENTIAL).
FT CARBOHYD 666 666 N-LINKED (GLCNAC...) (POTENTIAL).
FT VARSPLIC 657 687 DQEAPYLLRNLSDHTVAISSSTTLDCHANGV -> GEHCNK
FT KAVFSRISKFKSTRNDCTTQSNVKH (in isoform
FT sFlt1).
FT /FTId=VSP_002955.
FT VARSPLIC 688 1338 Missing (in isoform sFlt1).
FT /FTId=VSP_002956.
FT MUTAGEN 914 914 Y->F: NO LOSS OF PHOSPHORYLATION.
FT MUTAGEN 1213 1213 Y->F: LOSS OF PHOSPHORYLATION.
FT MUTAGEN 1242 1242 Y->F: LOSS OF PHOSPHORYLATION.
FT MUTAGEN 1327 1327 Y->F: LOSS OF PHOSPHORYLATION.
FT MUTAGEN 1333 1333 Y->F: LOSS OF PHOSPHORYLATION.
FT CONFLICT 779 779 L -> F (in Ref. 2).
FT STRAND 135 135
FT STRAND 144 148
FT TURN 150 151
FT STRAND 154 156
FT STRAND 160 160
FT TURN 163 164
FT STRAND 168 171
FT TURN 172 174
FT STRAND 175 177
FT STRAND 184 187
FT TURN 188 190
FT STRAND 191 194
FT HELIX 199 201
FT STRAND 203 211
FT TURN 212 213
FT STRAND 214 224
SQ SEQUENCE 1338 AA; 150733 MW; 54F1554E5590787F CRC64;
MVSYWDTGVL LCALLSCLLL TGSSSGSKLK DPELSLKGTQ HIMQAGQTLH LQCRGEAAHK
WSLPEMVSKE SERLSITKSA CGRNGKQFCS TLTLNTAQAN HTGFYSCKYL AVPTSKKKET
ESAIYIFISD TGRPFVEMYS EIPEIIHMTE GRELVIPCRV TSPNITVTLK KFPLDTLIPD
GKRIIWDSRK GFIISNATYK EIGLLTCEAT VNGHLYKTNY LTHRQTNTII DVQISTPRPV
KLLRGHTLVL NCTATTPLNT RVQMTWSYPD EKNKRASVRR RIDQSNSHAN IFYSVLTIDK
MQNKDKGLYT CRVRSGPSFK SVNTSVHIYD KAFITVKHRK QQVLETVAGK RSYRLSMKVK
AFPSPEVVWL KDGLPATEKS ARYLTRGYSL IIKDVTEEDA GNYTILLSIK QSNVFKNLTA
TLIVNVKPQI YEKAVSSFPD PALYPLGSRQ ILTCTAYGIP QPTIKWFWHP CNHNHSEARC
DFCSNNEESF ILDADSNMGN RIESITQRMA IIEGKNKMAS TLVVADSRIS GIYICIASNK
VGTVGRNISF YITDVPNGFH VNLEKMPTEG EDLKLSCTVN KFLYRDVTWI LLRTVNNRTM
HYSISKQKMA ITKEHSITLN LTIMNVSLQD SGTYACRARN VYTGEEILQK KEITIRDQEA
PYLLRNLSDH TVAISSSTTL DCHANGVPEP QITWFKNNHK IQQEPGIILG PGSSTLFIER
VTEEDEGVYH CKATNQKGSV ESSAYLTVQG TSDKSNLELI TLTCTCVAAT LFWLLLTLLI
RKMKRSSSEI KTDYLSIIMD PDEVPLDEQC ERLPYDASKW EFARERLKLG KSLGRGAFGK
VVQASAFGIK KSPTCRTVAV KMLKEGATAS EYKALMTELK ILTHIGHHLN VVNLLGACTK
QGGPLMVIVE YCKYGNLSNY LKSKRDLFFL NKDAALHMEP KKEKMEPGLE QGKKPRLDSV
TSSESFASSG FQEDKSLSDV EEEEDSDGFY KEPITMEDLI SYSFQVARGM EFLSSRKCIH
RDLAARNILL SENNVVKICD FGLARDIYKN PDYVRKGDTR LPLKWMAPES IFDKIYSTKS
DVWSYGVLLW EIFSLGGSPY PGVQMDEDFC SRLREGMRMR APEYSTPEIY QIMLDCWHRD
PKERPRFAEL VEKLGDLLQA NVQQDGKDYI PINAILTGNS GFTYSTPAFS EDFFKESISA
PKFNSGSSDD VRYVNAFKFM SLERIKTFEE LLPNATSMFD DYQGDSSTLL ASPMLKRFTW
TDSKPKASLK IDLRVTSKSK ESGLSDVSRP SFCHSSCGHV SEGKRRFTYD HAELERKIAC
CSPPPDYNSV VLYSTPPI
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