ID PGK1_HUMAN Reviewed; 417 AA.
AC P00558; Q5J7W1; Q6IBT6; Q8NI87;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 13-JUL-2010, entry version 129.
DE RecName: Full=Phosphoglycerate kinase 1;
DE EC=2.7.2.3;
DE AltName: Full=Primer recognition protein 2;
DE Short=PRP 2;
DE AltName: Full=Cell migration-inducing gene 10 protein;
GN Name=PGK1; Synonyms=PGKA; ORFNames=MIG10, OK/SW-cl.110;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX MEDLINE=83169680; PubMed=6188151; DOI=10.1073/pnas.80.2.472;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX MEDLINE=86016816; PubMed=2995995; DOI=10.1073/pnas.82.20.6965;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kim J.W.;
RT "Identification of a human migration-inducing gene 10 (MIG10).";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon adenocarcinoma;
RA Shichijo S., Itoh K.;
RT "Identification of immuno-peptidmics that are recognized by tumor-
RT reactive CTL generated from TIL of colon cancer patients.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Skin, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RX MEDLINE=85155507; PubMed=6099325; DOI=10.1016/0378-1119(84)90016-7;
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 [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
RX MEDLINE=90049205; PubMed=2814502; DOI=10.1126/science.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 [10]
RP PROTEIN SEQUENCE OF 2-417.
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 [11]
RP PROTEIN SEQUENCE OF 23-30; 76-86; 107-123; 157-171; 200-216; 221-264;
RP 280-297; 333-350; 366-382 AND 389-417, AND MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [12]
RP PARTIAL PROTEIN 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 [13]
RP REVIEW ON VARIANTS.
RX MEDLINE=97230014; PubMed=9075577; DOI=10.1006/bcmd.1996.0108;
RA Yoshida A.;
RT "Hematologically important mutations: molecular abnormalities of
RT phosphoglycerate kinase.";
RL Blood Cells Mol. Dis. 22:265-267(1996).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-196, AND MASS
RP SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17287340; DOI=10.1073/pnas.0611217104;
RA Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
RT "Global proteomic profiling of phosphopeptides using electron transfer
RT dissociation tandem mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203 AND THR-243, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18187866; DOI=10.2116/analsci.24.161;
RA Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
RT "Automated phosphoproteome analysis for cultured cancer cells by two-
RT dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
RL Anal. Sci. 24:161-166(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RA Colinge J., Superti-Furga G., Bennett K.L.;
RL Submitted (OCT-2008) to UniProtKB.
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-11; LYS-30; LYS-48; LYS-75;
RP LYS-86; LYS-97; LYS-131; LYS-146; LYS-199; LYS-267; LYS-291; LYS-323
RP AND LYS-406, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [21]
RP VARIANT CHRONIC HEMOLYTIC ANEMIA LYS-191 DEL.
RX MEDLINE=96230923; PubMed=8673469; DOI=10.1006/bcmd.1995.0020;
RA Yoshida A., Twele T.W., Dave V., Beutler E.;
RT "Molecular abnormality of a phosphoglycerate kinase variant (PGK-
RT Alabama).";
RL Blood Cells Mol. Dis. 21:179-181(1995).
RN [22]
RP VARIANT CHRONIC HEMOLYTIC ANEMIA/MENTAL RETARDATION VAL-164, AND
RP VARIANT RHABDOMYOLYSIS ASN-315.
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 [23]
RP VARIANT CHRONIC HEMOLYTIC ANEMIA ALA-252.
RX MEDLINE=96201344; PubMed=8615693; DOI=10.1006/abbi.1996.0089;
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 [24]
RP VARIANT CHRONIC HEMOLYTIC ANEMIA VAL-285.
RX MEDLINE=98415729; PubMed=9744480;
RX DOI=10.1002/(SICI)1098-1004(1998)12:4<280::AID-HUMU10>3.3.CO;2-Z;
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 [25]
RP VARIANT CONGENITAL NONSPHEROCYTIC ANEMIA PRO-88.
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 [26]
RP VARIANT CHRONIC HEMOLYTIC ANEMIA ARG-316.
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 [27]
RP VARIANT MUNCHEN ASN-268.
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 [28]
RP VARIANT MUNCHEN ASN-268, AND VARIANT ASN-352.
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 [29]
RP VARIANT CHRONIC HEMOLYTIC ANEMIA VAL-158.
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 chronic
RT hemolysis and myoglobinuria.";
RL Blood 79:1582-1585(1992).
RN [30]
RP VARIANT CHRONIC NONSPHEROCYTIC HEMOLYTIC ANEMIA MET-266.
RX MEDLINE=81223926; PubMed=6941312; DOI=10.1073/pnas.78.4.2587;
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 [31]
RP VARIANT CHRONIC HEMOLYTIC ANEMIA PRO-206.
RX MEDLINE=81054987; PubMed=6933565; DOI=10.1073/pnas.77.9.5461;
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 seems
CC that PGK-1 acts as a polymerase alpha cofactor protein (primer
CC recognition protein).
CC -!- CATALYTIC ACTIVITY: ATP + 3-phospho-D-glycerate = ADP + 3-phospho-
CC D-glyceroyl phosphate.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 2/5.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DISEASE: Defects in PGK1 are generally associated with chronic
CC hemolytic anemia [MIM:300653]; although it can be accompanied by
CC either mental retardation or muscular disease (rhabdomyolysis).
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC -!- WEB RESOURCE: Name=GeneReviews;
CC URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/PGK1";
CC -!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
CC polymorphism database;
CC URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=PGK1";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Phosphoglycerate kinase entry;
CC URL="http://en.wikipedia.org/wiki/Phosphoglycerate_kinase";
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DR EMBL; V00572; CAA23835.1; -; mRNA.
DR EMBL; L00160; AAA60078.1; -; mRNA.
DR EMBL; M11968; AAA60079.1; -; Genomic_DNA.
DR EMBL; M11958; AAA60079.1; JOINED; Genomic_DNA.
DR EMBL; M11959; AAA60079.1; JOINED; Genomic_DNA.
DR EMBL; M11960; AAA60079.1; JOINED; Genomic_DNA.
DR EMBL; M11961; AAA60079.1; JOINED; Genomic_DNA.
DR EMBL; M11962; AAA60079.1; JOINED; Genomic_DNA.
DR EMBL; M11963; AAA60079.1; JOINED; Genomic_DNA.
DR EMBL; M11964; AAA60079.1; JOINED; Genomic_DNA.
DR EMBL; M11965; AAA60079.1; JOINED; Genomic_DNA.
DR EMBL; M11966; AAA60079.1; JOINED; Genomic_DNA.
DR EMBL; M11967; AAA60079.1; JOINED; Genomic_DNA.
DR EMBL; AY423725; AAS00488.1; -; mRNA.
DR EMBL; AB062432; BAB93495.1; -; mRNA.
DR EMBL; CR456716; CAG32997.1; -; mRNA.
DR EMBL; AL049589; CAI42951.1; -; Genomic_DNA.
DR EMBL; BC023234; AAH23234.1; -; mRNA.
DR EMBL; BC103752; AAI03753.1; -; mRNA.
DR EMBL; BC104837; AAI04838.1; -; mRNA.
DR EMBL; BC113568; AAI13569.1; -; mRNA.
DR EMBL; M34017; AAA60103.1; -; Genomic_DNA.
DR IPI; IPI00169383; -.
DR PIR; I59050; KIHUG.
DR RefSeq; NP_000282.1; -.
DR UniGene; Hs.78771; -.
DR PDB; 2WZB; X-ray; 1.47 A; A=2-417.
DR PDB; 2WZC; X-ray; 1.50 A; A=2-417.
DR PDB; 2WZD; X-ray; 1.56 A; A=1-417.
DR PDB; 2ZGV; X-ray; 2.00 A; A=1-417.
DR PDB; 3C39; X-ray; 1.85 A; A/B=1-417.
DR PDB; 3C3A; X-ray; 2.30 A; A/B=1-417.
DR PDB; 3C3B; X-ray; 1.80 A; A/B=1-417.
DR PDB; 3C3C; X-ray; 2.40 A; A/B=1-417.
DR PDBsum; 2WZB; -.
DR PDBsum; 2WZC; -.
DR PDBsum; 2WZD; -.
DR PDBsum; 2ZGV; -.
DR PDBsum; 3C39; -.
DR PDBsum; 3C3A; -.
DR PDBsum; 3C3B; -.
DR PDBsum; 3C3C; -.
DR IntAct; P00558; 7.
DR MINT; MINT-1131047; -.
DR STRING; P00558; -.
DR PhosphoSite; P00558; -.
DR Aarhus/Ghent-2DPAGE; 3308; NEPHGE.
DR DOSAC-COBS-2DPAGE; P00558; -.
DR OGP; P00558; -.
DR REPRODUCTION-2DPAGE; IPI00169383; -.
DR REPRODUCTION-2DPAGE; P00558; -.
DR UCD-2DPAGE; P00558; -.
DR PeptideAtlas; P00558; -.
DR PRIDE; P00558; -.
DR Ensembl; ENST00000373316; ENSP00000362413; ENSG00000102144; Homo sapiens.
DR GeneID; 5230; -.
DR KEGG; hsa:5230; -.
DR NMPDR; fig|9606.3.peg.33025; -.
DR UCSC; uc004ecz.2; human.
DR CTD; 5230; -.
DR GeneCards; GC0XP077246; -.
DR H-InvDB; HIX0056104; -.
DR HGNC; HGNC:8896; PGK1.
DR HPA; CAB010065; -.
DR MIM; 300653; phenotype.
DR MIM; 311800; gene.
DR Orphanet; 713; Phosphoglycerate kinase 1 deficiency.
DR PharmGKB; PA33234; -.
DR eggNOG; prNOG16829; -.
DR HOGENOM; HBG453500; -.
DR HOVERGEN; HBG008177; -.
DR InParanoid; P00558; -.
DR OMA; NFANGTK; -.
DR OrthoDB; EOG94QWMF; -.
DR PhylomeDB; P00558; -.
DR BRENDA; 2.7.2.3; 247.
DR Pathway_Interaction_DB; hif1_tfpathway; HIF-1-alpha transcription factor network.
DR Reactome; REACT_1505; Integration of energy metabolism.
DR Reactome; REACT_15380; Diabetes pathways.
DR Reactome; REACT_474; Metabolism of carbohydrates.
DR NextBio; 20218; -.
DR ArrayExpress; P00558; -.
DR Bgee; P00558; -.
DR CleanEx; HS_PGK1; -.
DR Genevestigator; P00558; -.
DR GermOnline; ENSG00000102144; Homo sapiens.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; ISS:UniProtKB.
DR GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; ISS:UniProtKB.
DR InterPro; IPR001576; Phosphoglycerate_kinase.
DR InterPro; IPR015901; Phosphoglycerate_kinase_C.
DR InterPro; IPR015911; Phosphoglycerate_kinase_CS.
DR InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR Gene3D; G3DSA:3.40.50.1270; Phosphoglycerate_kinase_C; 1.
DR Gene3D; G3DSA:3.40.50.1260; Phosphoglycerate_kinase_N; 1.
DR PANTHER; PTHR11406; PGK; 1.
DR Pfam; PF00162; PGK; 1.
DR PIRSF; PIRSF000724; Pgk; 1.
DR PRINTS; PR00477; PHGLYCKINASE.
DR SUPFAM; SSF53748; PGK; 1.
DR PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Disease mutation; Glycolysis;
KW Hereditary hemolytic anemia; Kinase; Nucleotide-binding;
KW Phosphoprotein; Polymorphism; Transferase.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 417 Phosphoglycerate kinase 1.
FT /FTId=PRO_0000145831.
FT NP_BIND 373 376 ATP (By similarity).
FT REGION 24 26 Substrate binding (By similarity).
FT REGION 63 66 Substrate binding (By similarity).
FT BINDING 39 39 Substrate (By similarity).
FT BINDING 123 123 Substrate (By similarity).
FT BINDING 171 171 Substrate (By similarity).
FT BINDING 220 220 ATP (By similarity).
FT BINDING 313 313 ATP; via carbonyl oxygen (By similarity).
FT BINDING 344 344 ATP (By similarity).
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 11 11 N6-acetyllysine.
FT MOD_RES 30 30 N6-acetyllysine.
FT MOD_RES 48 48 N6-acetyllysine.
FT MOD_RES 75 75 N6-acetyllysine.
FT MOD_RES 76 76 Phosphotyrosine (By similarity).
FT MOD_RES 86 86 N6-acetyllysine.
FT MOD_RES 97 97 N6-acetyllysine.
FT MOD_RES 131 131 N6-acetyllysine.
FT MOD_RES 136 136 Phosphoserine.
FT MOD_RES 146 146 N6-acetyllysine.
FT MOD_RES 196 196 Phosphotyrosine.
FT MOD_RES 199 199 N6-acetyllysine.
FT MOD_RES 203 203 Phosphoserine.
FT MOD_RES 243 243 Phosphothreonine.
FT MOD_RES 267 267 N6-acetyllysine.
FT MOD_RES 291 291 N6-acetyllysine.
FT MOD_RES 323 323 N6-acetyllysine.
FT MOD_RES 390 390 Phosphoserine (By similarity).
FT MOD_RES 406 406 N6-acetyllysine.
FT VARIANT 88 88 L -> P (in congenital nonspherocytic
FT anemia; variant Matsue).
FT /FTId=VAR_006076.
FT VARIANT 158 158 G -> V (in chronic hemolytic anemia;
FT variant Shizuoka).
FT /FTId=VAR_006077.
FT VARIANT 164 164 D -> V (in chronic hemolytic anemia and
FT mental retardation; variant Amiens).
FT /FTId=VAR_006078.
FT VARIANT 191 191 Missing (in chronic hemolytic anemia;
FT variant Alabama).
FT /FTId=VAR_006079.
FT VARIANT 206 206 R -> P (in chronic hemolytic anemia;
FT variant Uppsala).
FT /FTId=VAR_006080.
FT VARIANT 252 252 E -> A (in chronic hemolytic anemia;
FT variant Antwerp).
FT /FTId=VAR_006081.
FT VARIANT 266 266 V -> M (in chronic nonspherocytic
FT hemolytic anemia; variant Tokyo).
FT /FTId=VAR_006082.
FT VARIANT 268 268 D -> N (in Munchen; 21% of activity).
FT /FTId=VAR_006083.
FT VARIANT 285 285 D -> V (in chronic hemolytic anemia;
FT variant Herlev; 50% of activity).
FT /FTId=VAR_006084.
FT VARIANT 315 315 D -> N (in rhabdomyolysis; variant
FT Creteil).
FT /FTId=VAR_006085.
FT VARIANT 316 316 C -> R (in chronic hemolytic anemia;
FT variant Michigan).
FT /FTId=VAR_006086.
FT VARIANT 352 352 T -> N.
FT /FTId=VAR_006087.
FT CONFLICT 39 39 Missing (in Ref. 10; AA sequence).
FT CONFLICT 370 370 I -> T (in Ref. 5; CAG32997).
FT HELIX 9 11
FT STRAND 18 22
FT STRAND 33 35
FT HELIX 38 52
FT STRAND 56 61
FT TURN 73 75
FT HELIX 79 89
FT STRAND 94 97
FT STRAND 99 101
FT HELIX 102 109
FT STRAND 115 119
FT HELIX 122 124
FT HELIX 126 129
FT HELIX 144 156
FT STRAND 159 163
FT HELIX 166 168
FT HELIX 174 177
FT STRAND 184 186
FT HELIX 188 202
FT STRAND 206 212
FT HELIX 218 220
FT HELIX 221 228
FT STRAND 232 236
FT HELIX 238 240
FT HELIX 241 249
FT HELIX 260 263
FT HELIX 266 276
FT STRAND 279 281
FT STRAND 284 293
FT STRAND 298 302
FT TURN 303 305
FT STRAND 312 316
FT HELIX 318 330
FT STRAND 332 338
FT HELIX 346 348
FT HELIX 350 364
FT STRAND 368 371
FT STRAND 388 392
FT HELIX 397 403
FT HELIX 409 412
SQ SEQUENCE 417 AA; 44615 MW; B5DFC7B5FA01767C CRC64;
MSLSNKLTLD KLDVKGKRVV MRVDFNVPMK NNQITNNQRI KAAVPSIKFC LDNGAKSVVL
MSHLGRPDGV PMPDKYSLEP VAVELKSLLG KDVLFLKDCV GPEVEKACAN PAAGSVILLE
NLRFHVEEEG KGKDASGNKV KAEPAKIEAF RASLSKLGDV YVNDAFGTAH RAHSSMVGVN
LPQKAGGFLM KKELNYFAKA LESPERPFLA ILGGAKVADK IQLINNMLDK VNEMIIGGGM
AFTFLKVLNN MEIGTSLFDE EGAKIVKDLM SKAEKNGVKI TLPVDFVTAD KFDENAKTGQ
ATVASGIPAG WMGLDCGPES SKKYAEAVTR AKQIVWNGPV GVFEWEAFAR GTKALMDEVV
KATSRGCITI IGGGDTATCC AKWNTEDKVS HVSTGGGASL ELLEGKVLPG VDALSNI
//
