LOCUS       NP_000282                417 aa            linear   PRI 28-APR-2025
DEFINITION  phosphoglycerate kinase 1 [Homo sapiens].
ACCESSION   NP_000282
VERSION     NP_000282.1
DBSOURCE    REFSEQ: accession NM_000291.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Gao,X., Pan,T., Gao,Y., Zhu,W., Liu,L., Duan,W., Han,C., Feng,B.,
            Yan,W., Song,Q., Liu,Y. and Yue,L.
  TITLE     Acetylation of PGK1 at lysine 323 promotes glycolysis, cell
            proliferation, and metastasis in luminal A breast cancer cells
  JOURNAL   BMC Cancer 24 (1), 1054 (2024)
   PUBMED   39192221
  REMARK    GeneRIF: Acetylation of PGK1 at lysine 323 promotes glycolysis,
            cell proliferation, and metastasis in luminal A breast cancer
            cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Guo,Z., Zhang,Y., Wang,H., Liao,L., Ma,L., Zhao,Y., Yang,R., Li,X.,
            Niu,J., Chu,Q., Fu,Y., Li,B. and Yang,C.
  TITLE     Hypoxia-induced downregulation of PGK1 crotonylation promotes
            tumorigenesis by coordinating glycolysis and the TCA cycle
  JOURNAL   Nat Commun 15 (1), 6915 (2024)
   PUBMED   39134530
  REMARK    GeneRIF: Hypoxia-induced downregulation of PGK1 crotonylation
            promotes tumorigenesis by coordinating glycolysis and the TCA
            cycle.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Muhtadi,R., Stewart,S., Bunert,F., Fatanmi,O.O., Wise,S.Y.,
            Gartner,C., Motzke,S., Ruf,C., Ostheim,P., Schule,S., Schwanke,D.,
            Singh,V.K., Port,M. and Abend,M.
  TITLE     PUM1 and PGK1 are Favorable Housekeeping Genes over Established
            Biodosimetry-related Housekeeping Genes such as HPRT1, ITFG1, DPM1,
            MRPS5, 18S rRNA and Others after Radiation Exposure
  JOURNAL   Radiat Res 201 (5), 487-498 (2024)
   PUBMED   38471523
  REMARK    GeneRIF: PUM1 and PGK1 are Favorable Housekeeping Genes over
            Established Biodosimetry-related Housekeeping Genes such as HPRT1,
            ITFG1, DPM1, MRPS5, 18S rRNA and Others after Radiation Exposure.
REFERENCE   4  (residues 1 to 417)
  AUTHORS   Zhang,Y., Wang,X., Liu,W., Lei,T., Qiao,T., Feng,W. and Song,W.
  TITLE     CircGLIS3 promotes gastric cancer progression by regulating the
            miR-1343-3p/PGK1 pathway and inhibiting vimentin phosphorylation
  JOURNAL   J Transl Med 22 (1), 251 (2024)
   PUBMED   38459513
  REMARK    GeneRIF: CircGLIS3 promotes gastric cancer progression by
            regulating the miR-1343-3p/PGK1 pathway and inhibiting vimentin
            phosphorylation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 417)
  AUTHORS   Lay,A.J., Jiang,X.M., Kisker,O., Flynn,E., Underwood,A., Condron,R.
            and Hogg,P.J.
  TITLE     Phosphoglycerate kinase acts in tumour angiogenesis as a disulphide
            reductase
  JOURNAL   Nature 408 (6814), 869-873 (2000)
   PUBMED   11130727
  REMARK    GeneRIF: Phosphoglycerate kinase is a moonlighting protein that
            functions as both a glycolytic enzyme and a disulfide reductase.
REFERENCE   6  (residues 1 to 417)
  AUTHORS   Maeda,M., Bawle,E.V., Kulkarni,R., Beutler,E. and Yoshida,A.
  TITLE     Molecular abnormalities of a phosphoglycerate kinase variant
            generated by spontaneous mutation
  JOURNAL   Blood 79 (10), 2759-2762 (1992)
   PUBMED   1586722
REFERENCE   7  (residues 1 to 417)
  AUTHORS   Fujii,H., Kanno,H., Hirono,A., Shiomura,T. and Miwa,S.
  TITLE     A single amino acid substitution (157 Gly----Val) in a
            phosphoglycerate kinase variant (PGK Shizuoka) associated with
            chronic hemolysis and myoglobinuria
  JOURNAL   Blood 79 (6), 1582-1585 (1992)
   PUBMED   1547346
REFERENCE   8  (residues 1 to 417)
  AUTHORS   Vishwanatha,J.K., Jindal,H.K. and Davis,R.G.
  TITLE     The role of primer recognition proteins in DNA replication:
            association with nuclear matrix in HeLa cells
  JOURNAL   J Cell Sci 101 (Pt 1), 25-34 (1992)
   PUBMED   1533225
REFERENCE   9  (residues 1 to 417)
  AUTHORS   Jindal,H.K. and Vishwanatha,J.K.
  TITLE     Functional identity of a primer recognition protein as
            phosphoglycerate kinase
  JOURNAL   J Biol Chem 265 (12), 6540-6543 (1990)
   PUBMED   2324090
  REMARK    GeneRIF: Generif: Phosphoglycerate kinase is a moonlighting protein
            that functions as both a glycolytic enzyme and a primer recognition
            protein of DNA polymerase alpha.
REFERENCE   10 (residues 1 to 417)
  AUTHORS   Chen,S.H., Donahue,R.P. and Scott,C.R.
  TITLE     Characterization of phosphoglycerate kinase from human spermatozoa
  JOURNAL   Fertil Steril 27 (6), 699-701 (1976)
   PUBMED   1278465
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC336483.1, BC103752.1,
            BU677171.1 and AL049589.15.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a glycolytic enzyme
            that catalyzes the conversion of 1,3-diphosphoglycerate to
            3-phosphoglycerate. The encoded protein may also act as a cofactor
            for polymerase alpha. Additionally, this protein is secreted by
            tumor cells where it participates in angiogenesis by functioning to
            reduce disulfide bonds in the serine protease, plasmin, which
            consequently leads to the release of the tumor blood vessel
            inhibitor angiostatin. The encoded protein has been identified as a
            moonlighting protein based on its ability to perform
            mechanistically distinct functions. Deficiency of the enzyme is
            associated with a wide range of clinical phenotypes hemolytic
            anemia and neurological impairment. Pseudogenes of this gene have
            been defined on chromosomes 19, 21 and the X chromosome. [provided
            by RefSeq, Jan 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.268563.1,
                                           SRR1803616.55464.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match              :: ENST00000373316.5/
                                               ENSP00000362413.4
            multifunctional gene product(s) :: PMID: 2324090, 11130727
            RefSeq Select criteria          :: based on single protein-coding
                                               transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq21.1"
     Protein         1..417
                     /product="phosphoglycerate kinase 1"
                     /EC_number="2.7.2.3"
                     /EC_number="2.7.11.1"
                     /note="primer recognition protein 2; cell
                     migration-inducing gene 10 protein; PRP 2; epididymis
                     secretory sperm binding protein Li 68p"
                     /calculated_mol_wt=44484
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P00558.3)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P00558.3)"
     Region          3..417
                     /region_name="PTZ00005"
                     /note="phosphoglycerate kinase; Provisional"
                     /db_xref="CDD:173310"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P00558.3)"
     Site            11
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P00558.3)"
     Site            order(24,26,39,63,123)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238195"
     Region          38..43
                     /region_name="Mitochondrial targeting region exposed
                     following cis-trans isomerization by PIN1 and recognized
                     by the TOM complex for mitochondrial translocation of the
                     protein. /evidence=ECO:0000269|PubMed:26942675"
                     /note="propagated from UniProtKB/Swiss-Prot (P00558.3)"
     Site            48
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P00558.3)"
     Site            75
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P00558.3)"
     Site            76
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P09411; propagated from
                     UniProtKB/Swiss-Prot (P00558.3)"
     Site            86
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P00558.3)"
     Site            91
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P09411; propagated from
                     UniProtKB/Swiss-Prot (P00558.3)"
     Site            97
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P00558.3)"
     Site            131
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P00558.3)"
     Site            146
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P00558.3)"
     Site            196
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (P00558.3)"
     Site            199
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P00558.3)"
     Site            order(201..204,392..394)
                     /site_type="other"
                     /note="hinge regions"
                     /db_xref="CDD:238195"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK1.
                     /evidence=ECO:0000269|PubMed:26942675,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P00558.3)"
     Site            order(239,313,337,339,341..344,374..376)
                     /site_type="other"
                     /note="ADP binding site [chemical binding]"
                     /db_xref="CDD:238195"
     Site            267
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P00558.3)"
     Site            291
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P00558.3)"
     Site            361
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P09411; propagated from
                     UniProtKB/Swiss-Prot (P00558.3)"
     Site            375
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:238195"
     CDS             1..417
                     /gene="PGK1"
                     /gene_synonym="HEL-S-68p; MIG10; PGKA"
                     /coded_by="NM_000291.4:94..1347"
                     /db_xref="CCDS:CCDS14438.1"
                     /db_xref="GeneID:5230"
                     /db_xref="HGNC:HGNC:8896"
                     /db_xref="MIM:311800"
ORIGIN      
        1 mslsnkltld kldvkgkrvv mrvdfnvpmk nnqitnnqri kaavpsikfc ldngaksvvl
       61 mshlgrpdgv pmpdkyslep vavelksllg kdvlflkdcv gpevekacan paagsville
      121 nlrfhveeeg kgkdasgnkv kaepakieaf raslsklgdv yvndafgtah rahssmvgvn
      181 lpqkaggflm kkelnyfaka lesperpfla ilggakvadk iqlinnmldk vnemiigggm
      241 aftflkvlnn meigtslfde egakivkdlm skaekngvki tlpvdfvtad kfdenaktgq
      301 atvasgipag wmgldcgpes skkyaeavtr akqivwngpv gvfeweafar gtkalmdevv
      361 katsrgciti igggdtatcc akwntedkvs hvstgggasl ellegkvlpg vdalsni
//
