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P18669

- PGAM1_HUMAN

UniProt

P18669 - PGAM1_HUMAN

Protein

Phosphoglycerate mutase 1

Gene

PGAM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 175 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase) and EC 3.1.3.13 (phosphatase), but with a reduced activity.

    Catalytic activityi

    2-phospho-D-glycerate = 3-phospho-D-glycerate.
    3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate.
    2,3-bisphospho-D-glycerate + H2O = 3-phospho-D-glycerate + phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei11 – 111Tele-phosphohistidine intermediate
    Sitei62 – 621Interaction with carboxyl group of phosphoglycerates
    Active sitei186 – 1861

    GO - Molecular functioni

    1. bisphosphoglycerate 2-phosphatase activity Source: UniProtKB-EC
    2. bisphosphoglycerate mutase activity Source: UniProtKB-EC
    3. phosphoglycerate mutase activity Source: UniProtKB
    4. protein binding Source: IntAct
    5. protein kinase binding Source: UniProtKB

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. gluconeogenesis Source: Reactome
    3. glucose metabolic process Source: Reactome
    4. glycolytic process Source: UniProt
    5. regulation of glycolytic process Source: UniProtKB
    6. regulation of pentose-phosphate shunt Source: UniProtKB
    7. respiratory burst Source: UniProtKB
    8. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Isomerase

    Keywords - Biological processi

    Glycolysis

    Enzyme and pathway databases

    BioCyciMetaCyc:HS10286-MONOMER.
    ReactomeiREACT_1383. Glycolysis.
    REACT_1520. Gluconeogenesis.
    SABIO-RKP18669.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoglycerate mutase 1 (EC:3.1.3.13, EC:5.4.2.11, EC:5.4.2.4)
    Alternative name(s):
    BPG-dependent PGAM 1
    Phosphoglycerate mutase isozyme B
    Short name:
    PGAM-B
    Gene namesi
    Name:PGAM1
    Synonyms:PGAMA
    ORF Names:CDABP0006
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:8888. PGAM1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProt
    2. cytosol Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. membrane Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33225.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 254253Phosphoglycerate mutase 1PRO_0000179825Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei14 – 141Phosphoserine3 Publications
    Modified residuei26 – 261PhosphotyrosineBy similarity
    Modified residuei31 – 311Phosphoserine1 Publication
    Modified residuei106 – 1061N6-acetyllysineBy similarity
    Modified residuei251 – 2511N6-acetyllysine; alternate1 Publication
    Modified residuei251 – 2511N6-succinyllysine; alternateBy similarity
    Modified residuei253 – 2531N6-acetyllysine1 Publication
    Modified residuei254 – 2541N6-acetyllysine1 Publication

    Post-translational modificationi

    Acetylated at Lys-253, Lys-253 and Lys-254 under high glucose condition. Acetylation increases catalytic activity. Under glucose restriction SIRT1 levels dramatically increase and it deacetylates the enzyme.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP18669.
    PaxDbiP18669.
    PRIDEiP18669.

    2D gel databases

    DOSAC-COBS-2DPAGEP18669.
    OGPiP18669.
    SWISS-2DPAGEP18669.
    UCD-2DPAGEP18669.

    PTM databases

    PhosphoSiteiP18669.

    Expressioni

    Tissue specificityi

    In mammalian tissues there are two types of phosphoglycerate mutase isozymes: type-M in muscles and type-B in other tissues.

    Gene expression databases

    BgeeiP18669.
    CleanExiHS_PGAM1.
    GenevestigatoriP18669.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PCNAP120042EBI-717905,EBI-358311

    Protein-protein interaction databases

    BioGridi111244. 18 interactions.
    IntActiP18669. 12 interactions.
    MINTiMINT-3008987.
    STRINGi9606.ENSP00000359991.

    Structurei

    Secondary structure

    1
    254
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 107
    Turni15 – 206
    Helixi32 – 4716
    Beta strandi53 – 575
    Helixi61 – 7313
    Beta strandi81 – 833
    Helixi85 – 873
    Helixi93 – 953
    Helixi100 – 1078
    Helixi109 – 1179
    Helixi133 – 1375
    Helixi140 – 1423
    Turni147 – 1493
    Helixi156 – 17015
    Helixi172 – 1765
    Beta strandi181 – 1855
    Helixi187 – 19812
    Helixi202 – 2076
    Beta strandi212 – 2143
    Beta strandi216 – 2205
    Beta strandi226 – 2283
    Helixi236 – 2427

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1LJDmodel-A1-254[»]
    1YFKX-ray2.70A/B1-254[»]
    1YJXX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L1-254[»]
    4GPIX-ray2.08B/C1-254[»]
    4GPZX-ray1.65A/B1-254[»]
    ProteinModelPortaliP18669.
    SMRiP18669. Positions 2-243.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP18669.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi122 – 13110Pro-rich

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0588.
    HOGENOMiHOG000221682.
    HOVERGENiHBG027528.
    InParanoidiP18669.
    KOiK01834.
    OMAiIKEWRRS.
    OrthoDBiEOG7XM2ZV.
    PhylomeDBiP18669.
    TreeFamiTF300007.

    Family and domain databases

    Gene3Di3.40.50.1240. 1 hit.
    HAMAPiMF_01039. PGAM_GpmA.
    InterProiIPR013078. His_Pase_superF_clade-1.
    IPR029033. His_PPase_superfam.
    IPR001345. PG/BPGM_mutase_AS.
    IPR005952. Phosphogly_mut1.
    [Graphical view]
    PANTHERiPTHR11931. PTHR11931. 1 hit.
    PfamiPF00300. His_Phos_1. 1 hit.
    [Graphical view]
    SMARTiSM00855. PGAM. 1 hit.
    [Graphical view]
    SUPFAMiSSF53254. SSF53254. 1 hit.
    TIGRFAMsiTIGR01258. pgm_1. 1 hit.
    PROSITEiPS00175. PG_MUTASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P18669-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAYKLVLIR HGESAWNLEN RFSGWYDADL SPAGHEEAKR GGQALRDAGY    50
    EFDICFTSVQ KRAIRTLWTV LDAIDQMWLP VVRTWRLNER HYGGLTGLNK 100
    AETAAKHGEA QVKIWRRSYD VPPPPMEPDH PFYSNISKDR RYADLTEDQL 150
    PSCESLKDTI ARALPFWNEE IVPQIKEGKR VLIAAHGNSL RGIVKHLEGL 200
    SEEAIMELNL PTGIPIVYEL DKNLKPIKPM QFLGDEETVR KAMEAVAAQG 250
    KAKK 254
    Length:254
    Mass (Da):28,804
    Last modified:January 23, 2007 - v2
    Checksum:i6DC0852BEBB22409
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04173 mRNA. Translation: AAA60071.1.
    AY007118 mRNA. Translation: AAG01990.1.
    BC010038 mRNA. Translation: AAH10038.1.
    BC011678 mRNA. Translation: AAH11678.1.
    BC053356 mRNA. Translation: AAH53356.1.
    BC066959 mRNA. Translation: AAH66959.1.
    BC073742 mRNA. Translation: AAH73742.1.
    CCDSiCCDS7458.1.
    PIRiA31782. PMHUYB.
    RefSeqiNP_002620.1. NM_002629.2.
    UniGeneiHs.632918.

    Genome annotation databases

    EnsembliENST00000334828; ENSP00000359991; ENSG00000171314.
    GeneIDi5223.
    KEGGihsa:5223.
    UCSCiuc001knh.3. human.

    Polymorphism databases

    DMDMi130348.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04173 mRNA. Translation: AAA60071.1 .
    AY007118 mRNA. Translation: AAG01990.1 .
    BC010038 mRNA. Translation: AAH10038.1 .
    BC011678 mRNA. Translation: AAH11678.1 .
    BC053356 mRNA. Translation: AAH53356.1 .
    BC066959 mRNA. Translation: AAH66959.1 .
    BC073742 mRNA. Translation: AAH73742.1 .
    CCDSi CCDS7458.1.
    PIRi A31782. PMHUYB.
    RefSeqi NP_002620.1. NM_002629.2.
    UniGenei Hs.632918.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1LJD model - A 1-254 [» ]
    1YFK X-ray 2.70 A/B 1-254 [» ]
    1YJX X-ray 2.80 A/B/C/D/E/F/G/H/I/J/K/L 1-254 [» ]
    4GPI X-ray 2.08 B/C 1-254 [» ]
    4GPZ X-ray 1.65 A/B 1-254 [» ]
    ProteinModelPortali P18669.
    SMRi P18669. Positions 2-243.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111244. 18 interactions.
    IntActi P18669. 12 interactions.
    MINTi MINT-3008987.
    STRINGi 9606.ENSP00000359991.

    PTM databases

    PhosphoSitei P18669.

    Polymorphism databases

    DMDMi 130348.

    2D gel databases

    DOSAC-COBS-2DPAGE P18669.
    OGPi P18669.
    SWISS-2DPAGE P18669.
    UCD-2DPAGE P18669.

    Proteomic databases

    MaxQBi P18669.
    PaxDbi P18669.
    PRIDEi P18669.

    Protocols and materials databases

    DNASUi 5223.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000334828 ; ENSP00000359991 ; ENSG00000171314 .
    GeneIDi 5223.
    KEGGi hsa:5223.
    UCSCi uc001knh.3. human.

    Organism-specific databases

    CTDi 5223.
    GeneCardsi GC10P099176.
    H-InvDB HIX0036336.
    HIX0120028.
    HGNCi HGNC:8888. PGAM1.
    MIMi 172250. gene.
    neXtProti NX_P18669.
    PharmGKBi PA33225.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0588.
    HOGENOMi HOG000221682.
    HOVERGENi HBG027528.
    InParanoidi P18669.
    KOi K01834.
    OMAi IKEWRRS.
    OrthoDBi EOG7XM2ZV.
    PhylomeDBi P18669.
    TreeFami TF300007.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS10286-MONOMER.
    Reactomei REACT_1383. Glycolysis.
    REACT_1520. Gluconeogenesis.
    SABIO-RK P18669.

    Miscellaneous databases

    ChiTaRSi PGAM1. human.
    EvolutionaryTracei P18669.
    GenomeRNAii 5223.
    NextBioi 20192.
    PROi P18669.
    SOURCEi Search...

    Gene expression databases

    Bgeei P18669.
    CleanExi HS_PGAM1.
    Genevestigatori P18669.

    Family and domain databases

    Gene3Di 3.40.50.1240. 1 hit.
    HAMAPi MF_01039. PGAM_GpmA.
    InterProi IPR013078. His_Pase_superF_clade-1.
    IPR029033. His_PPase_superfam.
    IPR001345. PG/BPGM_mutase_AS.
    IPR005952. Phosphogly_mut1.
    [Graphical view ]
    PANTHERi PTHR11931. PTHR11931. 1 hit.
    Pfami PF00300. His_Phos_1. 1 hit.
    [Graphical view ]
    SMARTi SM00855. PGAM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53254. SSF53254. 1 hit.
    TIGRFAMsi TIGR01258. pgm_1. 1 hit.
    PROSITEi PS00175. PG_MUTASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation of a cDNA encoding the B isozyme of human phosphoglycerate mutase (PGAM) and characterization of the PGAM gene family."
      Sakoda S., Shanske S., Dimauro S., Schon E.A.
      J. Biol. Chem. 263:16899-16905(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Pediatric leukemia cDNA sequencing project."
      Zhou J., Yu W., Tang H., Mei G., Tsang Y.T.M., Bouck J., Gibbs R.A., Margolin J.F.
      Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Leukemia.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain, Liver, Lymph, Skin and Uterus.
    4. "Sequence of the human erythrocyte phosphoglycerate mutase by microsequencer and mass spectrometry."
      Blouquit Y., Calvin M.C., Rosa R., Prome D., Prome J.-C., Pratbernou F., Cohen-Solal M., Rosa J.
      J. Biol. Chem. 263:16906-16910(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-254, CLEAVAGE OF INITIATOR METHIONINE.
    5. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 11-39; 47-61; 91-100; 118-138; 142-157; 163-176; 181-191 AND 223-240, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    6. "Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2."
      Rasmussen R.K., Ji H., Eddes J.S., Moritz R.L., Reid G.E., Simpson R.J., Dorow D.S.
      Electrophoresis 18:588-598(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 91-100.
      Tissue: Mammary carcinoma.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Regulation of glycolytic enzyme phosphoglycerate mutase-1 by Sirt1 protein-mediated deacetylation."
      Hallows W.C., Yu W., Denu J.M.
      J. Biol. Chem. 287:3850-3858(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-251; LYS-253 AND LYS-254, DEACETYLATION BY SIRT1.
    13. "Crystal structure of human B-type phosphoglycerate mutase bound with citrate."
      Wang Y., Wei Z., Liu L., Cheng Z., Lin Y., Ji F., Gong W.
      Biochem. Biophys. Res. Commun. 331:1207-1215(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH CITRATE, SUBUNIT.

    Entry informationi

    Entry nameiPGAM1_HUMAN
    AccessioniPrimary (citable) accession number: P18669
    Secondary accession number(s): Q9BWC0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 175 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3