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P15259

- PGAM2_HUMAN

UniProt

P15259 - PGAM2_HUMAN

Protein

Phosphoglycerate mutase 2

Gene

PGAM2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 3 (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. 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity Source: Ensembl
    2. bisphosphoglycerate 2-phosphatase activity Source: UniProtKB-EC
    3. bisphosphoglycerate mutase activity Source: UniProtKB-EC
    4. cofactor binding Source: Ensembl
    5. phosphoglycerate mutase activity 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: UniProtKB
    5. response to mercury ion Source: Ensembl
    6. small molecule metabolic process Source: Reactome
    7. spermatogenesis Source: Ensembl
    8. striated muscle contraction Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Isomerase

    Keywords - Biological processi

    Glycolysis

    Enzyme and pathway databases

    BioCyciMetaCyc:HS09121-MONOMER.
    ReactomeiREACT_1383. Glycolysis.
    REACT_1520. Gluconeogenesis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoglycerate mutase 2 (EC:3.1.3.13, EC:5.4.2.11, EC:5.4.2.4)
    Alternative name(s):
    BPG-dependent PGAM 2
    Muscle-specific phosphoglycerate mutase
    Phosphoglycerate mutase isozyme M
    Short name:
    PGAM-M
    Gene namesi
    Name:PGAM2
    Synonyms:PGAMM
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:8889. PGAM2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nucleus Source: UniProt

    Pathology & Biotechi

    Involvement in diseasei

    Glycogen storage disease 10 (GSD10) [MIM:261670]: A metabolic disorder characterized by myoglobinuria, increased serum creatine kinase levels, decreased phosphoglycerate mutase activity, myalgia, muscle pain, muscle cramps, exercise intolerance.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti89 – 891E → A in GSD10. 1 Publication
    VAR_006088
    Natural varianti90 – 901R → W in GSD10. 1 Publication
    VAR_006089
    Natural varianti97 – 971G → D in GSD10. 1 Publication
    VAR_013103

    Keywords - Diseasei

    Disease mutation, Glycogen storage disease

    Organism-specific databases

    MIMi261670. phenotype.
    Orphaneti97234. Glycogen storage disease due to phosphoglycerate mutase deficiency.
    PharmGKBiPA33226.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 253253Phosphoglycerate mutase 2PRO_0000179829Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki179 – 179Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki195 – 195Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

    Keywords - PTMi

    Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiP15259.
    PaxDbiP15259.
    PeptideAtlasiP15259.
    PRIDEiP15259.

    2D gel databases

    UCD-2DPAGEP15259.

    PTM databases

    PhosphoSiteiP15259.

    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

    BgeeiP15259.
    CleanExiHS_PGAM2.
    GenevestigatoriP15259.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi111245. 4 interactions.
    IntActiP15259. 4 interactions.
    STRINGi9606.ENSP00000297283.

    Structurei

    3D structure databases

    ProteinModelPortaliP15259.
    SMRiP15259. Positions 4-245.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi122 – 1254Poly-Pro

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0588.
    HOGENOMiHOG000221682.
    HOVERGENiHBG027528.
    InParanoidiP15259.
    KOiK01834.
    OMAiWTILEGT.
    OrthoDBiEOG7XM2ZV.
    PhylomeDBiP15259.
    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.

    P15259-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATHRLVMVR HGESTWNQEN RFCGWFDAEL SEKGTEEAKR GAKAIKDAKM    50
    EFDICYTSVL KRAIRTLWAI LDGTDQMWLP VVRTWRLNER HYGGLTGLNK 100
    AETAAKHGEE QVKIWRRSFD IPPPPMDEKH PYYNSISKER RYAGLKPGEL 150
    PTCESLKDTI ARALPFWNEE IVPQIKAGKR VLIAAHGNSL RGIVKHLEGM 200
    SDQAIMELNL PTGIPIVYEL NKELKPTKPM QFLGDEETVR KAMEAVAAQG 250
    KAK 253
    Length:253
    Mass (Da):28,766
    Last modified:January 23, 2007 - v3
    Checksum:i0FDC97631104FCF7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti14 – 141S → T in AAA60072. (PubMed:2822696)Curated
    Sequence conflicti65 – 651R → P in AAA60073. (PubMed:2549058)Curated
    Sequence conflicti85 – 851W → C(PubMed:2549058)Curated
    Sequence conflicti87 – 871L → F(PubMed:2549058)Curated
    Sequence conflicti87 – 871L → F(PubMed:2822696)Curated
    Sequence conflicti98 – 981L → F in AAA60072. (PubMed:2822696)Curated
    Sequence conflicti113 – 1142KI → RS in AAA60072. (PubMed:2822696)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti89 – 891E → A in GSD10. 1 Publication
    VAR_006088
    Natural varianti90 – 901R → W in GSD10. 1 Publication
    VAR_006089
    Natural varianti97 – 971G → D in GSD10. 1 Publication
    VAR_013103

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M55674, M55673 Genomic DNA. Translation: AAA64238.1.
    J05073 Genomic DNA. Translation: AAA60073.1.
    M18172 mRNA. Translation: AAA60072.1.
    BC001904 mRNA. Translation: AAH01904.1.
    BC073741 mRNA. Translation: AAH73741.1.
    CCDSiCCDS34624.1.
    PIRiJQ0750. PMHUYM.
    RefSeqiNP_000281.2. NM_000290.3.
    UniGeneiHs.632642.

    Genome annotation databases

    EnsembliENST00000297283; ENSP00000297283; ENSG00000164708.
    GeneIDi5224.
    KEGGihsa:5224.
    UCSCiuc003tjs.3. human.

    Polymorphism databases

    DMDMi130353.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M55674 , M55673 Genomic DNA. Translation: AAA64238.1 .
    J05073 Genomic DNA. Translation: AAA60073.1 .
    M18172 mRNA. Translation: AAA60072.1 .
    BC001904 mRNA. Translation: AAH01904.1 .
    BC073741 mRNA. Translation: AAH73741.1 .
    CCDSi CCDS34624.1.
    PIRi JQ0750. PMHUYM.
    RefSeqi NP_000281.2. NM_000290.3.
    UniGenei Hs.632642.

    3D structure databases

    ProteinModelPortali P15259.
    SMRi P15259. Positions 4-245.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111245. 4 interactions.
    IntActi P15259. 4 interactions.
    STRINGi 9606.ENSP00000297283.

    PTM databases

    PhosphoSitei P15259.

    Polymorphism databases

    DMDMi 130353.

    2D gel databases

    UCD-2DPAGE P15259.

    Proteomic databases

    MaxQBi P15259.
    PaxDbi P15259.
    PeptideAtlasi P15259.
    PRIDEi P15259.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000297283 ; ENSP00000297283 ; ENSG00000164708 .
    GeneIDi 5224.
    KEGGi hsa:5224.
    UCSCi uc003tjs.3. human.

    Organism-specific databases

    CTDi 5224.
    GeneCardsi GC07M044102.
    HGNCi HGNC:8889. PGAM2.
    MIMi 261670. phenotype.
    612931. gene.
    neXtProti NX_P15259.
    Orphaneti 97234. Glycogen storage disease due to phosphoglycerate mutase deficiency.
    PharmGKBi PA33226.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0588.
    HOGENOMi HOG000221682.
    HOVERGENi HBG027528.
    InParanoidi P15259.
    KOi K01834.
    OMAi WTILEGT.
    OrthoDBi EOG7XM2ZV.
    PhylomeDBi P15259.
    TreeFami TF300007.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS09121-MONOMER.
    Reactomei REACT_1383. Glycolysis.
    REACT_1520. Gluconeogenesis.

    Miscellaneous databases

    GenomeRNAii 5224.
    NextBioi 20196.
    PROi P15259.
    SOURCEi Search...

    Gene expression databases

    Bgeei P15259.
    CleanExi HS_PGAM2.
    Genevestigatori P15259.

    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 and characterization of the gene encoding the muscle-specific isozyme of human phosphoglycerate mutase."
      Castella-Escola J., Ojcius D.M., Leboulch P., Joulin V., Blouquit Y., Garel M.-C., Valentin C., Rosa R., Climent-Romeo F., Cohen-Solal M.
      Gene 91:225-232(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Structure of the gene encoding the muscle-specific subunit of human phosphoglycerate mutase."
      Tsujino S., Sakoda S., Mizuno R., Kobayashi T., Suzuki T., Kishimoto S., Shanske S., Dimauro S., Schon E.A.
      J. Biol. Chem. 264:15334-15337(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Isolation of a cDNA encoding the muscle-specific subunit of human phosphoglycerate mutase."
      Shanske S., Sakoda S., Hermodson M.A., Dimauro S., Schon E.A.
      J. Biol. Chem. 262:14612-14617(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "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: Lung.
    5. "Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
      Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
      Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-179 AND LYS-195.
      Tissue: Mammary cancer.
    6. "The molecular genetic basis of muscle phosphoglycerate mutase (PGAM) deficiency."
      Tsujino S., Shanske S., Sakoda S., Fenichel G., Dimauro S.
      Am. J. Hum. Genet. 52:472-477(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GSD10 ALA-89 AND TRP-90.
    7. "Manifesting heterozygotes in a Japanese family with a novel mutation in the muscle-specific phosphoglycerate mutase (PGAM-M) gene."
      Hadjigeorgiou G.M., Kawashima N., Bruno C., Andreu A.L., Sue C.M., Rigden D.J., Kawashima A., Shanske S., DiMauro S.
      Neuromuscul. Disord. 9:399-402(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GSD10 ASP-97.

    Entry informationi

    Entry nameiPGAM2_HUMAN
    AccessioniPrimary (citable) accession number: P15259
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 158 of the entry and version 3 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3