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Protein

Phosphoglycerate mutase 2

Gene

Pgam2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 intermediateBy similarity
Binding sitei62 – 621SubstrateBy similarity
Active sitei89 – 891Proton donor/acceptorBy similarity
Binding sitei100 – 1001SubstrateBy similarity
Sitei186 – 1861Transition state stabilizerBy similarity

GO - Molecular functioni

GO - Biological processi

  • gluconeogenesis Source: Ensembl
  • glycolytic process Source: MGI
  • Notch signaling pathway Source: MGI
  • response to mercury ion Source: Ensembl
  • spermatogenesis Source: Ensembl
  • striated muscle contraction Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Isomerase

Keywords - Biological processi

Glycolysis

Enzyme and pathway databases

ReactomeiR-MMU-70171. Glycolysis.
R-MMU-70263. 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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1933118. Pgam2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 253253Phosphoglycerate mutase 2PRO_0000179830Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31PhosphothreonineBy similarity
Modified residuei14 – 141PhosphoserineBy similarity
Modified residuei118 – 1181PhosphoserineCombined sources
Modified residuei121 – 1211PhosphothreonineBy similarity
Modified residuei132 – 1321PhosphotyrosineBy similarity
Modified residuei133 – 1331PhosphotyrosineBy similarity
Modified residuei135 – 1351PhosphoserineBy similarity
Modified residuei152 – 1521PhosphothreonineBy similarity
Cross-linki195 – 195Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO70250.
PaxDbiO70250.
PRIDEiO70250.

2D gel databases

SWISS-2DPAGEO70250.

PTM databases

iPTMnetiO70250.
PhosphoSiteiO70250.
SwissPalmiO70250.

Expressioni

Tissue specificityi

Testis.1 Publication

Gene expression databases

BgeeiO70250.
CleanExiMM_PGAM2.
ExpressionAtlasiO70250. baseline and differential.
GenevisibleiO70250. MM.

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with ENO1 (PubMed:23446454).By similarity1 Publication

Protein-protein interaction databases

BioGridi207767. 2 interactions.
IntActiO70250. 2 interactions.
MINTiMINT-4107290.
STRINGi10090.ENSMUSP00000020768.

Structurei

3D structure databases

ProteinModelPortaliO70250.
SMRiO70250. Positions 4-245.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni10 – 178Substrate bindingBy similarity
Regioni23 – 242Substrate bindingBy similarity
Regioni89 – 924Substrate bindingBy similarity
Regioni116 – 1172Substrate bindingBy similarity
Regioni187 – 1882Substrate bindingBy similarity

Compositional bias

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0235. Eukaryota.
COG0588. LUCA.
HOGENOMiHOG000221682.
HOVERGENiHBG027528.
InParanoidiO70250.
KOiK01834.
OMAiMSDAAIM.
OrthoDBiEOG7XM2ZV.
PhylomeDBiO70250.
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. 2 hits.
[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.

O70250-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTHRLVMVR HGESLWNQEN RFCGWFDAEL SEKGAEEAKR GATAIKDAKI
60 70 80 90 100
EFDICYTSVL KRAIRTLWTI LDVTDQMWVP VVRTWRLNER HYGGLTGLNK
110 120 130 140 150
AETAAKHGEE QVKIWRRSFD TPPPPMDEKH NYYTSISKDR RYAGLKPEEL
160 170 180 190 200
PTCESLKDTI ARALPFWNEE IAPKIKAGQR VLIAAHGNSL RGIVKHLEGM
210 220 230 240 250
SDQAIMELNL PTGIPIVYEL DQNLKPTKPM RFLGDEETVR KAMEAVAAQG

KAK
Length:253
Mass (Da):28,827
Last modified:January 23, 2007 - v3
Checksum:i477AF9EC59A15B86
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF029843 mRNA. Translation: AAC13263.1.
AF317587 Genomic DNA. Translation: AAK06662.1.
BC010750 mRNA. Translation: AAH10750.1.
CCDSiCCDS24404.1.
RefSeqiNP_061358.1. NM_018870.3.
UniGeneiMm.219627.

Genome annotation databases

EnsembliENSMUST00000020768; ENSMUSP00000020768; ENSMUSG00000020475.
GeneIDi56012.
KEGGimmu:56012.
UCSCiuc007hxe.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF029843 mRNA. Translation: AAC13263.1.
AF317587 Genomic DNA. Translation: AAK06662.1.
BC010750 mRNA. Translation: AAH10750.1.
CCDSiCCDS24404.1.
RefSeqiNP_061358.1. NM_018870.3.
UniGeneiMm.219627.

3D structure databases

ProteinModelPortaliO70250.
SMRiO70250. Positions 4-245.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207767. 2 interactions.
IntActiO70250. 2 interactions.
MINTiMINT-4107290.
STRINGi10090.ENSMUSP00000020768.

PTM databases

iPTMnetiO70250.
PhosphoSiteiO70250.
SwissPalmiO70250.

2D gel databases

SWISS-2DPAGEO70250.

Proteomic databases

EPDiO70250.
PaxDbiO70250.
PRIDEiO70250.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020768; ENSMUSP00000020768; ENSMUSG00000020475.
GeneIDi56012.
KEGGimmu:56012.
UCSCiuc007hxe.2. mouse.

Organism-specific databases

CTDi5224.
MGIiMGI:1933118. Pgam2.

Phylogenomic databases

eggNOGiKOG0235. Eukaryota.
COG0588. LUCA.
HOGENOMiHOG000221682.
HOVERGENiHBG027528.
InParanoidiO70250.
KOiK01834.
OMAiMSDAAIM.
OrthoDBiEOG7XM2ZV.
PhylomeDBiO70250.
TreeFamiTF300007.

Enzyme and pathway databases

ReactomeiR-MMU-70171. Glycolysis.
R-MMU-70263. Gluconeogenesis.

Miscellaneous databases

ChiTaRSiPgam2. mouse.
NextBioi311738.
PROiO70250.
SOURCEiSearch...

Gene expression databases

BgeeiO70250.
CleanExiMM_PGAM2.
ExpressionAtlasiO70250. baseline and differential.
GenevisibleiO70250. MM.

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. 2 hits.
[Graphical view]
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 1 hit.
TIGRFAMsiTIGR01258. pgm_1. 1 hit.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression analysis of a mouse gene coding phosphoglycerate mutase muscle-specific subunit."
    Wu G., Yu L., Tu Q., Jiang Y., Fan Y., Zhao S.
    Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Mouse phosphoglycerate mutase M and B isozymes: cDNA cloning, enzyme activity assay and mapping."
    Zhang J., Yu L., Fu Q., Gao J., Xie Y., Chen J., Zhang P., Liu Q., Zhao S.
    Gene 264:273-279(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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: Kidney.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney, Lung and Testis.
  5. "Disruption of a spermatogenic cell-specific mouse enolase 4 (eno4) gene causes sperm structural defects and male infertility."
    Nakamura N., Dai Q., Williams J., Goulding E.H., Willis W.D., Brown P.R., Eddy E.M.
    Biol. Reprod. 88:90-90(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ENO1, TISSUE SPECIFICITY.

Entry informationi

Entry nameiPGAM2_MOUSE
AccessioniPrimary (citable) accession number: O70250
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 144 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.