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Protein

Phosphoglycerate mutase 2

Gene

Pgam2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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 intermediate
Sitei62 – 621Interaction with carboxyl group of phosphoglycerates
Active sitei186 – 1861

GO - Molecular functioni

  1. 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity Source: RGD
  2. bisphosphoglycerate 2-phosphatase activity Source: UniProtKB-EC
  3. bisphosphoglycerate mutase activity Source: UniProtKB-EC
  4. cofactor binding Source: RGD
  5. phosphoglycerate mutase activity Source: RGD

GO - Biological processi

  1. gluconeogenesis Source: RGD
  2. glycolytic process Source: UniProtKB-KW
  3. response to inorganic substance Source: RGD
  4. response to mercury ion Source: RGD
  5. spermatogenesis Source: RGD
  6. striated muscle contraction Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Isomerase

Keywords - Biological processi

Glycolysis

Enzyme and pathway databases

ReactomeiREACT_217998. Gluconeogenesis.
REACT_225694. Glycolysis.
SABIO-RKP16290.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 14

Organism-specific databases

RGDi3313. Pgam2.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: RGD
  2. nucleus Source: RGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 253253Phosphoglycerate mutase 2PRO_0000179831Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

PaxDbiP16290.
PRIDEiP16290.

PTM databases

PhosphoSiteiP16290.

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

GenevestigatoriP16290.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

IntActiP16290. 7 interactions.
MINTiMINT-4588391.
STRINGi10116.ENSRNOP00000018227.

Structurei

3D structure databases

ProteinModelPortaliP16290.
SMRiP16290. Positions 2-246.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0588.
GeneTreeiENSGT00390000016700.
HOGENOMiHOG000221682.
HOVERGENiHBG027528.
InParanoidiP16290.
KOiK01834.
OMAiDEIAPQI.
OrthoDBiEOG7XM2ZV.
PhylomeDBiP16290.
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.

P16290-1 [UniParc]FASTAAdd to Basket

« Hide

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

KAK
Length:253
Mass (Da):28,755
Last modified:January 23, 2007 - v2
Checksum:i73F6118A1C73D545
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31835 mRNA. Translation: AAA41835.1.
Z17319 Genomic DNA. Translation: CAA78967.1.
PIRiA33793. PMRTYM.
RefSeqiNP_059024.1. NM_017328.2.
UniGeneiRn.9738.

Genome annotation databases

EnsembliENSRNOT00000018227; ENSRNOP00000018227; ENSRNOG00000013532.
GeneIDi24959.
KEGGirno:24959.
UCSCiRGD:3313. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31835 mRNA. Translation: AAA41835.1.
Z17319 Genomic DNA. Translation: CAA78967.1.
PIRiA33793. PMRTYM.
RefSeqiNP_059024.1. NM_017328.2.
UniGeneiRn.9738.

3D structure databases

ProteinModelPortaliP16290.
SMRiP16290. Positions 2-246.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP16290. 7 interactions.
MINTiMINT-4588391.
STRINGi10116.ENSRNOP00000018227.

PTM databases

PhosphoSiteiP16290.

Proteomic databases

PaxDbiP16290.
PRIDEiP16290.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000018227; ENSRNOP00000018227; ENSRNOG00000013532.
GeneIDi24959.
KEGGirno:24959.
UCSCiRGD:3313. rat.

Organism-specific databases

CTDi5224.
RGDi3313. Pgam2.

Phylogenomic databases

eggNOGiCOG0588.
GeneTreeiENSGT00390000016700.
HOGENOMiHOG000221682.
HOVERGENiHBG027528.
InParanoidiP16290.
KOiK01834.
OMAiDEIAPQI.
OrthoDBiEOG7XM2ZV.
PhylomeDBiP16290.
TreeFamiTF300007.

Enzyme and pathway databases

ReactomeiREACT_217998. Gluconeogenesis.
REACT_225694. Glycolysis.
SABIO-RKP16290.

Miscellaneous databases

NextBioi604991.
PROiP16290.

Gene expression databases

GenevestigatoriP16290.

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]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Skeletal muscle.
  2. "The gene encoding rat phosphoglycerate mutase subunit M: cloning and promoter analysis in skeletal muscle cells."
    Ruiz-Lozano P., de Lecea L., Buesa C., Perez de la Osa P., Lepage D., Gualberto A., Walsh K., Pons G.
    Gene 147:243-248(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiPGAM2_RAT
AccessioniPrimary (citable) accession number: P16290
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 126 of the entry and version 2 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.