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P15259

- PGAM2_HUMAN

UniProt

P15259 - PGAM2_HUMAN

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Protein

Phosphoglycerate mutase 2

Gene
PGAM2, PGAMM
Organism
Homo sapiens (Human)
Status
Reviewed - 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.UniRule annotation

Catalytic activityi

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

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
Complete GO annotation...

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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 2UniRule annotationPRO_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.

Family & Domainsi

Compositional bias

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

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141S → T in AAA60072. 1 Publication
Sequence conflicti65 – 651R → P in AAA60073. 1 Publication
Sequence conflicti85 – 851W → C1 Publication
Sequence conflicti87 – 871L → F1 Publication
Sequence conflicti87 – 871L → F1 Publication
Sequence conflicti98 – 981L → F in AAA60072. 1 Publication
Sequence conflicti113 – 1142KI → RS in AAA60072. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 157 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

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