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P15259 (PGAM2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PGAM2
Synonyms:PGAMM
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length253 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_01039

Catalytic activity

2-phospho-D-glycerate = 3-phospho-D-glycerate. HAMAP-Rule MF_01039

3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate. HAMAP-Rule MF_01039

2,3-bisphospho-D-glycerate + H2O = 3-phospho-D-glycerate + phosphate. HAMAP-Rule MF_01039

Subunit structure

Homodimer.

Tissue specificity

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

Involvement in disease

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. Ref.6 Ref.7

Sequence similarities

Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.

Ontologies

Keywords
   Biological processGlycolysis
   DiseaseDisease mutation
Glycogen storage disease
   Molecular functionHydrolase
Isomerase
   PTMIsopeptide bond
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Traceable author statement. Source: Reactome

gluconeogenesis

Traceable author statement. Source: Reactome

glucose metabolic process

Traceable author statement. Source: Reactome

glycolysis

Inferred from mutant phenotype PubMed 6262916. Source: UniProtKB

response to mercury ion

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

striated muscle contraction

Inferred from mutant phenotype PubMed 6262916. Source: UniProtKB

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

nucleus

Inferred from electronic annotation. Source: Ensembl

   Molecular_function2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity

Inferred from electronic annotation. Source: Ensembl

bisphosphoglycerate 2-phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

bisphosphoglycerate mutase activity

Inferred from electronic annotation. Source: UniProtKB-EC

cofactor binding

Inferred from electronic annotation. Source: Ensembl

phosphoglycerate mutase activity

Inferred from mutant phenotype PubMed 6262916. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 253253Phosphoglycerate mutase 2 HAMAP-Rule MF_01039
PRO_0000179829

Regions

Compositional bias122 – 1254Poly-Pro HAMAP-Rule MF_01039

Sites

Active site111Tele-phosphohistidine intermediate
Active site1861
Site621Interaction with carboxyl group of phosphoglycerates

Amino acid modifications

Cross-link179Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.5
Cross-link195Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.5

Natural variations

Natural variant891E → A in GSD10. Ref.6
VAR_006088
Natural variant901R → W in GSD10. Ref.6
VAR_006089
Natural variant971G → D in GSD10. Ref.7
VAR_013103

Experimental info

Sequence conflict141S → T in AAA60072. Ref.3
Sequence conflict651R → P in AAA60073. Ref.2
Sequence conflict851W → C Ref.2
Sequence conflict871L → F Ref.2
Sequence conflict871L → F Ref.3
Sequence conflict981L → F in AAA60072. Ref.3
Sequence conflict113 – 1142KI → RS in AAA60072. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P15259 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 0FDC97631104FCF7

FASTA25328,766
        10         20         30         40         50         60 
MATHRLVMVR HGESTWNQEN RFCGWFDAEL SEKGTEEAKR GAKAIKDAKM EFDICYTSVL 

        70         80         90        100        110        120 
KRAIRTLWAI LDGTDQMWLP VVRTWRLNER HYGGLTGLNK AETAAKHGEE QVKIWRRSFD 

       130        140        150        160        170        180 
IPPPPMDEKH PYYNSISKER RYAGLKPGEL PTCESLKDTI ARALPFWNEE IVPQIKAGKR 

       190        200        210        220        230        240 
VLIAAHGNSL RGIVKHLEGM SDQAIMELNL PTGIPIVYEL NKELKPTKPM QFLGDEETVR 

       250 
KAMEAVAAQG KAK 

« Hide

References

« Hide 'large scale' references
[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.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRPMHUYM. JQ0750.
RefSeqNP_000281.2. NM_000290.3.
UniGeneHs.632642.

3D structure databases

ProteinModelPortalP15259.
SMRP15259. Positions 4-245.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111245. 3 interactions.
IntActP15259. 4 interactions.
STRING9606.ENSP00000297283.

PTM databases

PhosphoSiteP15259.

Polymorphism databases

DMDM130353.

2D gel databases

UCD-2DPAGEP15259.

Proteomic databases

PaxDbP15259.
PeptideAtlasP15259.
PRIDEP15259.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000297283; ENSP00000297283; ENSG00000164708.
GeneID5224.
KEGGhsa:5224.
UCSCuc003tjs.3. human.

Organism-specific databases

CTD5224.
GeneCardsGC07M044102.
HGNCHGNC:8889. PGAM2.
MIM261670. phenotype.
612931. gene.
neXtProtNX_P15259.
Orphanet97234. Glycogen storage disease due to phosphoglycerate mutase deficiency.
PharmGKBPA33226.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0588.
HOGENOMHOG000221682.
HOVERGENHBG027528.
InParanoidP15259.
KOK01834.
OMANDEIAPQ.
OrthoDBEOG7XM2ZV.
PhylomeDBP15259.
TreeFamTF300007.

Enzyme and pathway databases

BioCycMetaCyc:HS09121-MONOMER.
ReactomeREACT_111217. Metabolism.

Gene expression databases

BgeeP15259.
CleanExHS_PGAM2.
GenevestigatorP15259.

Family and domain databases

HAMAPMF_01039. PGAM_GpmA.
InterProIPR013078. His_Pase_superF_clade-1.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]
PANTHERPTHR11931. PTHR11931. 1 hit.
PfamPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTSM00855. PGAM. 1 hit.
[Graphical view]
TIGRFAMsTIGR01258. pgm_1. 1 hit.
PROSITEPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi5224.
NextBio20196.
PROP15259.
SOURCESearch...

Entry information

Entry namePGAM2_HUMAN
AccessionPrimary (citable) accession number: P15259
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 153 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM