P15259 (PGAM2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphoglycerate mutase 2
EC=3.1.3.13
EC=5.4.2.1
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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	253 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
Catalytic activity	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.
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 process	Glycolysis
Disease	Disease mutation Glycogen storage disease
Molecular function	Hydrolase Isomerase
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	gluconeogenesis Traceable author statement. Source: Reactome glycolysis Inferred from mutant phenotype PubMed 6262916. Source: UniProtKB response to mercury ion Inferred from electronic annotation. Source: Compara small molecule metabolic process Traceable author statement. Source: Reactome spermatogenesis Inferred from electronic annotation. Source: Compara striated muscle contraction Inferred from mutant phenotype PubMed 6262916. Source: UniProtKB
Cellular_component	cytosol Traceable author statement. Source: Reactome nucleus Inferred from electronic annotation. Source: Compara
Molecular_function	2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity Inferred from electronic annotation. Source: Compara bisphosphoglycerate 2-phosphatase activity Inferred from electronic annotation. Source: EC bisphosphoglycerate mutase activity Inferred from electronic annotation. Source: EC cofactor binding Inferred from electronic annotation. Source: Compara phosphoglycerate mutase activity Inferred from mutant phenotype PubMed 6262916. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 253	253	Phosphoglycerate mutase 2		PRO_0000179829
Regions
	Compositional bias	122 – 125	4	Poly-Pro
Sites
	Active site	11	1	Tele-phosphohistidine intermediate
	Active site	186	1
	Site	62	1	Interaction with carboxyl group of phosphoglycerates
Amino acid modifications
	Modified residue	92	1	Phosphotyrosine By similarity
	Cross-link	179		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.5
	Cross-link	195		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.5
Natural variations
	Natural variant	89	1	E → A in GSD10. Ref.6		VAR_006088
	Natural variant	90	1	R → W in GSD10. Ref.6		VAR_006089
	Natural variant	97	1	G → D in GSD10. Ref.7		VAR_013103
Experimental info
	Sequence conflict	14	1	S → T in AAA60072. Ref.3
	Sequence conflict	65	1	R → P in AAA60073. Ref.2
	Sequence conflict	85	1	W → C Ref.2
	Sequence conflict	87	1	L → F Ref.2
	Sequence conflict	87	1	L → F Ref.3
	Sequence conflict	98	1	L → F in AAA60072. Ref.3
	Sequence conflict	113 – 114	2	KI → RS in AAA60072. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P15259 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 0FDC97631104FCF7	FASTA	253	28,766
	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

References

	« Hide 'large scale' referencesShow '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, MASS SPECTROMETRY. 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

GeneReviews

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.
IPI	IPI00218570.
PIR	PMHUYM. JQ0750.
RefSeq	NP_000281.2. NM_000290.3.
UniGene	Hs.632642.
3D structure databases
ProteinModelPortal	P15259.
ModBase	Search...
Protein-protein interaction databases
IntAct	P15259. 4 interactions.
STRING	9606.ENSP00000297283.
PTM databases
PhosphoSite	P15259.
Polymorphism databases
DMDM	130353.
2D gel databases
UCD-2DPAGE	P15259.
Proteomic databases
PaxDb	P15259.
PeptideAtlas	P15259.
PRIDE	P15259.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000297283; ENSP00000297283; ENSG00000164708.
GeneID	5224.
KEGG	hsa:5224.
UCSC	uc003tjs.3. human.
Organism-specific databases
CTD	5224.
GeneCards	GC07M044102.
HGNC	HGNC:8889. PGAM2.
MIM	261670. phenotype. 612931. gene.
neXtProt	NX_P15259.
Orphanet	97234. Myopathy due to phosphoglycerate mutase deficiency.
PharmGKB	PA33226.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0588.
HOGENOM	HOG000221682.
HOVERGEN	HBG027528.
InParanoid	P15259.
KO	K01834.
OMA	VYELDQA.
OrthoDB	EOG4MCX10.
PhylomeDB	P15259.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
Gene expression databases
Bgee	P15259.
CleanEx	HS_PGAM2.
Genevestigator	P15259.
GermOnline	ENSG00000164708. Homo sapiens.
Family and domain databases
InterPro	IPR013078. His_Pase_superF_clade-1. IPR001345. PG/BPGM_mutase_AS. IPR005952. Phosphogly_mut1. [Graphical view]
PANTHER	PTHR11931. PTHR11931. 1 hit.
Pfam	PF00300. His_Phos_1. 1 hit. [Graphical view]
SMART	SM00855. PGAM. 1 hit. [Graphical view]
TIGRFAMs	TIGR01258. pgm_1. 1 hit.
PROSITE	PS00175. PG_MUTASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	5224.
NextBio	20196.
SOURCE	Search...

Entry information

Entry name

PGAM2_HUMAN

Accession

Primary (citable) accession number: P15259

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 145 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.