Phosphoglycerate mutase 2 - Rattus norvegicus (Rat)

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P16290 (PGAM2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 115. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	253 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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.
Sequence similarities	Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.

Ontologies

Keywords
Biological process	Glycolysis
Molecular function	Hydrolase Isomerase
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	gluconeogenesis Inferred from direct assay PubMed 15720133. Source: RGD glycolysis Inferred from electronic annotation. Source: UniProtKB-KW response to mercury ion Inferred from mutant phenotype PubMed 2850701. Source: RGD spermatogenesis Inferred from expression pattern PubMed 7867621. Source: RGD striated muscle contraction Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Inferred from direct assay PubMed 2158448. Source: RGD nucleus Inferred from direct assay PubMed 2158448. Source: RGD
Molecular_function	2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity Inferred from mutant phenotype PubMed 2850701. Source: RGD bisphosphoglycerate 2-phosphatase activity Inferred from electronic annotation. Source: EC bisphosphoglycerate mutase activity Inferred from electronic annotation. Source: EC cofactor binding Inferred from mutant phenotype PubMed 2850701. Source: RGD
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_0000179831

Regions

Compositional bias

122 – 125

Poly-Pro

Sites

Active site

Tele-phosphohistidine intermediate

Active site

186

Site

Interaction with carboxyl group of phosphoglycerates

Amino acid modifications

Modified residue

Phosphotyrosine By similarity

Cross-link

179

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Cross-link

195

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P16290 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 73F6118A1C73D545
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FASTA

253

28,755

        10         20         30         40         50         60 
MATHRLVMVR HGESSWNQEN RFCGWFDAEL SEKGAEEAKR GATAIKDAKI EFDICYTSVL 

        70         80         90        100        110        120 
KRAIRTLWTI LDVTDQMWVP VVRTWRLNER HYGGLTGLNK AETAAKHGEE QVKIWRRSFD 

       130        140        150        160        170        180 
TPPPPMDEKH NYYASISKDR RYAGLKPEEL PTCESLKDTI ARALPFWNEE IAPKIKAGKR 

       190        200        210        220        230        240 
VLIAAHGNSL RGIVKHLEGM SDQAIMELNL PTGIPIVYEL NQELKPTKPM RFLGDEETVR 

       250 
KAMEAVAAQG KAK

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References

[1]	"Sequence of rat skeletal muscle phosphoglycerate mutase cDNA." Castella-Escola J., Montoliu L., Pons G., Puigdomenech P., Cohen-Solal M., Carreras J., Rigau J., Climent F. Biochem. Biophys. Res. Commun. 165:1345-1351(1989) [PubMed] [Europe PMC] [Abstract] 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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M31835 mRNA. Translation: AAA41835.1. Z17319 Genomic DNA. Translation: CAA78967.1.
IPI	IPI00231506.
PIR	PMRTYM. A33793.
RefSeq	NP_059024.1. NM_017328.2.
UniGene	Rn.9738.
3D structure databases
ProteinModelPortal	P16290.
SMR	P16290. Positions 2-246.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-4588391.
STRING	10116.ENSRNOP00000018227.
PTM databases
PhosphoSite	P16290.
Proteomic databases
PaxDb	P16290.
PRIDE	P16290.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000018227; ENSRNOP00000018227; ENSRNOG00000013532.
GeneID	24959.
KEGG	rno:24959.
UCSC	RGD:3313. rat.
Organism-specific databases
CTD	5224.
RGD	3313. Pgam2.
Phylogenomic databases
eggNOG	COG0588.
GeneTree	ENSGT00390000016700.
HOGENOM	HOG000221682.
HOVERGEN	HBG027528.
InParanoid	P16290.
KO	K01834.
OMA	VYELDQA.
OrthoDB	EOG4MCX10.
Enzyme and pathway databases
SABIO-RK	P16290.
Gene expression databases
Genevestigator	P16290.
GermOnline	ENSRNOG00000013532. Rattus norvegicus.
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
NextBio	604991.

Entry information

Entry name

PGAM2_RAT

Accession

Primary (citable) accession number: P16290

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 115 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents