[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=11961099 [NCBI, ExPASy, EBI, Israel, Japan] Betran E., Wang W., Jin L., Long M.; "Evolution of the phosphoglycerate mutase processed gene in human and chimpanzee revealing the origin of a new primate gene."; Mol. Biol. Evol. 19:654-663(2002).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1371/journal.pbio.0030357; PubMed=16201836 [NCBI, ExPASy, EBI, Israel, Japan] Marques A.C., Dupanloup I., Vinckenbosch N., Reymond A., Kaessmann H.; "Emergence of young human genes after a burst of retroposition in primates."; PLoS Biol. 3:1970-1979(2005).

Comments

CATALYTIC ACTIVITY: 2-phospho-D-glycerate = 3-phospho-D-glycerate.
CATALYTIC ACTIVITY: 3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate.
CATALYTIC ACTIVITY: 2,3-bisphospho-D-glycerate + H₂O = 3-phospho-D-glycerate + phosphate.
MISCELLANEOUS: This is the product of a processed gene created by retroposition from mRNA of an expressed gene. This gene seems to be expressed.
SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF465746; AAM27297.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ120648; ABB92433.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001009163.1; -.

3D structure databases

HSSP

P31217; 1E58. [HSSP ENTRY / PDB]

SMR

Q8MKE8; 2-246.

ModBase

Q8MKE8.

Ontologies

GO:0004083;	Molecular function: bisphosphoglycerate 2-phosphatase activity (inferred from electronic annotation from EC).
GO:0004082;	Molecular function: bisphosphoglycerate mutase activity (inferred from electronic annotation from EC).
GO:0004619;	Molecular function: phosphoglycerate mutase activity (inferred from electronic annotation from EC).
GO:0006096;	Biological process: glycolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR001345; PG/BPGM_mutase.
IPR013078; PG_mutase.
IPR005952; Phosphogly_mut1.
Graphical view of domain structure.

PANTHER

PTHR11931; Phosphogly_mut1; 1.

Pfam

PF00300; PGAM; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01258; pgm_1; 1.

PROSITE

PS00175; PG_MUTASE; 1.

ProtoNet

Q8MKE8.

Genome annotation databases

Ensembl

ENSPTRG00000028245; Pan troglodytes. [Contig view]

GeneID

494122; -.

KEGG

ptr:494122; -.

Phylogenomic databases

HOVERGEN

Q8MKE8; -.

Other

LinkHub

Q8MKE8; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetylation; Glycolysis; Hydrolase; Isomerase; Phosphoprotein.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 254`	`254`	`Probable phosphoglycerate mutase 4.`	`PRO_0000179833`
`COMPBIAS`	`122 131`	`10`	`Pro-rich.`
`ACT_SITE`	`11 11`		`Tele-phosphohistidine intermediate (By similarity).`
`ACT_SITE`	`186 186`		`By similarity.`
`SITE`	`62 62`	`1`	`Interaction with carboxyl group of phosphoglycerates (By similarity).`
`MOD_RES`	`92 92`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`106 106`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`118 118`		`Phosphoserine (By similarity).`
`MOD_RES`	`119 119`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`133 133`		`Phosphotyrosine (By similarity).`

Sequence information

Length: 254 AA [This is the length of the unprocessed precursor]

Molecular weight: 28809 Da [This is the MW of the unprocessed precursor]

CRC64: 0F073CDE449EDD39 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAYKLVLIR HGESTWNLEN RFSCWYDADL SPAGHEEAKR GGQALRDAGY EFDICLTSVQ 

        70         80         90        100        110        120 
KRVIRTLWTV LDAIDQMWLP VVRTWRLNER HYGGLTALNK AETAAKHGEA QVKIWRRSYD 

       130        140        150        160        170        180 
VPPPPMEPDH PFYSNISKDR RYADLTEDQL PSYESPKDTI ARALPFWNEE IVPQIKEGKR 

       190        200        210        220        230        240 
VLIAAHGNSL QGIAKHVEGL SEEAIMELNL PTGIPIVYEL DKNLKPIKPM QFLGDEETVC 

       250 
KAMEAVAAQG KAKK

Q8MKE8 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools