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Collapse Statistics
226 human active and 11 inactive phosphatases in total;
194 phosphatases have substrate data;
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305 protein substrates;
89 non-protein substrates;
1114 dephosphorylation interactions;
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213 KEGG pathways;
206 NCI Nature PID pathways
560 Reactome pathways;
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last update: 18 Feb, 2016

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BPGM

Gene Name BPGM (QuickGO)
Structure of phosphatase catalytic domain

PDB ID: 2HHJ
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SynonymsBPGM
Protein NameBisphosphoglycerate mutase
Alternative Name(s)
Bisphosphoglycerate mutase (BPGM) (EC 5.4.2.4) (2,3-bisphosphoglycerate mutase, erythrocyte) (2,3-bisphosphoglycerate synthase) (EC 3.1.3.13) (EC 5.4.2.1) (BPG-dependent PGAM)
Ensembl Gene IDENSG00000172331
EntrezGene ID669
UniProt AC (Human)P07738 (protein sequence)
Enzyme ClassEC 3.1.3.13, 5.4.2.1, 5.4.2.4 (BRENDA )
Molecular Weight30005
Protein Length259
Phosphatase activityactive
Protein DomainInterPro | Pfam3D Structure * PDB | PDBe | DrugPort
* ModBase | SwissModel
Structure-based FamilyFamily 8 (CATH: 3.40.50.1240)Historical ClassPhosphoglycerate mutase
Localization cytoplasm; extracellular region (PubMed: 14718574, 1320611 | Europe PMC)
Catalytic SiteCatalytic Site Atlas Target by Small MoleculesN/A
Gene ExpressionGene Expression Atlas

The Human Protein Atlas

Function and DiseaseOMIM
Protein-protein Interaction Database STRING | IntAct | MINT
Kinase Database Phospho.ELM | PhosphoSite | NetworKIN
Function (UniProt annotation)
FUNCTION: Plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of 2,3-bisphosphoglycerate (2,3-BPG). Also exhibits mutase (EC 5.4.2.1) and phosphatase (EC 3.1.3.13) activities.
Catalytic Activity (UniProt annotation)
CATALYTIC ACTIVITY: 3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate.; CATALYTIC ACTIVITY: 2-phospho-D-glycerate = 3-phospho-D-glycerate.; CATALYTIC ACTIVITY: 2,3-bisphospho-D-glycerate + H(2)O = 3-phospho-D-glycerate + phosphate.
Protein Sequence
MSKYKLIMLR HGEGAWNKEN RFCSWVDQKL NSEGMEEARN CGKQLKALNF EFDLVFTSVL NRSIHTAWLI LEELGQEWVP VESSWRLNER HYGALIGLNR EQMALNHGEE QVRLWRRSYN VTPPPIEESH PYYQEIYNDR RYKVCDVPLD QLPRSESLKD VLERLLPYWN ERIAPEVLRG KTILISAHGN SSRALLKHLE GISDEDIINI TLPTGVPILL ELDENLRAVG PHQFLGDQEA IQAAIKKVED QGKVKQAKK
ELM motif
N/A
Gene Ontology
GO:0004083bisphosphoglycerate 2-phosphatase activity
GO:0004082bisphosphoglycerate mutase activity
GO:0006096glycolysis
GO:0004619phosphoglycerate mutase activity
GO:0007585respiratory gaseous exchange

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