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ENZYME entry: EC 3.9.1.3

Accepted Name
Phosphohistidine phosphatase.
Alternative Name(s)
PHP.
Protein histidine phosphatase.
Reaction catalysed
A [protein]-N-phospho-L-histidine + H(2)O <=> a [protein]-L-histidine + phosphate
Comment(s)
  • This eukaryotic enzyme dephosphorylates phosphorylated histidine residues within proteins and peptides.
  • The enzyme acts on phosphate groups attached to both the pros- and tele-nitrogen atoms, but the pros- position is somewhat preferred (by a factor of two at the most).
  • The substrate specificity depends on the amino acid sequence or structural context of the phosphohistidine in a phosphoprotein.
  • The enzyme is also active on free phosphoramidate and peptide-bound phospholysine.
Cross-references
BRENDA3.9.1.3
EC2PDB3.9.1.3
ExplorEnz3.9.1.3
PRIAM enzyme-specific profiles3.9.1.3
KEGG Ligand Database for Enzyme Nomenclature3.9.1.3
IUBMB Enzyme Nomenclature3.9.1.3
IntEnz3.9.1.3
MEDLINEFind literature relating to 3.9.1.3
MetaCyc3.9.1.3
UniProtKB/Swiss-Prot
Q32PA4, PHP14_BOVIN;  Q9NRX4, PHP14_HUMAN;  Q9DAK9, PHP14_MOUSE;  
P59083, PHP14_PIG;  Q5R8L6, PHP14_PONAB;  P83468, PHP14_RABIT;  

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All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.9.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.9.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.-.-.-