Due to scheduled maintenance work, this service may not be available on Monday January 22nd between 08.00 am and 9.00 am CEST.
To improve security and privacy, we are moving our web pages and services from HTTP to HTTPS.
To give users of web services time to transition to HTTPS, we will support separate HTTP and HTTPS services until the end of 2017.
From January 2018 most HTTP traffic will be automatically redirected to HTTPS. [more...]
View this page in https

ENZYME entry: EC

Accepted Name
Phosphatidylinositol-4,5-bisphosphate 4-phosphatase.
Alternative Name(s)
PtdIns-4,5-P(2) 4-phosphatase.
Reaction catalysed
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H(2)O <=> 1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate
  • Two pathways exist in mammalian cells to degrade 1-phosphatidyl- 1D-myo-inositol 4,5-bisphosphate (PtdIns(4,5)P(2)).
  • One is catalyzed by this enzyme and the other by EC, where the product is PtdIns4P.
  • The enzyme from human is specific for PtdIns(4,5)P(2) as substrate, as it cannot use PtdIns(3,4,5)P(3), PtdIns(3,4)P(2), PtdIns(3,5)P(2), PtdIns5P, PtdIns4P or PtdIns3P.
  • In humans, the enzyme is localized to late endosomal/lysosomal membranes.
  • It can control nuclear levels of PtdIns5P and thereby control p53- dependent apoptosis.
  • Formerly EC 3.1.3.n3.
PRIAM enzyme-specific profiles3.1.3.78
KEGG Ligand Database for Enzyme Nomenclature3.1.3.78
IUBMB Enzyme Nomenclature3.1.3.78
MEDLINEFind literature relating to
Q07566, IPGD_SHIFL;  Q55286, IPGD_SHISO;  Q86T03, PP4P1_HUMAN;  
Q9CZX7, PP4P2_MOUSE;  Q4V888, PP4P2_RAT;  Q5EAU3, PP4P2_XENLA;  
Q6DIE4, PP4P2_XENTR;  Q32PR0, T55BA_DANRE;  Q66I51, T55BB_DANRE;  

View entry in original ENZYME format
View entry in raw text format (no links)

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 3.1.3.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.1.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.-.-.-