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protein kinase (C-mu protein kinase D1, PRKD1, PKD, PKD1, PRKCM)

Function: - Ca+2-independent, phospholipid-dependent - serine/threonine kinase - interacts via its N-terminal region with CENTA1 - activated by diacylglycerol & phorbol esters - autophosphorylated (putative) Structure: - belongs to the protein kinase superfamily, CAMK Ser/Thr protein kinase family, PKC subfamily - contains 1 PH domain - contains 2 phorbol-ester/DAG-type Zn+2 fingers - contains 1 protein kinase domain

General

protein kinase C (PKC) zinc finger protein

Properties

SIZE: entity length = 912 aa MW = 102 kD COMPARTMENT: plasma membrane* CELL: most cell types* ORGANISM: eukaryote* MOTIF: alanine-rich region {17-26} MOTIF: alanine residue (SEVERAL) Zinc finger NAME: Zinc finger SITE: 146-196 EFFECTOR-BOUND: Zn+2 arginine-rich region {200-203} MOTIF: arginine residue (SEVERAL) Ser phosphorylation site {S205} Thr phosphorylation site {T210} Zinc finger NAME: Zinc finger SITE: 270-320 EFFECTOR-BOUND: Zn+2 PH domain {422-541} kinase domain SITE: 583-839 MOTIF: ATP-binding site NAME: ATP-binding site SITE: 589-597 ATP-binding site NAME: ATP-binding site SITE: 612-612 aspartate residue {D706} Ser phosphorylation site {S910} STATE: active state

Database Correlations

OMIM 605435 UniProt Q15139 PFAM correlations Entrez Gene 5587 Kegg hsa:5587 ENZYME 2.7.11.13

References

  1. UniProt :accession Q15139
  2. Atlas of genetics & cytogenetics in oncology & Haematology http://atlasgeneticsoncology.org/genes/PRKCMID41860ch14q11.html