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protein kinase C-epsilon (PKC-N, PRKCE)

Function: - Ca+2-independent, phospholipid-dependent - serine/hreonine kinase - activated by diacylglycerol - forms a ternary complex with TRIM63 & GN2BL1 - 3 specific sites a) Thr-566 (activation loop of the kinase domain) b) Thr-710 (turn motif) c) Ser-729 (hydrophobic region) need to be phosphorylated for its full activation - phosphorylation on Thr-566 by PDPK1 triggers autophosphorylation on Ser-729 - PDGF activates PKC epsilon [2] Structure: - C1 domain, containing the phorbol ester/DAG-type region 1 is the diacylglycerol sensor - C2 domain is a non-Ca+2 binding domain - belongs to the protein kinase superfamily, AGC Ser/Thr protein kinase family, PKC subfamily - contains 1 AGC-kinase C-terminal domain - contains 1 C2 domain - contains 2 phorbol-ester/DAG-type Zn+2 fingers - contains 1 protein kinase domain

General

protein kinase C type-B

Properties

SIZE: entity length = 737 aa MW = 84 kD COMPARTMENT: plasma membrane* CELL: most cell types* ORGANISM: eukaryote* STATE: active state MOTIF: C2 domain {1-99} MOTIF: binding site FOR-BINDING-OF: phospholipid Ca+2-binding site Zinc finger NAME: Zinc finger SITE: 169-220 EFFECTOR-BOUND: Zn+2 Zinc finger NAME: Zinc finger SITE: 242-292 EFFECTOR-BOUND: Zn+2 Ser phosphorylation site {S337} Thr phosphorylation site {T349} kinase domain SITE: 408-668 MOTIF: ATP-binding site NAME: ATP-binding site SITE: 414-422 ATP-binding site NAME: ATP-binding site SITE: 437-437 aspartate residue {D532} Thr phosphorylation site {T566} AGC-kinase C-terminal {669-737} MOTIF: Thr phosphorylation site {T703} Thr phosphorylation site {T710} Ser phosphorylation site {S729}

Database Correlations

OMIM 176975 UniProt Q02156 PFAM correlations Entrez Gene 5581 KEGG correlations ENZYME 2.7.11.13

References

  1. UniProt :accession Q02156
  2. Moriya S, Kazlauskas A, Akimoto K, Hirai S, Mizuno K, Takenawa T, Fukui Y, Watanabe Y, Ozaki S, Ohno S. Platelet-derived growth factor activates protein kinase C epsilon through redundant and independent signaling pathways involving phospholipase C gamma or phosphatidylinositol 3-kinase. Proc Natl Acad Sci U S A. 1996 Jan 9;93(1):151-5. PMID: 8552594