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protein kinase C-alpha (PKC-III, PRKCA, PKCA PRKACA)

Function: - Ca+2-activated, phospholipid-dependent serine/threonine kinase - may play a role in cell motility by phosphorylating CSPG4 - activated by diacylglycerol - phosphorylates a range of cellular proteins - interacts with CENTA1, CSPG4 & PRKCABP - binds to SDPR in the presence of phosphatidylserine Cofactor: - binds 3 Ca+2 per subunit - Ca+2 bound to the C2 domain (putative) Structure: - 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

Interactions

molecular events

General

protein kinase C type-A zinc finger protein

Properties

SIZE: entity length = 672 aa MW = 77 kD COMPARTMENT: plasma membrane* CELL: most cell types* ORGANISM: eukaryote* MOTIF: Zinc finger NAME: Zinc finger SITE: 36-86 EFFECTOR-BOUND: Zn+2 Zinc finger NAME: Zinc finger SITE: 101-151 EFFECTOR-BOUND: Zn+2 C2 domain {172-260} MOTIF: binding site FOR-BINDING-OF: phospholipid Ca+2-binding site SITE: 186-186 Ca+2-binding site SITE: 187-187 Ca+2-binding site SITE: 193-193 Ser phosphorylation site {S226} Ca+2-binding site SITE: 246-246 Ca+2-binding site SITE: 247-247 Ca+2-binding site SITE: 248-248 Ca+2-binding site SITE: 252-252 Ca+2-binding site SITE: 254-254 Ser phosphorylation site {S319} kinase domain SITE: 339-597 MOTIF: ATP-binding site NAME: ATP-binding site SITE: 345-353 ATP-binding site NAME: ATP-binding site SITE: 368-368 aspartate residue {D463} Thr phosphorylation site {T494} Thr phosphorylation site {T495} Thr phosphorylation site {T497} Thr phosphorylation site {T501} AGC-kinase C-terminal {598-668} MOTIF: Thr phosphorylation site {T631} Thr phosphorylation site {T638} Ser phosphorylation site {S657} Tyr phosphorylation site {Y658} STATE: active state MISC-INFO: RECOGNITION-MOTIF :SEQUENCE XRXX[S*]XRX INHIBITOR = SPHINGOSINE

Database Correlations

OMIM 176960 UniProt P17252 PFAM correlations Entrez Gene 5578 Kegg hsa:5578 ENZYME 2.7.11.13

References

  1. Kemp BE, Pearson RB. Protein kinase recognition sequence motifs. Trends Biochem Sci. 1990 Sep;15(9):342-6. Review. PMID: 2238044
  2. UniProt :accession P17252