[1]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA-I AND BETA-II).
DOI=10.1016/0092-8674(86)90874-3; PubMed=3755379 [NCBI, ExPASy, EBI, Israel, Japan]
Knopf J.L.,
Lee M.-H.,
Sultzman L.A.,
Kriz R.W.,
Loomis C.R.,
Hewick R.M.,
Bell R.M.;
"Cloning and expression of multiple protein kinase C cDNAs.";
Cell 46:491-502(1986).
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[2]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS BETA-I AND BETA-II).
TISSUE=Brain;
DOI=10.1016/0014-5793(86)81010-9; PubMed=2428667 [NCBI, ExPASy, EBI, Israel, Japan]
Ono Y.,
Kurokawa T.,
Fujii T.,
Kawahara K.,
Igarashi K.,
Kikkawa U.,
Ogita K.,
Nishizuka Y.;
"Two types of complementary DNAs of rat brain protein kinase C. Heterogeneity determined by alternative splicing.";
FEBS Lett. 206:347-352(1986).
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[3]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-I).
TISSUE=Fibroblast;
DOI=10.1016/S0092-8674(88)80027-8; PubMed=3345563 [NCBI, ExPASy, EBI, Israel, Japan]
Housey G.M.,
Johnson M.D.,
Hsiao W.L.W.,
O'Brian C.A.,
Murphy J.P.,
Kirschmeier P.,
Weinstein I.B.;
"Overproduction of protein kinase C causes disordered growth control in rat fibroblasts.";
Cell 52:343-354(1988).
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[4]
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NUCLEOTIDE SEQUENCE [MRNA] OF 448-671 (ISOFORM BETA-I).
DOI=10.1016/0014-5793(86)80724-4; PubMed=3755404 [NCBI, ExPASy, EBI, Israel, Japan]
Ono Y.,
Kurokawa T.,
Kawahara K.,
Nishimura O.,
Marumoto R.,
Igarashi K.,
Sugino Y.,
Kikkawa U.,
Ogita K.,
Nishizuka Y.;
"Cloning of rat brain protein kinase C complementary DNA.";
FEBS Lett. 203:111-115(1986).
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[5]
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NUCLEOTIDE SEQUENCE [MRNA] OF 448-671 (ISOFORM BETA-I).
PubMed=3469647 [NCBI, ExPASy, EBI, Israel, Japan]
Housey G.M.,
O'Brian C.A.,
Johnson M.D.,
Kirschmeier P.,
Weinstein I.B.;
"Isolation of cDNA clones encoding protein kinase C: evidence for a protein kinase C-related gene family.";
Proc. Natl. Acad. Sci. U.S.A. 84:1065-1069(1987).
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[6]
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PROTEIN SEQUENCE OF 500-520 AND 636-663 (ISOFORM BETA-II), AND PHOSPHORYLATION AT THR-500; THR-642 AND SER-661.
DOI=10.1016/S0960-9822(95)00277-6; PubMed=8749392 [NCBI, ExPASy, EBI, Israel, Japan]
Keranen L.M.,
Dutil E.M.,
Newton A.C.;
"Protein kinase C is regulated in vivo by three functionally distinct phosphorylations.";
Curr. Biol. 5:1394-1403(1995).
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[7]
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PHOSPHORYLATION AT SER-16; THR-17; THR-314; THR-324; THR-635 AND THR-642, AND MUTAGENESIS OF 16-SER-THR-17; THR-314; THR-324; THR-635 AND THR-642.
PubMed=8327493 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang J.,
Wang L.,
Petrin J.,
Bishop W.R.,
Bond R.W.;
"Characterization of site-specific mutants altered at protein kinase C beta 1 isozyme autophosphorylation sites.";
Proc. Natl. Acad. Sci. U.S.A. 90:6130-6134(1993).
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[8]
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PHOSPHORYLATION AT THR-642 (ISOFORM BETA-I), AND MUTAGENESIS OF THR-635 AND THR-642.
PubMed=8034726 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang J.,
Wang L.,
Schwartz J.,
Bond R.W.,
Bishop W.R.;
"Phosphorylation of Thr642 is an early event in the processing of newly synthesized protein kinase C beta 1 and is essential for its activation.";
J. Biol. Chem. 269:19578-19584(1994).
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[9]
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PHOSPHORYLATION AT THR-500, AND MUTAGENESIS OF THR-500.
PubMed=7961692 [NCBI, ExPASy, EBI, Israel, Japan]
Orr J.W.,
Newton A.C.;
"Requirement for negative charge on 'activation loop' of protein kinase C.";
J. Biol. Chem. 269:27715-27718(1994).
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[10]
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X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 157-288.
DOI=10.1016/S0969-2126(98)00139-7; PubMed=9817842 [NCBI, ExPASy, EBI, Israel, Japan]
Sutton R.B.,
Sprang S.R.;
"Structure of the protein kinase Cbeta phospholipid-binding C2 domain complexed with Ca2+.";
Structure 6:1395-1405(1998).
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- FUNCTION: This is a calcium-activated, phospholipid-dependent, serine- and threonine-specific enzyme. PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters. May be considered as a novel component of the NF-kappa-B signaling axis responsible for the survival and activation of B-cells after BCR cross-linking.
- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
- COFACTOR: Binds 3 calcium ions per subunit. The ions are bound to the C2 domain.
- SUBUNIT: Interacts with PDK1 (By similarity).
- INTERACTION:
Q8WV44-2:TRIM41 (xeno); NbExp=3; IntAct=EBI-397092, EBI-726015;
P61864:UBI1 (xeno); NbExp=1; IntAct=EBI-397092, EBI-19797;
- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein.
- ALTERNATIVE PRODUCTS:
2 named isoforms [FASTA] produced by alternative splicing.
- PTM: Phosphorylation on Thr-500 of isoform beta-I, within the activation loop, renders it competent to autophosphorylate. Subsequent autophosphorylation of Thr-642 maintains catalytic competence, and autophosphorylation on Ser-661 appears to release the kinase into the cytosol. Similarly, isoform beta-II is autophosphorylated on 'Thr-641' and 'Ser-660', subsequent to phosphorylation on Thr-500. Autophosphorylated on other sites i.e. in the N-terminal and hinge regions have no effect on PKC activity.
- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.
- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
- SIMILARITY: Contains 1 C2 domain.
- SIMILARITY: Contains 2 phorbol-ester/DAG-type zinc fingers.
- SIMILARITY: Contains 1 protein kinase domain.
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