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PRKCB
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2I0E
Identifiers
Aliases	PRKCB, PKC-beta, PKCB, PRKCB1, PRKCB2, protein kinase C beta, PKCbeta, PKCI(2)
External IDs	OMIM: 176970; MGI: 97596; HomoloGene: 56424; GeneCards: PRKCB; OMA:PRKCB - orthologs
Gene location (Human) Chr. Chromosome 16 (human) Band 16p12.2-p12.1 Start 23,835,983 bp End 24,220,611 bp
Gene location (Mouse) Chr. Chromosome 7 (mouse) Band 7 F2|7 65.75 cM Start 121,887,974 bp End 122,233,625 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in middle temporal gyrus orbitofrontal cortex frontal pole Brodmann area 23 Brodmann area 46 superior frontal gyrus Brodmann area 10 Parietal Lobe Region I of hippocampus proper postcentral gyrus Top expressed in dorsal striatum olfactory tubercle primary motor cortex perirhinal cortex Region I of hippocampus proper cingulate gyrus CA3 field superior frontal gyrus visual cortex prefrontal cortex More reference expression data BioGPS n/a
Gene ontology Molecular function transferase activity nucleotide binding protein kinase activity protein kinase C activity histone binding zinc ion binding calcium channel regulator activity chromatin binding metal ion binding kinase activity protein serine/threonine kinase activity protein binding androgen receptor binding nuclear receptor coactivator activity histone kinase activity (H3-T6 specific) ATP binding protein kinase C binding calcium-dependent protein kinase C activity Cellular component cytoplasm membrane plasma membrane extracellular exosome nucleus nucleoplasm cytosol calyx of Held presynaptic cytosol Biological process B cell receptor signaling pathway cellular response to carbohydrate stimulus positive regulation of vascular endothelial growth factor receptor signaling pathway positive regulation of B cell receptor signaling pathway intracellular signal transduction response to hypoxia regulation of transcription, DNA-templated adaptive immune response phosphorylation immune system process regulation of transcription by RNA polymerase II cellular calcium ion homeostasis transcription, DNA-templated positive regulation of angiogenesis platelet activation protein phosphorylation B cell activation negative regulation of insulin receptor signaling pathway mitotic nuclear membrane disassembly negative regulation of glucose transmembrane transport positive regulation of NF-kappaB transcription factor activity peptidyl-serine phosphorylation positive regulation of I-kappaB kinase/NF-kappaB signaling calcium ion transport signal transduction lipoprotein transport apoptotic process regulation of myeloid cell differentiation chromatin organization presynaptic modulation of chemical synaptic transmission positive regulation of nucleic acid-templated transcription regulation of synaptic vesicle exocytosis Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5579 18751 Ensembl ENSG00000166501 ENSMUSG00000052889 UniProt P05771 P68404 RefSeq (mRNA) NM_212535 NM_002738 NM_008855 NM_001316672 RefSeq (protein) NP_002729 NP_997700 NP_001303601 NP_032881 Location (UCSC) Chr 16: 23.84 – 24.22 Mb Chr 7: 121.89 – 122.23 Mb PubMed search
Wikidata
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Protein kinase C beta type is an enzyme that in humans is encoded by the PRKCB gene.

Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC family members also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play a distinct role in cells. The protein encoded by this gene is one of the PKC family members. This protein kinase has been reported to be involved in many different cellular functions, such as B cell activation, apoptosis induction, endothelial cell proliferation, and intestinal sugar absorption. Studies in mice also suggest that this kinase may also regulate neuronal functions and correlate fear-induced conflict behavior after stress. Alternatively spliced transcript variants encoding distinct isoforms have been reported. This gene could be associated with autism.

Interactions

PRKCB1 has been shown to interact with RIPK4, beta adrenergic receptor kinase, PDLIM5 and GNB2L1.

See also

• Protein kinase C

References

1. ^ GRCh38: Ensembl release 89: ENSG00000166501 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000052889 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Kubo K, Ohno S, Suzuki K (September 1987). "Nucleotide sequence of the 3' portion of a human gene for protein kinase C beta I/beta II". Nucleic Acids Research. 15 (17): 7179–80. doi:10.1093/nar/15.17.7179. PMC 306204. PMID 3658678.
6. "Entrez Gene: PRKCB1 protein kinase C, beta 1".
7. Philippi A, Roschmann E, Tores F, Lindenbaum P, Benajou A, Germain-Leclerc L, et al. (October 2005). "Haplotypes in the gene encoding protein kinase c-beta (PRKCB1) on chromosome 16 are associated with autism". Molecular Psychiatry. 10 (10): 950–60. doi:10.1038/sj.mp.4001704. PMID 16027742.
8. Lintas C, Sacco R, Garbett K, Mirnics K, Militerni R, Bravaccio C, et al. (July 2009). "Involvement of the PRKCB1 gene in autistic disorder: significant genetic association and reduced neocortical gene expression". Molecular Psychiatry. 14 (7): 705–18. doi:10.1038/mp.2008.21. PMID 18317465.
9. Chen L, Haider K, Ponda M, Cariappa A, Rowitch D, Pillai S (June 2001). "Protein kinase C-associated kinase (PKK), a novel membrane-associated, ankyrin repeat-containing protein kinase". The Journal of Biological Chemistry. 276 (24): 21737–44. doi:10.1074/jbc.M008069200. PMID 11278382.
10. Yang XL, Zhang YL, Lai ZS, Xing FY, Liu YH (April 2003). "Pleckstrin homology domain of G protein-coupled receptor kinase-2 binds to PKC and affects the activity of PKC kinase". World Journal of Gastroenterology. 9 (4): 800–3. doi:10.3748/wjg.v9.i4.800. PMC 4611453. PMID 12679936.
11. Kuroda S, Tokunaga C, Kiyohara Y, Higuchi O, Konishi H, Mizuno K, et al. (December 1996). "Protein-protein interaction of zinc finger LIM domains with protein kinase C". The Journal of Biological Chemistry. 271 (49): 31029–32. doi:10.1074/jbc.271.49.31029. PMID 8940095.
12. Ron D, Jiang Z, Yao L, Vagts A, Diamond I, Gordon A (September 1999). "Coordinated movement of RACK1 with activated betaIIPKC". The Journal of Biological Chemistry. 274 (38): 27039–46. doi:10.1074/jbc.274.38.27039. PMID 10480917.

Further reading

• Mochly-Rosen D (April 1995). "Localization of protein kinases by anchoring proteins: a theme in signal transduction". Science. 268 (5208): 247–51. Bibcode:1995Sci...268..247M. doi:10.1126/science.7716516. PMID 7716516.
• Ali A, Hoeflich KP, Woodgett JR (August 2001). "Glycogen synthase kinase-3: properties, functions, and regulation". Chemical Reviews. 101 (8): 2527–40. doi:10.1021/cr000110o. PMID 11749387.
• Slater SJ, Ho C, Stubbs CD (June 2002). "The use of fluorescent phorbol esters in studies of protein kinase C-membrane interactions". Chemistry and Physics of Lipids. 116 (1–2): 75–91. doi:10.1016/S0009-3084(02)00021-X. PMID 12093536.

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