PRKCH

PRKCH
Identifiers
Aliases	PRKCH, PKC-L, PKCL, PRKCL, nPKC-eta, protein kinase C eta
External IDs	OMIM: 605437; MGI: 97600; HomoloGene: 84384; GeneCards: PRKCH; OMA:PRKCH - orthologs
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2FK9, 3TXO
Enzyme activity EC # BRENDA ExPASy KEGG MetaCyc 2.7.11.13 ↗ ↗ ↗ ↗
Gene location (Human) Chr. Chromosome 14 (human) Band 14q23.1 Start 61,187,559 bp End 61,550,976 bp
Gene location (Mouse) Chr. Chromosome 12 (mouse) Band 12|12 C3 Start 73,631,570 bp End 73,824,959 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in parotid gland granulocyte blood lymph node tonsil upper lobe of left lung thymus right lung visceral pleura epithelium of colon Top expressed in right lung lobe esophagus hair follicle gastrula endothelial cell of lymphatic vessel transitional epithelium of urinary bladder blood thymus lip nucleus accumbens More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity nucleotide binding protein kinase activity protein kinase C activity metal ion binding kinase activity protein serine/threonine kinase activity calcium-independent protein kinase C activity enzyme binding ATP binding protein binding Cellular component cytoplasm cytosol membrane cell-cell junction plasma membrane extracellular exosome intracellular anatomical structure Biological process positive regulation of B cell receptor signaling pathway cell differentiation intracellular signal transduction phosphorylation regulation of bicellular tight junction assembly positive regulation of keratinocyte differentiation negative regulation of glial cell apoptotic process protein kinase C signaling platelet activation protein phosphorylation positive regulation of macrophage derived foam cell differentiation positive regulation of NF-kappaB transcription factor activity peptidyl-serine phosphorylation positive regulation of glial cell proliferation signal transduction positive regulation of protein localization to plasma membrane Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5583 18755 Ensembl ENSG00000027075 ENSMUSG00000021108 UniProt P24723 P23298 RefSeq (mRNA) NM_006255 NM_008856 NM_001313977 RefSeq (protein) NP_006246 NP_001300906 NP_032882 Location (UCSC) Chr 14: 61.19 – 61.55 Mb Chr 12: 73.63 – 73.82 Mb PubMed search
Wikidata
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Protein kinase C eta type is an enzyme that in humans is encoded by the PRKCH gene.

Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and the 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. It is a calcium-independent and phospholipids-dependent protein kinase. It is predominantly expressed in epithelial tissues and has been shown to reside specifically in the cell nucleus. This protein kinase can regulate keratinocyte differentiation by activating the MAP kinase MAPK13 (p38delta)-activated protein kinase cascade that targets CCAAT/enhancer-binding protein alpha (CEBPA). It is also found to mediate the transcription activation of the transglutaminase 1 (TGM1) gene.

Further reading

• Greif H, Ben-Chaim J, Shimon T, et al. (1992). "The protein kinase C-related PKC-L(eta) gene product is localized in the cell nucleus". Mol. Cell. Biol. 12 (3): 1304–11. doi:10.1128/mcb.12.3.1304-1311.1992. PMC 369563. PMID 1545811.
• Liyanage M, Frith D, Livneh E, Stabel S (1992). "Protein kinase C group B members PKC-delta, -epsilon, -zeta and PKC-L(eta). Comparison of properties of recombinant proteins in vitro and in vivo". Biochem. J. 283 (3): 781–7. doi:10.1042/bj2830781. PMC 1130954. PMID 1590767.
• Ruegg CL, Strand M (1991). "A synthetic peptide with sequence identity to the transmembrane protein GP41 of HIV-1 inhibits distinct lymphocyte activation pathways dependent on protein kinase C and intracellular calcium influx". Cell. Immunol. 137 (1): 1–13. doi:10.1016/0008-8749(91)90051-C. PMID 1832084.
• Chowdhury IH, Koyanagi Y, Kobayashi S, et al. (1990). "The phorbol ester TPA strongly inhibits HIV-1-induced syncytia formation but enhances virus production: possible involvement of protein kinase C pathway". Virology. 176 (1): 126–32. doi:10.1016/0042-6822(90)90237-L. PMID 1970444.
• Ruegg CL, Strand M (1990). "Inhibition of protein kinase C and anti-CD3-induced Ca2+ influx in Jurkat T cells by a synthetic peptide with sequence identity to HIV-1 gp41". J. Immunol. 144 (10): 3928–35. doi:10.4049/jimmunol.144.10.3928. PMID 2139676.
• Jakobovits A, Rosenthal A, Capon DJ (1990). "Trans-activation of HIV-1 LTR-directed gene expression by tat requires protein kinase C." EMBO J. 9 (4): 1165–70. doi:10.1002/j.1460-2075.1990.tb08223.x. PMC 551792. PMID 2182321.
• Fields AP, Bednarik DP, Hess A, May WS (1988). "Human immunodeficiency virus induces phosphorylation of its cell surface receptor". Nature. 333 (6170): 278–80. Bibcode:1988Natur.333..278F. doi:10.1038/333278a0. PMID 3259291. S2CID 4254146.
• Chirmule N, Goonewardena H, Pahwa S, et al. (1995). "HIV-1 envelope glycoproteins induce activation of activated protein-1 in CD4+ T cells". J. Biol. Chem. 270 (33): 19364–9. doi:10.1074/jbc.270.33.19364. PMID 7642615.
• Ward NE, Gravitt KR, O'Brian CA (1995). "Inhibition of protein kinase C by a synthetic peptide corresponding to cytoplasmic domain residues 828-848 of the human immunodeficiency virus type 1 envelope glycoprotein". Cancer Lett. 88 (1): 37–40. doi:10.1016/0304-3835(94)03610-U. PMID 7850771.
• Palmer RH, Ridden J, Parker PJ (1995). "Identification of multiple, novel, protein kinase C-related gene products". FEBS Lett. 356 (1): 5–8. doi:10.1016/0014-5793(94)01202-4. PMID 7988719.
• Gupta S, Aggarwal S, Kim C, Gollapudi S (1994). "Human immunodeficiency virus-1 recombinant gp120 induces changes in protein kinase C isozymes--a preliminary report". Int. J. Immunopharmacol. 16 (3): 197–204. doi:10.1016/0192-0561(94)90013-2. PMID 8206685.
• Parada NA, Cruikshank WW, Danis HL, et al. (1996). "IL-16- and other CD4 ligand-induced migration is dependent upon protein kinase C." Cell. Immunol. 168 (1): 100–6. doi:10.1006/cimm.1996.0054. PMID 8599832.
• Denning MF, Dlugosz AA, Threadgill DW, et al. (1996). "Activation of the epidermal growth factor receptor signal transduction pathway stimulates tyrosine phosphorylation of protein kinase C delta". J. Biol. Chem. 271 (10): 5325–31. doi:10.1074/jbc.271.10.5325. PMID 8621384.
• Ueda E, Ohno S, Kuroki T, et al. (1996). "The eta isoform of protein kinase C mediates transcriptional activation of the human transglutaminase 1 gene". J. Biol. Chem. 271 (16): 9790–4. doi:10.1074/jbc.271.16.9790. PMID 8621660.
• Conant K, Ma M, Nath A, Major EO (1996). "Extracellular human immunodeficiency virus type 1 Tat protein is associated with an increase in both NF-kappa B binding and protein kinase C activity in primary human astrocytes". J. Virol. 70 (3): 1384–9. doi:10.1128/JVI.70.3.1384-1389.1996. PMC 189957. PMID 8627654.
• Holmes AM (1996). "In vitro phosphorylation of human immunodeficiency virus type 1 Tat protein by protein kinase C: evidence for the phosphorylation of amino acid residue serine-46". Arch. Biochem. Biophys. 335 (1): 8–12. doi:10.1006/abbi.1996.0476. PMID 8914829.
• Borgatti P, Zauli G, Cantley LC, Capitani S (1998). "Extracellular HIV-1 Tat protein induces a rapid and selective activation of protein kinase C (PKC)-alpha, and -epsilon and -zeta isoforms in PC12 cells". Biochem. Biophys. Res. Commun. 242 (2): 332–7. doi:10.1006/bbrc.1997.7877. PMID 9446795.
• Zidovetzki R, Wang JL, Chen P, et al. (1998). "Human immunodeficiency virus Tat protein induces interleukin 6 mRNA expression in human brain endothelial cells via protein kinase C- and cAMP-dependent protein kinase pathways". AIDS Res. Hum. Retroviruses. 14 (10): 825–33. doi:10.1089/aid.1998.14.825. PMID 9671211.