PRKD3

Serine/threonine-protein kinase D3 (PKD3) or PKC-nu is an enzyme that in humans is encoded by the PRKD3 gene.

PRKD3
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2D9Z
Identifiers
Aliases	PRKD3, EPK2, PKC-NU, PKD3, PRKCN, nPKC-NU, protein kinase D3
External IDs	OMIM: 607077; MGI: 1922542; HomoloGene: 2055; GeneCards: PRKD3; OMA:PRKD3 - orthologs
Gene location (Human) Chr. Chromosome 2 (human) Band 2p22.2 Start 37,250,502 bp End 37,324,833 bp
Gene location (Mouse) Chr. Chromosome 17 (mouse) Band 17|17 E3 Start 79,256,834 bp End 79,328,245 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Achilles tendon buccal mucosa cell sperm corpus epididymis tail of epididymis skin of hip parietal pleura tibia cartilage tissue superficial temporal artery Top expressed in Rostral migratory stream internal carotid artery saccule external carotid artery vas deferens condyle efferent ductule fossa otic placode renal corpuscle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity nucleotide binding protein kinase activity protein kinase C activity protein binding ATP binding metal ion binding kinase activity protein serine/threonine kinase activity Cellular component membrane nucleoplasm cytosol cytoplasm Biological process protein phosphorylation protein kinase C-activating G protein-coupled receptor signaling pathway intracellular signal transduction phosphorylation sphingolipid biosynthetic process protein kinase D signaling Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 23683 75292 Ensembl ENSG00000115825 ENSMUSG00000024070 UniProt O94806 Q8K1Y2 RefSeq (mRNA) NM_005813 NM_001171004 NM_001171005 NM_029239 RefSeq (protein) NP_005804 NP_001164475 NP_001164476 NP_083515 Location (UCSC) Chr 2: 37.25 – 37.32 Mb Chr 17: 79.26 – 79.33 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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. The protein encoded by this gene is one of the PKC family members. This kinase can be activated rapidly by the agonists of G protein-coupled receptors. It resides in both cytoplasm and nucleus, and its nuclear accumulation is found to be dramatically enhanced in response to its activation. This kinase can also be activated after B-cell antigen receptor (BCR) engagement, which requires intact phospholipase C gamma and the involvement of other PKC family members.

Further reading

• Ali A, Hoeflich KP, Woodgett JR (2002). "Glycogen synthase kinase-3: properties, functions, and regulation". Chem. Rev. 101 (8): 2527–40. doi:10.1021/cr000110o. PMID 11749387.
• 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.
• Schultz SJ, Nigg EA (1994). "Identification of 21 novel human protein kinases, including 3 members of a family related to the cell cycle regulator nimA of Aspergillus nidulans". Cell Growth Differ. 4 (10): 821–30. PMID 8274451.
• 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.
• Mayne M, Holden CP, Nath A, Geiger JD (2000). "Release of calcium from inositol 1,4,5-trisphosphate receptor-regulated stores by HIV-1 Tat regulates TNF-alpha production in human macrophages". J. Immunol. 164 (12): 6538–42. doi:10.4049/jimmunol.164.12.6538. PMID 10843712.
• Fang X, Yu SX, Lu Y, et al. (2000). "Phosphorylation and inactivation of glycogen synthase kinase 3 by protein kinase A". Proc. Natl. Acad. Sci. U.S.A. 97 (22): 11960–5. Bibcode:2000PNAS...9711960F. doi:10.1073/pnas.220413597. PMC 17277. PMID 11035810.
• Badou A, Bennasser Y, Moreau M, et al. (2000). "Tat Protein of Human Immunodeficiency Virus Type 1 Induces Interleukin-10 in Human Peripheral Blood Monocytes: Implication of Protein Kinase C-Dependent Pathway". J. Virol. 74 (22): 10551–62. doi:10.1128/JVI.74.22.10551-10562.2000. PMC 110929. PMID 11044099.
• Park IW, Wang JF, Groopman JE (2001). "HIV-1 Tat promotes monocyte chemoattractant protein-1 secretion followed by transmigration of monocytes". Blood. 97 (2): 352–8. doi:10.1182/blood.V97.2.352. PMID 11154208.
• Bennasser Y, Yamina B, Contreras X, et al. (2002). "[HIV-1 Tat protein induces IL-10 production by human monocytes: implications of the PKC and calcium pathway]". J. Soc. Biol. 195 (3): 319–26. PMID 11833470.
• Fang X, Yu S, Tanyi JL, et al. (2002). "Convergence of Multiple Signaling Cascades at Glycogen Synthase Kinase 3: Edg Receptor-Mediated Phosphorylation and Inactivation by Lysophosphatidic Acid through a Protein Kinase C-Dependent Intracellular Pathway". Mol. Cell. Biol. 22 (7): 2099–110. doi:10.1128/MCB.22.7.2099-2110.2002. PMC 133668. PMID 11884598.
• Bennasser Y, Bahraoui E (2002). "HIV-1 Tat protein induces interleukin-10 in human peripheral blood monocytes: involvement of protein kinase C-betaII and -delta". FASEB J. 16 (6): 546–54. doi:10.1096/fj.01-0775com. PMID 11919157. S2CID 84545613.
• Dai F, Yu L, He H, et al. (2002). "Human serum and glucocorticoid-inducible kinase-like kinase (SGKL) phosphorylates glycogen syntheses kinase 3 beta (GSK-3beta) at serine-9 through direct interaction". Biochem. Biophys. Res. Commun. 293 (4): 1191–6. doi:10.1016/S0006-291X(02)00349-2. PMID 12054501.
• Efimova T, Deucher A, Kuroki T, et al. (2002). "Novel protein kinase C isoforms regulate human keratinocyte differentiation by activating a p38 delta mitogen-activated protein kinase cascade that targets CCAAT/enhancer-binding protein alpha". J. Biol. Chem. 277 (35): 31753–60. doi:10.1074/jbc.M205098200. PMID 12080077.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Bennasser Y, Badou A, Tkaczuk J, Bahraoui E (2003). "Signaling pathways triggered by HIV-1 Tat in human monocytes to induce TNF-alpha". Virology. 303 (1): 174–80. doi:10.1006/viro.2002.1676. PMID 12482669.