PRKCQ

PRKCQ
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1XJD, 2ENJ, 2ENN, 2ENZ, 2JED, 4Q9Z, 4RA5, 5F9E
Identifiers
Aliases	PRKCQ, PRKCT, nPKC-theta, protein kinase C theta
External IDs	OMIM: 600448; MGI: 97601; HomoloGene: 21263; GeneCards: PRKCQ; OMA:PRKCQ - orthologs
Gene location (Human) Chr. Chromosome 10 (human) Band 10p15.1 Start 6,427,143 bp End 6,580,301 bp
Gene location (Mouse) Chr. Chromosome 2 (mouse) Band 2 A1|2 8.42 cM Start 11,176,919 bp End 11,306,033 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in triceps brachii muscle glutes biceps brachii vastus lateralis muscle Skeletal muscle tissue of biceps brachii Skeletal muscle tissue of rectus abdominis thoracic diaphragm deltoid muscle muscle of thigh tibialis anterior muscle Top expressed in habenula ankle temporal muscle retinal pigment epithelium sternocleidomastoid muscle digastric muscle Epithelium of choroid plexus muscle of thigh seminiferous tubule choroid plexus of fourth ventricle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity nucleotide binding protein kinase C activity metal ion binding kinase activity protein binding ATP binding protein serine/threonine kinase activity protein kinase activity Cellular component cytoplasm cytosol membrane plasma membrane intracellular anatomical structure immunological synapse microtubule organizing center aggresome Biological process intracellular signal transduction regulation of transcription, DNA-templated positive regulation of telomere capping phosphorylation immune system process positive regulation of telomere maintenance via telomerase positive regulation of T-helper 2 cell activation positive regulation of interleukin-4 production axon guidance platelet activation Fc-epsilon receptor signaling pathway protein phosphorylation negative regulation of T cell apoptotic process negative regulation of insulin receptor signaling pathway positive regulation of T cell activation membrane protein ectodomain proteolysis positive regulation of NF-kappaB transcription factor activity peptidyl-serine phosphorylation positive regulation of T-helper 17 type immune response regulation of cell growth positive regulation of T cell proliferation positive regulation of telomerase activity cell chemotaxis positive regulation of interleukin-17 production inflammatory response T cell receptor signaling pathway regulation of platelet aggregation regulation of megakaryocyte differentiation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5588 18761 Ensembl ENSG00000065675 ENSMUSG00000026778 UniProt Q04759 Q02111 RefSeq (mRNA) NM_001242413 NM_001282644 NM_001282645 NM_006257 NM_001323265 NM_001323266 NM_001323267 NM_008859 NM_178075 RefSeq (protein) NP_001229342 NP_001269573 NP_001269574 NP_001310194 NP_001310195 NP_001310196 NP_006248 NP_032885 Location (UCSC) Chr 10: 6.43 – 6.58 Mb Chr 2: 11.18 – 11.31 Mb PubMed search
Wikidata
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Protein kinase C theta (PKC-θ) is an enzyme that in humans is encoded by the PRKCQ gene.

Function

Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by 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. It is a calcium-independent and phospholipid-dependent protein kinase. This kinase is important for T-cell activation. It is required for the activation of the transcription factors NF-kappaB and AP-1, and may link the T cell receptor (TCR) signaling complex to the activation of the transcription factors.

Interactions

PRKCQ has been shown to interact with:

• AKT1
• FYN,
• GLRX3, and
• VAV1.

PRKCQ has been shown to phosphorylate CARD11 as part of the NF-κB signaling pathway.

Inhibitors

• (R)-2-((S)-4-(3-Chloro-5-fluoro-6-(1H-pyrazolo[3,4-b]pyridin- 3-yl)pyridin-2-yl)piperazin-2-yl)-3-methylbutan-2-ol

See also

• Protein kinase C

Further reading

• Meller N, Altman A, Isakov N (1998). "New perspectives on PKCtheta, a member of the novel subfamily of protein kinase C.". Stem Cells. 16 (3): 178–92. doi:10.1002/stem.160178. PMID 9617893.
• Greenway AL, Holloway G, McPhee DA, Ellis P, Cornall A, Lidman M (2004). "HIV-1 Nef control of cell signalling molecules: multiple strategies to promote virus replication". J. Biosci. 28 (3): 323–35. doi:10.1007/BF02970151. PMID 12734410.
• 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, Hamamoto Y, Yoshiyama H, Yoshida T, Yamamoto N (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. 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. 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. doi:10.1038/333278a0. PMID 3259291.
• Chirmule N, Goonewardena H, Pahwa S, Pasieka R, Kalyanaraman VS, Pahwa S (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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
• Chang JD, Xu Y, Raychowdhury MK, Ware JA (1993). "Molecular cloning and expression of a cDNA encoding a novel isoenzyme of protein kinase C (nPKC). A new member of the nPKC family expressed in skeletal muscle, megakaryoblastic cells, and platelets". J. Biol. Chem. 268 (19): 14208–14. PMID 7686153.
• Erdel M, Baier-Bitterlich G, Duba C, Isakov N, Altman A, Utermann G, Baier G (1995). "Mapping of the human protein kinase C-theta (PRKCQ) gene locus to the short arm of chromosome 10 (10p15) by FISH". Genomics. 25 (2): 595–7. doi:10.1016/0888-7543(95)80068-W. PMID 7790001.
• 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.
• 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, Ryan TC, Center DM (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.
• 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. PMC 189957. PMID 8627654.
• Smith BL, Krushelnycky BW, Mochly-Rosen D, Berg P (1996). "The HIV nef protein associates with protein kinase C theta". J. Biol. Chem. 271 (28): 16753–7. doi:10.1074/jbc.271.17.9906. PMID 8663223.{{cite journal}}: CS1 maint: unflagged free DOI (link)
• Meller N, Liu YC, Collins TL, Bonnefoy-Bérard N, Baier G, Isakov N, Altman A (1996). "Direct interaction between protein kinase C theta (PKC theta) and 14-3-3 tau in T cells: 14-3-3 overexpression results in inhibition of PKC theta translocation and function". Mol. Cell. Biol. 16 (10): 5782–91. PMC 231579. PMID 8816492.
• 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.
• Monks CR, Kupfer H, Tamir I, Barlow A, Kupfer A (1997). "Selective modulation of protein kinase C-theta during T-cell activation". Nature. 385 (6611): 83–6. doi:10.1038/385083a0. PMID 8985252.
• Datta R, Kojima H, Yoshida K, Kufe D (1997). "Caspase-3-mediated cleavage of protein kinase C theta in induction of apoptosis". J. Biol. Chem. 272 (33): 20317–20. doi:10.1074/jbc.272.33.20317. PMID 9252332.{{cite journal}}: CS1 maint: unflagged free DOI (link)