PRKCD

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PRKCD
Protein PRKCD PDB 1bdy.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases PRKCD, ALPS3, CVID9, MAY1, PKCD, nPKC-delta, protein kinase C delta
External IDs OMIM: 176977 MGI: 97598 HomoloGene: 55963 GeneCards: PRKCD
EC number 2.7.10.2
Gene location (Human)
Chromosome 3 (human)
Chr. Chromosome 3 (human)[1]
Chromosome 3 (human)
Genomic location for PRKCD
Genomic location for PRKCD
Band 3p21.1 Start 53,156,009 bp[1]
End 53,192,717 bp[1]
RNA expression pattern
PBB GE PRKCD 202545 at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_011103
NM_001310682

RefSeq (protein)

NP_001297611
NP_035233

Location (UCSC) Chr 3: 53.16 – 53.19 Mb Chr 3: 30.6 – 30.63 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Protein kinase C delta type (or PKC-δ) is an enzyme that in humans is encoded by the PRKCD gene.[5]

Function[edit]

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 distinct roles in cells. The protein encoded by this gene is one of the PKC family members. Studies both in human and mice demonstrate that this kinase is involved in B cell signaling and in the regulation of growth, apoptosis, and differentiation of a variety of cell types.[6] Protein kinase C delta is also regulated by phosphorylation on various serine/threonine (e.g. T50, T141, S304, T451, T505, S506, T507, S643, S664) and tyrosine residues including Y311 (by SRC).[7][8]

Interactions[edit]

PRKCD has been shown to interact with:

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000163932 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000021948 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". 
  4. ^ "Mouse PubMed Reference:". 
  5. ^ Huppi K, Siwarski D, Goodnight J, Mischak H (June 1994). "Assignment of the protein kinase C delta polypeptide gene (PRKCD) to human chromosome 3 and mouse chromosome 14". Genomics. 19 (1): 161–2. PMID 8188219. doi:10.1006/geno.1994.1028. 
  6. ^ "Entrez Gene: PRKCD protein kinase C, delta". 
  7. ^ Welman A, Griffiths JR, Whetton AD, Dive C (December 2007). "Protein kinase C delta is phosphorylated on five novel Ser/Thr sites following inducible overexpression in human colorectal cancer cells". Protein Sci. 16 (12): 2711–5. PMC 2222818Freely accessible. PMID 17965192. doi:10.1110/ps.072874607. 
  8. ^ Blake RA, Garcia-Paramio P, Parker PJ, Courtneidge SA (April 1999). "Src promotes PKCdelta degradation". Cell Growth Differ. 10 (4): 231–41. PMID 10319993. 
  9. ^ Storz P, Hausser A, Link G, Dedio J, Ghebrehiwet B, Pfizenmaier K, Johannes FJ (August 2000). "Protein kinase C [micro] is regulated by the multifunctional chaperon protein p32". J. Biol. Chem. 275 (32): 24601–7. PMID 10831594. doi:10.1074/jbc.M002964200. 
  10. ^ Keshamouni, V. G. (17 April 2002). "Mechanism of 17-beta -Estradiol-induced Erk1/2 Activation in Breast Cancer Cells. A ROLE FOR HER2 AND PKC-delta". Journal of Biological Chemistry. 277 (25): 22558–22565. PMID 11960991. doi:10.1074/jbc.M202351200. 
  11. ^ Braiman L, Alt A, Kuroki T, Ohba M, Bak A, Tennenbaum T, Sampson SR (April 2001). "Insulin induces specific interaction between insulin receptor and protein kinase C delta in primary cultured skeletal muscle". Mol. Endocrinol. 15 (4): 565–74. PMID 11266508. doi:10.1210/mend.15.4.0612. 
  12. ^ Rosenzweig T, Braiman L, Bak A, Alt A, Kuroki T, Sampson SR (June 2002). "Differential effects of tumor necrosis factor-alpha on protein kinase C isoforms alpha and delta mediate inhibition of insulin receptor signaling". Diabetes. 51 (6): 1921–30. PMID 12031982. doi:10.2337/diabetes.51.6.1921. 
  13. ^ Ren J, Li Y, Kufe D (May 2002). "Protein kinase C delta regulates function of the DF3/MUC1 carcinoma antigen in beta-catenin signaling". J. Biol. Chem. 277 (20): 17616–22. PMID 11877440. doi:10.1074/jbc.M200436200. 
  14. ^ Kumar V, Pandey P, Sabatini D, Kumar M, Majumder PK, Bharti A, Carmichael G, Kufe D, Kharbanda S (March 2000). "Functional interaction between RAFT1/FRAP/mTOR and protein kinase cdelta in the regulation of cap-dependent initiation of translation". EMBO J. 19 (5): 1087–97. PMC 305647Freely accessible. PMID 10698949. doi:10.1093/emboj/19.5.1087. 
  15. ^ Han JM, Kim JH, Lee BD, Lee SD, Kim Y, Jung YW, Lee S, Cho W, Ohba M, Kuroki T, Suh PG, Ryu SH (March 2002). "Phosphorylation-dependent regulation of phospholipase D2 by protein kinase C delta in rat Pheochromocytoma PC12 cells". J. Biol. Chem. 277 (10): 8290–7. PMID 11744693. doi:10.1074/jbc.M108343200. 
  16. ^ Yoshida K, Kufe D (December 2001). "Negative regulation of the SHPTP1 protein tyrosine phosphatase by protein kinase C delta in response to DNA damage". Mol. Pharmacol. 60 (6): 1431–8. PMID 11723252. 
  17. ^ Phillips-Mason PJ, Kaur H, Burden-Gulley SM, Craig SE, Brady-Kalnay SM. "Identification of phospholipase C gamma1 as a protein tyrosine phosphatase mu substrate that regulates cell migration". J. Cell. Biochem. 112 (1): 39–48. PMC 3031780Freely accessible. PMID 20506511. doi:10.1002/jcb.22710. 
  18. ^ Hodgkinson CP, Sale GJ (January 2002). "Regulation of both PDK1 and the phosphorylation of PKC-zeta and -delta by a C-terminal PRK2 fragment". Biochemistry. 41 (2): 561–9. PMID 11781095. doi:10.1021/bi010719z. 
  19. ^ Brodie C, Steinhart R, Kazimirsky G, Rubinfeld H, Hyman T, Ayres JN, Hur GM, Toth A, Yang D, Garfield SH, Stone JC, Blumberg PM (July 2004). "PKCdelta associates with and is involved in the phosphorylation of RasGRP3 in response to phorbol esters". Mol. Pharmacol. 66 (1): 76–84. PMID 15213298. doi:10.1124/mol.66.1.76. 
  20. ^ Leitges M, Gimborn K, Elis W, Kalesnikoff J, Hughes MR, Krystal G, Huber M (June 2002). "Protein kinase C-delta is a negative regulator of antigen-induced mast cell degranulation". Mol. Cell. Biol. 22 (12): 3970–80. PMC 133855Freely accessible. PMID 12024011. doi:10.1128/mcb.22.12.3970-3980.2002. 
  21. ^ Kristof AS, Marks-Konczalik J, Billings E, Moss J (September 2003). "Stimulation of signal transducer and activator of transcription-1 (STAT1)-dependent gene transcription by lipopolysaccharide and interferon-gamma is regulated by mammalian target of rapamycin". J. Biol. Chem. 278 (36): 33637–44. PMID 12807916. doi:10.1074/jbc.M301053200. 

Further reading[edit]