PRKCD

Protein-coding gene in the species Homo sapiens
PRKCD
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2YUU, 1YRK

Identifiers
AliasesPRKCD, ALPS3, CVID9, MAY1, PKCD, nPKC-delta, protein kinase C delta
External IDsOMIM: 176977; MGI: 97598; HomoloGene: 55963; GeneCards: PRKCD; OMA:PRKCD - orthologs
EC number2.7.10.2
Gene location (Human)
Chromosome 3 (human)
Chr.Chromosome 3 (human)[1]
Chromosome 3 (human)
Genomic location for PRKCD
Genomic location for PRKCD
Band3p21.1Start53,156,009 bp[1]
End53,192,717 bp[1]
Gene location (Mouse)
Chromosome 14 (mouse)
Chr.Chromosome 14 (mouse)[2]
Chromosome 14 (mouse)
Genomic location for PRKCD
Genomic location for PRKCD
Band14 B|14 18.82 cMStart30,317,311 bp[2]
End30,348,167 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • monocyte

  • granulocyte

  • right adrenal cortex

  • right uterine tube

  • mucosa of transverse colon

  • left adrenal gland

  • left adrenal cortex

  • right lobe of thyroid gland

  • left lobe of thyroid gland

  • rectum
Top expressed in
  • lateral geniculate nucleus

  • granulocyte

  • medial dorsal nucleus

  • medial geniculate nucleus

  • lateral septal nucleus

  • pyloric antrum

  • seminiferous tubule

  • epithelium of stomach

  • large intestine

  • colon
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • kinase activity
  • ATP binding
  • protein kinase activity
  • non-membrane spanning protein tyrosine kinase activity
  • metal ion binding
  • kinase binding
  • enzyme binding
  • insulin receptor substrate binding
  • transferase activity
  • protein binding
  • calcium-independent protein kinase C activity
  • protein kinase binding
  • nucleotide binding
  • enzyme activator activity
  • protein serine/threonine kinase activity
  • protein kinase C activity
Cellular component
  • cytoplasm
  • cytosol
  • membrane
  • cell-cell junction
  • perinuclear region of cytoplasm
  • nucleus
  • nuclear matrix
  • endoplasmic reticulum
  • extracellular exosome
  • plasma membrane
  • nucleoplasm
  • extracellular region
  • azurophil granule lumen
Biological process
  • intrinsic apoptotic signaling pathway in response to oxidative stress
  • termination of signal transduction
  • interferon-gamma-mediated signaling pathway
  • negative regulation of protein binding
  • positive regulation of endodeoxyribonuclease activity
  • platelet activation
  • protein phosphorylation
  • cellular senescence
  • negative regulation of insulin receptor signaling pathway
  • positive regulation of sphingomyelin catabolic process
  • cell chemotaxis
  • cell cycle
  • negative regulation of inflammatory response
  • positive regulation of protein dephosphorylation
  • Fc-gamma receptor signaling pathway involved in phagocytosis
  • positive regulation of apoptotic signaling pathway
  • stimulatory C-type lectin receptor signaling pathway
  • cellular response to hydroperoxide
  • negative regulation of peptidyl-tyrosine phosphorylation
  • defense response to bacterium
  • negative regulation of MAP kinase activity
  • positive regulation of response to DNA damage stimulus
  • positive regulation of protein import into nucleus
  • interleukin-10 production
  • regulation of actin cytoskeleton organization
  • negative regulation of actin filament polymerization
  • regulation of mRNA stability
  • phosphorylation
  • protein stabilization
  • regulation of signaling receptor activity
  • negative regulation of filopodium assembly
  • cellular response to angiotensin
  • interleukin-12 production
  • peptidyl-threonine phosphorylation
  • positive regulation of ceramide biosynthetic process
  • neutrophil activation
  • intracellular signal transduction
  • negative regulation of glial cell apoptotic process
  • negative regulation of platelet aggregation
  • positive regulation of phospholipid scramblase activity
  • B cell proliferation
  • immunoglobulin mediated immune response
  • positive regulation of glucosylceramide catabolic process
  • peptidyl-tyrosine phosphorylation
  • positive regulation of superoxide anion generation
  • activation of protein kinase activity
  • signal transduction
  • cellular response to hydrogen peroxide
  • peptidyl-serine phosphorylation
  • apoptotic process
  • neutrophil degranulation
  • execution phase of apoptosis
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

5580

18753

Ensembl

ENSG00000163932

ENSMUSG00000021948

UniProt

Q05655

P28867

RefSeq (mRNA)
NM_006254
NM_212539
NM_001316327
NM_001354676
NM_001354678

NM_001354679
NM_001354680

NM_011103
NM_001310682

RefSeq (protein)
NP_001303256
NP_006245
NP_997704
NP_001341605
NP_001341607

NP_001341608
NP_001341609

NP_001297611
NP_035233

Location (UCSC)Chr 3: 53.16 – 53.19 MbChr 14: 30.32 – 30.35 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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

Function

Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by the second messenger diacylglycerol.[6] 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.[7] 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).[8][9]

Interactions

PRKCD has been shown to interact with:

References

  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:". 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. ^ 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. doi:10.1006/geno.1994.1028. PMID 8188219.
  6. ^ Kikkawa, Ushio (2002). "Protein Kinase Cδ (PKCδ): Activaton Mechanisms and Functions". The Journal of Biochemistry. 132 (6): 831–839. doi:10.1093/oxfordjournals.jbchem.a003294. PMID 12473183. Retrieved June 30, 2008.
  7. ^ "Entrez Gene: PRKCD protein kinase C, delta".
  8. ^ 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. doi:10.1110/ps.072874607. PMC 2222818. PMID 17965192.
  9. ^ Blake RA, Garcia-Paramio P, Parker PJ, Courtneidge SA (April 1999). "Src promotes PKCdelta degradation". Cell Growth Differ. 10 (4): 231–41. PMID 10319993.
  10. ^ 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. doi:10.1074/jbc.M002964200. PMID 10831594.
  11. ^ 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. doi:10.1074/jbc.M202351200. PMID 11960991.
  12. ^ 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. doi:10.1210/mend.15.4.0612. PMID 11266508.
  13. ^ 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. doi:10.2337/diabetes.51.6.1921. PMID 12031982.
  14. ^ 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. doi:10.1074/jbc.M200436200. PMID 11877440.
  15. ^ 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. doi:10.1093/emboj/19.5.1087. PMC 305647. PMID 10698949.
  16. ^ 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. doi:10.1074/jbc.M108343200. PMID 11744693.
  17. ^ 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. doi:10.1124/mol.60.6.1431. PMID 11723252.
  18. ^ Phillips-Mason PJ, Kaur H, Burden-Gulley SM, Craig SE, Brady-Kalnay SM (2011). "Identification of phospholipase C gamma1 as a protein tyrosine phosphatase mu substrate that regulates cell migration". J. Cell. Biochem. 112 (1): 39–48. doi:10.1002/jcb.22710. PMC 3031780. PMID 20506511.
  19. ^ 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. doi:10.1021/bi010719z. PMID 11781095.
  20. ^ 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. doi:10.1124/mol.66.1.76. PMID 15213298. S2CID 5774849.
  21. ^ 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. doi:10.1128/mcb.22.12.3970-3980.2002. PMC 133855. PMID 12024011.
  22. ^ 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. doi:10.1074/jbc.M301053200. PMID 12807916.

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.
  • Slater SJ, Ho C, Stubbs CD (2003). "The use of fluorescent phorbol esters in studies of protein kinase C-membrane interactions". Chem. Phys. Lipids. 116 (1–2): 75–91. doi:10.1016/S0009-3084(02)00021-X. PMID 12093536.
  • Brodie C, Blumberg PM (2003). "Regulation of cell apoptosis by protein kinase c delta". Apoptosis. 8 (1): 19–27. doi:10.1023/A:1021640817208. PMID 12510148. S2CID 19677299.
  • v
  • t
  • e
  • 1bdy: C2 DOMAIN FROM PROTEIN KINASE C DELTA
    1bdy: C2 DOMAIN FROM PROTEIN KINASE C DELTA
  • 1ptq: PROTEIN KINASE C DELTA CYS2 DOMAIN
    1ptq: PROTEIN KINASE C DELTA CYS2 DOMAIN
  • 1ptr: PROTEIN KINASE C DELTA CYS2 DOMAIN COMPLEXED WITH PHORBOL-13-ACETATE
    1ptr: PROTEIN KINASE C DELTA CYS2 DOMAIN COMPLEXED WITH PHORBOL-13-ACETATE
  • 1yrk: The C2 Domain of PKC<delta> is a new Phospho-Tyrosine Binding Domain
    1yrk: The C2 Domain of PKC<delta> is a new Phospho-Tyrosine Binding Domain
  • v
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Non-specific serine/threonine protein kinases (EC 2.7.11.1)
Pyruvate dehydrogenase kinase (EC 2.7.11.2)
Dephospho-(reductase kinase) kinase (EC 2.7.11.3)
3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)
(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)
(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)
Myosin-heavy-chain kinase (EC 2.7.11.7)
Fas-activated serine/threonine kinase (EC 2.7.11.8)
Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)
  • -
IκB kinase (EC 2.7.11.10)
cAMP-dependent protein kinase (EC 2.7.11.11)
cGMP-dependent protein kinase (EC 2.7.11.12)
Protein kinase C (EC 2.7.11.13)
Rhodopsin kinase (EC 2.7.11.14)
Beta adrenergic receptor kinase (EC 2.7.11.15)
G-protein coupled receptor kinases (EC 2.7.11.16)
Ca2+/calmodulin-dependent (EC 2.7.11.17)
Myosin light-chain kinase (EC 2.7.11.18)
Phosphorylase kinase (EC 2.7.11.19)
Elongation factor 2 kinase (EC 2.7.11.20)
Polo kinase (EC 2.7.11.21)
Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)
Polo kinase (EC 2.7.11.21)
Cyclin-dependent kinase (EC 2.7.11.22)
(RNA-polymerase)-subunit kinase (EC 2.7.11.23)
Mitogen-activated protein kinase (EC 2.7.11.24)
MAP3K (EC 2.7.11.25)
Tau-protein kinase (EC 2.7.11.26)
(acetyl-CoA carboxylase) kinase (EC 2.7.11.27)
  • -
Tropomyosin kinase (EC 2.7.11.28)
  • -
Low-density-lipoprotein receptor kinase (EC 2.7.11.29)
  • -
Receptor protein serine/threonine kinase (EC 2.7.11.30)
MAP2K
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