PRKD3

Protein-coding gene in the species Homo sapiens
PRKD3
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2D9Z

Identifiers
AliasesPRKD3, EPK2, PKC-NU, PKD3, PRKCN, nPKC-NU, protein kinase D3
External IDsOMIM: 607077; MGI: 1922542; HomoloGene: 2055; GeneCards: PRKD3; OMA:PRKD3 - orthologs
Gene location (Human)
Chromosome 2 (human)
Chr.Chromosome 2 (human)[1]
Chromosome 2 (human)
Genomic location for PRKD3
Genomic location for PRKD3
Band2p22.2Start37,250,502 bp[1]
End37,324,833 bp[1]
Gene location (Mouse)
Chromosome 17 (mouse)
Chr.Chromosome 17 (mouse)[2]
Chromosome 17 (mouse)
Genomic location for PRKD3
Genomic location for PRKD3
Band17|17 E3Start79,256,834 bp[2]
End79,328,245 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • Achilles tendon

  • sperm

  • corpus epididymis

  • parietal pleura

  • tibia

  • superficial temporal artery

  • caput epididymis

  • stromal cell of endometrium

  • visceral pleura

  • ganglionic eminence
Top expressed in
  • internal carotid artery

  • saccule

  • external carotid artery

  • vas deferens

  • condyle

  • fossa

  • otic placode

  • renal corpuscle

  • cumulus cell

  • left lung lobe
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
SpeciesHumanMouse
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 MbChr 17: 79.26 – 79.33 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Serine/threonine-protein kinase D3 (PKD3) or PKC-nu is an enzyme that in humans is encoded by the PRKD3 gene.[5][6]

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.[6]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000115825 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000024070 – 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. ^ Hayashi A, Seki N, Hattori A, Kozuma S, Saito T (Jun 1999). "PKCnu, a new member of the protein kinase C family, composes a fourth subfamily with PKCmu". Biochim Biophys Acta. 1450 (1): 99–106. doi:10.1016/S0167-4889(99)00040-3. PMID 10231560.
  6. ^ a b "Entrez Gene: PRKD3 protein kinase D3".

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.
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  • 2d9z: Solution structure of the PH domain of Protein kinase C, nu type from human
    2d9z: Solution structure of the PH domain of Protein kinase C, nu type from human
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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)
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Tropomyosin kinase (EC 2.7.11.28)
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Low-density-lipoprotein receptor kinase (EC 2.7.11.29)
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Receptor protein serine/threonine kinase (EC 2.7.11.30)
MAP2K
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