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{{Infobox_gene}}
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'''Serine/threonine-protein kinase D3''' (PKD3) or PKC-nu  is an [[enzyme]] that in humans is encoded by the ''PRKD3'' [[gene]].<ref name="pmid10231560">{{cite journal |vauthors=Hayashi A, Seki N, Hattori A, Kozuma S, Saito T | title = PKCnu, a new member of the protein kinase C family, composes a fourth subfamily with PKCmu | journal = Biochim Biophys Acta | volume = 1450 | issue = 1 | pages = 99–106 |date=Jun 1999 | pmid = 10231560 | pmc =  | doi =10.1016/S0167-4889(99)00040-3 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PRKD3 protein kinase D3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23683| accessdate = }}</ref>
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{{GNF_Protein_box
| image = PBB_Protein_PRKD3_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2d9z.
| PDB = {{PDB2|2d9z}}
| Name = Protein kinase D3
| HGNCid = 9408
| Symbol = PRKD3
| AltSymbols =; PKD3; EPK2; PKC-NU; PRKCN; nPKC-NU
| OMIM = 607077
| ECnumber = 
| Homologene = 2055
| MGIid = 1922542
| GeneAtlas_image1 = PBB_GE_PRKD3_218236_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_PRKD3_211084_x_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004697 |text = protein kinase C activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0019992 |text = diacylglycerol binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
  | Component =  
  | Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007205 |text = protein kinase C activation}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 23683
    | Hs_Ensembl = ENSG00000115825
    | Hs_RefseqProtein = NP_005804
    | Hs_RefseqmRNA = NM_005813
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 37331149
    | Hs_GenLoc_end = 37398541
    | Hs_Uniprot = O94806
    | Mm_EntrezGene = 75292
    | Mm_Ensembl = ENSMUSG00000024070
    | Mm_RefseqmRNA = NM_029239
    | Mm_RefseqProtein = NP_083515
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 17
    | Mm_GenLoc_start = 78855620
    | Mm_GenLoc_end = 78925773
    | Mm_Uniprot = Q5FWX6
  }}
}}
'''Protein kinase D3''', also known as '''PRKD3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PRKD3 protein kinase D3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23683| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = 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 phopholipase C gamma and the involvement of other PKC family members.<ref name="entrez">{{cite web | title = Entrez Gene: PRKD3 protein kinase D3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23683| accessdate = }}</ref>
| summary_text = [[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.<ref name="entrez" />
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Ali A, Hoeflich KP, Woodgett JR |title=Glycogen synthase kinase-3: properties, functions, and regulation. |journal=Chem. Rev. |volume=101 |issue= 8 |pages= 2527-40 |year= 2002 |pmid= 11749387 |doi=  }}
*{{cite journal  |vauthors=Ali A, Hoeflich KP, Woodgett JR |title=Glycogen synthase kinase-3: properties, functions, and regulation |journal=Chem. Rev. |volume=101 |issue= 8 |pages= 2527–40 |year= 2002 |pmid= 11749387 |doi=10.1021/cr000110o }}
*{{cite journal  | author=Jakobovits A, Rosenthal A, Capon DJ |title=Trans-activation of HIV-1 LTR-directed gene expression by tat requires protein kinase C. |journal=EMBO J. |volume=9 |issue= 4 |pages= 1165-70 |year= 1990 |pmid= 2182321 |doi=  }}
*{{cite journal  |vauthors=Jakobovits A, Rosenthal A, Capon DJ |title=Trans-activation of HIV-1 LTR-directed gene expression by tat requires protein kinase C |journal=EMBO J. |volume=9 |issue= 4 |pages= 1165–70 |year= 1990 |pmid= 2182321 |doi= | pmc=551792 }}
*{{cite journal  | author=Schultz SJ, Nigg EA |title=Identification of 21 novel human protein kinases, including 3 members of a family related to the cell cycle regulator nimA of Aspergillus nidulans. |journal=Cell Growth Differ. |volume=4 |issue= 10 |pages= 821-30 |year= 1994 |pmid= 8274451 |doi=  }}
*{{cite journal  |vauthors=Schultz SJ, Nigg EA |title=Identification of 21 novel human protein kinases, including 3 members of a family related to the cell cycle regulator nimA of Aspergillus nidulans |journal=Cell Growth Differ. |volume=4 |issue= 10 |pages= 821–30 |year= 1994 |pmid= 8274451 |doi=  }}
*{{cite journal  | author=Conant K, Ma M, Nath A, Major EO |title=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. |journal=J. Virol. |volume=70 |issue= 3 |pages= 1384-9 |year= 1996 |pmid= 8627654 |doi=  }}
*{{cite journal  |vauthors=Conant K, Ma M, Nath A, Major EO |title=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 |journal=J. Virol. |volume=70 |issue= 3 |pages= 1384–9 |year= 1996 |pmid= 8627654 |doi= | pmc=189957 }}
*{{cite journal  | author=Holmes AM |title=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. |journal=Arch. Biochem. Biophys. |volume=335 |issue= 1 |pages= 8-12 |year= 1996 |pmid= 8914829 |doi= 10.1006/abbi.1996.0476 }}
*{{cite journal  | author=Holmes AM |title=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 |journal=Arch. Biochem. Biophys. |volume=335 |issue= 1 |pages= 8–12 |year= 1996 |pmid= 8914829 |doi= 10.1006/abbi.1996.0476 }}
*{{cite journal  | author=Borgatti P, Zauli G, Cantley LC, Capitani S |title=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. |journal=Biochem. Biophys. Res. Commun. |volume=242 |issue= 2 |pages= 332-7 |year= 1998 |pmid= 9446795 |doi=  }}
*{{cite journal  |vauthors=Borgatti P, Zauli G, Cantley LC, Capitani S |title=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 |journal=Biochem. Biophys. Res. Commun. |volume=242 |issue= 2 |pages= 332–7 |year= 1998 |pmid= 9446795 |doi=10.1006/bbrc.1997.7877 }}
*{{cite journal | author=Zidovetzki R, Wang JL, Chen P, ''et al.'' |title=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. |journal=AIDS Res. Hum. Retroviruses |volume=14 |issue= 10 |pages= 825-33 |year= 1998 |pmid= 9671211 |doi=  }}
*{{cite journal   |vauthors=Zidovetzki R, Wang JL, Chen P, etal |title=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 |journal=AIDS Res. Hum. Retroviruses |volume=14 |issue= 10 |pages= 825–33 |year= 1998 |pmid= 9671211 |doi=10.1089/aid.1998.14.825 }}
*{{cite journal  | author=Hayashi A, Seki N, Hattori A, ''et al.'' |title=PKCnu, a new member of the protein kinase C family, composes a fourth subfamily with PKCmu. |journal=Biochim. Biophys. Acta |volume=1450 |issue= 1 |pages= 99-106 |year= 1999 |pmid= 10231560 |doi=  }}
*{{cite journal  |vauthors=Mayne M, Holden CP, Nath A, Geiger JD |title=Release of calcium from inositol 1,4,5-trisphosphate receptor-regulated stores by HIV-1 Tat regulates TNF-alpha production in human macrophages |journal=J. Immunol. |volume=164 |issue= 12 |pages= 6538–42 |year= 2000 |pmid= 10843712 |doi=  10.4049/jimmunol.164.12.6538}}
*{{cite journal | author=Mayne M, Holden CP, Nath A, Geiger JD |title=Release of calcium from inositol 1,4,5-trisphosphate receptor-regulated stores by HIV-1 Tat regulates TNF-alpha production in human macrophages. |journal=J. Immunol. |volume=164 |issue= 12 |pages= 6538-42 |year= 2000 |pmid= 10843712 |doi=  }}
*{{cite journal   |vauthors=Fang X, Yu SX, Lu Y, etal |title=Phosphorylation and inactivation of glycogen synthase kinase 3 by protein kinase A |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 22 |pages= 11960–5 |year= 2000 |pmid= 11035810 |doi= 10.1073/pnas.220413597 | pmc=17277 }}
*{{cite journal | author=Fang X, Yu SX, Lu Y, ''et al.'' |title=Phosphorylation and inactivation of glycogen synthase kinase 3 by protein kinase A. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 22 |pages= 11960-5 |year= 2000 |pmid= 11035810 |doi= 10.1073/pnas.220413597 }}
*{{cite journal   |vauthors=Badou A, Bennasser Y, Moreau M, etal |title=Tat Protein of Human Immunodeficiency Virus Type 1 Induces Interleukin-10 in Human Peripheral Blood Monocytes: Implication of Protein Kinase C-Dependent Pathway |journal=J. Virol. |volume=74 |issue= 22 |pages= 10551–62 |year= 2000 |pmid= 11044099 |doi=10.1128/JVI.74.22.10551-10562.2000  | pmc=110929  }}
*{{cite journal  | author=Badou A, Bennasser Y, Moreau M, ''et al.'' |title=Tat protein of human immunodeficiency virus type 1 induces interleukin-10 in human peripheral blood monocytes: implication of protein kinase C-dependent pathway. |journal=J. Virol. |volume=74 |issue= 22 |pages= 10551-62 |year= 2000 |pmid= 11044099 |doi= }}
*{{cite journal  |vauthors=Park IW, Wang JF, Groopman JE |title=HIV-1 Tat promotes monocyte chemoattractant protein-1 secretion followed by transmigration of monocytes |journal=Blood |volume=97 |issue= 2 |pages= 352–8 |year= 2001 |pmid= 11154208 |doi=10.1182/blood.V97.2.352  }}
*{{cite journal | author=Park IW, Wang JF, Groopman JE |title=HIV-1 Tat promotes monocyte chemoattractant protein-1 secretion followed by transmigration of monocytes. |journal=Blood |volume=97 |issue= 2 |pages= 352-8 |year= 2001 |pmid= 11154208 |doi=  }}
*{{cite journal   |vauthors=Bennasser Y, Yamina B, Contreras X, etal |title=[HIV-1 Tat protein induces IL-10 production by human monocytes: implications of the PKC and calcium pathway] |journal=J. Soc. Biol. |volume=195 |issue= 3 |pages= 319–26 |year= 2002 |pmid= 11833470 |doi=  }}
*{{cite journal | author=Bennasser Y, Yamina B, Contreras X, ''et al.'' |title=[HIV-1 Tat protein induces IL-10 production by human monocytes: implications of the PKC and calcium pathway] |journal=J. Soc. Biol. |volume=195 |issue= 3 |pages= 319-26 |year= 2002 |pmid= 11833470 |doi= }}
*{{cite journal   |vauthors=Fang X, Yu S, Tanyi JL, etal |title=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 |journal=Mol. Cell. Biol. |volume=22 |issue= 7 |pages= 2099–110 |year= 2002 |pmid= 11884598 |doi=10.1128/MCB.22.7.2099-2110.2002  | pmc=133668  }}
*{{cite journal  | author=Fang X, Yu S, Tanyi JL, ''et al.'' |title=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. |journal=Mol. Cell. Biol. |volume=22 |issue= 7 |pages= 2099-110 |year= 2002 |pmid= 11884598 |doi=  }}
*{{cite journal  |vauthors=Bennasser Y, Bahraoui E |title=HIV-1 Tat protein induces interleukin-10 in human peripheral blood monocytes: involvement of protein kinase C-betaII and -delta |journal=FASEB J. |volume=16 |issue= 6 |pages= 546–54 |year= 2002 |pmid= 11919157 |doi=10.1096/fj.01-0775com }}
*{{cite journal | author=Bennasser Y, Bahraoui E |title=HIV-1 Tat protein induces interleukin-10 in human peripheral blood monocytes: involvement of protein kinase C-betaII and -delta. |journal=FASEB J. |volume=16 |issue= 6 |pages= 546-54 |year= 2002 |pmid= 11919157 |doi= }}
*{{cite journal   |vauthors=Dai F, Yu L, He H, etal |title=Human serum and glucocorticoid-inducible kinase-like kinase (SGKL) phosphorylates glycogen syntheses kinase 3 beta (GSK-3beta) at serine-9 through direct interaction |journal=Biochem. Biophys. Res. Commun. |volume=293 |issue= 4 |pages= 1191–6 |year= 2002 |pmid= 12054501 |doi= 10.1016/S0006-291X(02)00349-2 }}
*{{cite journal | author=Dai F, Yu L, He H, ''et al.'' |title=Human serum and glucocorticoid-inducible kinase-like kinase (SGKL) phosphorylates glycogen syntheses kinase 3 beta (GSK-3beta) at serine-9 through direct interaction. |journal=Biochem. Biophys. Res. Commun. |volume=293 |issue= 4 |pages= 1191-6 |year= 2002 |pmid= 12054501 |doi= 10.1016/S0006-291X(02)00349-2 }}
*{{cite journal   |vauthors=Efimova T, Deucher A, Kuroki T, etal |title=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 |journal=J. Biol. Chem. |volume=277 |issue= 35 |pages= 31753–60 |year= 2002 |pmid= 12080077 |doi= 10.1074/jbc.M205098200 }}
*{{cite journal | author=Efimova T, Deucher A, Kuroki T, ''et al.'' |title=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. |journal=J. Biol. Chem. |volume=277 |issue= 35 |pages= 31753-60 |year= 2002 |pmid= 12080077 |doi= 10.1074/jbc.M205098200 }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  |vauthors=Bennasser Y, Badou A, Tkaczuk J, Bahraoui E |title=Signaling pathways triggered by HIV-1 Tat in human monocytes to induce TNF-alpha |journal=Virology |volume=303 |issue= 1 |pages= 174–80 |year= 2003 |pmid= 12482669 |doi=10.1006/viro.2002.1676 }}
*{{cite journal  | author=Bennasser Y, Badou A, Tkaczuk J, Bahraoui E |title=Signaling pathways triggered by HIV-1 Tat in human monocytes to induce TNF-alpha. |journal=Virology |volume=303 |issue= 1 |pages= 174-80 |year= 2003 |pmid= 12482669 |doi= }}
}}
}}
{{refend}}
{{refend}}


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Latest revision as of 18:42, 7 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Serine/threonine-protein kinase D3 (PKD3) or PKC-nu is an enzyme that in humans is encoded by the PRKD3 gene.[1][2]

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.[2]

References

  1. ↑ 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.
  2. ↑ 2.0 2.1 "Entrez Gene: PRKD3 protein kinase D3".

Further reading


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