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PRKD3

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From Wikipedia, the free encyclopedia

Protein-coding gene in the species Homo sapiens

PRKD3

Available structures

PDB

Ortholog search:PDBe RCSB

List of PDB id codes
2D9Z

Identifiers

Aliases

PRKD3, EPK2, PKC-NU, PKD3, PRKCN, nPKC-NU, protein kinase D3

External IDs

OMIM:607077;MGI:1922542;HomoloGene:2055;GeneCards:PRKD3;OMA:PRKD3 - orthologs

Gene location (Human)

Chr.	Chromosome 2 (human)^[1]

Band	2p22.2	Start	37,250,502bp^[1]
Band	2p22.2	End	37,324,833bp^[1]

Gene location (Mouse)

Chr.	Chromosome 17 (mouse)^[2]

Band	17\|17 E3	Start	79,256,834bp^[2]
Band	17\|17 E3	End	79,328,245bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

Achilles tendon

buccal mucosa cell

sperm

corpus epididymis

tail of epididymis

skin of hip

parietal pleura

tibia

cartilage tissue

superficial temporal artery

Top expressed in

Rostral migratory stream

internal carotid artery

saccule

external carotid artery

vas deferens

condyle

efferent ductule

fossa

otic placode

renal corpuscle

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

Species

Human

Mouse

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 Mb

Chr 17: 79.26 – 79.33 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Serine/threonine-protein kinase D3 (PKD3) or PKC-nu is anenzyme that in humans is encoded by thePRKD3gene.^[5]^[6]

Protein kinase C (PKC) is a family ofserine- and threonine-specific protein kinases that can be activated by calcium and the second messengerdiacylglycerol. 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 forphorbol 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 ofG 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 afterB-cell antigen receptor (BCR) engagement, which requires intactphospholipase C gamma and the involvement of other PKC family members.^[6]

References

[edit]

^^a ^b ^cGRCh38: Ensembl release 89: ENSG00000115825 –Ensembl, May 2017
^^a ^b ^cGRCm38: Ensembl release 89: ENSMUSG00000024070 –Ensembl, May 2017
^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^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.
^^a ^b"Entrez Gene: PRKD3 protein kinase D3".

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.

v t e PDB gallery
2d9z: Solution structure of the PH domain of Protein kinase C, nu type from human

Kinases:Serine/threonine-specific protein kinases (EC 2.7.11-12)

Serine/threonine-specific protein kinases (EC 2.7.11.1-EC 2.7.11.20)

Non-specific serine/threonine protein kinases (EC 2.7.11.1)	LATS1 LATS2 MAST1 MAST2 STK38 STK38L CIT ROCK1 SGK SGK2 SGK3 Protein kinase B AKT1 AKT2 AKT3 Ataxia telangiectasia mutated mTOR EIF-2 kinases PKR HRI EIF2AK3 EIF2AK4 Wee1 WEE1
Pyruvate dehydrogenase kinase (EC 2.7.11.2)	PDK1 PDK2 PDK3 PDK4
Dephospho-(reductase kinase) kinase (EC 2.7.11.3)	AMP-activated protein kinase α PRKAA1 PRKAA2 β PRKAB1 PRKAB2 γ PRKAG1 PRKAG2 PRKAG3
3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)	BCKDK BCKDHA BCKDHB
(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)	IDH2 IDH3A IDH3B IDH3G
(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)	STK4
Myosin-heavy-chain kinase (EC 2.7.11.7)	Aurora kinase Aurora A kinase Aurora B kinase Aurora C kinase
Fas-activated serine/threonine kinase (EC 2.7.11.8)	FASTK STK10
Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)	-
IκB kinase (EC 2.7.11.10)	CHUK IKK2 TBK1 IKBKE IKBKG IKBKAP
cAMP-dependent protein kinase (EC 2.7.11.11)	Protein kinase A PRKACG PRKACB PRKACA PRKY
cGMP-dependent protein kinase (EC 2.7.11.12)	Protein kinase G PRKG1
Protein kinase C (EC 2.7.11.13)	Protein kinase C Protein kinase Cζ PKC alpha PRKCB1 PRKCD PRKCE PRKCH PRKCG PRKCI PRKCQ Protein kinase N1 PKN2 PKN3
Rhodopsin kinase (EC 2.7.11.14)	Rhodopsin kinase
Beta adrenergic receptor kinase (EC 2.7.11.15)	Beta adrenergic receptor kinase Beta adrenergic receptor kinase-2
G-protein coupled receptor kinases (EC 2.7.11.16)	GRK4 GRK5 GRK6
Ca2+/calmodulin-dependent (EC 2.7.11.17)	BRSK2 CAMK1 CAMK1A CAMK1B CAMK1D CAMK1G CAMK2 CAMK2A CAMK2B CAMK2D CAMK2G CAMK4 MLCK CASK CHEK1 CHEK2 DAPK1 DAPK2 DAPK3 STK11 MAPKAPK2 MAPKAPK3 MAPKAPK5 MARK1 MARK2 MARK3 MARK4 MELK MKNK1 MKNK2 NUAK1 NUAK2 OBSCN PASK PHKG1 PHKG2 PIM1 PIM2 PKD1 PRKD2 PRKD3 PSKH1 SNF1LK2 KIAA0999 STK40 SNF1LK SNRK SPEG TSSK2 Kalirin TRIB1 TRIB2 TRIB3 TRIO Titin DCLK1
Myosin light-chain kinase (EC 2.7.11.18)	MYLK MYLK2 MYLK3 MYLK4
Phosphorylase kinase (EC 2.7.11.19)	PHKA1 PHKA2 PHKB PHKG1 PHKG2
Elongation factor 2 kinase (EC 2.7.11.20)	EEF2K STK19
Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4

Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)

Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4
Cyclin-dependent kinase (EC 2.7.11.22)	CDK1 CDK2 CDKL2 CDK3 CDK4 CDK5 CDKL5 CDK6 CDK7 CDK8 CDK9 CDK10 CDK12 CDC2L5 PCTK1 PCTK2 PCTK3 PFTK1 CDC2L1
(RNA-polymerase)-subunit kinase (EC 2.7.11.23)	RPS6KA5 RPS6KA4 P70S6 kinase P70-S6 Kinase 1 RPS6KB2 RPS6KA2 RPS6KA3 RPS6KA1 RPS6KC1
Mitogen-activated protein kinase (EC 2.7.11.24)	Extracellular signal-regulated MAPK1 MAPK3 MAPK4 MAPK6 MAPK7 MAPK12 MAPK15 C-Jun N-terminal MAPK8 MAPK9 MAPK10 P38 mitogen-activated protein MAPK11 MAPK13 MAPK14
MAP3K (EC 2.7.11.25)	MAP kinase kinase kinases MAP3K1 MAP3K2 MAP3K3 MAP3K4 MAP3K5 MAP3K6 MAP3K7 MAP3K8 RAFs ARAF BRAF KSR1 KSR2 MLKs MAP3K12 MAP3K13 MAP3K9 MAP3K10 MAP3K11 MAP3K7 ZAK CDC7 MAP3K14
Tau-protein kinase (EC 2.7.11.26)	TPK1 TTK GSK-3
(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)	Bone morphogenetic protein receptors BMPR1 BMPR1A BMPR1B BMPR2 ACVR1 ACVR1B ACVR1C ACVR2A ACVR2B ACVRL1 Anti-Müllerian hormone receptor

Dual-specificity kinases (EC 2.7.12)

MAP2K	MAP2K1 MAP2K2 MAP2K3 MAP2K4 MAP2K5 MAP2K6 MAP2K7

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1Oxidoreductases (list) EC2Transferases (list) EC3Hydrolases (list) EC4Lyases (list) EC5Isomerases (list) EC6Ligases (list) EC7Translocases (list)

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