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PRKD2

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From Wikipedia, the free encyclopedia

Protein-coding gene in the species Homo sapiens

PRKD2

Available structures

PDB

Ortholog search:PDBe RCSB

List of PDB id codes
2COA,3BGM,4NNX,4NNY

Identifiers

Aliases

PRKD2, PKD2, nPKC-D2, HSPC187, protein kinase D2

External IDs

OMIM:607074;MGI:2141917;HomoloGene:9516;GeneCards:PRKD2;OMA:PRKD2 - orthologs

Gene location (Human)

Chr.	Chromosome 19 (human)^[1]

Band	19q13.32	Start	46,674,275bp^[1]
Band	19q13.32	End	46,717,127bp^[1]

Gene location (Mouse)

Chr.	Chromosome 7 (mouse)^[2]

Band	7\|7 A2	Start	16,576,827bp^[2]
Band	7\|7 A2	End	16,604,389bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

vena cava

superficial temporal artery

Skeletal muscle tissue of rectus abdominis

granulocyte

spleen

body of tongue

pylorus

lactiferous duct

cardia

skin of leg

Top expressed in

thymus

granulocyte

mesenteric lymph nodes

spleen

blood

primary oocyte

right lung

right lung lobe

left lung

external carotid artery

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	transferase activity protein kinase activity nucleotide binding protein kinase C activity metal ion binding kinase activity protein binding ATP binding protein serine/threonine kinase activity protein kinase C binding
Cellular component	cytoplasm Golgi apparatus membrane nucleoplasm nucleus cytosol plasma membrane intracellular anatomical structure
Biological process	positive regulation of vascular endothelial growth factor receptor signaling pathway intracellular signal transduction positive regulation of endothelial cell proliferation adaptive immune response phosphorylation immune system process endothelial tube morphogenesis positive regulation of fibroblast growth factor receptor signaling pathway positive regulation of T cell receptor signaling pathway positive regulation of endothelial cell chemotaxis positive regulation of DNA-binding transcription factor activity cell death protein kinase D signaling positive regulation of intracellular signal transduction positive regulation of peptidyl-serine phosphorylation positive regulation of angiogenesis positive regulation of endothelial cell migration protein phosphorylation positive regulation of histone deacetylase activity positive regulation of CREB transcription factor activity vascular endothelial growth factor receptor signaling pathway cell adhesion positive regulation of NF-kappaB transcription factor activity positive regulation of interleukin-2 production angiogenesis positive regulation of interleukin-8 production positive regulation of blood vessel endothelial cell migration positive regulation of DNA biosynthetic process positive regulation of ERK1 and ERK2 cascade positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway protein autophosphorylation cellular response to vascular endothelial growth factor stimulus T cell receptor signaling pathway positive regulation of transcription by RNA polymerase II positive regulation of cell adhesion sphingolipid biosynthetic process peptidyl-serine phosphorylation peptidyl-threonine phosphorylation
Sources:Amigo /QuickGO

Orthologs

Species

Human

Mouse

Entrez


25865


101540

Ensembl


ENSG00000105287


ENSMUSG00000041187

UniProt


Q9BZL6


Q8BZ03

RefSeq (mRNA)


NM_001079880 NM_001079881 NM_001079882 NM_016457


NM_001252458 NM_178900

RefSeq (protein)


NP_001073349 NP_001073350 NP_001073351 NP_057541


NP_001239387 NP_849231

Location (UCSC)

Chr 19: 46.67 – 46.72 Mb

Chr 7: 16.58 – 16.6 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Serine/threonine-protein kinase D2 or PKD2 is anenzyme that in humans is encoded by thePRKD2gene.^[5]^[6]^[7]

Function

[edit]

The protein encoded by this gene belongs to theprotein kinase D (PKD) family ofserine/threonine protein kinases, a subfamily ofprotein kinase C. This kinase can be activated byphorbol esters as well as bygastrin via thecholecystokinin B receptor (CCKBR) in gastric cancer cells. It can bind todiacylglycerol (DAG) in thetrans-Golgi network (TGN) and may regulatebasolateral membrane protein exit from TGN.Alternative splicing results in multiple transcript variants encoding different isoforms.^[7]

References

[edit]

^^a ^b ^cGRCh38: Ensembl release 89: ENSG00000105287 –Ensembl, May 2017
^^a ^b ^cGRCm38: Ensembl release 89: ENSMUSG00000041187 –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.
^Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z (Nov 2000)."Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells".Genome Res.10 (10):1546–60.doi:10.1101/gr.140200.PMC 310934.PMID 11042152.
^Sturany S, Van Lint J, Muller F, Wilda M, Hameister H, Hocker M, Brey A, Gern U, Vandenheede J, Gress T, Adler G, Seufferlein T (May 2001)."Molecular cloning and characterization of the human protein kinase D2. A novel member of the protein kinase D family of serine threonine kinases".J Biol Chem.276 (5):3310–8.doi:10.1074/jbc.M008719200.PMID 11062248.
^^a ^b"Entrez Gene: PRKD2 protein kinase D2".

Sturany S, Van Lint J, Gilchrist A, et al. (2002)."Mechanism of activation of protein kinase D2(PKD2) by the CCK(B)/gastrin receptor".J. Biol. Chem.277 (33):29431–6.doi:10.1074/jbc.M200934200.PMID 12058027.
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.
Rey O, Yuan J, Rozengurt E (2003). "Intracellular redistribution of protein kinase D2 in response to G-protein-coupled receptor agonists".Biochem. Biophys. Res. Commun.302 (4):817–24.doi:10.1016/S0006-291X(03)00269-9.PMID 12646243.
Ota T, Suzuki Y, Nishikawa T, et al. (2004)."Complete sequencing and characterization of 21,243 full-length human cDNAs".Nat. Genet.36 (1):40–5.doi:10.1038/ng1285.PMID 14702039.
Yeaman C, Ayala MI, Wright JR, et al. (2004)."Protein kinase D regulates basolateral membrane protein exit from trans-Golgi network".Nat. Cell Biol.6 (2):106–12.doi:10.1038/ncb1090.PMC 3372901.PMID 14743217.
Mihailovic T, Marx M, Auer A, et al. (2005)."Protein kinase D2 mediates activation of nuclear factor kappaB by Bcr-Abl in Bcr-Abl+ human myeloid leukemia cells".Cancer Res.64 (24):8939–44.doi:10.1158/0008-5472.CAN-04-0981.PMID 15604256.
Parra M, Kasler H, McKinsey TA, et al. (2005)."Protein kinase D1 phosphorylates HDAC7 and induces its nuclear export after T-cell receptor activation".J. Biol. Chem.280 (14):13762–70.doi:10.1074/jbc.M413396200.PMID 15623513.
Auer A, von Blume J, Sturany S, et al. (2006)."Role of the regulatory domain of protein kinase D2 in phorbol ester binding, catalytic activity, and nucleocytoplasmic shuttling".Mol. Biol. Cell.16 (9):4375–85.doi:10.1091/mbc.E05-03-0251.PMC 1196345.PMID 15975900.
Kim JE, Tannenbaum SR, White FM (2005). "Global phosphoproteome of HT-29 human colon adenocarcinoma cells".J. Proteome Res.4 (4):1339–46.doi:10.1021/pr050048h.PMID 16083285.
Kimura K, Wakamatsu A, Suzuki Y, et al. (2006)."Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes".Genome Res.16 (1):55–65.doi:10.1101/gr.4039406.PMC 1356129.PMID 16344560.
Jackson LN, Li J, Chen LA, et al. (2006)."Overexpression of wild-type PKD2 leads to increased proliferation and invasion of BON endocrine cells".Biochem. Biophys. Res. Commun.348 (3):945–9.doi:10.1016/j.bbrc.2006.07.142.PMC 2430871.PMID 16899224.
Chiu TT, Leung WY,Moyer MP, et al. (2007). "Protein kinase D2 mediates lysophosphatidic acid-induced interleukin 8 production in nontransformed human colonic epithelial cells through NF-kappaB".Am. J. Physiol., Cell Physiol.292 (2): C767–77.doi:10.1152/ajpcell.00308.2006.PMID 16928771.S2CID 2220790.
Irie A, Harada K, Tsukamoto H, et al. (2007)."Protein kinase D2 contributes to either IL-2 promoter regulation or induction of cell death upon TCR stimulation depending on its activity in Jurkat cells".Int. Immunol.18 (12):1737–47.doi:10.1093/intimm/dxl108.PMID 17077180.
Olsen JV, Blagoev B, Gnad F, et al. (2006)."Global, in vivo, and site-specific phosphorylation dynamics in signaling networks".Cell.127 (3):635–48.doi:10.1016/j.cell.2006.09.026.PMID 17081983.S2CID 7827573.
Kollers S, Musilova P, Rubes J, Rocha D (2007). "Comparative mapping reveals multiple rearrangements between pig chromosome 6 and human 19q13".Anim. Genet.37 (6):595–6.doi:10.1111/j.1365-2052.2006.01516.x.PMID 17121608.
Wissing J, Jänsch L, Nimtz M, et al. (2007)."Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry".Mol. Cell. Proteomics.6 (3):537–47.doi:10.1074/mcp.T600062-MCP200.hdl:10033/19756.PMID 17192257.

v t e PDB gallery
2coa: Solution structure of the PH domain of protein kinase C, D2 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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