PRKD2

Protein kinase D2

PDB rendering based on 2coa.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
2COA, 3BGM

Identifiers

Symbols

PRKD2 ; PKD2; nPKC-D2

External IDs

OMIM: 607074 MGI: 2141917 HomoloGene: 9516 IUPHAR: 2173 ChEMBL: 4900 GeneCards: PRKD2 Gene

EC number

2.7.11.13

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

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 19:
47.18 – 47.22 Mb

Chr 7:
16.84 – 16.87 Mb

PubMed search

Serine/threonine-protein kinase D2 or protein kinase C δ2 (PKC-δ2) is an enzyme that in humans is encoded by the PRKD2 gene.^[1]^[2]^[3]

Function

The protein encoded by this gene belongs to the protein kinase D (PKD) family of serine/threonine protein kinases, a subfamily of protein kinase c. This kinase can be activated by phorbol esters as well as by gastrin via the cholecystokinin B receptor (CCKBR) in gastric cancer cells. It can bind to diacylglycerol (DAG) in the trans-Golgi network (TGN) and may regulate basolateral membrane protein exit from TGN. Alternative splicing results in multiple transcript variants encoding different isoforms.^[3]

References

↑ 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.
↑ 3.0 3.1 "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. 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.
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.
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. PMID 17192257.

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 Mammalian target of rapamycin EIF-2 kinases PKR HRI EIF2AK3 EIF2AK4 Wee1 WEE1

Pyruvate dehydrogenase kinase (EC 2.7.11.2)	PDK1 PDK2 PDK3

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)) (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

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 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 CDC2L5 CRKRS 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

Biochemistry overview
Enzymes overview
By EC number: 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
2.1
- 2
- 3
- 4
- 5
- 6
- 7
  - 2.7.10
  - 11-12
- 8
3.1
- - 3.1.3.48
- 2
- 3
- 4
  - 3.4.21
  - 22
  - 23
  - 24
- 5
- 6
- 7
4.1
- 2
- 3
- 4
- 5
- 6
5.1
- 2
- 3
- 4
- 99
6.1-3
- 4
- 5-6

PRKD2

Function

References

Further reading