PRKD2

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	MGI: 2141917 HomoloGene: 9516 GeneCards: PRKD2
Gene location (Human)
Chr.	Chromosome 19 (human)[1]
End	46,717,127 bp[1]
Gene location (Mouse)
Chr.	Chromosome 7 (mouse)[2]
End	16,870,464 bp[2]
RNA expression pattern
	; ;
	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; • cell nucleus; • cytosol; • plasma membrane; • intracellular;
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 sequence-specific 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 from RNA polymerase II promoter; • positive regulation of cell adhesion; • sphingolipid biosynthetic process; • peptidyl-serine phosphorylation; • peptidyl-threonine phosphorylation;
	Sources:Amigo / QuickGO
Orthologs
	25865
	101540
	ENSG00000105287
	ENSMUSG00000041187
	Q9BZL6
	Q8BZ03
	NM_001079880; NM_001079881; NM_001079882; NM_016457
	NM_001252458; NM_178900
	NP_001073349; NP_001073350; NP_001073351; NP_057541
	NP_001239387; NP_849231
	Wikidata
View/Edit Human	View/Edit Mouse

Serine/threonine-protein kinase D2 or PKD2 is an enzyme that in humans is encoded by the PRKD2 gene.^[5]^[6]^[7]

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.^[7]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000105287 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000041187 - Ensembl, May 2017
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ 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.
1 2 "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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000105287 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000041187 - Ensembl, May 2017

[3] "Human PubMed Reference:".

[4] "Mouse PubMed Reference:".

[pmid11042152-5] 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.

[pmid11062248-6] 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.

[entrez-7] 1 2 "Entrez Gene: PRKD2 protein kinase D2".

Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme 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	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

PRKD2

Function

References

Further reading