PRKD2

Protein kinase D2
PDB rendering based on 2coa.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2COA​, 3BGM​, 4NNX​, 4NNY​
Identifiers
Symbols	PRKD2 ; HSPC187; 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 • nucleoplasm • cytoplasm • Golgi apparatus • plasma membrane Biological process • angiogenesis • positive regulation of endothelial cell proliferation • adaptive immune response • 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 • protein kinase D signaling • activation of mitophagy in response to mitochondrial depolarization • 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
Entrez	25865	101540
Ensembl	ENSG00000105287	ENSMUSG00000041187
UniProt	Q9BZL6	Q8BZ03
RefSeq (mRNA)	NM_001079880	NM_001252458
RefSeq (protein)	NP_001073349	NP_001239387
Location (UCSC)	Chr 19: 46.67 – 46.72 Mb	Chr 7: 16.84 – 16.87 Mb
PubMed search

Serine/threonine-protein kinase D2 or PKD2 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

1. 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.
2. 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. "Entrez Gene: PRKD2 protein kinase D2".

Further reading

• 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.