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	OMIM: 607074; MGI: 2141917; HomoloGene: 9516; GeneCards: PRKD2; OMA:PRKD2 - orthologs
Gene location (Human) Chr. Chromosome 19 (human) Band 19q13.32 Start 46,674,275 bp End 46,717,127 bp
Gene location (Mouse) Chr. Chromosome 7 (mouse) Band 7|7 A2 Start 16,576,827 bp End 16,604,389 bp
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
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.

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.

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. 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.