PRKD2

From Wikipedia, the free encyclopedia

Protein kinase D2

PDB rendering based on 2coa.

Available structures: 2coa

Identifiers

Symbol(s)

PRKD2; PKD2; HSPC187

External IDs

OMIM: 607074 MGI: 2141917 HomoloGene: 9516

Gene ontology
Molecular Function:	• nucleotide binding • protein serine/threonine kinase activity • ATP binding • zinc ion binding • transferase activity • diacylglycerol binding • metal ion binding
Cellular Component:	• intracellular
Biological Process:	• protein amino acid phosphorylation • intracellular signaling cascade

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001079880 (mRNA)
NP_001073349 (protein)

NM_178900 (mRNA)
NP_849231 (protein)

Location

Chr 19: 51.87 - 51.91 Mb

Chr 7: 16 - 16.03 Mb

Pubmed search

[1]

[2]

Protein kinase D2, also known as PRKD2, is a human gene.^[1]

The protein encoded by this gene belongs to the protein kinase D (PKD) family of serine/threonine protein kinases. 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.^[1]

[edit] References

^ ^a ^b Entrez Gene: PRKD2 protein kinase D2.

[edit] Further reading

Zhang QH, Ye M, Wu XY, et al. (2001). "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. PMID 11042152.
Sturany S, Van Lint J, Muller F, et al. (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.
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. 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. 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. 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. 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. 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. 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.