- PRKD2
Protein kinase D2, also known as PRKD2, is a human
gene .cite web | title = Entrez Gene: PRKD2 protein kinase D2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=25865| accessdate = ]PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: PRKD2 protein kinase D2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=25865| accessdate = ]References
Further reading
PBB_Further_reading
citations =
*cite journal | author=Zhang QH, Ye M, Wu XY, "et al." |title=Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. |journal=Genome Res. |volume=10 |issue= 10 |pages= 1546–60 |year= 2001 |pmid= 11042152 |doi=
*cite journal | author=Sturany S, Van Lint J, Muller F, "et al." |title=Molecular cloning and characterization of the human protein kinase D2. A novel member of the protein kinase D family of serine threonine kinases. |journal=J. Biol. Chem. |volume=276 |issue= 5 |pages= 3310–8 |year= 2001 |pmid= 11062248 |doi= 10.1074/jbc.M008719200
*cite journal | author=Sturany S, Van Lint J, Gilchrist A, "et al." |title=Mechanism of activation of protein kinase D2(PKD2) by the CCK(B)/gastrin receptor. |journal=J. Biol. Chem. |volume=277 |issue= 33 |pages= 29431–6 |year= 2002 |pmid= 12058027 |doi= 10.1074/jbc.M200934200
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Rey O, Yuan J, Rozengurt E |title=Intracellular redistribution of protein kinase D2 in response to G-protein-coupled receptor agonists. |journal=Biochem. Biophys. Res. Commun. |volume=302 |issue= 4 |pages= 817–24 |year= 2003 |pmid= 12646243 |doi=
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Yeaman C, Ayala MI, Wright JR, "et al." |title=Protein kinase D regulates basolateral membrane protein exit from trans-Golgi network. |journal=Nat. Cell Biol. |volume=6 |issue= 2 |pages= 106–12 |year= 2004 |pmid= 14743217 |doi= 10.1038/ncb1090
*cite journal | author=Mihailovic T, Marx M, Auer A, "et al." |title=Protein kinase D2 mediates activation of nuclear factor kappaB by Bcr-Abl in Bcr-Abl+ human myeloid leukemia cells. |journal=Cancer Res. |volume=64 |issue= 24 |pages= 8939–44 |year= 2005 |pmid= 15604256 |doi= 10.1158/0008-5472.CAN-04-0981
*cite journal | author=Parra M, Kasler H, McKinsey TA, "et al." |title=Protein kinase D1 phosphorylates HDAC7 and induces its nuclear export after T-cell receptor activation. |journal=J. Biol. Chem. |volume=280 |issue= 14 |pages= 13762–70 |year= 2005 |pmid= 15623513 |doi= 10.1074/jbc.M413396200
*cite journal | author=Auer A, von Blume J, Sturany S, "et al." |title=Role of the regulatory domain of protein kinase D2 in phorbol ester binding, catalytic activity, and nucleocytoplasmic shuttling. |journal=Mol. Biol. Cell |volume=16 |issue= 9 |pages= 4375–85 |year= 2006 |pmid= 15975900 |doi= 10.1091/mbc.E05-03-0251
*cite journal | author=Kim JE, Tannenbaum SR, White FM |title=Global phosphoproteome of HT-29 human colon adenocarcinoma cells. |journal=J. Proteome Res. |volume=4 |issue= 4 |pages= 1339–46 |year= 2005 |pmid= 16083285 |doi= 10.1021/pr050048h
*cite journal | author=Kimura K, Wakamatsu A, Suzuki Y, "et al." |title=Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. |journal=Genome Res. |volume=16 |issue= 1 |pages= 55–65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406
*cite journal | author=Jackson LN, Li J, Chen LA, "et al." |title=Overexpression of wild-type PKD2 leads to increased proliferation and invasion of BON endocrine cells. |journal=Biochem. Biophys. Res. Commun. |volume=348 |issue= 3 |pages= 945–9 |year= 2006 |pmid= 16899224 |doi= 10.1016/j.bbrc.2006.07.142
*cite journal | author=Chiu TT, Leung WY, Moyer MP, "et al." |title=Protein kinase D2 mediates lysophosphatidic acid-induced interleukin 8 production in nontransformed human colonic epithelial cells through NF-kappaB. |journal=Am. J. Physiol., Cell Physiol. |volume=292 |issue= 2 |pages= C767–77 |year= 2007 |pmid= 16928771 |doi= 10.1152/ajpcell.00308.2006
*cite journal | author=Irie A, Harada K, Tsukamoto H, "et al." |title=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. |journal=Int. Immunol. |volume=18 |issue= 12 |pages= 1737–47 |year= 2007 |pmid= 17077180 |doi= 10.1093/intimm/dxl108
*cite journal | author=Olsen JV, Blagoev B, Gnad F, "et al." |title=Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. |journal=Cell |volume=127 |issue= 3 |pages= 635–48 |year= 2006 |pmid= 17081983 |doi= 10.1016/j.cell.2006.09.026
*cite journal | author=Kollers S, Musilova P, Rubes J, Rocha D |title=Comparative mapping reveals multiple rearrangements between pig chromosome 6 and human 19q13. |journal=Anim. Genet. |volume=37 |issue= 6 |pages= 595–6 |year= 2007 |pmid= 17121608 |doi= 10.1111/j.1365-2052.2006.01516.x
*cite journal | author=Wissing J, Jänsch L, Nimtz M, "et al." |title=Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry. |journal=Mol. Cell Proteomics |volume=6 |issue= 3 |pages= 537–47 |year= 2007 |pmid= 17192257 |doi= 10.1074/mcp.T600062-MCP200PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes
Wikimedia Foundation. 2010.
