PRKD2: Difference between revisions

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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Serine/threonine-protein kinase D2''' or PKD2 is an [[enzyme]] that in humans is encoded by the ''PRKD2'' [[gene]].<ref name="pmid11042152">{{cite journal |vauthors=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 | 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 |date=Nov 2000 | pmid = 11042152 | pmc = 310934 | doi =10.1101/gr.140200  }}</ref><ref name="pmid11062248">{{cite journal |vauthors=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 | 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 |date=May 2001 | pmid = 11062248 | pmc = | doi = 10.1074/jbc.M008719200 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PRKD2 protein kinase D2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=25865| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_PRKD2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2coa.
| PDB = {{PDB2|2coa}}
| Name = Protein kinase D2
| HGNCid = 17293
| Symbol = PRKD2
| AltSymbols =; PKD2; HSPC187
| OMIM = 607074
| ECnumber = 
| Homologene = 9516
| MGIid = 2141917
| GeneAtlas_image1 = PBB_GE_PRKD2_209282_at_tn.png
| GeneAtlas_image2 = PBB_GE_PRKD2_38269_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0019992 |text = diacylglycerol binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 25865
    | Hs_Ensembl = ENSG00000105287
    | Hs_RefseqProtein = NP_001073349
    | Hs_RefseqmRNA = NM_001079880
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 19
    | Hs_GenLoc_start = 51869417
    | Hs_GenLoc_end = 51911597
    | Hs_Uniprot = Q9BZL6
    | Mm_EntrezGene = 101540
    | Mm_Ensembl = ENSMUSG00000041187
    | Mm_RefseqmRNA = NM_178900
    | Mm_RefseqProtein = NP_849231
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 7
    | Mm_GenLoc_start = 16001456
    | Mm_GenLoc_end = 16028881
    | Mm_Uniprot = Q3V3F5
  }}
}}
'''Protein kinase D2''', also known as '''PRKD2''', is a human [[gene]].<ref name="entrez">{{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 = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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|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 [[Cell membrane#Membrane polarity|basolateral membrane]] protein exit from TGN. [[Alternative splicing]] results in multiple transcript variants encoding different isoforms.<ref name="entrez"/>
{{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.<ref name="entrez">{{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 = }}</ref>
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{cite journal   |vauthors=Sturany S, Van Lint J, Gilchrist A, etal |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 }}
| citations =
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |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 | pmc=139241 }}
*{{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  |vauthors=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=10.1016/S0006-291X(03)00269-9 }}
*{{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   |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |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=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   |vauthors=Yeaman C, Ayala MI, Wright JR, etal |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 |pmc=3372901}}
*{{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   |vauthors=Mihailovic T, Marx M, Auer A, etal |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=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   |vauthors=Parra M, Kasler H, McKinsey TA, etal |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=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   |vauthors=Auer A, von Blume J, Sturany S, etal |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 | pmc=1196345 |url=http://www.molbiolcell.org/content/16/9/4375.full.pdf }}
*{{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  |vauthors=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=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   |vauthors=Kimura K, Wakamatsu A, Suzuki Y, etal |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 | pmc=1356129 }}
*{{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   |vauthors=Jackson LN, Li J, Chen LA, etal |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 | pmc=2430871 }}
*{{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   |vauthors=Chiu TT, Leung WY, Moyer MP, etal |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=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   |vauthors=Irie A, Harada K, Tsukamoto H, etal |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=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   |vauthors=Olsen JV, Blagoev B, Gnad F, etal |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=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  |vauthors=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=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   |vauthors=Wissing J, Jänsch L, Nimtz M, etal |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-MCP200 }}
*{{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-MCP200 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{PDB Gallery|geneid=25865}}
{{WikiDoc Sources}}
{{Serine/threonine-specific protein kinases}}
{{Enzymes}}
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[[Category:EC 2.7.11]]
 
 
{{gene-19-stub}}

Latest revision as of 14:28, 4 November 2018

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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. ↑ 3.0 3.1 "Entrez Gene: PRKD2 protein kinase D2".

Further reading


Retrieved from "https://www.wikidoc.org/index.php?title=PRKD2&oldid=1529843"