PRKD2
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RefSeq (protein) | |||||||||
Location (UCSC) | Chr 19: 46.67 – 46.72 Mb | Chr 7: 16.58 – 16.6 Mb | |||||||
PubMed search | [3] | [4] |
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.[5][6][7]
Function
The protein encoded by this gene belongs to the
trans-Golgi network (TGN) and may regulate basolateral membrane protein exit from TGN. Alternative splicing results in multiple transcript variants encoding different isoforms.[7]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000105287 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000041187 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- PMID 11042152.
- PMID 11062248.
- ^ a b "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. 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. 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. 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. 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. 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. 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. 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. 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. 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. PMID 16899224.
- Chiu TT, Leung WY, 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. 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. 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. 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. PMID 17192257.