Protein kinase D1

Protein kinase D1
Identifiers
Symbols	PRKD1; PKC-MU; PKCM; PKD; PRKCM
External IDs	OMIM: 605435 MGI: 99879 HomoloGene: 55680 GeneCards: PRKD1 Gene
EC number	2.7.11.13
Gene Ontology Molecular function • nucleotide binding • protein serine/threonine kinase activity • protein serine/threonine kinase activity • protein kinase C activity • protein binding • ATP binding • metal ion binding Cellular component • nucleus • cytoplasm • Golgi apparatus • trans-Golgi network • cytosol • cytosol • plasma membrane • integral to plasma membrane • cell-cell junction • cell cortex Biological process • positive regulation of endothelial cell proliferation • sphingolipid metabolic process • apoptotic process • inflammatory response • Golgi organization • signal transduction • integrin-mediated signaling pathway • intracellular protein kinase cascade • intracellular protein kinase cascade • nervous system development • cell proliferation • positive regulation of endothelial cell migration • regulation of keratinocyte proliferation • positive regulation of neuron projection development • peptidyl-serine phosphorylation • sphingolipid biosynthetic process • cell differentiation • positive regulation of CREB transcription factor activity • cellular response to oxidative stress • endothelial cell chemotaxis • cellular response to vascular endothelial growth factor stimulus • cellular response to vascular endothelial growth factor stimulus • positive regulation of I-kappaB kinase/NF-kappaB cascade • positive regulation of blood vessel endothelial cell migration • positive regulation of blood vessel endothelial cell migration • small molecule metabolic process • innate immune response • positive regulation of osteoblast differentiation • positive regulation of angiogenesis • positive regulation of angiogenesis • negative regulation of endocytosis • positive regulation of transcription from RNA polymerase II promoter • protein autophosphorylation • vascular endothelial growth factor receptor signaling pathway • Golgi vesicle transport • positive regulation of NF-kappaB transcription factor activity • negative regulation of cell death • regulation of integrin-mediated signaling pathway Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	5587	18760
Ensembl	ENSG00000184304	ENSMUSG00000002688
UniProt	Q15139	Q62101
RefSeq (mRNA)	NM_002742.2	NM_008858.3
RefSeq (protein)	NP_002733.2	NP_032884.2
Location (UCSC)	Chr 14: 30.05 – 30.66 Mb	Chr 12: 51.44 – 51.75 Mb
PubMed search	[1]	[2]

Serine/threonine-protein kinase D1 is an enzyme that in humans is encoded by the PRKD1 gene.

Members of the protein kinase C (PKC) family function in many extracellular receptor-mediated signal transduction pathways. See PRKCA (MIM 176960) for further background information. The PRKCM gene encodes a cytosolic serine-threonine kinase that binds to the trans-Golgi network and regulates the fission of transport carriers specifically destined to the cell surface.[supplied by OMIM]

Interactions

Protein kinase D1 has been shown to interact with Centaurin, alpha 1, C1QBP, YWHAQ, Metallothionein 2A and Bruton's tyrosine kinase.

Further reading

• Van Lint J, Rykx A, Maeda Y, et al. (2002). "Protein kinase D: an intracellular traffic regulator on the move". Trends Cell Biol. 12 (4): 193–200. doi:10.1016/S0962-8924(02)02262-6. PMID 11978539. 
• Busch H, Eisenhart-Rothe BV (1976). "[Old and new dangers of blood transfusion (author's transl)]". MMW, Münchener medizinische Wochenschrift 118 (22): 713–8. PMID 5668. 
• Jakobovits A, Rosenthal A, Capon DJ (1990). "Trans-activation of HIV-1 LTR-directed gene expression by tat requires protein kinase C". EMBO J. 9 (4): 1165–70. PMC 551792. PMID 2182321. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=551792. 
• Davis RJ, Czech MP (1985). "Tumor-promoting phorbol diesters cause the phosphorylation of epidermal growth factor receptors in normal human fibroblasts at threonine-654". Proc. Natl. Acad. Sci. U.S.A. 82 (7): 1974–8. doi:10.1073/pnas.82.7.1974. PMC 397463. PMID 2984676. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=397463. 
• Davis RJ, Czech MP (1985). "Platelet-derived growth factor mimics phorbol diester action on epidermal growth factor receptor phosphorylation at threonine-654". Proc. Natl. Acad. Sci. U.S.A. 82 (12): 4080–4. doi:10.1073/pnas.82.12.4080. PMC 397938. PMID 2987962. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=397938. 
• Conant K, Ma M, Nath A, Major EO (1996). "Extracellular human immunodeficiency virus type 1 Tat protein is associated with an increase in both NF-kappa B binding and protein kinase C activity in primary human astrocytes". J. Virol. 70 (3): 1384–9. PMC 189957. PMID 8627654. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=189957. 
• Sidorenko SP, Law CL, Klaus SJ, et al. (1996). "Protein kinase C mu (PKC mu) associates with the B cell antigen receptor complex and regulates lymphocyte signaling". Immunity 5 (4): 353–63. doi:10.1016/S1074-7613(00)80261-7. PMID 8885868. 
• Holmes AM (1996). "In vitro phosphorylation of human immunodeficiency virus type 1 Tat protein by protein kinase C: evidence for the phosphorylation of amino acid residue serine-46". Arch. Biochem. Biophys. 335 (1): 8–12. doi:10.1006/abbi.1996.0476. PMID 8914829. 
• Borgatti P, Zauli G, Cantley LC, Capitani S (1998). "Extracellular HIV-1 Tat protein induces a rapid and selective activation of protein kinase C (PKC)-alpha, and -epsilon and -zeta isoforms in PC12 cells". Biochem. Biophys. Res. Commun. 242 (2): 332–7. doi:10.1006/bbrc.1997.7877. PMID 9446795. 
• Zidovetzki R, Wang JL, Chen P, et al. (1998). "Human immunodeficiency virus Tat protein induces interleukin 6 mRNA expression in human brain endothelial cells via protein kinase C- and cAMP-dependent protein kinase pathways". AIDS Res. Hum. Retroviruses 14 (10): 825–33. doi:10.1089/aid.1998.14.825. PMID 9671211. 
• Waldron RT, Iglesias T, Rozengurt E (1999). "The pleckstrin homology domain of protein kinase D interacts preferentially with the eta isoform of protein kinase C". J. Biol. Chem. 274 (14): 9224–30. doi:10.1074/jbc.274.14.9224. PMID 10092595. 
• Hausser A, Storz P, Link G, et al. (1999). "Protein kinase C mu is negatively regulated by 14-3-3 signal transduction proteins". J. Biol. Chem. 274 (14): 9258–64. doi:10.1074/jbc.274.14.9258. PMID 10092600. 
• Jamora C, Yamanouye N, Van Lint J, et al. (1999). "Gbetagamma-mediated regulation of Golgi organization is through the direct activation of protein kinase D". Cell 98 (1): 59–68. doi:10.1016/S0092-8674(00)80606-6. PMID 10412981. 
• Bagowski CP, Stein-Gerlach M, Choidas A, Ullrich A (1999). "Cell-type specific phosphorylation of threonines T654 and T669 by PKD defines the signal capacity of the EGF receptor". EMBO J. 18 (20): 5567–76. doi:10.1093/emboj/18.20.5567. PMC 1171625. PMID 10523301. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1171625. 
• Johannes FJ, Hausser A, Storz P, et al. (1999). "Bruton's tyrosine kinase (Btk) associates with protein kinase C mu". FEBS Lett. 461 (1–2): 68–72. doi:10.1016/S0014-5793(99)01424-6. PMID 10561498. 
• Storz P, Hausser A, Link G, et al. (2000). "Protein kinase C [micro] is regulated by the multifunctional chaperon protein p32". J. Biol. Chem. 275 (32): 24601–7. doi:10.1074/jbc.M002964200. PMID 10831594. 
• Mayne M, Holden CP, Nath A, Geiger JD (2000). "Release of calcium from inositol 1,4,5-trisphosphate receptor-regulated stores by HIV-1 Tat regulates TNF-alpha production in human macrophages". J. Immunol. 164 (12): 6538–42. PMID 10843712. 
• Matthews SA, Iglesias T, Rozengurt E, Cantrell D (2000). "Spatial and temporal regulation of protein kinase D (PKD)". EMBO J. 19 (12): 2935–45. doi:10.1093/emboj/19.12.2935. PMC 203351. PMID 10856238. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=203351. 
• Vertommen D, Rider M, Ni Y, et al. (2000). "Regulation of protein kinase D by multisite phosphorylation. Identification of phosphorylation sites by mass spectrometry and characterization by site-directed mutagenesis". J. Biol. Chem. 275 (26): 19567–76. doi:10.1074/jbc.M001357200. PMID 10867018.