Serine/threonine-protein kinase D3
Also known as: EPK2, PRKCN, PRKD3
Function
Converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. Involved in resistance to oxidative stress (By similarity).
Classification
- Family (Pfam)
- PF00130 C1_1, PF00169 PH, PF00069 Pkinase, PF25525 Ubiquitin_PRKD1_N
- InterPro
- C1-like_sf, DAG/PE-bd, Kinase-like_dom_sf, PH-like_dom_sf, PH_domain, PKC_DAG/PE, Prot_kinase_dom, Protein_kinase_ATP_BS, Protein_Kinase_C_mu-related, Ser/Thr_kinase_AS, Ubiquitin_PRKD1-3_N
- Functional cluster
- Protein Serine/Threonine Kinases
Experimental structures · PDB · 1
- 2D9Z NMR
A predicted model is available from AlphaFold.
Gene Ontology · 13
- GO:0005829 cytosol
- GO:0005886 plasma membrane
- GO:0005524 ATP binding
- GO:0004697 diacylglycerol-dependent serine/threonine kinase activity
- GO:0004699 diacylglycerol-dependent, calcium-independent serine/threonine kinase activity
- GO:0016301 kinase activity
- GO:0106310 protein serine kinase activity
- GO:0004674 protein serine/threonine kinase activity
- GO:0008270 zinc ion binding
- GO:0035556 intracellular signal transduction
- GO:0007200 phospholipase C-activating G protein-coupled receptor signaling pathway
- GO:0006468 protein phosphorylation
- GO:0030148 sphingolipid biosynthetic process
Drugs targeting this protein · 5
- GSK-690693 inhibitor
- SOTRASTAURIN inhibitor
- UCN-01 inhibitor
- CEP-2563 DIHYDROCHLORIDE inhibitor
- MIDOSTAURIN inhibitor
Related proteins · sequence + function similarity
- Serine/threonine-protein kinase D3 0.99
- Serine/threonine-protein kinase D1 0.96
- Serine/threonine-protein kinase D1 0.96
- Serine/threonine-protein kinase D1 0.95
- Serine/threonine-protein kinase D2 0.86
- Serine/threonine-protein kinase D2 0.85
- Serine/threonine-protein kinase D2 0.85
- Serine/threonine-protein kinase N2 0.76
- Serine/threonine-protein kinase N2 0.75
- Serine/threonine-protein kinase N2 0.75
- Serine/threonine-protein kinase N2 0.73
- Serine/threonine-protein kinase dkf-2 0.73
Co-cited proteins · studied together in the literature
- Serine/threonine-protein kinase D2 1 shared papers
- Serine/threonine-protein kinase D1 1 shared papers
Literature · 12 cited papers
- Toward a comprehensive characterization of a human cancer cell phosphoproteome. J. Proteome Res. · 2013
- Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci. Signal. · 2010
- Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal. Chem. · 2009
- Large-scale proteomics analysis of the human kinome. Mol. Cell. Proteomics · 2009
- Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol. Cell · 2008
- A quantitative atlas of mitotic phosphorylation. Proc. Natl. Acad. Sci. U.S.A. · 2008
- Selective binding of phorbol esters and diacylglycerol by individual C1 domains of the PKD family. Biochem. J. · 2008
- Patterns of somatic mutation in human cancer genomes. Nature · 2007
- A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat. Biotechnol. · 2006
- Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature · 2005
- The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. · 2004
- PKCnu, a new member of the protein kinase C family, composes a fourth subfamily with PKCmu. Biochim. Biophys. Acta · 1999
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