Protein kinase D1
mammalian protein found in Homo sapiens
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Summary
Protein kinase D1 is a protein[1]. It is known by 8 alternative names across languages and contexts.[2]
Key Facts
- Physically interacts with: sotrastaurin[3], gsk-690693[4]
- Part of: Protein kinase-like domain superfamily[5], PH-like domain superfamily[6], protein kinase C mu-related[7], pleckstrin homology domain, protein family[8], Protein kinase C-like, phorbol ester/diacylglycerol-binding domain, protein family[9], Diacylglycerol/phorbol-ester binding domain, protein family[10], Protein kinase domain, protein family[11], Protein kinase, ATP binding site, protein family[12], Serine/threonine-protein kinase, active site, protein family[13]
- Has part(s): diacylglycerol/phorbol-ester binding[14], protein kinase C-like, phorbol ester/diacylglycerol-binding domain[15], protein kinase, ATP binding site[16], pleckstrin homology domain[17], protein kinase domain[18], serine/threonine-protein kinase, active site[19]
- Molecular function: transferase activity[20], nucleotide binding[21], protein kinase activity[22], protein kinase C activity[23], metal ion binding[24], kinase activity[25], protein binding[26], identical protein binding[27], ATP binding[28], protein serine/threonine kinase activity[29]
- Cell component: Golgi apparatus[30], membrane[31], plasma membrane[32], integral component of plasma membrane[33], autophagosome membrane[34], cytoplasm[35], trans-Golgi network[36], cytosol[37]
- Biological process: negative regulation of endocytosis[38], cell differentiation[39], intracellular signal transduction[40], positive regulation of endothelial cell proliferation[41], regulation of protein stability[42], Golgi organization[43], phosphorylation[44], immune system process[45], positive regulation of endothelial cell chemotaxis[46], protein kinase D signaling[47], sphingolipid biosynthetic process[48], negative regulation of cell death[49], nervous system development[50], positive regulation of peptidyl-serine phosphorylation[51]