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PredicateObject
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Serine/threonine-protein kinase VPS15
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VPS15_YEAST
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http://www.biopax.org/relea...
2.7.11.1, Golgi-retention defective mutant protein 8, Vacuolar protein sorting-associated protein 15
http://www.biopax.org/relea...
FUNCTION: Serine/threonine-protein kinase required for cytoplasm to vacuole transport (Cvt) and autophagy as a part of the autophagy-specific VPS34 PI3-kinase complex I. This complex is essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure. Is also involved in endosome-to-Golgi retrograde transport as part of the VPS34 PI3-kinase complex II. This second complex is required for the endosome-to-Golgi retrieval of PEP1 and KEX2, and the recruitment of VPS5 and VPS7, two components of the retromer complex, to endosomal membranes (probably through the synthesis of a specific pool of phosphatidylinositol 3-phosphate recruiting the retromer to the endosomes). By regulating VPS34 kinase activity, VPS15 appears to be essential for the efficient delivery of soluble hydrolases to the yeast vacuole. CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. SUBUNIT: Component of the autophagy-specific VPS34 PI3-kinase complex I composed of VPS15, VPS30, VPS34 and ATG14; and of the VPS34 PI3-kinase complex II composed of VPS15, VPS30, VPS34 and VPS38. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane; Lipid-anchor. Endosome membrane; Lipid-anchor. DOMAIN: Truncation of 30 residues from the C-terminus results in a temperature-conditional defect in protein sorting. PTM: Autophosphorylated. MISCELLANEOUS: Present with 279 molecules/cell in log phase SD medium. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. SIMILARITY: Contains 4 HEAT repeats. SIMILARITY: Contains 1 protein kinase domain. SIMILARITY: Contains 6 WD repeats. GENE SYNONYMS: GRD8 VAC4 VPL19. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
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