Q6FRH8 · VPS15_CANGA
- Proteinnon-specific serine/threonine protein kinase
- GeneVPS15
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1410 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
Serine/threonine-protein kinase that plays a role in signaling in modulation of host immune response, intracellular survival and virulence (PubMed:25223215).
Required for impediment of phagosomal maturation in THP-1 macrophages (PubMed:25223215).
Regulatory subunit of the autophagy-specific VPS34 PI3-kinase complex I essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure (By similarity).
Within the PS34 PI3-kinase complex I, VPS15-mediated phosphorylation of VPS34 may be required for recruiting VPS34 to the membrane but not for activation of its PI3K activity (PubMed:25223215).
Is also involved in endosome-to-Golgi retrograde transport as part of the VPS34 PI3-kinase complex II (By similarity).
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 similarity).
By regulating VPS34 kinase activity, VPS15 appears to be essential for the efficient delivery of soluble hydrolases to the yeast vacuole (By similarity).
Required for impediment of phagosomal maturation in THP-1 macrophages (PubMed:25223215).
Regulatory subunit of the autophagy-specific VPS34 PI3-kinase complex I essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure (By similarity).
Within the PS34 PI3-kinase complex I, VPS15-mediated phosphorylation of VPS34 may be required for recruiting VPS34 to the membrane but not for activation of its PI3K activity (PubMed:25223215).
Is also involved in endosome-to-Golgi retrograde transport as part of the VPS34 PI3-kinase complex II (By similarity).
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 similarity).
By regulating VPS34 kinase activity, VPS15 appears to be essential for the efficient delivery of soluble hydrolases to the yeast vacuole (By similarity).
Catalytic activity
- L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+This reaction proceeds in the forward direction.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endosome membrane | |
Cellular Component | Golgi apparatus | |
Cellular Component | late endosome | |
Cellular Component | nucleus-vacuole junction | |
Cellular Component | phosphatidylinositol 3-kinase complex, class III, type I | |
Cellular Component | phosphatidylinositol 3-kinase complex, class III, type II | |
Cellular Component | vacuole-isolation membrane contact site | |
Molecular Function | ATP binding | |
Molecular Function | histone H2AS1 kinase activity | |
Molecular Function | ubiquitin binding | |
Biological Process | cellular response to potassium ion starvation | |
Biological Process | late endosome to vacuole transport | |
Biological Process | pexophagy | |
Biological Process | phosphatidylinositol phosphate biosynthetic process | |
Biological Process | positive regulation of transcription elongation by RNA polymerase II | |
Biological Process | protein localization to vacuole | |
Biological Process | protein phosphorylation | |
Biological Process | protein retention in Golgi apparatus | |
Biological Process | protein targeting to vacuole | |
Biological Process | vacuole inheritance |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namenon-specific serine/threonine protein kinase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Nakaseomyces
Accessions
- Primary accessionQ6FRH8
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Golgi apparatus, trans-Golgi network membrane ; Lipid-anchor
Endosome membrane ; Lipid-anchor
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Leads to large vacuoles and defective respiratory growth (PubMed:25223215).
Blocks maturation of the phagosomes and renders cells hyperadherent to epithelial cells and susceptible to the antimicrobial arsenal of primary murine and cultured human macrophages, as well as to thermal, salt, oxidative, genotoxic, cell wall and cell membrane stresses (PubMed:25223215).
Displays defects in protein trafficking (PubMed:25223215).
Blocks maturation of the phagosomes and renders cells hyperadherent to epithelial cells and susceptible to the antimicrobial arsenal of primary murine and cultured human macrophages, as well as to thermal, salt, oxidative, genotoxic, cell wall and cell membrane stresses (PubMed:25223215).
Displays defects in protein trafficking (PubMed:25223215).
Miscellaneous
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000458894 | 1-1410 | non-specific serine/threonine protein kinase | |||
Sequence: MGGQLSLLAQTAPSIGIFSYIDILDETHYVSQLNNSRFLKTCKALDPNGEIVVKVFIKPKEDSSLEKIIQRLKREAVLLSALPNVLNYSKIFESTRCGYLVRQHLKTNLYDRLSTRPYFTEIETKFVVFQLLQALKDIHDLDVIHGDIKTENLLLTSWDWVVLSDFCSNIKPAYIPDDNPGEFSFYFDTSKRRACYLAPEKFDSAKASGDGVHQATKEMDIFSLGCCIAELYLDGAALFNLSQLFKYKSGDYTLNDILPQTISKSSPVLKDILQDMLQVDPKKRLSAHELLEKYRTIYFPDTFYDFLYDYCKTLVTLGTSVPCADQIEVNTTLQDHLGSIDEILIKIYCDFGRICKSLKLPVLDQEDMNYNTKDSFLRVSDKLLRLENYETDKITASIQNEVSLIILVFLCKEFRNLQFPENKVKALQLILAFSLFVLDDTKLDRTLPYLVAALEDDSTRVKVMAMNCVTTLIKEVKHPNQLNENIFVDYLLPRVQALLQNGQEESLVRVAIASNLSDLALKANLFQEYCHTMQSSTIPNIVHDFESIEVIRKYSRKLQQLFEDLTVSILTDPEISVKVALLKNILPLCKYFGREKTNDVILSHLITYLNDRDPALRMYLVECISGIAILLGPITMEQYILPLIIQTITDEEELVVVSVLKNLKDLLKTRFVNKKYFYDITKFLSPLILHPNSWIRNFVLTTLVECINQMSKAEVYCVLYPVLRPFFDFDVDFTGDMLISCAKLPVSRNTYNLLRSWNNRSKKTFFWQRVTTNYVDAFGNSTINFVDKRYVKENYGLKTMKVESNIHLHTNENENIPLTLEDKFWIDKFKNSGLTDNELWKIVALREYVVRSSRSSSKKPETVTSIVSKLSLTPSNFSIENVMPNTVFFDIEFLHPETLTFNDLDVTNTNSIKESESNTFTDNHSKVIEMKGSLIFKTPRIPTTLSNLKNIYVQLEPTNNHSEGHAHLSARNQPANFIVKSSYEGQDKIIEKYLKQLNILPSLKEYKEFGFVSENTTAEADVINLHGKFVRSYPQIFDGTLLQSEVLLGTKSFMIYGSDQGALTVWDIDRLANEKSITRPLYYECSAEITCIKGLSGYDSFCVGLKSSEILIFRISLSKNGKAKNLQELICIRSLNLIGENSSEYPIQIECCPNNDQFQLVVLSNYSNVYLFDIRTMKVIEKLELNADYGCTISMVLDDKNNLLFFGTVSGIIEMWDARYFVQIRAWTFGESLPINKLAIMEQENKSLLVVCGGVDSAFFTLWNIEKLSCKHVFVRSNEQPSLDSFNVIDADKLDKLAFEKNNSNIKPIVQIFNNKVLYMDDIGRLLHILDTRNPEKSSTFAGSKVELHSFSVLQVTASLTMSLQKHNYQKEVNNSNYTSSRVMTVNVFQLKNKPYMLLTDEEGYINIYT |
Post-translational modification
Autophosphorylated.
Keywords
- PTM
Interaction
Subunit
Component of the autophagy-specific VPS34 PI3-kinase complex I composed of VPS15, VPS30, VPS34, ATG14 and ATG38; and of the VPS34 PI3-kinase complex II composed of VPS15, VPS30, VPS34 and VPS38.
Protein-protein interaction databases
Family & Domains
Features
Showing features for domain, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 27-299 | Protein kinase | ||||
Sequence: THYVSQLNNSRFLKTCKALDPNGEIVVKVFIKPKEDSSLEKIIQRLKREAVLLSALPNVLNYSKIFESTRCGYLVRQHLKTNLYDRLSTRPYFTEIETKFVVFQLLQALKDIHDLDVIHGDIKTENLLLTSWDWVVLSDFCSNIKPAYIPDDNPGEFSFYFDTSKRRACYLAPEKFDSAKASGDGVHQATKEMDIFSLGCCIAELYLDGAALFNLSQLFKYKSGDYTLNDILPQTISKSSPVLKDILQDMLQVDPKKRLSAHELLEKYRTIYF | ||||||
Repeat | 441-478 | HEAT 1 | ||||
Sequence: TKLDRTLPYLVAALEDDSTRVKVMAMNCVTTLIKEVKH | ||||||
Repeat | 485-525 | HEAT 2 | ||||
Sequence: NIFVDYLLPRVQALLQNGQEESLVRVAIASNLSDLALKANL | ||||||
Repeat | 556-594 | HEAT 3 | ||||
Sequence: RKLQQLFEDLTVSILTDPEISVKVALLKNILPLCKYFGR | ||||||
Repeat | 596-633 | HEAT 4 | ||||
Sequence: KTNDVILSHLITYLNDRDPALRMYLVECISGIAILLGP | ||||||
Repeat | 635-672 | HEAT 5 | ||||
Sequence: TMEQYILPLIIQTITDEEELVVVSVLKNLKDLLKTRFV | ||||||
Repeat | 1037-1076 | WD 1 | ||||
Sequence: FDGTLLQSEVLLGTKSFMIYGSDQGALTVWDIDRLANEKS | ||||||
Repeat | 1187-1226 | WD 2 | ||||
Sequence: ADYGCTISMVLDDKNNLLFFGTVSGIIEMWDARYFVQIRA | ||||||
Repeat | 1230-1273 | WD 3 | ||||
Sequence: GESLPINKLAIMEQENKSLLVVCGGVDSAFFTLWNIEKLSCKHV |
Sequence similarities
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,410
- Mass (Da)161,501
- Last updated2004-07-19 v1
- Checksum8FCA4E775FCF85E2
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CR380954 EMBL· GenBank· DDBJ | CAG60099.1 EMBL· GenBank· DDBJ | Genomic DNA |