P40343 · VPS27_YEAST
- ProteinVacuolar protein sorting-associated protein 27
- GeneVPS27
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids622 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB) and recruits ESCRT-I to the MVB outer membrane (PubMed:11416128, PubMed:11872141, PubMed:12055639, PubMed:12900393, PubMed:14581452, PubMed:1493335, PubMed:15086794, PubMed:15107463, PubMed:15166140, PubMed:17135292, PubMed:18508771, PubMed:3062374, PubMed:9265642).
Controls exit from the prevacuolar compartment (PVC) in both the forward direction to the vacuole and the return to the Golgi (PubMed:11208109, PubMed:8649377, PubMed:9015300).
Allows VPS10 to return to the (trans-Golgi network) TGN from the PVC (PubMed:8649377).
Might also function as an alternate adapter in the COPIb clathrin-like coat (PubMed:17101773).
Controls exit from the prevacuolar compartment (PVC) in both the forward direction to the vacuole and the return to the Golgi (PubMed:11208109, PubMed:8649377, PubMed:9015300).
Allows VPS10 to return to the (trans-Golgi network) TGN from the PVC (PubMed:8649377).
Might also function as an alternate adapter in the COPIb clathrin-like coat (PubMed:17101773).
Miscellaneous
Present with 172 molecules/cell in log phase SD medium.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 176 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 179 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 192 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 195 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 200 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 203 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 222 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 225 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Keywords
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameVacuolar protein sorting-associated protein 27
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP40343
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endosome membrane ; Peripheral membrane protein
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 185-186 | Decreases the association to PtdIns3P containing membranes. | ||||
Sequence: LL → AA | ||||||
Mutagenesis | 193 | Decreases the association to PtdIns3P containing membranes. | ||||
Sequence: R → A | ||||||
Mutagenesis | 270 | Strongly reduces the ubiquitin-binding activity. | ||||
Sequence: S → D | ||||||
Mutagenesis | 313 | Strongly reduces the ubiquitin-binding activity. | ||||
Sequence: S → D |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 13 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000065893 | 1-622 | Vacuolar protein sorting-associated protein 27 | |||
Sequence: MSVSTPSELDALIEQATSESIPNGDLDLPIALEISDVLRSRRVNPKDSMRCIKKRILNTADNPNTQLSSWKLTNICVKNGGTPFIKEICSREFMDTMEHVILREDSNEELSELVKTILYELYVAFKNDSQLNYVAKVYDKLISRGIKFPEKLTLSNSPTAMFDSKTPADWIDSDACMICSKKFSLLNRKHHCRSCGGVFCQEHSSNSIPLPDLGIYEPVRVCDSCFEDYDLKRHDDSKKSKKHRHKRKKDRDYSTPEDEEELIRKAIELSLKESRNSASSEPIVPVVESKNEVKRQEIEEEEDPDLKAAIQESLREAEEAKLRSERQKASRQMQPQQPSPQPQPIHSVDLSDEEKDSIYMFASLVEKMKSRPLNEILEDSKLQNLAQRVFASKARLNYALNDKAQKYNTLIEMNGKISEIMNIYDRLLEQQLQSINLSQQYTLPQVPSDPYNYLTENVQNPAESYQTPPLQQLSSHQYKPQQDVSRQQSVKANSSPTTNIDHLKTIDVTPHAQQKPQSHVELAPSDPPYPKEEAEDEGTQAVQDEESSTQESRERPYPVETENGETSINKRPQGITRYDFPTVPARKFVQPESTVPLPASSSEIPIKEERPPSPQEELLIEL | ||||||
Modified residue | 157 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 294 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Modified residue | 495 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 613 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Component of the ESCRT-0 complex composed of HSE1 and VPS27 (PubMed:12055639, PubMed:14581452, PubMed:15086794).
Interacts with ENT3 and ENT5, the ESCRT-I subunits VPS23 and VPS28 and with the COPIb subunits SEC27, SEC28 and SEC33 (PubMed:12900393, PubMed:15107463, PubMed:17101773).
May form a complex composed of VPS27, HSE1 and DOA1 (PubMed:18508771).
Interacts with DOA1 (PubMed:18508771).
Interacts with ubiquitin (PubMed:11988742, PubMed:12750381, PubMed:14581452).
Interacts with ENT3 and ENT5, the ESCRT-I subunits VPS23 and VPS28 and with the COPIb subunits SEC27, SEC28 and SEC33 (PubMed:12900393, PubMed:15107463, PubMed:17101773).
May form a complex composed of VPS27, HSE1 and DOA1 (PubMed:18508771).
Interacts with DOA1 (PubMed:18508771).
Interacts with ubiquitin (PubMed:11988742, PubMed:12750381, PubMed:14581452).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P40343 | HSE1 P38753 | 9 | EBI-20380, EBI-1382 | |
BINARY | P40343 | SEC28 P40509 | 2 | EBI-20380, EBI-4884 | |
BINARY | P40343 | STP22 P25604 | 8 | EBI-20380, EBI-411625 | |
XENO | P40343 | UBB P0CG53 | 6 | EBI-20380, EBI-5333021 |
Complex viewer
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, zinc finger, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 18-149 | VHS | ||||
Sequence: SESIPNGDLDLPIALEISDVLRSRRVNPKDSMRCIKKRILNTADNPNTQLSSWKLTNICVKNGGTPFIKEICSREFMDTMEHVILREDSNEELSELVKTILYELYVAFKNDSQLNYVAKVYDKLISRGIKFP | ||||||
Zinc finger | 170-230 | FYVE-type; atypical | ||||
Sequence: WIDSDACMICSKKFSLLNRKHHCRSCGGVFCQEHSSNSIPLPDLGIYEPVRVCDSCFEDYD | ||||||
Region | 236-260 | Disordered | ||||
Sequence: DSKKSKKHRHKRKKDRDYSTPEDEE | ||||||
Domain | 258-277 | UIM 1 | ||||
Sequence: DEEELIRKAIELSLKESRNS | ||||||
Domain | 301-320 | UIM 2 | ||||
Sequence: EEDPDLKAAIQESLREAEEA | ||||||
Region | 317-348 | Disordered | ||||
Sequence: AEEAKLRSERQKASRQMQPQQPSPQPQPIHSV | ||||||
Compositional bias | 462-520 | Polar residues | ||||
Sequence: AESYQTPPLQQLSSHQYKPQQDVSRQQSVKANSSPTTNIDHLKTIDVTPHAQQKPQSHV | ||||||
Region | 462-622 | Disordered | ||||
Sequence: AESYQTPPLQQLSSHQYKPQQDVSRQQSVKANSSPTTNIDHLKTIDVTPHAQQKPQSHVELAPSDPPYPKEEAEDEGTQAVQDEESSTQESRERPYPVETENGETSINKRPQGITRYDFPTVPARKFVQPESTVPLPASSSEIPIKEERPPSPQEELLIEL |
Domain
The FYVE domain is involved in the binding to phosphatidylinositol 3-phosphate (PtdIns3P) which is required for the association to endosomal membranes.
Both IUM domains are necessary for efficient binding to ubiquitin.
Sequence similarities
Belongs to the VPS27 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length622
- Mass (Da)70,974
- Last updated2010-10-05 v3
- Checksum76C4501B0EBC9C84
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 321-322 | in Ref. 1; AAA96002 | ||||
Sequence: KL → NV | ||||||
Compositional bias | 462-520 | Polar residues | ||||
Sequence: AESYQTPPLQQLSSHQYKPQQDVSRQQSVKANSSPTTNIDHLKTIDVTPHAQQKPQSHV |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U24218 EMBL· GenBank· DDBJ | AAA96002.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X77395 EMBL· GenBank· DDBJ | CAA54574.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z71620 EMBL· GenBank· DDBJ | CAA96282.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006947 EMBL· GenBank· DDBJ | DAA10547.1 EMBL· GenBank· DDBJ | Genomic DNA |