P0CS27 · VPS27_CRYNB

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.

Features

Showing features for binding site.

1750100200300400500600700
TypeIDPosition(s)Description
Binding site194Zn2+ (UniProtKB | ChEBI)
Binding site197Zn2+ (UniProtKB | ChEBI)
Binding site224Zn2+ (UniProtKB | ChEBI)
Binding site227Zn2+ (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentearly endosome
Cellular Componentendosome membrane
Molecular Functionmetal ion binding
Molecular Functionphosphatidylinositol binding
Molecular Functionubiquitin binding
Biological Processendocytic recycling
Biological Processintracellular protein transport
Biological Processreceptor internalization
Biological Processvacuolar transport

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Vacuolar protein sorting-associated protein 27

Gene names

    • Name
      VPS27
    • Ordered locus names
      CNBE3700

Organism names

Accessions

  • Primary accession
    P0CS27
  • Secondary accessions
    • Q55S12
    • Q5KGG4

Organism-specific databases

Subcellular Location

Endosome membrane
; Peripheral membrane protein

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004103261-750Vacuolar protein sorting-associated protein 27

Interaction

Subunit

Component of the ESCRT-0 complex composed of HSE1 and VPS27.

Structure

Family & Domains

Features

Showing features for domain, zinc finger, region, compositional bias.

Type
IDPosition(s)Description
Domain24-153VHS
Zinc finger172-232FYVE-type; degenerate
Domain253-272UIM 1
Region268-292Disordered
Domain294-313UIM 2
Region314-336Disordered
Region447-530Disordered
Compositional bias473-523Polar residues
Region564-739Disordered
Compositional bias600-639Polar residues
Compositional bias651-712Polar residues

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    750
  • Mass (Da)
    82,859
  • Last updated
    2011-06-28 v1
  • MD5 Checksum
    41FE9B2C9D384928091D32FC4FF4DF89
MSWLWGSTTNPQFEELAEKACSPLNLPYPQSEDIATALEVADMIRSKAIQPKMAMQSLKKRIASKNGRVQMYAIGLTDTCIKNGGDHFLLEVASKEFVDELSNLIKATTTSPEVKQMLIKYFQQWALAFKSKSELSFFVEVYNELRASGITFPPPPAPVPSHLLTTTTAPAWVDSDACMRCRSAFTFTNRKHHCRNCGLVFDQACSSHSMPLPKYGITEEVRVCDGCWAKAGRNKADAPAPAVPGRTPRSRADLDADLQRAIELSLAESQHSQNRHHSHFTPSEPPLAHGTVEDEDEQMRLAIEASLRDMEARPSAPAGLGEAPEPEYRPLPTFDLSPRENETILTFSNTMDQMAAYGERDLRRFPHAHVLAEQANTVGGRLRRNVEEKSTKQQMLMEMQDKLSQAVNLYGQILDGQQAYAAKRAHEEQARRYQQQQSYYTQQYQPQPQLYGQYPPNGYQAFVPPQQAYQPPQPQPEAQAQHAPSLYPTMPYTTPNFTSPPQERVYPQQSHSSPYSQWSPAPSHVQPGLARQASVVVPPVSSPVPAGVQRQASMTYGAPIPVAEQSQRQQQQYASAPPFASGAAPVDIPSAPPPVNLSTHPNSPQRHSYIPSHPQTQTQTQYESQPQEIPSQQDMQYGASAPPPDSLGSYVSEGTVGSAKSGLEQEHAASQIQPQPQPQASAQTQTQSQSQLQAQPQQNQYAAQTQLPAGMYNAASFPQPLPPTIFPDAPVEAPKGLEKEEKEEALLIEL

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias473-523Polar residues
Compositional bias600-639Polar residues
Compositional bias651-712Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AAEY01000028
EMBL· GenBank· DDBJ
EAL20449.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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