Q06677 · SWA2_YEAST

Function

function

Cofactor for the uncoating of clathrin-coated vesicles (CCVs) by Hsp70-type chaperones (SSA1/2/3 and SSB1/2). Coat disassembly is important for fusion of vesicles with target membranes and for recycling components of clathrin coats to the cytoplasm for further rounds of vesicle formation. Binds to assembled clathrin and recruits the ATP-activated chaperone to CCVs. Stimulates the ATPase activity of the clathrin-associated Hsp70-type chaperone SSA1, which then disrupts clathrin-clathrin interactions, leading to release of the clathrin coat. In addition, prevents unproductive clathrin assembly in the cell. Also required for cortical endoplasmic reticulum inheritance.

Miscellaneous

Present with 768 molecules/cell in log phase SD medium.

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 Componentcytoplasm
Cellular Componentcytosol
Cellular Componentendoplasmic reticulum membrane
Cellular Componentintracellular membrane-bounded organelle
Cellular Componentvesicle
Molecular Functionclathrin binding
Molecular Functionubiquitin binding
Biological Processclathrin coat disassembly
Biological Processclathrin-dependent endocytosis
Biological Processendoplasmic reticulum inheritance

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Auxilin-like clathrin uncoating factor SWA2
  • Alternative names
    • Bud site selection protein 24
    • DnaJ-related protein SWA2 (J protein SWA2)
    • Synthetic lethal with ARF1 protein 2

Gene names

    • Name
      SWA2
    • Synonyms
      AUX1, BUD24
    • ORF names
      D9798.10
    • Ordered locus names
      YDR320C

Organism names

Accessions

  • Primary accession
    Q06677
  • Secondary accessions
    • D6VSV1

Proteomes

Organism-specific databases

Subcellular Location

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis388In SWA2-1/SWA2-TPR; partial loss of clathrin disassembly function. In SWA2-TPR-J; complete loss of clathrin disassembly function; when associated with 631-AAA-633.
Mutagenesis631-633In SWA2-J; abolishes ATPase stimulation activity. In SWA2-TPR-J; complete loss of clathrin disassembly function; when associated with R-388.

Variants

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The viewer provides 25 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00002706211-668Auxilin-like clathrin uncoating factor SWA2
Modified residue52Phosphoserine
Modified residue64Phosphoserine
Modified residue264Phosphoserine
Modified residue308Phosphoserine
Modified residue312Phosphoserine

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Interacts with the clathrin light and heavy chains CLC1 and CHC1, respectively. Binds to clathrin with its N-terminal domain containing 3 clathrin-binding (CB) motifs. Association with clathrin is transient. Binds to polyubiquitin and ubiquitinated proteins.

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, compositional bias, domain, repeat.

TypeIDPosition(s)Description
Region1-95Disordered
Region1-100CB1
Compositional bias12-38Polar residues
Compositional bias73-95Polar residues
Domain140-180UBA
Region238-302CB2
Region302-323Disordered
Region303-362CB3
Compositional bias304-321Polar residues
Region339-359Disordered
Repeat374-407TPR 1
Repeat412-445TPR 2
Repeat467-500TPR 3
Region511-556Disordered
Compositional bias525-554Polar residues
Domain603-668J

Domain

The TPR repeats and the J domain are required for interaction with Hsp70-type chaperones. The J domain is responsible for stimulating the ATPase activity of the chaperone.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    668
  • Mass (Da)
    75,020
  • Last updated
    1996-11-01 v1
  • Checksum
    CCDF1F78315E3D44
MSDPFAHLLTSLKNKDSASASKETTPQSSNSPSITGSAVADVARTDKSPNDSLHSISAPPLIPSPKVDFSAPPLVPTNSTTKSNTANNTPPSALANTDDDFNQLFGMGTVTTTDTIQKPDEDYYGSKEDHLYNGDDALVDEVKDMEIARLMSLGLSIEEATEFYENDVTYERYLEILKSKQKERNDLAIRKKESGIKMEKSGLSNIVGTDSNNLFSMATDFFNKGKKLVDQWTSFPPEANDRLNNYSKTHDKVEDYDLPQVNDSPNRILFEDNEVVENLPPADNPDQDLLTDFETKIDITKRTAPDVSHSSSPTSGILIEENSRRNEPLIEDSLLDFSEGNLTNSKSNEDSTLFNENSNTDSTIPISDIELSGYNEFKAKGTSLFKNGDYINSLQEYEKSLNTLPLNHPLRIIALSNIIASQLKIGEYSKSIENSSMALELFPSSKAKWKNKISNSDPERSFNDIWPKIMIRRAESFEHLESFKKALETYQELIKKNFFDDKIMQGKRRCQDFINPPPVKKSMPVKKKTTTTSPATKKQNLTASSSNSPISVDSTSEIKKRELENAKLALYDKVFEKISSWKDGKDDDIRHLLANLSSLLTWCNWKDVSMQDLVMPKRVKITYMKAVAKTHPDKIPESLSLENKMIAENIFSTLSIAWDKFKLQNDIN

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias12-38Polar residues
Compositional bias73-95Polar residues
Compositional bias304-321Polar residues
Compositional bias525-554Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U32517
EMBL· GenBank· DDBJ
AAB64756.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006938
EMBL· GenBank· DDBJ
DAA12161.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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