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Protein

Auxilin-like clathrin uncoating factor SWA2

Gene

SWA2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

GO - Molecular functioni

  • clathrin binding Source: SGD
  • ubiquitin binding Source: SGD

GO - Biological processi

  • clathrin coat disassembly Source: SGD
  • endoplasmic reticulum inheritance Source: SGD
  • positive regulation of ATPase activity Source: SGD
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:G3O-29878-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Auxilin-like clathrin uncoating factor SWA2
Alternative name(s):
Bud site selection protein 24
DnaJ-related protein SWA2
Short name:
J protein SWA2
Synthetic lethal with ARF1 protein 2
Gene namesi
Name:SWA2
Synonyms:AUX1, BUD24
Ordered Locus Names:YDR320C
ORF Names:D9798.10
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR320C.
SGDiS000002728. SWA2.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi388 – 3881G → R in 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. 2 Publications
Mutagenesisi631 – 6333HPD → AAA in SWA2-J; abolishes ATPase stimulation activity. In SWA2-TPR-J; complete loss of clathrin disassembly function; when associated with R-388. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 668668Auxilin-like clathrin uncoating factor SWA2PRO_0000270621Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei52 – 521PhosphoserineCombined sources
Modified residuei64 – 641PhosphoserineCombined sources
Modified residuei264 – 2641PhosphoserineCombined sources
Modified residuei308 – 3081PhosphoserineCombined sources
Modified residuei312 – 3121PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ06677.

PTM databases

iPTMnetiQ06677.

Interactioni

Subunit structurei

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.3 Publications

GO - Molecular functioni

  • clathrin binding Source: SGD
  • ubiquitin binding Source: SGD

Protein-protein interaction databases

BioGridi32376. 172 interactions.
DIPiDIP-2847N.
IntActiQ06677. 7 interactions.
MINTiMINT-1722120.

Structurei

Secondary structure

1
668
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi140 – 15314Combined sources
Helixi158 – 16710Combined sources
Helixi171 – 1799Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PGYNMR-A137-183[»]
ProteinModelPortaliQ06677.
SMRiQ06677. Positions 137-183, 377-444, 577-664.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ06677.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini140 – 18041UBAAdd
BLAST
Repeati374 – 40734TPR 1Add
BLAST
Repeati412 – 44534TPR 2Add
BLAST
Repeati467 – 50034TPR 3Add
BLAST
Domaini603 – 66866JAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 100100CB1Add
BLAST
Regioni238 – 30265CB2Add
BLAST
Regioni303 – 36260CB3Add
BLAST

Domaini

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.1 Publication

Sequence similaritiesi

Contains 1 J domain.Curated
Contains 3 TPR repeats.Curated
Contains 1 UBA domain.Curated

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

HOGENOMiHOG000001055.
InParanoidiQ06677.
OMAiMEIARLM.
OrthoDBiEOG7FR7RC.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
1.25.40.10. 1 hit.
InterProiIPR001623. DnaJ_domain.
IPR015228. SWA2_UBA.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
IPR009060. UBA-like.
[Graphical view]
PfamiPF09145. Ubiq-assoc. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 3 hits.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
SSF46934. SSF46934. 1 hit.
SSF48452. SSF48452. 1 hit.
PROSITEiPS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q06677-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDPFAHLLT SLKNKDSASA SKETTPQSSN SPSITGSAVA DVARTDKSPN
60 70 80 90 100
DSLHSISAPP LIPSPKVDFS APPLVPTNST TKSNTANNTP PSALANTDDD
110 120 130 140 150
FNQLFGMGTV TTTDTIQKPD EDYYGSKEDH LYNGDDALVD EVKDMEIARL
160 170 180 190 200
MSLGLSIEEA TEFYENDVTY ERYLEILKSK QKERNDLAIR KKESGIKMEK
210 220 230 240 250
SGLSNIVGTD SNNLFSMATD FFNKGKKLVD QWTSFPPEAN DRLNNYSKTH
260 270 280 290 300
DKVEDYDLPQ VNDSPNRILF EDNEVVENLP PADNPDQDLL TDFETKIDIT
310 320 330 340 350
KRTAPDVSHS SSPTSGILIE ENSRRNEPLI EDSLLDFSEG NLTNSKSNED
360 370 380 390 400
STLFNENSNT DSTIPISDIE LSGYNEFKAK GTSLFKNGDY INSLQEYEKS
410 420 430 440 450
LNTLPLNHPL RIIALSNIIA SQLKIGEYSK SIENSSMALE LFPSSKAKWK
460 470 480 490 500
NKISNSDPER SFNDIWPKIM IRRAESFEHL ESFKKALETY QELIKKNFFD
510 520 530 540 550
DKIMQGKRRC QDFINPPPVK KSMPVKKKTT TTSPATKKQN LTASSSNSPI
560 570 580 590 600
SVDSTSEIKK RELENAKLAL YDKVFEKISS WKDGKDDDIR HLLANLSSLL
610 620 630 640 650
TWCNWKDVSM QDLVMPKRVK ITYMKAVAKT HPDKIPESLS LENKMIAENI
660
FSTLSIAWDK FKLQNDIN
Length:668
Mass (Da):75,020
Last modified:November 1, 1996 - v1
Checksum:iCCDF1F78315E3D44
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U32517 Genomic DNA. Translation: AAB64756.1.
BK006938 Genomic DNA. Translation: DAA12161.1.
PIRiS59786.
RefSeqiNP_010606.1. NM_001180628.1.

Genome annotation databases

EnsemblFungiiYDR320C; YDR320C; YDR320C.
GeneIDi851918.
KEGGisce:YDR320C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U32517 Genomic DNA. Translation: AAB64756.1.
BK006938 Genomic DNA. Translation: DAA12161.1.
PIRiS59786.
RefSeqiNP_010606.1. NM_001180628.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PGYNMR-A137-183[»]
ProteinModelPortaliQ06677.
SMRiQ06677. Positions 137-183, 377-444, 577-664.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32376. 172 interactions.
DIPiDIP-2847N.
IntActiQ06677. 7 interactions.
MINTiMINT-1722120.

PTM databases

iPTMnetiQ06677.

Proteomic databases

MaxQBiQ06677.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR320C; YDR320C; YDR320C.
GeneIDi851918.
KEGGisce:YDR320C.

Organism-specific databases

EuPathDBiFungiDB:YDR320C.
SGDiS000002728. SWA2.

Phylogenomic databases

HOGENOMiHOG000001055.
InParanoidiQ06677.
OMAiMEIARLM.
OrthoDBiEOG7FR7RC.

Enzyme and pathway databases

BioCyciYEAST:G3O-29878-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ06677.
PROiQ06677.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
1.25.40.10. 1 hit.
InterProiIPR001623. DnaJ_domain.
IPR015228. SWA2_UBA.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
IPR009060. UBA-like.
[Graphical view]
PfamiPF09145. Ubiq-assoc. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 3 hits.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
SSF46934. SSF46934. 1 hit.
SSF48452. SSF48452. 1 hit.
PROSITEiPS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "The auxilin-like phosphoprotein Swa2p is required for clathrin function in yeast."
    Gall W.E., Higginbotham M.A., Chen C.-Y., Ingram M.F., Cyr D.M., Graham T.R.
    Curr. Biol. 10:1349-1358(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, MUTAGENESIS OF GLY-388, INTERACTION WITH CLC1.
  4. "A yeast DNA J protein required for uncoating of clathrin-coated vesicles in vivo."
    Pishvaee B., Costaguta G., Yeung B.G., Ryazantsev S., Greener T., Greene L.E., Eisenberg E., McCaffery J.M., Payne G.S.
    Nat. Cell Biol. 2:958-963(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Aux1p/Swa2p is required for cortical endoplasmic reticulum inheritance in Saccharomyces cerevisiae."
    Du Y., Pypaert M., Novick P., Ferro-Novick S.
    Mol. Biol. Cell 12:2614-2628(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ENDOPLASMIC RETICULUM INHERITANCE.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; SER-264; SER-308 AND SER-312, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  8. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64 AND SER-264, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-64 AND SER-264, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Solution structure of the ubiquitin-binding domain in Swa2p from Saccharomyces cerevisiae."
    Chim N., Gall W.E., Xiao J., Harris M.P., Graham T.R., Krezel A.M.
    Proteins 54:784-793(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 137-183, INTERACTION WITH UBIQUITIN.
  11. "Dissection of Swa2p/auxilin domain requirements for cochaperoning Hsp70 clathrin-uncoating activity in vivo."
    Xiao J., Kim L.S., Graham T.R.
    Mol. Biol. Cell 17:3281-3290(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAINS, INTERACTION WITH CHC1, MUTAGENESIS OF GLY-388 AND 631-HIS--ASP-633.

Entry informationi

Entry nameiSWA2_YEAST
AccessioniPrimary (citable) accession number: Q06677
Secondary accession number(s): D6VSV1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 768 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.