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Q03714

- USA1_YEAST

UniProt

Q03714 - USA1_YEAST

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Protein

U1 SNP1-associating protein 1

Gene
USA1, YML029W
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Scaffold protein of the endoplasmic reticulum-associated degradation (ERAD) (also known as endoplasmic reticulum quality control, ERQC) pathway involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Component of the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD-M). Has multiple functions in ERAD including recruitment of DER1 to the HRD1 ubiquitin ligase, and regulation of HRD1 activity. Involved in oligomerization of HRD1, which is required for ERAD-L, and in HRD1 autoubiquitination and degradation.

GO - Molecular functioni

  1. identical protein binding Source: IntAct
  2. protein binding Source: IntAct
  3. protein complex scaffold Source: SGD

GO - Biological processi

  1. ER-associated ubiquitin-dependent protein catabolic process Source: SGD
  2. mRNA splicing, via spliceosome Source: SGD
  3. positive regulation of protein oligomerization Source: SGD
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:G3O-32630-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
U1 SNP1-associating protein 1
Gene namesi
Name:USA1
Ordered Locus Names:YML029W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XIII

Organism-specific databases

CYGDiYML029w.
SGDiS000004491. USA1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 536536Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei537 – 55923Helical; Reviewed predictionAdd
BLAST
Topological domaini560 – 5634Extracellular Reviewed prediction
Transmembranei564 – 58320Helical; Reviewed predictionAdd
BLAST
Topological domaini584 – 838255Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: SGD
  2. Hrd1p ubiquitin ligase ERAD-L complex Source: SGD
  3. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Disruption phenotypei

Impaired degradation of proteins with misfolded lumenal domains such as CPY*, a mutant, misfolded form of carboxypeptidase Y which is a known ERAD-L substrate. Impaired degradation of proteins with misfolded intramembrane domains. Impaired trans-ubiquitination and degradation of the HRD1 ligase. Degradation of proteins with misfolded cytosolic domains is not affected. Interaction of substrate with HRD1 is reduced; in USA1 and YOS9 double mutants this interaction is completely abolished.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 838838U1 SNP1-associating protein 1PRO_0000114926Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei374 – 3741Phosphoserine1 Publication
Modified residuei376 – 3761Phosphoserine2 Publications
Modified residuei379 – 3791Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ03714.
PaxDbiQ03714.
PeptideAtlasiQ03714.

Expressioni

Gene expression databases

GenevestigatoriQ03714.

Interactioni

Subunit structurei

Component of the HRD1 complex which contains HRD1, HRD3, USA1, DER1, YOS9, CDC48, NPL4, UFD1 AND UBX2/SEL1. The complex is composed of the core membrane complex, consisting of the E3 ligase HRD1 and its cofactors HRD3, DER1 and USA1, the substrate recruiting factor YOS9, and the heterotrimeric UFD1-NPL4-CDC48/p97 (UNC) ATPase complex recruited by UBX2/SEL1. Interacts with DER1, HRD1, HRD3, YOS9, UBX2, and CDC48.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-27760,EBI-27760
DER1P383073EBI-27760,EBI-5761

Protein-protein interaction databases

BioGridi35140. 84 interactions.
DIPiDIP-6423N.
IntActiQ03714. 25 interactions.
MINTiMINT-673269.
STRINGi4932.YML029W.

Structurei

3D structure databases

ProteinModelPortaliQ03714.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini259 – 31860Ubiquitin-likeAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni31 – 240210Required for ERAD-L functionAdd
BLAST
Regioni319 – 418100Important for HRD1 oligomer formationAdd
BLAST
Regioni345 – 535191Interaction with HRD1Add
BLAST
Regioni437 – 49054Required for ERAD-L function and HRD1 oligomer formationAdd
BLAST
Regioni584 – 838255Interaction with DER1Add
BLAST

Domaini

The ubiquitin-like domain is required for HRD1 trans-ubiquitination and degradation. Reported to be involved in ERAD-M but not ERAD-L function (1 Publication). However, a contradictory report states that it is not required for either ERAD-L or ERAD-M function (1 Publication). Reported to be required for HRD1 oligomer formation (1 Publication). However, a contradictory report does not observe any defects in oligomerization following deletion of the domain (1 Publication).

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG42991.
HOGENOMiHOG000066037.
KOiK14024.
OMAiNSHIAND.
OrthoDBiEOG7R83BZ.

Family and domain databases

InterProiIPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q03714-1 [UniParc]FASTAAdd to Basket

« Hide

MSEYLAQTPC KFTIWSSEID LIRTNLLVNA HPLSTVGRLL QYIHYQIYKQ    50
LRAIYQPEEQ CTNSEIPHTP LNSINTYFLS YEGRELSATC LLKDITSSSH 100
PDSNHFIRLQ LEKRTSPSGS AFDLEYDMEG EFNSMNIQFE INTLSSQRIF 150
NSMEPNLPIG TTLARLEKLA LERIKDFEKS AGNLCGIKED HSVSDLQGFI 200
IKGKQTPMFL NYGSDSDYYK DLNLVDLIGI DFAPAHNSFF TFLFKMNHEQ 250
NSHIANDEER FVLEFISDAT LSITQMNVKP DTTVKQVKDF ICSVYTHSLN 300
LRRNDIKLIY KGQLLHENNF AGNSSKISEY IKEPHEVKVH VQINQEYTES 350
GPGFWNEVFN NPNIFQFMPP DTRSQSPVSF APTQGRSPAA IRGEERGIPY 400
VTESGNDIVP TDELYRKCII NGDEVVFIPV SELNPQSSYL SVIKGDYGEI 450
KIPISSNDYR INGDNILLSP SAIEQLESAL NFKIERPRDS TLLHPSGEHV 500
RAADNTSSAN DNNTVENDES AWNRRVVRPL RNSFPLLLVL IRTFYLIGYN 550
SLVPFFIILE FGSFLPWKYI ILLSLLFIFR TVWNTQEVWN LWRDYLHLNE 600
IDEVKFSQIK EFINSNSLTL NFYKKCKDTQ SAIDLLMIPN LHEQRLSVYS 650
KYDIEYDTNT PDVGQLNLLF IKVLSGEIPK DALDELFKEF FELYETTRNM 700
NTLYPQDSLN ELLLMIWKES QKKDINTLPK YRRWFQTLCS QIAEHNVLDV 750
VLRYIIPDPV NDRVITAVIK NFVLFWVTLL PYVKEKLDDI VAQRARDREQ 800
PAPSAQQQEN EDEALIIPDE EEPTATGAQP HLYIPDED 838
Length:838
Mass (Da):96,653
Last modified:November 1, 1997 - v1
Checksum:i9B93ECA6C5421FD6
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z46659 Genomic DNA. Translation: CAA86626.1.
BK006946 Genomic DNA. Translation: DAA09869.1.
PIRiS49750.
RefSeqiNP_013683.1. NM_001182387.1.

Genome annotation databases

EnsemblFungiiYML029W; YML029W; YML029W.
GeneIDi854979.
KEGGisce:YML029W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z46659 Genomic DNA. Translation: CAA86626.1 .
BK006946 Genomic DNA. Translation: DAA09869.1 .
PIRi S49750.
RefSeqi NP_013683.1. NM_001182387.1.

3D structure databases

ProteinModelPortali Q03714.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 35140. 84 interactions.
DIPi DIP-6423N.
IntActi Q03714. 25 interactions.
MINTi MINT-673269.
STRINGi 4932.YML029W.

Proteomic databases

MaxQBi Q03714.
PaxDbi Q03714.
PeptideAtlasi Q03714.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YML029W ; YML029W ; YML029W .
GeneIDi 854979.
KEGGi sce:YML029W.

Organism-specific databases

CYGDi YML029w.
SGDi S000004491. USA1.

Phylogenomic databases

eggNOGi NOG42991.
HOGENOMi HOG000066037.
KOi K14024.
OMAi NSHIAND.
OrthoDBi EOG7R83BZ.

Enzyme and pathway databases

BioCyci YEAST:G3O-32630-MONOMER.

Miscellaneous databases

NextBioi 978094.

Gene expression databases

Genevestigatori Q03714.

Family and domain databases

InterProi IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view ]
SUPFAMi SSF54236. SSF54236. 1 hit.
PROSITEi PS50053. UBIQUITIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  4. "Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins."
    Carvalho P., Goder V., Rapoport T.A.
    Cell 126:361-373(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE HRD1 COMPLEX, INTERACTION WITH UBX2; HRD1; HRD3; DER1; YOS9 AND CDC48, DISRUPTION PHENOTYPE.
  5. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
    Kim H., Melen K., Oesterberg M., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.
  6. "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-376 AND SER-379, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  7. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: FUNCTION, INTERACTION WITH DER1 AND HRD1, DISRUPTION PHENOTYPE.
  9. "Usa1 protein facilitates substrate ubiquitylation through two separate domains."
    Kim I., Li Y., Muniz P., Rao H.
    PLoS ONE 4:E7604-E7604(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HRD1 AND HRD3, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, CHARACTERIZATION OF UBIQUITIN-LIKE DOMAIN, CHARACTERIZATION OF FUNCTIONAL REGIONS.
  10. "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-374; SER-376 AND SER-379, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Retrotranslocation of a misfolded luminal ER protein by the ubiquitin-ligase Hrd1p."
    Carvalho P., Stanley A.M., Rapoport T.A.
    Cell 143:579-591(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HRD1, DISRUPTION PHENOTYPE, CHARACTERIZATION OF UBIQUITIN-LIKE DOMAIN, CHARACTERIZATION OF FUNCTIONAL REGIONS.
  12. "Usa1p is required for optimal function and regulation of the Hrd1p endoplasmic reticulum-associated degradation ubiquitin ligase."
    Carroll S.M., Hampton R.Y.
    J. Biol. Chem. 285:5146-5156(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, CHARACTERIZATION OF UBIQUITIN-LIKE DOMAIN.

Entry informationi

Entry nameiUSA1_YEAST
AccessioniPrimary (citable) accession number: Q03714
Secondary accession number(s): D6VZE5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: September 3, 2014
This is version 120 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 1890 molecules/cell in log phase SD medium.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi