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Protein

Coupling of ubiquitin conjugation to ER degradation protein 1

Gene

CUE1

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

Component of the endoplasmic reticulum-associated protein degradation (ERAD) pathway. Recruits the soluble ubiquitin-conjugating enzyme UBC7 to the cytoplasmic face of the endoplasmic reticulum membrane where it functions in degradation of misfolded or regulated proteins localized in the endoplasmic reticulum (ER) lumen or membrane via the ubiquitin-proteasome system. Targets the E2 conjugating enzyme UBC7 to the DOA10 ubiquitin ligase complex, which is part of the ERAD-C pathway responsible for the rapid degradation of membrane proteins with misfolded cytoplasmic domains, and to 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 also a role in cold adaptation, perhaps through effects on sterol biosynthesis.11 Publications

GO - Molecular functioni

  • ubiquitin binding Source: SGD
  • ubiquitin-protein transferase activator activity Source: SGD

GO - Biological processi

  • ER-associated ubiquitin-dependent protein catabolic process Source: SGD
  • establishment of protein localization to endoplasmic reticulum membrane Source: SGD
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

BioCyciYEAST:G3O-32938-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Coupling of ubiquitin conjugation to ER degradation protein 1
Alternative name(s):
Kinetochore-defect suppressor 4
Gene namesi
Name:CUE1
Synonyms:KIS4
Ordered Locus Names:YMR264W
ORF Names:YM8156.06
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YMR264W.
SGDiS000004877. CUE1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66Lumenal1 Publication
Transmembranei7 – 2317HelicalSequence analysisAdd
BLAST
Topological domaini24 – 203180Cytoplasmic1 PublicationAdd
BLAST

GO - Cellular componenti

  • Doa10p ubiquitin ligase complex Source: SGD
  • Hrd1p ubiquitin ligase ERAD-L complex Source: SGD
  • integral component of endoplasmic reticulum membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 203203Coupling of ubiquitin conjugation to ER degradation protein 1PRO_0000203346Add
BLAST

Proteomic databases

MaxQBiP38428.

Interactioni

Subunit structurei

Forms a heterodimer with UBC7. Interacts with SSM4/DOA10 and UBX2/SEL1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SSM4P403182EBI-27580,EBI-18208

GO - Molecular functioni

  • ubiquitin binding Source: SGD

Protein-protein interaction databases

BioGridi35442. 113 interactions.
DIPiDIP-4399N.
IntActiP38428. 8 interactions.
MINTiMINT-531548.

Structurei

Secondary structure

1
203
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi67 – 7610Combined sources
Helixi82 – 9211Combined sources
Helixi95 – 1039Combined sources
Turni112 – 1143Combined sources
Helixi151 – 1544Combined sources
Helixi168 – 1703Combined sources
Helixi173 – 19220Combined sources
Helixi196 – 2027Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MYXNMR-A45-115[»]
4JQUX-ray1.81B151-203[»]
ProteinModelPortaliP38428.
SMRiP38428. Positions 151-203.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini65 – 10743CUEPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the CUE1 family.Curated
Contains 1 CUE domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000248336.
InParanoidiP38428.
KOiK14022.
OMAiHPEQIRY.
OrthoDBiEOG7JX3GD.

Family and domain databases

InterProiIPR003892. CUE.
[Graphical view]
PfamiPF02845. CUE. 1 hit.
[Graphical view]
SMARTiSM00546. CUE. 1 hit.
[Graphical view]
PROSITEiPS51140. CUE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P38428-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEDSRLLITL ILVFGVIFLK KFFQSNQHPS AQRLSATGVN AHGRPQGSTQ
60 70 80 90 100
NALRRTGRVN GGHPVTTQMV ETVQNLAPNL HPEQIRYSLE NTGSVEETVE
110 120 130 140 150
RYLRGDEFSF PPGFEPSRAP MGANAAVDNN AAGGGEFNDP RKKNMICAEN
160 170 180 190 200
LLDKFHVDLN EDMSNLSFKD LDIEERKRLL VWQARKNLET KLQSDKDLQS

LLT
Length:203
Mass (Da):22,763
Last modified:November 1, 1997 - v2
Checksum:i3F795BD78DAC3D5B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 481S → P in AAA35221 (Ref. 4) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49260 Genomic DNA. Translation: CAA89247.1.
AY557973 Genomic DNA. Translation: AAS56299.1.
M88172 Genomic DNA. Translation: AAA35221.1.
BK006946 Genomic DNA. Translation: DAA10164.1.
PIRiS54476.
RefSeqiNP_013991.1. NM_001182771.1.

Genome annotation databases

EnsemblFungiiYMR264W; YMR264W; YMR264W.
GeneIDi855306.
KEGGisce:YMR264W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49260 Genomic DNA. Translation: CAA89247.1.
AY557973 Genomic DNA. Translation: AAS56299.1.
M88172 Genomic DNA. Translation: AAA35221.1.
BK006946 Genomic DNA. Translation: DAA10164.1.
PIRiS54476.
RefSeqiNP_013991.1. NM_001182771.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MYXNMR-A45-115[»]
4JQUX-ray1.81B151-203[»]
ProteinModelPortaliP38428.
SMRiP38428. Positions 151-203.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35442. 113 interactions.
DIPiDIP-4399N.
IntActiP38428. 8 interactions.
MINTiMINT-531548.

Proteomic databases

MaxQBiP38428.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR264W; YMR264W; YMR264W.
GeneIDi855306.
KEGGisce:YMR264W.

Organism-specific databases

EuPathDBiFungiDB:YMR264W.
SGDiS000004877. CUE1.

Phylogenomic databases

HOGENOMiHOG000248336.
InParanoidiP38428.
KOiK14022.
OMAiHPEQIRY.
OrthoDBiEOG7JX3GD.

Enzyme and pathway databases

BioCyciYEAST:G3O-32938-MONOMER.

Miscellaneous databases

PROiP38428.

Family and domain databases

InterProiIPR003892. CUE.
[Graphical view]
PfamiPF02845. CUE. 1 hit.
[Graphical view]
SMARTiSM00546. CUE. 1 hit.
[Graphical view]
PROSITEiPS51140. CUE. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "A large open reading frame in the yeast genome containing homology to the cif1 gene."
    Manning A.M., Rosenbloom C.L., Beaudet A.L.
    Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-158.
  5. "Role of Cue1p in ubiquitination and degradation at the ER surface."
    Biederer T., Volkwein C., Sommer T.
    Science 278:1806-1809(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-29, TOPOLOGY, FUNCTION, INTERACTION WITH UBC7.
  6. "Suppressors of the ndc10-2 mutation: a role for the ubiquitin system in Saccharomyces cerevisiae kinetochore function."
    Kopski K.M., Huffaker T.C.
    Genetics 147:409-420(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Proteins of the endoplasmic-reticulum-associated degradation pathway: domain detection and function prediction."
    Ponting C.P.
    Biochem. J. 351:527-535(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN.
  8. "Ubiquitin-mediated proteolysis of a short-lived regulatory protein depends on its cellular localization."
    Lenk U., Sommer T.
    J. Biol. Chem. 275:39403-39410(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Degradation signals recognized by the Ubc6p-Ubc7p ubiquitin-conjugating enzyme pair."
    Gilon T., Chomsky O., Kulka R.G.
    Mol. Cell. Biol. 20:7214-7219(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "A regulatory link between ER-associated protein degradation and the unfolded-protein response."
    Friedlander R., Jarosch E., Urban J., Volkwein C., Sommer T.
    Nat. Cell Biol. 2:379-384(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Sec61p-independent degradation of the tail-anchored ER membrane protein Ubc6p."
    Walter J., Urban J., Volkwein C., Sommer T.
    EMBO J. 20:3124-3131(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH UBC7.
  12. "In vivo action of the HRD ubiquitin ligase complex: mechanisms of endoplasmic reticulum quality control and sterol regulation."
    Gardner R.G., Shearer A.G., Hampton R.Y.
    Mol. Cell. Biol. 21:4276-4291(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Mutant membrane protein of the budding yeast spindle pole body is targeted to the endoplasmic reticulum degradation pathway."
    McBratney S., Winey M.
    Genetics 162:567-578(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "A ubiquitin-binding motif required for intramolecular monoubiquitylation, the CUE domain."
    Shih S.C., Prag G., Francis S.A., Sutanto M.A., Hurley J.H., Hicke L.
    EMBO J. 22:1273-1281(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN.
  15. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  16. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  17. "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, INTERACTION WITH SSM4 AND UBX2.
  18. "Endoplasmic reticulum-associated degradation is required for cold adaptation and regulation of sterol biosynthesis in the yeast Saccharomyces cerevisiae."
    Loertscher J., Larson L.L., Matson C.K., Parrish M.L., Felthauser A., Sturm A., Tachibana C., Bard M., Wright R.
    Eukaryot. Cell 5:712-722(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  19. "Endoplasmic reticulum-associated degradation of cytochrome P450 CYP3A4 in Saccharomyces cerevisiae: further characterization of cellular participants and structural determinants."
    Liao M., Faouzi S., Karyakin A., Correia M.A.
    Mol. Pharmacol. 69:1897-1904(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiCUE1_YEAST
AccessioniPrimary (citable) accession number: P38428
Secondary accession number(s): D6W090, Q03507
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: November 1, 1997
Last modified: July 6, 2016
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 589 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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 XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: 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.