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Protein

Ubiquitin-conjugating enzyme E2 7

Gene

UBC7

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

Catalyzes the covalent attachment of ubiquitin to other proteins. Functions in degradation of misfolded or regulated proteins localized in the endoplasmic reticulum (ER) lumen or membrane via the ubiquitin-proteasome system. Cognate E2 conjugating enzyme for 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 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). Involved in resistance to cadmium poisoning.PROSITE-ProRule annotation7 Publications

Catalytic activityi

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.PROSITE-ProRule annotation1 Publication

Pathway:iprotein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.PROSITE-ProRule annotation
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei89 – 891Glycyl thioester intermediate

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ligase activity Source: UniProtKB-KW
  • ubiquitin-protein transferase activity Source: SGD

GO - Biological processi

  • chromatin assembly or disassembly Source: SGD
  • ER-associated ubiquitin-dependent protein catabolic process Source: SGD
  • fungal-type cell wall organization Source: SGD
  • response to cadmium ion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Cadmium resistance, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Cadmium, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-32727-MONOMER.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme E2 7 (EC:6.3.2.19)
Alternative name(s):
Ubiquitin carrier protein
Ubiquitin-conjugating enzyme E2-18 kDa
Ubiquitin-protein ligase
Gene namesi
Name:UBC7
Synonyms:QRI8
Ordered Locus Names:YMR022W
ORF Names:YM9711.12
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XIII

Organism-specific databases

CYGDiYMR022w.
EuPathDBiFungiDB:YMR022W.
SGDiS000004624. UBC7.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi39 – 391C → S: No effect; when associated with S-141. 1 Publication
Mutagenesisi81 – 811N → A: Impairs degradation of UBC7-substrates, but does not prevent protein degradation.
Mutagenesisi89 – 891C → A or S: Prevents polyubiquitin chain attachment and protein degradation. 1 Publication
Mutagenesisi141 – 1411C → S: No effect; when associated with S-39. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 165165Ubiquitin-conjugating enzyme E2 7PRO_0000082554Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki89 – 89Glycyl cysteine thioester (Cys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

Autoubiquitinated at Cys-89; undergoes 'Lys-48'-linked polyubiquitination, which leads to proteasome-dependent protein degradation. Degradation is autoregulated when its levels exceed that of its binding partner CUE1.1 Publication

Keywords - PTMi

Thioester bond, Ubl conjugation

Proteomic databases

MaxQBiQ02159.
PaxDbiQ02159.
PeptideAtlasiQ02159.

Expressioni

Inductioni

By cadmium.

Interactioni

Subunit structurei

Forms a heterodimer with CUE1. Interacts with SSM4/DOA10 and HDR1. Interacts with UFD4.5 Publications

Protein-protein interaction databases

BioGridi35193. 172 interactions.
DIPiDIP-6583N.
IntActiQ02159. 609 interactions.
MINTiMINT-683595.

Structurei

Secondary structure

1
165
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 1918Combined sources
Beta strandi24 – 307Combined sources
Beta strandi33 – 4210Combined sources
Turni48 – 514Combined sources
Beta strandi53 – 597Combined sources
Turni62 – 654Combined sources
Beta strandi70 – 756Combined sources
Beta strandi86 – 883Combined sources
Helixi91 – 933Combined sources
Beta strandi102 – 1043Combined sources
Turni105 – 1084Combined sources
Helixi116 – 12813Combined sources
Helixi132 – 1343Combined sources
Helixi138 – 1469Combined sources
Helixi148 – 16215Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2UCZX-ray2.93A1-165[»]
4JQUX-ray1.81A2-165[»]
ProteinModelPortaliQ02159.
SMRiQ02159. Positions 2-165.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ02159.

Family & Domainsi

Sequence similaritiesi

Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00730000110436.
HOGENOMiHOG000233454.
InParanoidiQ02159.
KOiK04555.
OMAiKMKFTCD.
OrthoDBiEOG7SBP18.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q02159-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKTAQKRLL KELQQLIKDS PPGIVAGPKS ENNIFIWDCL IQGPPDTPYA
60 70 80 90 100
DGVFNAKLEF PKDYPLSPPK LTFTPSILHP NIYPNGEVCI SILHSPGDDP
110 120 130 140 150
NMYELAEERW SPVQSVEKIL LSVMSMLSEP NIESGANIDA CILWRDNRPE
160
FERQVKLSIL KSLGF
Length:165
Mass (Da):18,520
Last modified:July 1, 1993 - v1
Checksum:iD3D297847DBB462D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66829 Genomic DNA. Translation: CAA47302.1.
X69100 Genomic DNA. Translation: CAA48846.1.
Z49211 Genomic DNA. Translation: CAA89125.1.
AY558116 Genomic DNA. Translation: AAS56442.1.
BK006946 Genomic DNA. Translation: DAA09920.1.
PIRiS28951.
RefSeqiNP_013735.1. NM_001182518.1.

Genome annotation databases

EnsemblFungiiYMR022W; YMR022W; YMR022W.
GeneIDi855036.
KEGGisce:YMR022W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66829 Genomic DNA. Translation: CAA47302.1.
X69100 Genomic DNA. Translation: CAA48846.1.
Z49211 Genomic DNA. Translation: CAA89125.1.
AY558116 Genomic DNA. Translation: AAS56442.1.
BK006946 Genomic DNA. Translation: DAA09920.1.
PIRiS28951.
RefSeqiNP_013735.1. NM_001182518.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2UCZX-ray2.93A1-165[»]
4JQUX-ray1.81A2-165[»]
ProteinModelPortaliQ02159.
SMRiQ02159. Positions 2-165.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35193. 172 interactions.
DIPiDIP-6583N.
IntActiQ02159. 609 interactions.
MINTiMINT-683595.

Proteomic databases

MaxQBiQ02159.
PaxDbiQ02159.
PeptideAtlasiQ02159.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR022W; YMR022W; YMR022W.
GeneIDi855036.
KEGGisce:YMR022W.

Organism-specific databases

CYGDiYMR022w.
EuPathDBiFungiDB:YMR022W.
SGDiS000004624. UBC7.

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00730000110436.
HOGENOMiHOG000233454.
InParanoidiQ02159.
KOiK04555.
OMAiKMKFTCD.
OrthoDBiEOG7SBP18.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciYEAST:G3O-32727-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ02159.
NextBioi978248.
PROiQ02159.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "QRI8, a novel ubiquitin-conjugating enzyme in Saccharomyces cerevisiae."
    Vassal A., Boulet A., Decoster E., Faye G.
    Biochim. Biophys. Acta 1132:211-213(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204510 / AB320.
  2. "Resistance to cadmium mediated by ubiquitin-dependent proteolysis."
    Jungmann J., Reins H.-A., Schobert C., Jentsch S.
    Nature 361:369-371(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. "Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MAT alpha 2 repressor."
    Chen P., Johnson P., Sommer T., Jentsch S., Hochstrasser M.
    Cell 74:357-369(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Bacterial expression of the Saccharomyces cerevisiae ubiquitin-conjugating enzyme Ubc7."
    Yamazaki R.K., Chau V.
    Protein Expr. Purif. 7:122-127(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY.
  8. "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: FUNCTION, INTERACTION WITH CUE1.
  9. "Degradation signal masking by heterodimerization of MATalpha2 and MATa1 blocks their mutual destruction by the ubiquitin-proteasome pathway."
    Johnson P.R., Swanson R., Rakhilina L., Hochstrasser M.
    Cell 94:217-227(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation."
    Swanson R., Locher M., Hochstrasser M.
    Genes Dev. 15:2660-2674(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "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.
  12. "Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation."
    Bays N.W., Gardner R.G., Seelig L.P., Joazeiro C.A., Hampton R.Y.
    Nat. Cell Biol. 3:24-29(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HDR1.
  13. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  14. "Ubx2 links the Cdc48 complex to ER-associated protein degradation."
    Neuber O., Jarosch E., Volkwein C., Walter J., Sommer T.
    Nat. Cell Biol. 7:993-998(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SSM4.
  15. "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.
  16. "Autoregulation of an E2 enzyme by ubiquitin-chain assembly on its catalytic residue."
    Ravid T., Hochstrasser M.
    Nat. Cell Biol. 9:422-427(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT CYS-89, INTERACTION WITH UFD4, MUTAGENESIS OF CYS-39; CYS-89 AND CYS-141.
  17. "Crystal structure of a class I ubiquitin conjugating enzyme (Ubc7) from Saccharomyces cerevisiae at 2.9-A resolution."
    Cook W.J., Martin P.D., Edwards B.F.P., Yamazaki R.K., Chau V.
    Biochemistry 36:1621-1627(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.93 ANGSTROMS).

Entry informationi

Entry nameiUBC7_YEAST
AccessioniPrimary (citable) accession number: Q02159
Secondary accession number(s): D6VZJ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: July 22, 2015
This is version 143 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 2100 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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 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.