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Q02159 (UBC7_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:UBC7
Synonyms:QRI8
Ordered Locus Names:YMR022W
ORF Names:YM9711.12
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length165 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.15

Catalytic activity

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine. Ref.7

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Forms a heterodimer with CUE1. Interacts with SSM4/DOA10 and HDR1. Interacts with UFD4. Ref.8 Ref.12 Ref.14 Ref.15 Ref.16

Subcellular location

Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Note: Anchored via the membrane protein CUE1 to the endoplasmic reticulum membrane.

Induction

By cadmium.

Post-translational modification

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.

Miscellaneous

Present with 2100 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 165165Ubiquitin-conjugating enzyme E2 7
PRO_0000082554

Sites

Active site891Glycyl thioester intermediate

Amino acid modifications

Cross-link89Glycyl cysteine thioester (Cys-Gly) (interchain with G-Cter in ubiquitin)

Experimental info

Mutagenesis391C → S: No effect; when associated with S-141. Ref.16
Mutagenesis811N → A: Impairs degradation of UBC7-substrates, but does not prevent protein degradation.
Mutagenesis891C → A or S: Prevents polyubiquitin chain attachment and protein degradation. Ref.16
Mutagenesis1411C → S: No effect; when associated with S-39. Ref.16

Secondary structure

.............................. 165
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q02159 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: D3D297847DBB462D

FASTA16518,520
        10         20         30         40         50         60 
MSKTAQKRLL KELQQLIKDS PPGIVAGPKS ENNIFIWDCL IQGPPDTPYA DGVFNAKLEF 

        70         80         90        100        110        120 
PKDYPLSPPK LTFTPSILHP NIYPNGEVCI SILHSPGDDP NMYELAEERW SPVQSVEKIL 

       130        140        150        160 
LSVMSMLSEP NIESGANIDA CILWRDNRPE FERQVKLSIL KSLGF 

« Hide

References

« Hide 'large scale' references
[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]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
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]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS28951.
RefSeqNP_013735.1. NM_001182518.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2UCZX-ray2.93A1-165[»]
4JQUX-ray1.81A2-165[»]
ProteinModelPortalQ02159.
SMRQ02159. Positions 2-165.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35193. 171 interactions.
DIPDIP-6583N.
IntActQ02159. 609 interactions.
MINTMINT-683595.
STRING4932.YMR022W.

Proteomic databases

MaxQBQ02159.
PaxDbQ02159.
PeptideAtlasQ02159.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYMR022W; YMR022W; YMR022W.
GeneID855036.
KEGGsce:YMR022W.

Organism-specific databases

CYGDYMR022w.
SGDS000004624. UBC7.

Phylogenomic databases

eggNOGCOG5078.
GeneTreeENSGT00730000110436.
HOGENOMHOG000233454.
KOK04555.
OMADMFHPNI.
OrthoDBEOG7SBP18.

Enzyme and pathway databases

BioCycYEAST:G3O-32727-MONOMER.
UniPathwayUPA00143.

Gene expression databases

GenevestigatorQ02159.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 1 hit.
PROSITEPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ02159.
NextBio978248.
PROQ02159.

Entry information

Entry nameUBC7_YEAST
AccessionPrimary (citable) accession number: Q02159
Secondary accession number(s): D6VZJ6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: July 9, 2014
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways