Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q02159

- UBC7_YEAST

UniProt

Q02159 - UBC7_YEAST

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Ubiquitin-conjugating enzyme E2 7

Gene

UBC7

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - 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.7 PublicationsPROSITE-ProRule annotation

Catalytic activityi

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.1 PublicationPROSITE-ProRule annotation

Pathwayi

Sites

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

GO - Molecular functioni

  1. acid-amino acid ligase activity Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. ubiquitin-protein transferase activity Source: SGD

GO - Biological processi

  1. chromatin assembly or disassembly Source: SGD
  2. ER-associated ubiquitin-dependent protein catabolic process Source: SGD
  3. fungal-type cell wall organization Source: SGD
  4. 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: Chromosome XIII

Organism-specific databases

CYGDiYMR022w.
SGDiS000004624. UBC7.

Subcellular locationi

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

GO - Cellular componenti

  1. Doa10p ubiquitin ligase complex Source: SGD
  2. endoplasmic reticulum membrane Source: SGD
  3. 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.

Gene expression databases

GenevestigatoriQ02159.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi35193. 171 interactions.
DIPiDIP-6583N.
IntActiQ02159. 609 interactions.
MINTiMINT-683595.
STRINGi4932.YMR022W.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
OMAiDMFHPNI.
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi S28951.
RefSeqi NP_013735.1. NM_001182518.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2UCZ X-ray 2.93 A 1-165 [» ]
4JQU X-ray 1.81 A 2-165 [» ]
ProteinModelPortali Q02159.
SMRi Q02159. Positions 2-165.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 35193. 171 interactions.
DIPi DIP-6583N.
IntActi Q02159. 609 interactions.
MINTi MINT-683595.
STRINGi 4932.YMR022W.

Proteomic databases

MaxQBi Q02159.
PaxDbi Q02159.
PeptideAtlasi Q02159.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YMR022W ; YMR022W ; YMR022W .
GeneIDi 855036.
KEGGi sce:YMR022W.

Organism-specific databases

CYGDi YMR022w.
SGDi S000004624. UBC7.

Phylogenomic databases

eggNOGi COG5078.
GeneTreei ENSGT00730000110436.
HOGENOMi HOG000233454.
InParanoidi Q02159.
KOi K04555.
OMAi DMFHPNI.
OrthoDBi EOG7SBP18.

Enzyme and pathway databases

UniPathwayi UPA00143 .
BioCyci YEAST:G3O-32727-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q02159.
NextBioi 978248.
PROi Q02159.

Gene expression databases

Genevestigatori Q02159.

Family and domain databases

Gene3Di 3.10.110.10. 1 hit.
InterProi IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view ]
Pfami PF00179. UQ_con. 1 hit.
[Graphical view ]
SUPFAMi SSF54495. SSF54495. 1 hit.
PROSITEi PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 134 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