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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: -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

Miscellaneous

Present with 2100 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.PROSITE-ProRule annotation1 Publication

Pathwayi: protein 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)DescriptionActionsGraphical viewLength
Active sitei89Glycyl thioester intermediate1

GO - Molecular functioni

GO - Biological processi

  • chromatin assembly or disassembly Source: SGD
  • fungal-type cell wall organization Source: SGD
  • protein polyubiquitination Source: GO_Central
  • response to cadmium ion Source: UniProtKB-KW
  • ubiquitin-dependent ERAD pathway Source: SGD

Keywordsi

Molecular functionTransferase
Biological processCadmium resistance, Ubl conjugation pathway
LigandATP-binding, Cadmium, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-32727-MONOMER
ReactomeiR-SCE-8866652 Synthesis of active ubiquitin: roles of E1 and E2 enzymes
R-SCE-983168 Antigen processing: Ubiquitination & Proteasome degradation
UniPathwayiUPA00143

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme E2 7 (EC:2.3.2.231 Publication)
Alternative name(s):
E2 ubiquitin-conjugating enzyme 7
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
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YMR022W
SGDiS000004624 UBC7

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi39C → S: No effect; when associated with S-141. 1 Publication1
Mutagenesisi81N → A: Impairs degradation of UBC7-substrates, but does not prevent protein degradation. 1
Mutagenesisi89C → A or S: Prevents polyubiquitin chain attachment and protein degradation. 1 Publication1
Mutagenesisi141C → S: No effect; when associated with S-39. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000825541 – 165Ubiquitin-conjugating enzyme E2 7Add BLAST165

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki89Glycyl 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
PRIDEiQ02159

Expressioni

Inductioni

By cadmium.

Interactioni

Subunit structurei

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi35193, 248 interactors
DIPiDIP-6583N
IntActiQ02159, 624 interactors
STRINGi4932.YMR022W

Structurei

Secondary structure

1165
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 19Combined sources18
Beta strandi24 – 30Combined sources7
Beta strandi33 – 42Combined sources10
Turni48 – 51Combined sources4
Beta strandi53 – 59Combined sources7
Turni62 – 65Combined sources4
Beta strandi70 – 75Combined sources6
Beta strandi86 – 88Combined sources3
Helixi91 – 93Combined sources3
Beta strandi102 – 104Combined sources3
Turni105 – 108Combined sources4
Helixi116 – 128Combined sources13
Helixi132 – 134Combined sources3
Helixi138 – 146Combined sources9
Helixi148 – 162Combined sources15

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ02159

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

GeneTreeiENSGT00730000110436
HOGENOMiHOG000233454
InParanoidiQ02159
KOiK04555
OMAiPKMQFTC
OrthoDBiEOG092C50OL

Family and domain databases

CDDicd00195 UBCc, 1 hit
Gene3Di3.10.110.10, 1 hit
InterProiView protein in InterPro
IPR000608 UBQ-conjugat_E2
IPR023313 UBQ-conjugating_AS
IPR016135 UBQ-conjugating_enzyme/RWD
PfamiView protein in Pfam
PF00179 UQ_con, 1 hit
SUPFAMiSSF54495 SSF54495, 1 hit
PROSITEiView protein in PROSITE
PS00183 UBIQUITIN_CONJUGAT_1, 1 hit
PS50127 UBIQUITIN_CONJUGAT_2, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiUBC7_YEAST
AccessioniPrimary (citable) accession number: Q02159
Secondary accession number(s): D6VZJ6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: March 28, 2018
This is version 166 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health