Ubiquitin-conjugating enzyme E2 7 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Contribute

Send feedback

Read comments (?) or add your own

Q02159 (UBC7_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 122. History...

Clusters with 100%, 90%, 50% identity |

Documents (5) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	UBC7
Synonyms:	QRI8
Ordered Locus Names:	YMR022W
ORF Names:	YM9711.12

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	165 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Cadmium resistance Ubl conjugation pathway
Cellular component	Endoplasmic reticulum Membrane
Ligand	ATP-binding Cadmium Nucleotide-binding
Molecular function	Ligase
PTM	Thioester bond Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ER-associated protein catabolic process Inferred from direct assay PubMed 12105183. Source: SGD chromatin assembly or disassembly Inferred from mutant phenotype PubMed 15643069. Source: SGD fungal-type cell wall organization Inferred from genetic interaction PubMed 18971375. Source: SGD response to cadmium ion Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	endoplasmic reticulum membrane Inferred from direct assay Ref.8. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-protein ligase activity Inferred from direct assay Ref.7. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 165

165

Ubiquitin-conjugating enzyme E2 7

PRO_0000082554

Sites

Active site

Glycyl thioester intermediate

Amino acid modifications

Cross-link

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

Experimental info

Mutagenesis

C → S: No effect; when associated with S-141. Ref.16

Mutagenesis

N → A: Impairs degradation of UBC7-substrates, but does not prevent protein degradation.

Mutagenesis

C → A or S: Prevents polyubiquitin chain attachment and protein degradation. Ref.16

Mutagenesis

141

C → S: No effect; when associated with S-39. Ref.16

Secondary structure

165

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q02159 [UniParc].

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

FASTA

165

18,520

        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' referencesShow '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. Barrell B.G. Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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. 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.

PIR

S28951.

RefSeq

NP_013735.1. NM_001182518.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2UCZ	X-ray	2.93	A	1-165	[»]

ProteinModelPortal

Q02159.

SMR

Q02159. Positions 2-165.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6583N.

IntAct

Q02159. 612 interactions.

MINT

MINT-683595.

STRING

4932.YMR022W.

Proteomic databases

PaxDb

Q02159.

PeptideAtlas

Q02159.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YMR022W; YMR022W; YMR022W.

GeneID

855036.

KEGG

sce:YMR022W.

Organism-specific databases

CYGD

YMR022w.

SGD

S000004624. UBC7.

Phylogenomic databases

eggNOG

COG5078.

GeneTree

ENSGT00530000063258.

HOGENOM

HOG000233454.

K04555.

OMA

RRLMAEY.

OrthoDB

EOG4X6GJN.

Enzyme and pathway databases

BioCyc

YEAST:G3O-32727-MONOMER.

UniPathway

UPA00143.

Gene expression databases

Genevestigator

Q02159.

GermOnline

YMR022W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

3.10.110.10. 1 hit.

InterPro

IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]

Pfam

PF00179. UQ_con. 1 hit.
[Graphical view]

SUPFAM

SSF54495. UBQ-conjugat/RWD-like. 1 hit.

PROSITE

PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q02159.

NextBio

978248.

Entry information

Entry name

UBC7_YEAST

Accession

Primary (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:	May 29, 2013
This is version 122 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XIII

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents