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P33296 (UBC6_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-conjugating enzyme E2 6

EC=6.3.2.19
Alternative name(s):
Ubiquitin carrier protein UBC6
Ubiquitin-protein ligase UBC6
Gene names
Name:UBC6
Synonyms:DOA2
Ordered Locus Names:YER100W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length250 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. Ref.5 Ref.6 Ref.7

Catalytic activity

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

Pathway

Protein modification; protein ubiquitination.

Subcellular location

Endoplasmic reticulum membrane.

Miscellaneous

Present with 1900 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RSP5P399402EBI-19745,EBI-16219

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 250250Ubiquitin-conjugating enzyme E2 6
PRO_0000082552

Regions

Topological domain1 – 232232Cytoplasmic Potential
Transmembrane233 – 24917Helical; Potential

Sites

Active site871Glycyl thioester intermediate

Amino acid modifications

Modified residue1391Phosphoserine Ref.11
Modified residue1781Phosphothreonine Ref.9 Ref.10

Experimental info

Mutagenesis871C → S: Loss of activity.

Sequences

Sequence LengthMass (Da)Tools
P33296 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 6D80C35ECC9CF5AD

FASTA25028,383
        10         20         30         40         50         60 
MATKQAHKRL TKEYKLMVEN PPPYILARPN EDNILEWHYI ITGPADTPYK GGQYHGTLTF 

        70         80         90        100        110        120 
PSDYPYKPPA IRMITPNGRF KPNTRLCLSM SDYHPDTWNP GWSVSTILNG LLSFMTSDEA 

       130        140        150        160        170        180 
TTGSITTSDH QKKTLARNSI SYNTFQNVRF KLIFPEVVQE NVETLEKRKL DEGDAANTGD 

       190        200        210        220        230        240 
ETEDPFTKAA KEKVISLEEI LDPEDRIRAE QALRQSENNS KKDGKEPNDS SSMVYIGIAI 

       250 
FLFLVGLFMK 

« Hide

References

« Hide 'large scale' references
[1]"A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum."
Sommer T., Jentsch S.
Nature 365:176-179(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome V."
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. expand/collapse author list , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.
Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"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].
[5]"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.
[6]"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.
[7]"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.
[8]"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.
[9]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[10]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X73234 Genomic DNA. Translation: CAA51706.1.
U18839 Genomic DNA. Translation: AAB64655.1.
BK006939 Genomic DNA. Translation: DAA07761.1.
PIRS36769.
RefSeqNP_011026.3. NM_001178991.3.

3D structure databases

ProteinModelPortalP33296.
SMRP33296. Positions 6-160.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36846. 87 interactions.
DIPDIP-1713N.
IntActP33296. 8 interactions.
MINTMINT-393639.
STRING4932.YER100W.

Proteomic databases

PaxDbP33296.
PeptideAtlasP33296.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYER100W; YER100W; YER100W.
GeneID856837.
KEGGsce:YER100W.

Organism-specific databases

CYGDYER100w.
SGDS000000902. UBC6.

Phylogenomic databases

eggNOGCOG5078.
GeneTreeENSGT00530000063379.
HOGENOMHOG000170329.
KOK04554.
OMAFMTGDES.
OrthoDBEOG70S7GF.

Enzyme and pathway databases

BioCycYEAST:G3O-30265-MONOMER.
UniPathwayUPA00143.

Gene expression databases

GenevestigatorP33296.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 1 hit.
PROSITEPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio983144.
PROP33296.

Entry information

Entry nameUBC6_YEAST
AccessionPrimary (citable) accession number: P33296
Secondary accession number(s): D3DM07
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: March 19, 2014
This is version 125 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 V

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways