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P15731 (UBC4_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 145. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-conjugating enzyme E2 4

EC=6.3.2.19
Alternative name(s):
Ubiquitin carrier protein 4
Ubiquitin-protein ligase 4
Gene names
Name:UBC4
Ordered Locus Names:YBR082C
ORF Names:YBR0745
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length148 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the covalent attachment of ubiquitin to other proteins. Mediates the selective degradation of short-lived and abnormal proteins. Mediates ubiquitination of PEX5. Ref.7

Catalytic activity

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

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with TUL1. Ref.5

Induction

By heat shock and cadmium.

Post-translational modification

The N-terminus is blocked.

Miscellaneous

Present with 13500 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

EGD2P388792EBI-19735,EBI-6379

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 148148Ubiquitin-conjugating enzyme E2 4
PRO_0000082545

Sites

Active site861Glycyl thioester intermediate

Amino acid modifications

Modified residue121Phosphoserine Ref.8

Secondary structure

...................... 148
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P15731 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 8E96137D3EB20F80

FASTA14816,456
        10         20         30         40         50         60 
MSSSKRIAKE LSDLERDPPT SCSAGPVGDD LYHWQASIMG PADSPYAGGV FFLSIHFPTD 

        70         80         90        100        110        120 
YPFKPPKISF TTKIYHPNIN ANGNICLDIL KDQWSPALTL SKVLLSICSL LTDANPDDPL 

       130        140 
VPEIAHIYKT DRPKYEATAR EWTKKYAV 

« Hide

References

« Hide 'large scale' references
[1]"Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short-lived and abnormal proteins."
Seufert W., Jentsch S.
EMBO J. 9:543-550(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 40-64 AND 119-125.
[2]"Sequence analysis of a 31 kb DNA fragment from the right arm of Saccharomyces cerevisiae chromosome II."
van der Aart Q.J.M., Barthe C., Doignon F., Aigle M., Crouzet M., Steensma H.Y.
Yeast 10:959-964(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"Complete DNA sequence of yeast chromosome II."
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. expand/collapse author list , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"A transmembrane ubiquitin ligase required to sort membrane proteins into multivesicular bodies."
Reggiori F., Pelham H.R.B.
Nat. Cell Biol. 4:117-123(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TUL1.
[6]"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].
[7]"A conserved cysteine is essential for Pex4p-dependent ubiquitination of the peroxisomal import receptor Pex5p."
Williams C., van den Berg M., Sprenger R.R., Distel B.
J. Biol. Chem. 282:22534-22543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"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 SER-12, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Sites of ubiquitin attachment in Saccharomyces cerevisiae."
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Tertiary structures of class I ubiquitin-conjugating enzymes are highly conserved: crystal structure of yeast Ubc4."
Cook W.J., Jeffrey L.C., Xu Y., Chau V.
Biochemistry 32:13809-13817(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X17493 Genomic DNA. Translation: CAA35528.1.
X76294 Genomic DNA. Translation: CAA53942.1.
Z35951 Genomic DNA. Translation: CAA85027.1.
BK006936 Genomic DNA. Translation: DAA07201.1.
PIRS22857.
RefSeqNP_009638.1. NM_001178430.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QCQX-ray2.70A1-148[»]
ProteinModelPortalP15731.
SMRP15731. Positions 1-148.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32786. 261 interactions.
DIPDIP-6596N.
IntActP15731. 4 interactions.
MINTMINT-677321.
STRING4932.YBR082C.

Proteomic databases

PeptideAtlasP15731.
PRIDEP15731.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBR082C; YBR082C; YBR082C.
GeneID852376.
KEGGsce:YBR082C.

Organism-specific databases

CYGDYBR082c.
SGDS000000286. UBC4.

Phylogenomic databases

GeneTreeENSGT00740000115416.
HOGENOMHOG000233455.
KOK06689.
OMAIAHIYKQ.
OrthoDBEOG7SBP18.

Enzyme and pathway databases

BioCycYEAST:G3O-29050-MONOMER.
UniPathwayUPA00143.

Gene expression databases

GenevestigatorP15731.

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

EvolutionaryTraceP15731.
NextBio971168.

Entry information

Entry nameUBC4_YEAST
AccessionPrimary (citable) accession number: P15731
Secondary accession number(s): D6VQ81
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: April 16, 2014
This is version 145 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 II

Yeast (Saccharomyces cerevisiae) chromosome II: 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