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P15731

- UBC4_YEAST

UniProt

P15731 - UBC4_YEAST

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Protein
Ubiquitin-conjugating enzyme E2 4
Gene
UBC4, YBR082C, YBR0745
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. Mediates the selective degradation of short-lived and abnormal proteins. Mediates ubiquitination of PEX5.1 Publication

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei86 – 861Glycyl thioester intermediate

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. acid-amino acid ligase activity Source: InterPro
  3. protein binding Source: IntAct
  4. protein binding, bridging Source: SGD
  5. ubiquitin binding Source: SGD
  6. ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

  1. cellular response to heat Source: SGD
  2. protein monoubiquitination Source: SGD
  3. protein polyubiquitination Source: UniProtKB
  4. protein ubiquitination Source: SGD
  5. ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Stress response, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29050-MONOMER.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme E2 4 (EC:6.3.2.19)
Alternative name(s):
Ubiquitin carrier protein 4
Ubiquitin-protein ligase 4
Gene namesi
Name:UBC4
Ordered Locus Names:YBR082C
ORF Names:YBR0745
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome II

Organism-specific databases

CYGDiYBR082c.
SGDiS000000286. UBC4.

Subcellular locationi

GO - Cellular componenti

  1. proteasome complex Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 148148Ubiquitin-conjugating enzyme E2 4
PRO_0000082545Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei12 – 121Phosphoserine1 Publication

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP15731.
PeptideAtlasiP15731.
PRIDEiP15731.

Expressioni

Inductioni

By heat shock and cadmium.

Gene expression databases

GenevestigatoriP15731.

Interactioni

Subunit structurei

Interacts with TUL1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
EGD2P388792EBI-19735,EBI-6379

Protein-protein interaction databases

BioGridi32786. 261 interactions.
DIPiDIP-6596N.
IntActiP15731. 4 interactions.
MINTiMINT-677321.
STRINGi4932.YBR082C.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 1413
Beta strandi20 – 278
Beta strandi30 – 4011
Beta strandi50 – 567
Turni59 – 624
Beta strandi67 – 704
Helixi88 – 903
Turni91 – 933
Helixi100 – 11213
Helixi122 – 1309
Helixi132 – 14615

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QCQX-ray2.70A1-148[»]
ProteinModelPortaliP15731.
SMRiP15731. Positions 1-148.

Miscellaneous databases

EvolutionaryTraceiP15731.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00740000115416.
HOGENOMiHOG000233455.
KOiK06689.
OMAiNDLGRDP.
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.

P15731-1 [UniParc]FASTAAdd to Basket

« Hide

MSSSKRIAKE LSDLERDPPT SCSAGPVGDD LYHWQASIMG PADSPYAGGV    50
FFLSIHFPTD YPFKPPKISF TTKIYHPNIN ANGNICLDIL KDQWSPALTL 100
SKVLLSICSL LTDANPDDPL VPEIAHIYKT DRPKYEATAR EWTKKYAV 148
Length:148
Mass (Da):16,456
Last modified:April 1, 1990 - v1
Checksum:i8E96137D3EB20F80
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X17493 Genomic DNA. Translation: CAA35528.1.
X76294 Genomic DNA. Translation: CAA53942.1.
Z35951 Genomic DNA. Translation: CAA85027.1.
BK006936 Genomic DNA. Translation: DAA07201.1.
PIRiS22857.
RefSeqiNP_009638.1. NM_001178430.1.

Genome annotation databases

EnsemblFungiiYBR082C; YBR082C; YBR082C.
GeneIDi852376.
KEGGisce:YBR082C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X17493 Genomic DNA. Translation: CAA35528.1 .
X76294 Genomic DNA. Translation: CAA53942.1 .
Z35951 Genomic DNA. Translation: CAA85027.1 .
BK006936 Genomic DNA. Translation: DAA07201.1 .
PIRi S22857.
RefSeqi NP_009638.1. NM_001178430.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1QCQ X-ray 2.70 A 1-148 [» ]
ProteinModelPortali P15731.
SMRi P15731. Positions 1-148.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32786. 261 interactions.
DIPi DIP-6596N.
IntActi P15731. 4 interactions.
MINTi MINT-677321.
STRINGi 4932.YBR082C.

Proteomic databases

MaxQBi P15731.
PeptideAtlasi P15731.
PRIDEi P15731.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YBR082C ; YBR082C ; YBR082C .
GeneIDi 852376.
KEGGi sce:YBR082C.

Organism-specific databases

CYGDi YBR082c.
SGDi S000000286. UBC4.

Phylogenomic databases

GeneTreei ENSGT00740000115416.
HOGENOMi HOG000233455.
KOi K06689.
OMAi NDLGRDP.
OrthoDBi EOG7SBP18.

Enzyme and pathway databases

UniPathwayi UPA00143 .
BioCyci YEAST:G3O-29050-MONOMER.

Miscellaneous databases

EvolutionaryTracei P15731.
NextBioi 971168.

Gene expression databases

Genevestigatori P15731.

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. "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.
    , 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. 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. 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).

Entry informationi

Entry nameiUBC4_YEAST
AccessioniPrimary (citable) accession number: P15731
Secondary accession number(s): D6VQ81
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: September 3, 2014
This is version 148 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 13500 molecules/cell in log phase SD medium.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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 II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

External Data

Dasty 3

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