Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P15731

- UBC4_YEAST

UniProt

P15731 - UBC4_YEAST

Protein

Ubiquitin-conjugating enzyme E2 4

Gene

UBC4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 PublicationPROSITE-ProRule annotation

    Catalytic activityi

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

    Pathwayi

    Sites

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

    GO - Molecular functioni

    1. acid-amino acid ligase activity Source: InterPro
    2. ATP binding Source: UniProtKB-KW
    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

    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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 148148Ubiquitin-conjugating enzyme E2 4PRO_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. 262 interactions.
    DIPiDIP-6596N.
    IntActiP15731. 4 interactions.
    MINTiMINT-677321.
    STRINGi4932.YBR082C.

    Structurei

    Secondary structure

    1
    148
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15731.

    Family & Domainsi

    Sequence similaritiesi

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

    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. 262 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

    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: October 1, 2014
    This is version 149 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.1 Publication

    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