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Q02159

- UBC7_YEAST

UniProt

Q02159 - UBC7_YEAST

Protein

Ubiquitin-conjugating enzyme E2 7

Gene

UBC7

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 1 (01 Jul 1993)
      Previous versions | rss
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    Functioni

    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.7 PublicationsPROSITE-ProRule annotation

    Catalytic activityi

    ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.1 PublicationPROSITE-ProRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei89 – 891Glycyl thioester intermediate

    GO - Molecular functioni

    1. acid-amino acid ligase activity Source: InterPro
    2. ATP binding Source: UniProtKB-KW
    3. ubiquitin-protein transferase activity Source: SGD

    GO - Biological processi

    1. chromatin assembly or disassembly Source: SGD
    2. ER-associated ubiquitin-dependent protein catabolic process Source: SGD
    3. fungal-type cell wall organization Source: SGD
    4. response to cadmium ion Source: UniProtKB-KW

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Cadmium resistance, Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Cadmium, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32727-MONOMER.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:UBC7
    Synonyms:QRI8
    Ordered Locus Names:YMR022W
    ORF Names:YM9711.12
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIII

    Organism-specific databases

    CYGDiYMR022w.
    SGDiS000004624. UBC7.

    Subcellular locationi

    Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side
    Note: Anchored via the membrane protein CUE1 to the endoplasmic reticulum membrane.

    GO - Cellular componenti

    1. Doa10p ubiquitin ligase complex Source: SGD
    2. endoplasmic reticulum membrane Source: SGD
    3. Hrd1p ubiquitin ligase ERAD-L complex Source: SGD

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi39 – 391C → S: No effect; when associated with S-141. 1 Publication
    Mutagenesisi81 – 811N → A: Impairs degradation of UBC7-substrates, but does not prevent protein degradation.
    Mutagenesisi89 – 891C → A or S: Prevents polyubiquitin chain attachment and protein degradation. 1 Publication
    Mutagenesisi141 – 1411C → S: No effect; when associated with S-39. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 165165Ubiquitin-conjugating enzyme E2 7PRO_0000082554Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki89 – 89Glycyl cysteine thioester (Cys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

    Post-translational modificationi

    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 CUE1.1 Publication

    Keywords - PTMi

    Thioester bond, Ubl conjugation

    Proteomic databases

    MaxQBiQ02159.
    PaxDbiQ02159.
    PeptideAtlasiQ02159.

    Expressioni

    Inductioni

    By cadmium.

    Gene expression databases

    GenevestigatoriQ02159.

    Interactioni

    Subunit structurei

    Forms a heterodimer with CUE1. Interacts with SSM4/DOA10 and HDR1. Interacts with UFD4.5 Publications

    Protein-protein interaction databases

    BioGridi35193. 171 interactions.
    DIPiDIP-6583N.
    IntActiQ02159. 609 interactions.
    MINTiMINT-683595.
    STRINGi4932.YMR022W.

    Structurei

    Secondary structure

    1
    165
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi2 – 1918
    Beta strandi24 – 307
    Beta strandi33 – 4210
    Turni48 – 514
    Beta strandi53 – 597
    Turni62 – 654
    Beta strandi70 – 756
    Beta strandi86 – 883
    Helixi91 – 933
    Beta strandi102 – 1043
    Turni105 – 1084
    Helixi116 – 12813
    Helixi132 – 1343
    Helixi138 – 1469
    Helixi148 – 16215

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2UCZX-ray2.93A1-165[»]
    4JQUX-ray1.81A2-165[»]
    ProteinModelPortaliQ02159.
    SMRiQ02159. Positions 2-165.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ02159.

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5078.
    GeneTreeiENSGT00730000110436.
    HOGENOMiHOG000233454.
    KOiK04555.
    OMAiDMFHPNI.
    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.

    Q02159-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKTAQKRLL KELQQLIKDS PPGIVAGPKS ENNIFIWDCL IQGPPDTPYA    50
    DGVFNAKLEF PKDYPLSPPK LTFTPSILHP NIYPNGEVCI SILHSPGDDP 100
    NMYELAEERW SPVQSVEKIL LSVMSMLSEP NIESGANIDA CILWRDNRPE 150
    FERQVKLSIL KSLGF 165
    Length:165
    Mass (Da):18,520
    Last modified:July 1, 1993 - v1
    Checksum:iD3D297847DBB462D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRiS28951.
    RefSeqiNP_013735.1. NM_001182518.1.

    Genome annotation databases

    EnsemblFungiiYMR022W; YMR022W; YMR022W.
    GeneIDi855036.
    KEGGisce:YMR022W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    PIRi S28951.
    RefSeqi NP_013735.1. NM_001182518.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2UCZ X-ray 2.93 A 1-165 [» ]
    4JQU X-ray 1.81 A 2-165 [» ]
    ProteinModelPortali Q02159.
    SMRi Q02159. Positions 2-165.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35193. 171 interactions.
    DIPi DIP-6583N.
    IntActi Q02159. 609 interactions.
    MINTi MINT-683595.
    STRINGi 4932.YMR022W.

    Proteomic databases

    MaxQBi Q02159.
    PaxDbi Q02159.
    PeptideAtlasi Q02159.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YMR022W ; YMR022W ; YMR022W .
    GeneIDi 855036.
    KEGGi sce:YMR022W.

    Organism-specific databases

    CYGDi YMR022w.
    SGDi S000004624. UBC7.

    Phylogenomic databases

    eggNOGi COG5078.
    GeneTreei ENSGT00730000110436.
    HOGENOMi HOG000233454.
    KOi K04555.
    OMAi DMFHPNI.
    OrthoDBi EOG7SBP18.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    BioCyci YEAST:G3O-32727-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q02159.
    NextBioi 978248.
    PROi Q02159.

    Gene expression databases

    Genevestigatori Q02159.

    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. "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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. 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. 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).

    Entry informationi

    Entry nameiUBC7_YEAST
    AccessioniPrimary (citable) accession number: Q02159
    Secondary accession number(s): D6VZJ6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 133 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 2100 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, 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 XIII
      Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

    External Data

    Dasty 3