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Q9VTY6

- UBE2C_DROME

UniProt

Q9VTY6 - UBE2C_DROME

Protein

Ubiquitin-conjugating enzyme E2 C

Gene

vih

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Catalyzes the covalent attachment of ubiquitin to other proteins. Acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. Acts by initiating polyubiquitin chains on APC/C substrates, leading to the degradation of APC/C substrates by the proteasome and promoting mitotic exit.2 PublicationsPROSITE-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 sitei116 – 1161Glycyl thioester intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
    2. exit from mitosis Source: UniProtKB
    3. regulation of cell cycle Source: FlyBase

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_181662. Separation of Sister Chromatids.
    REACT_182058. Senescence-Associated Secretory Phenotype (SASP).
    REACT_210493. Inactivation of APC/C via direct inhibition of the APC/C complex.
    REACT_224351. Regulation of APC/C activators between G1/S and early anaphase.
    REACT_33104. APC/C:Cdc20 mediated degradation of Cyclin B.
    REACT_92044. APC/C:Cdc20 mediated degradation of Securin.
    SignaLinkiQ9VTY6.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-conjugating enzyme E2 C (EC:6.3.2.19)
    Alternative name(s):
    Ubiquitin carrier protein C
    Ubiquitin carrier protein vihar
    Ubiquitin-protein ligase C
    Gene namesi
    Name:vih
    Synonyms:Ubch10
    ORF Names:CG10682
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3L

    Organism-specific databases

    FlyBaseiFBgn0264848. vih.

    Subcellular locationi

    Cytoplasm 1 Publication. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 1 Publication
    Note: Localizes in the cytoplasm of mitotic cells but also associates with centrosomes, and its own degradation is initiated at the metaphase-anaphase transition.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. microtubule organizing center Source: UniProtKB-SubCell
    3. ubiquitin ligase complex Source: FlyBase

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Disruption phenotypei

    Embryonic lethality. Both homozygous and hemizygous females show maternal effect lethality and produce syncytial embryos that fail to develop as a result of mitotic defects.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 178178Ubiquitin-conjugating enzyme E2 CPRO_0000390471Add
    BLAST

    Post-translational modificationi

    Ubiquitinated by the APC/C complex, leading to its degradation at the metaphase-anaphase transition.1 Publication

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    PaxDbiQ9VTY6.
    PRIDEiQ9VTY6.

    Expressioni

    Gene expression databases

    BgeeiQ9VTY6.

    Interactioni

    Subunit structurei

    Component of the APC/C complex.

    Protein-protein interaction databases

    BioGridi68841. 7 interactions.
    MINTiMINT-845845.
    STRINGi7227.FBpp0075690.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9VTY6.
    SMRiQ9VTY6. Positions 33-175.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5078.
    GeneTreeiENSGT00730000110854.
    InParanoidiQ9VTY6.
    KOiK06688.
    OMAiAELWDKD.
    PhylomeDBiQ9VTY6.

    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.

    Q9VTY6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAQNISPEQS GGAGGGGSKH SDDSMPVKDN HAVSKRLHKE LMNLMMANER    50
    GISAFPDGEN IFKWVGTIAG PRNTVYSGQT YRLSLDFPNS YPYAAPVVKF 100
    LTSCFHPNVD LQGAICLDIL KDKWSALYDV RTILLSIQSL LGEPNNESPL 150
    NAQAAMMWND QKEYKKYLDA FYEKHKDT 178
    Length:178
    Mass (Da):19,832
    Last modified:May 1, 2000 - v1
    Checksum:i7EF04EE68FEDC7AB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF410850 mRNA. Translation: AAL02117.1.
    AE014296 Genomic DNA. Translation: AAF49909.1.
    BT028772 mRNA. Translation: ABI34153.1.
    RefSeqiNP_648582.1. NM_140325.3.
    UniGeneiDm.3505.

    Genome annotation databases

    EnsemblMetazoaiFBtr0075958; FBpp0075690; FBgn0027936.
    GeneIDi44118.
    KEGGidme:Dmel_CG10682.
    UCSCiCG10682-RA. d. melanogaster.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF410850 mRNA. Translation: AAL02117.1 .
    AE014296 Genomic DNA. Translation: AAF49909.1 .
    BT028772 mRNA. Translation: ABI34153.1 .
    RefSeqi NP_648582.1. NM_140325.3.
    UniGenei Dm.3505.

    3D structure databases

    ProteinModelPortali Q9VTY6.
    SMRi Q9VTY6. Positions 33-175.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 68841. 7 interactions.
    MINTi MINT-845845.
    STRINGi 7227.FBpp0075690.

    Proteomic databases

    PaxDbi Q9VTY6.
    PRIDEi Q9VTY6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0075958 ; FBpp0075690 ; FBgn0027936 .
    GeneIDi 44118.
    KEGGi dme:Dmel_CG10682.
    UCSCi CG10682-RA. d. melanogaster.

    Organism-specific databases

    CTDi 44118.
    FlyBasei FBgn0264848. vih.

    Phylogenomic databases

    eggNOGi COG5078.
    GeneTreei ENSGT00730000110854.
    InParanoidi Q9VTY6.
    KOi K06688.
    OMAi AELWDKD.
    PhylomeDBi Q9VTY6.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_181662. Separation of Sister Chromatids.
    REACT_182058. Senescence-Associated Secretory Phenotype (SASP).
    REACT_210493. Inactivation of APC/C via direct inhibition of the APC/C complex.
    REACT_224351. Regulation of APC/C activators between G1/S and early anaphase.
    REACT_33104. APC/C:Cdc20 mediated degradation of Cyclin B.
    REACT_92044. APC/C:Cdc20 mediated degradation of Securin.
    SignaLinki Q9VTY6.

    Miscellaneous databases

    GenomeRNAii 44118.
    NextBioi 836806.
    PROi Q9VTY6.

    Gene expression databases

    Bgeei Q9VTY6.

    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. "The E2-C vihar is required for the correct spatiotemporal proteolysis of cyclin B and itself undergoes cyclical degradation."
      Mathe E., Kraft C., Giet R., Deak P., Peters J.-M., Glover D.M.
      Curr. Biol. 14:1723-1733(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, UBIQUITINATION, DISRUPTION PHENOTYPE.
    2. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    3. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    4. Stapleton M., Carlson J., Chavez C., Frise E., George R., Pacleb J., Park S., Wan K.H., Yu C., Celniker S.E.
      Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
    5. "Identification of a physiological E2 module for the human anaphase-promoting complex."
      Williamson A., Wickliffe K.E., Mellone B.G., Song L., Karpen G.H., Rape M.
      Proc. Natl. Acad. Sci. U.S.A. 106:18213-18218(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiUBE2C_DROME
    AccessioniPrimary (citable) accession number: Q9VTY6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2009
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 107 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3