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Q9VX25

- UBE2S_DROME

UniProt

Q9VX25 - UBE2S_DROME

Protein

Ubiquitin-conjugating enzyme E2 S

Gene

CG8188

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 2 (05 Jul 2004)
      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 specifically elongating polyubiquitin chains initiated by the E2 enzyme vih/UbcH10 on APC/C substrates, enhancing the degradation of APC/C substrates by the proteasome and promoting mitotic exit.1 PublicationPROSITE-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 sitei98 – 981Glycyl thioester intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
    2. exit from mitosis Source: UniProtKB
    3. imaginal disc-derived wing morphogenesis Source: FlyBase
    4. protein ubiquitination Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Cell cycle, Cell division, Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiQ9VX25.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-conjugating enzyme E2 S (EC:6.3.2.19)
    Alternative name(s):
    Ubiquitin carrier protein S
    Ubiquitin-protein ligase S
    Gene namesi
    ORF Names:CG8188
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome X

    Organism-specific databases

    FlyBaseiFBgn0030863. CG8188.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 209209Ubiquitin-conjugating enzyme E2 SPRO_0000390440Add
    BLAST

    Proteomic databases

    PaxDbiQ9VX25.

    Expressioni

    Gene expression databases

    BgeeiQ9VX25.

    Interactioni

    Protein-protein interaction databases

    BioGridi59074. 9 interactions.
    IntActiQ9VX25. 1 interaction.
    MINTiMINT-895042.
    STRINGi7227.FBpp0099891.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9VX25.
    SMRiQ9VX25. Positions 9-159.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5078.
    GeneTreeiENSGT00730000110565.
    InParanoidiQ9VX25.
    KOiK10583.
    OMAiPDLGIKH.
    OrthoDBiEOG73JKXD.
    PhylomeDBiQ9VX25.

    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.

    Q9VX25-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSQYSNVEN LSPQTIRQVM RELQEMETTP PEGIKVLINE SDVTDIQALI    50
    DGPAGTPYAA GIFRVKLTLN KDFPLTPPKA YFLTKIFHPN VAANGEICVN 100
    TLKKDWKPDL GIKHILLTIK CLLIVPNPES ALNEEAGKML LERYDDYSQR 150
    ARMMTEIHAQ PAKCGVGAVG DAKDDGGPST KKHAGLDKKL QDKKKEKLLK 200
    EKKRMLKRL 209
    Length:209
    Mass (Da):23,337
    Last modified:July 5, 2004 - v2
    Checksum:i65A528912E50A477
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ151896 mRNA. Translation: AAZ57341.1.
    DQ151897 mRNA. Translation: AAZ57342.1.
    AE014298 Genomic DNA. Translation: ABC67190.1.
    AE014298 Genomic DNA. Translation: AAF48756.2.
    BT031269 mRNA. Translation: ABY20510.1.
    RefSeqiNP_001033852.1. NM_001038763.1.
    NP_573237.2. NM_133009.2.
    UniGeneiDm.11521.

    Genome annotation databases

    EnsemblMetazoaiFBtr0074476; FBpp0074250; FBgn0030863.
    FBtr0100463; FBpp0099891; FBgn0030863.
    GeneIDi32751.
    KEGGidme:Dmel_CG8188.
    UCSCiCG8188-RA. d. melanogaster.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ151896 mRNA. Translation: AAZ57341.1 .
    DQ151897 mRNA. Translation: AAZ57342.1 .
    AE014298 Genomic DNA. Translation: ABC67190.1 .
    AE014298 Genomic DNA. Translation: AAF48756.2 .
    BT031269 mRNA. Translation: ABY20510.1 .
    RefSeqi NP_001033852.1. NM_001038763.1.
    NP_573237.2. NM_133009.2.
    UniGenei Dm.11521.

    3D structure databases

    ProteinModelPortali Q9VX25.
    SMRi Q9VX25. Positions 9-159.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 59074. 9 interactions.
    IntActi Q9VX25. 1 interaction.
    MINTi MINT-895042.
    STRINGi 7227.FBpp0099891.

    Proteomic databases

    PaxDbi Q9VX25.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0074476 ; FBpp0074250 ; FBgn0030863 .
    FBtr0100463 ; FBpp0099891 ; FBgn0030863 .
    GeneIDi 32751.
    KEGGi dme:Dmel_CG8188.
    UCSCi CG8188-RA. d. melanogaster.

    Organism-specific databases

    FlyBasei FBgn0030863. CG8188.

    Phylogenomic databases

    eggNOGi COG5078.
    GeneTreei ENSGT00730000110565.
    InParanoidi Q9VX25.
    KOi K10583.
    OMAi PDLGIKH.
    OrthoDBi EOG73JKXD.
    PhylomeDBi Q9VX25.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    SignaLinki Q9VX25.

    Miscellaneous databases

    ChiTaRSi CG8188. drosophila.
    GenomeRNAii 32751.
    NextBioi 780178.
    PROi Q9VX25.

    Gene expression databases

    Bgeei Q9VX25.

    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. "Full length sequences of assorted Drosophila melanogaster cDNAs."
      Murphy T.D.
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C., Celniker S.E.
      Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo.
    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, CATALYTIC ACTIVITY, PATHWAY.

    Entry informationi

    Entry nameiUBE2S_DROME
    AccessioniPrimary (citable) accession number: Q9VX25
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2009
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 108 of the entry and version 2 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