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P25153

- UBCD6_DROME

UniProt

P25153 - UBCD6_DROME

Protein

Ubiquitin-conjugating enzyme E2-17 kDa

Gene

UbcD6

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Catalyzes the covalent attachment of ubiquitin to other proteins. Required for postreplication repair of UV-damaged DNA.

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei88 – 881Glycyl thioester intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

    1. acid-amino acid ligase activity Source: InterPro
    2. ATP binding Source: UniProtKB-KW
    3. p53 binding Source: BHF-UCL
    4. protein domain specific binding Source: BHF-UCL
    5. ubiquitin-protein transferase activity Source: BHF-UCL

    GO - Biological processi

    1. centrosome organization Source: FlyBase
    2. centrosome separation Source: FlyBase
    3. DNA repair Source: FlyBase
    4. endocytic recycling Source: FlyBase
    5. mitochondrion degradation Source: FlyBase
    6. mitotic spindle organization Source: FlyBase
    7. negative regulation of DNA damage response, signal transduction by p53 class mediator Source: BHF-UCL
    8. negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: BHF-UCL
    9. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: BHF-UCL
    10. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: BHF-UCL

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    DNA damage, DNA repair, Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_180708. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinkiP25153.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-conjugating enzyme E2-17 kDa (EC:6.3.2.19)
    Alternative name(s):
    Ubiquitin carrier protein
    Ubiquitin-protein ligase
    Gene namesi
    Name:UbcD6
    Synonyms:Dhr6
    ORF Names:CG2013
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0004436. UbcD6.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: BHF-UCL
    2. nucleus Source: BHF-UCL

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 151151Ubiquitin-conjugating enzyme E2-17 kDaPRO_0000082523Add
    BLAST

    Proteomic databases

    PaxDbiP25153.

    Expressioni

    Gene expression databases

    BgeeiP25153.

    Interactioni

    Protein-protein interaction databases

    BioGridi65824. 1 interaction.
    STRINGi7227.FBpp0078490.

    Structurei

    3D structure databases

    ProteinModelPortaliP25153.
    SMRiP25153. Positions 2-149.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5078.
    GeneTreeiENSGT00730000110565.
    InParanoidiP25153.
    KOiK10573.
    OMAiPVPDNVM.
    OrthoDBiEOG7M0NTH.
    PhylomeDBiP25153.

    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.

    P25153-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTPARRRLM RDFKRLQEDP PTGVSGAPTD NNIMIWNAVI FGPHDTPFED    50
    GTFKLTIEFT EEYPNKPPTV RFVSKVFHPN VYADGGICLD ILQNRWSPTY 100
    DVSAILTSIQ SLLSDPNPNS PANSTAAQLY KENRREYEKR VKACVEQSFI 150
    D 151
    Length:151
    Mass (Da):17,152
    Last modified:June 1, 2001 - v2
    Checksum:iCC4B35992E4A9220
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti99 – 991T → R in AAA28308. (PubMed:1902572)Curated
    Sequence conflicti99 – 991T → R in AAA28309. (PubMed:1902572)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63792 mRNA. Translation: AAA28308.1.
    M64435, M63791 Genomic DNA. Translation: AAA28309.1.
    AE014297 Genomic DNA. Translation: AAF52079.1.
    BT003481 mRNA. Translation: AAO39484.1.
    PIRiA39392.
    RefSeqiNP_001246916.1. NM_001259987.2.
    NP_524230.2. NM_079506.4.
    UniGeneiDm.2229.

    Genome annotation databases

    EnsemblMetazoaiFBtr0078849; FBpp0078490; FBgn0004436.
    FBtr0306106; FBpp0297243; FBgn0004436.
    GeneIDi40610.
    KEGGidme:Dmel_CG2013.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63792 mRNA. Translation: AAA28308.1 .
    M64435 , M63791 Genomic DNA. Translation: AAA28309.1 .
    AE014297 Genomic DNA. Translation: AAF52079.1 .
    BT003481 mRNA. Translation: AAO39484.1 .
    PIRi A39392.
    RefSeqi NP_001246916.1. NM_001259987.2.
    NP_524230.2. NM_079506.4.
    UniGenei Dm.2229.

    3D structure databases

    ProteinModelPortali P25153.
    SMRi P25153. Positions 2-149.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 65824. 1 interaction.
    STRINGi 7227.FBpp0078490.

    Proteomic databases

    PaxDbi P25153.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0078849 ; FBpp0078490 ; FBgn0004436 .
    FBtr0306106 ; FBpp0297243 ; FBgn0004436 .
    GeneIDi 40610.
    KEGGi dme:Dmel_CG2013.

    Organism-specific databases

    CTDi 40610.
    FlyBasei FBgn0004436. UbcD6.

    Phylogenomic databases

    eggNOGi COG5078.
    GeneTreei ENSGT00730000110565.
    InParanoidi P25153.
    KOi K10573.
    OMAi PVPDNVM.
    OrthoDBi EOG7M0NTH.
    PhylomeDBi P25153.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_180708. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinki P25153.

    Miscellaneous databases

    GenomeRNAii 40610.
    NextBioi 819645.
    PROi P25153.

    Gene expression databases

    Bgeei P25153.

    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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Head.

    Entry informationi

    Entry nameiUBCD6_DROME
    AccessioniPrimary (citable) accession number: P25153
    Secondary accession number(s): Q9VN70
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 124 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