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Q9VH90

- TRBID_DROME

UniProt

Q9VH90 - TRBID_DROME

Protein

Ubiquitin thioesterase trabid

Gene

trbd

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 108 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Positive regulator of the Wnt signaling pathway. Specifically cleaves 'Lys-63'-linked ubiquitin chains. May act by deubiquitinating APC protein, a negative regulator of Wnt-mediated transcription By similarity. Required for an efficient wg response, but not for other signaling responses, in the eye.By similarity1 Publication

    Catalytic activityi

    Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei518 – 5181NucleophileBy similarity
    Active sitei658 – 6581Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri5 – 3632RanBP2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri89 – 11830RanBP2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri232 – 26130RanBP2-type 3PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. cysteine-type peptidase activity Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. ubiquitin thiolesterase activity Source: UniProtKB
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. positive regulation of Wnt signaling pathway Source: UniProtKB
    2. protein K63-linked deubiquitination Source: UniProtKB
    3. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Ubl conjugation pathway, Wnt signaling pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Protein family/group databases

    MEROPSiC64.004.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin thioesterase trabid (EC:3.4.19.12)
    Short name:
    dTrbd
    Gene namesi
    Name:trbd
    ORF Names:CG9448
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0037734. trbd.

    Pathology & Biotechi

    Disruption phenotypei

    Flies are viable and fertile, suggesting functional redundancy.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 778778Ubiquitin thioesterase trabidPRO_0000361559Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei770 – 7701Phosphoserine1 Publication
    Modified residuei771 – 7711Phosphoserine1 Publication
    Modified residuei775 – 7751Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9VH90.
    PRIDEiQ9VH90.

    Expressioni

    Gene expression databases

    BgeeiQ9VH90.

    Interactioni

    Subunit structurei

    Interacts with Apc.1 Publication

    Protein-protein interaction databases

    BioGridi66338. 9 interactions.
    MINTiMINT-803912.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9VH90.
    SMRiQ9VH90. Positions 470-717.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini507 – 665159OTUPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi191 – 23040Gln-richAdd
    BLAST

    Domaini

    The OTU domain mediates the deubiquitinating activity.By similarity
    The RanBP2-type zinc fingers mediate the specific interaction with 'Lys-63'-linked ubiquitin.By similarity

    Sequence similaritiesi

    Belongs to the peptidase C64 family.Curated
    Contains 1 OTU domain.PROSITE-ProRule annotation
    Contains 3 RanBP2-type zinc fingers.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri5 – 3632RanBP2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri89 – 11830RanBP2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri232 – 26130RanBP2-type 3PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG253754.
    GeneTreeiENSGT00530000062989.
    InParanoidiQ9VH90.
    KOiK11862.
    OMAiVENNYSA.
    OrthoDBiEOG7R56SB.
    PhylomeDBiQ9VH90.

    Family and domain databases

    Gene3Di4.10.1060.10. 1 hit.
    InterProiIPR003323. OTU.
    IPR001876. Znf_RanBP2.
    [Graphical view]
    PfamiPF02338. OTU. 1 hit.
    PF00641. zf-RanBP. 1 hit.
    [Graphical view]
    SMARTiSM00547. ZnF_RBZ. 3 hits.
    [Graphical view]
    PROSITEiPS50802. OTU. 1 hit.
    PS01358. ZF_RANBP2_1. 3 hits.
    PS50199. ZF_RANBP2_2. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9VH90-1 [UniParc]FASTAAdd to Basket

    « Hide

    MCDTKDDAQK WKCETCTYEN YPSSLKCTMC QASKPLLNED IFRLSPAQES    50
    CTVAEEAAAV EVAVMSPTPS STCYSLQPQS QARQSNVADS EKWPCKVCTY 100
    LNWPRSLRCV QCCTKRGGEA IERGKKDMDN EADGDRAGEA LQALRISGSE 150
    ENLANKPVQL IGATASHRLS LSRGIDDATH LNNLANASHN QSQSQHRQPV 200
    LQQQMQLQLQ PQQQRESSSS AAVPPQQQKQ CYVSKWACNS CTYENWPRSI 250
    KCSMCGKTRE REISGSQNDL HASSSLNSQE ENQQQLQQPN VDTVSVNNSF 300
    NKKHIYQLGS SETINNCDTL QERQERRQRQ IRRQVDWQWL NACLGVVENN 350
    YSAVEAYLSC GGNPARSLTS TEIAALNRNS AFDVGHTLIH LAIRFHREEM 400
    LPMLLDQISG SGPGIKRVPS YVAPDLAADI RRHFANTLRL RKSGLPCHYV 450
    QKHATFALPA EIEELPIPIQ EQLYDELLDR DAQKQLETPP PALNWSLEIT 500
    ARLSSRMFVL WNRSAGDCLL DSAMQATWGV FDRDNILRRA LADTLHQCGH 550
    VFFTRWKEYE MLQASMLHFT LEDSQFEEDW STLLSLAGQP GSSLEQLHIF 600
    ALAHILRRPI IVYGVKYVKS FRGEDIGYAR FEGVYLPLFW DQNFCTKSPI 650
    ALGYTRGHFS ALVPMEPFTR IDGRRDDVED VTYLPLMDCE LKLLPIHFLT 700
    QSEVGNEESM MRQWLDVCVT DGGLLVAQQK LSKRPLLVAQ MLEEWLNHYR 750
    RIAQVITAPF IRRPQITHYS SDGDSDEE 778
    Length:778
    Mass (Da):88,199
    Last modified:May 1, 2000 - v1
    Checksum:i57AAF0A860032F07
    GO

    Sequence cautioni

    The sequence AAL39403.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014297 Genomic DNA. Translation: AAF54429.1.
    AY058438 mRNA. Translation: AAL13667.1.
    AY069258 mRNA. Translation: AAL39403.1. Different initiation.
    RefSeqiNP_649931.1. NM_141674.2.
    UniGeneiDm.2210.

    Genome annotation databases

    EnsemblMetazoaiFBtr0082091; FBpp0081569; FBgn0037734.
    GeneIDi41179.
    KEGGidme:Dmel_CG9448.
    UCSCiCG9448-RA. d. melanogaster.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014297 Genomic DNA. Translation: AAF54429.1 .
    AY058438 mRNA. Translation: AAL13667.1 .
    AY069258 mRNA. Translation: AAL39403.1 . Different initiation.
    RefSeqi NP_649931.1. NM_141674.2.
    UniGenei Dm.2210.

    3D structure databases

    ProteinModelPortali Q9VH90.
    SMRi Q9VH90. Positions 470-717.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 66338. 9 interactions.
    MINTi MINT-803912.

    Protein family/group databases

    MEROPSi C64.004.

    Proteomic databases

    PaxDbi Q9VH90.
    PRIDEi Q9VH90.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0082091 ; FBpp0081569 ; FBgn0037734 .
    GeneIDi 41179.
    KEGGi dme:Dmel_CG9448.
    UCSCi CG9448-RA. d. melanogaster.

    Organism-specific databases

    CTDi 41179.
    FlyBasei FBgn0037734. trbd.

    Phylogenomic databases

    eggNOGi NOG253754.
    GeneTreei ENSGT00530000062989.
    InParanoidi Q9VH90.
    KOi K11862.
    OMAi VENNYSA.
    OrthoDBi EOG7R56SB.
    PhylomeDBi Q9VH90.

    Miscellaneous databases

    GenomeRNAii 41179.
    NextBioi 822587.
    PROi Q9VH90.

    Gene expression databases

    Bgeei Q9VH90.

    Family and domain databases

    Gene3Di 4.10.1060.10. 1 hit.
    InterProi IPR003323. OTU.
    IPR001876. Znf_RanBP2.
    [Graphical view ]
    Pfami PF02338. OTU. 1 hit.
    PF00641. zf-RanBP. 1 hit.
    [Graphical view ]
    SMARTi SM00547. ZnF_RBZ. 3 hits.
    [Graphical view ]
    PROSITEi PS50802. OTU. 1 hit.
    PS01358. ZF_RANBP2_1. 3 hits.
    PS50199. ZF_RANBP2_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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.
    2. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Head.
    4. "Trabid, a new positive regulator of Wnt-induced transcription with preference for binding and cleaving K63-linked ubiquitin chains."
      Tran H., Hamada F., Schwarz-Romond T., Bienz M.
      Genes Dev. 22:528-542(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH APC, DISRUPTION PHENOTYPE.
    5. "Phosphoproteome analysis of Drosophila melanogaster embryos."
      Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
      J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-770; SER-771 AND SER-775, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.

    Entry informationi

    Entry nameiTRBID_DROME
    AccessioniPrimary (citable) accession number: Q9VH90
    Secondary accession number(s): Q8T9K1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 20, 2009
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 108 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. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3