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Q9VH90

- TRBID_DROME

UniProt

Q9VH90 - TRBID_DROME

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Protein
Ubiquitin thioesterase trabid
Gene
trbd, CG9448
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.1 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 – 5181Nucleophile By similarity
Active sitei658 – 6581Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri5 – 3632RanBP2-type 1
Add
BLAST
Zinc fingeri89 – 11830RanBP2-type 2
Add
BLAST
Zinc fingeri232 – 26130RanBP2-type 3
Add
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. Wnt signaling pathway Source: UniProtKB-KW
  2. positive regulation of Wnt signaling pathway Source: UniProtKB
  3. protein K63-linked deubiquitination Source: UniProtKB
Complete GO annotation...

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 trabid
PRO_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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini507 – 665159OTU
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi191 – 23040Gln-rich
Add
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.
Contains 1 OTU domain.

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

« Hide 'large scale' publications
  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: July 9, 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. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi