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Reviewed, UniProtKB/Swiss-Prot Q9VH90 (TRBID_DROME)

Last modified July 7, 2009. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Ubiquitin thioesterase Trabid
      Short name=dTrbd
    EC=3.1.2.-
Gene names
ORF Names: CG9448
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length778 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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.

Subunit structure

Interacts with Apc. Ref.4

Domain

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.

Disruption phenotype

Flies are viable and fertile, suggesting functional redundancy. Ref.4

Sequence similarities

Belongs to the peptidase C64 family.

Contains 1 OTU domain.

Contains 3 RanBP2-type zinc fingers.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q9VBX91EBI-149336,EBI-137645

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 778778Ubiquitin thioesterase Trabid
PRO_0000361559

Regions

Domain507 – 665159OTU
Zinc finger5 – 3632RanBP2-type 1
Zinc finger89 – 11830RanBP2-type 2
Zinc finger232 – 26130RanBP2-type 3
Compositional bias191 – 23040Gln-rich

Sites

Active site5181 By similarity
Active site6581 By similarity

Amino acid modifications

Modified residue7701Phosphoserine Ref.5
Modified residue7711Phosphoserine Ref.5
Modified residue7751Phosphoserine Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9VH90-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 57AAF0A860032F07

FASTA77888,199
        10         20         30         40         50         60 
MCDTKDDAQK WKCETCTYEN YPSSLKCTMC QASKPLLNED IFRLSPAQES CTVAEEAAAV 

        70         80         90        100        110        120 
EVAVMSPTPS STCYSLQPQS QARQSNVADS EKWPCKVCTY LNWPRSLRCV QCCTKRGGEA 

       130        140        150        160        170        180 
IERGKKDMDN EADGDRAGEA LQALRISGSE ENLANKPVQL IGATASHRLS LSRGIDDATH 

       190        200        210        220        230        240 
LNNLANASHN QSQSQHRQPV LQQQMQLQLQ PQQQRESSSS AAVPPQQQKQ CYVSKWACNS 

       250        260        270        280        290        300 
CTYENWPRSI KCSMCGKTRE REISGSQNDL HASSSLNSQE ENQQQLQQPN VDTVSVNNSF 

       310        320        330        340        350        360 
NKKHIYQLGS SETINNCDTL QERQERRQRQ IRRQVDWQWL NACLGVVENN YSAVEAYLSC 

       370        380        390        400        410        420 
GGNPARSLTS TEIAALNRNS AFDVGHTLIH LAIRFHREEM LPMLLDQISG SGPGIKRVPS 

       430        440        450        460        470        480 
YVAPDLAADI RRHFANTLRL RKSGLPCHYV QKHATFALPA EIEELPIPIQ EQLYDELLDR 

       490        500        510        520        530        540 
DAQKQLETPP PALNWSLEIT ARLSSRMFVL WNRSAGDCLL DSAMQATWGV FDRDNILRRA 

       550        560        570        580        590        600 
LADTLHQCGH VFFTRWKEYE MLQASMLHFT LEDSQFEEDW STLLSLAGQP GSSLEQLHIF 

       610        620        630        640        650        660 
ALAHILRRPI IVYGVKYVKS FRGEDIGYAR FEGVYLPLFW DQNFCTKSPI ALGYTRGHFS 

       670        680        690        700        710        720 
ALVPMEPFTR IDGRRDDVED VTYLPLMDCE LKLLPIHFLT QSEVGNEESM MRQWLDVCVT 

       730        740        750        760        770 
DGGLLVAQQK LSKRPLLVAQ MLEEWLNHYR RIAQVITAPF IRRPQITHYS SDGDSDEE 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[2]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
[3]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
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: 18281465] [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: 18327897] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-770; SER-771 AND SER-775, MASS SPECTROMETRY.
Tissue: Embryo.

Cross-references

Sequence databases

AE014297 Genomic DNA. Translation: AAF54429.1.
AY058438 mRNA. Translation: AAL13667.1.
AY069258 mRNA. Translation: AAL39403.1. Different initiation.
RefSeqNP_649931.1.
UniGeneDm.2210

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ9VH90. 5 interactions.

Protein family/group databases

MEROPSC64.004.

Proteomic databases

PRIDEQ9VH90.

Genome annotation databases

EnsemblFBgn0037734. Drosophila melanogaster. [Contig view]
GeneID41179.
KEGGdme:Dmel_CG9448.
NMPDRfig|7227.3.peg.11946.

Organism-specific databases

FlyBaseFBgn0037734. CG9448.

Phylogenomic databases

HOGENOMQ9VH90.
OMAQ9VH90. ESPVINW.

Gene expression databases

ArrayExpressQ9VH90.

Family and domain databases

InterProIPR003323. OTU.
IPR001876. Znf_RanBP2.
[Graphical view]
PfamPF02338. OTU. 1 hit.
PF00641. zf-RanBP. 1 hit.
[Graphical view]
SMARTSM00547. ZnF_RBZ. 3 hits.
[Graphical view]
PROSITEPS50802. OTU. 1 hit.
PS01358. ZF_RANBP2_1. 3 hits.
PS50199. ZF_RANBP2_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio822587.

Entry information

Entry nameTRBID_DROME
AccessionPrimary (citable) accession number: Q9VH90
Secondary accession number(s): Q8T9K1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: May 1, 2000
Last modified: July 7, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents