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Q9VL00

- OTUBL_DROME

UniProt

Q9VL00 - OTUBL_DROME

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Protein
Ubiquitin thioesterase otubain-like
Gene
CG4968
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 2 out of 5 - Experimental evidence at transcript leveli

Functioni

Possible hydrolase that can remove conjugated ubiquitin from proteins in vitro and may therefore play an important regulatory role at the level of protein turnover by preventing degradation By similarity.

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 sitei72 – 721 By similarity
Active sitei75 – 751Nucleophile By similarity
Active sitei255 – 2551 By similarity

GO - Molecular functioni

  1. cysteine-type peptidase activity Source: UniProtKB-KW
  2. omega peptidase activity Source: InterPro

GO - Biological processi

  1. cellular amino acid metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Protein family/group databases

MEROPSiC65.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin thioesterase otubain-like (EC:3.4.19.12)
Alternative name(s):
Ubiquitin-specific-processing protease otubain-like
Short name:
Deubiquitinating enzyme otubain-like
Gene namesi
ORF Names:CG4968
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0032214. CG4968.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 262262Ubiquitin thioesterase otubain-like
PRO_0000221012Add
BLAST

Proteomic databases

PaxDbiQ9VL00.
PRIDEiQ9VL00.

Expressioni

Gene expression databases

BgeeiQ9VL00.

Interactioni

Protein-protein interaction databases

BioGridi60470. 2 interactions.
IntActiQ9VL00. 1 interaction.
MINTiMINT-327859.
STRINGi7227.FBpp0079577.

Structurei

3D structure databases

ProteinModelPortaliQ9VL00.
SMRiQ9VL00. Positions 31-260.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini64 – 262199OTU
Add
BLAST

Sequence similaritiesi

Belongs to the peptidase C65 family.
Contains 1 OTU domain.

Phylogenomic databases

eggNOGiCOG5539.
GeneTreeiENSGT00390000006979.
InParanoidiQ9VL00.
KOiK09602.
OMAiVEPMYKE.
OrthoDBiEOG71K64D.
PhylomeDBiQ9VL00.

Family and domain databases

InterProiIPR003323. OTU.
IPR019400. Peptidase_C65_otubain.
IPR016615. Ubiquitin_thioesterase_Otubain.
[Graphical view]
PfamiPF10275. Peptidase_C65. 1 hit.
[Graphical view]
PIRSFiPIRSF013503. Ubiquitin_thioesterase_Otubain. 1 hit.
PROSITEiPS50802. OTU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9VL00-1 [UniParc]FASTAAdd to Basket

« Hide

MEPFTHNDGN RDELIIQQKR DIEKEISDTT PLVSEQLPLT CLYAEYSGDE    50
IFTAKIQDLS KKYKFIRRTR PDGNCFFRAF AYSYLEYLIS NTSAYQEFKK 100
LAEESKEKLV QLGFPSFTLE DFHETFMEVI QRVSPDNAGG HSTVQDELHK 150
IFNEQGYSDY VVVYLRLITS GKLQEEADFY QNFIEGDLTI EAFRHLEVEP 200
MYKESDHIHI IALCTALGAG VRVEYLDRGE GGTVKAHDFP EGSEPRIYLI 250
YRPGHYDILY PN 262
Length:262
Mass (Da):30,372
Last modified:May 1, 2000 - v1
Checksum:i5F65662D161DFCD2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014134 Genomic DNA. Translation: AAF52905.1.
AY061382 mRNA. Translation: AAL28930.1.
RefSeqiNP_609375.1. NM_135531.3.
UniGeneiDm.385.

Genome annotation databases

EnsemblMetazoaiFBtr0079987; FBpp0079577; FBgn0032214.
GeneIDi34384.
KEGGidme:Dmel_CG4968.
UCSCiCG4968-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014134 Genomic DNA. Translation: AAF52905.1 .
AY061382 mRNA. Translation: AAL28930.1 .
RefSeqi NP_609375.1. NM_135531.3.
UniGenei Dm.385.

3D structure databases

ProteinModelPortali Q9VL00.
SMRi Q9VL00. Positions 31-260.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 60470. 2 interactions.
IntActi Q9VL00. 1 interaction.
MINTi MINT-327859.
STRINGi 7227.FBpp0079577.

Protein family/group databases

MEROPSi C65.001.

Proteomic databases

PaxDbi Q9VL00.
PRIDEi Q9VL00.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0079987 ; FBpp0079577 ; FBgn0032214 .
GeneIDi 34384.
KEGGi dme:Dmel_CG4968.
UCSCi CG4968-RA. d. melanogaster.

Organism-specific databases

FlyBasei FBgn0032214. CG4968.

Phylogenomic databases

eggNOGi COG5539.
GeneTreei ENSGT00390000006979.
InParanoidi Q9VL00.
KOi K09602.
OMAi VEPMYKE.
OrthoDBi EOG71K64D.
PhylomeDBi Q9VL00.

Miscellaneous databases

GenomeRNAii 34384.
NextBioi 788236.
PROi Q9VL00.

Gene expression databases

Bgeei Q9VL00.

Family and domain databases

InterProi IPR003323. OTU.
IPR019400. Peptidase_C65_otubain.
IPR016615. Ubiquitin_thioesterase_Otubain.
[Graphical view ]
Pfami PF10275. Peptidase_C65. 1 hit.
[Graphical view ]
PIRSFi PIRSF013503. Ubiquitin_thioesterase_Otubain. 1 hit.
PROSITEi PS50802. OTU. 1 hit.
[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: Embryo.

Entry informationi

Entry nameiOTUBL_DROME
AccessioniPrimary (citable) accession number: Q9VL00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 90 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

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