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Protein

Ubiquitin thioesterase otubain-like

Gene

CG4968

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: 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 – 721By similarity
Active sitei75 – 751NucleophileBy similarity
Active sitei255 – 2551By similarity

GO - Molecular functioni

  1. ubiquitin-specific protease activity Source: FlyBase

GO - Biological processi

  1. protein K48-linked deubiquitination Source: FlyBase
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 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0032214. CG4968.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 262262Ubiquitin thioesterase otubain-likePRO_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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini64 – 262199OTUPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C65 family.Curated
Contains 1 OTU domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5539.
GeneTreeiENSGT00390000006979.
InParanoidiQ9VL00.
KOiK09602.
OMAiRVEYMDR.
OrthoDBiEOG71K64D.
PhylomeDBiQ9VL00.

Family and domain databases

InterProiIPR003323. OTU.
IPR016615. Otubain.
IPR019400. Peptidase_C65_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

        10         20         30         40         50
MEPFTHNDGN RDELIIQQKR DIEKEISDTT PLVSEQLPLT CLYAEYSGDE
60 70 80 90 100
IFTAKIQDLS KKYKFIRRTR PDGNCFFRAF AYSYLEYLIS NTSAYQEFKK
110 120 130 140 150
LAEESKEKLV QLGFPSFTLE DFHETFMEVI QRVSPDNAGG HSTVQDELHK
160 170 180 190 200
IFNEQGYSDY VVVYLRLITS GKLQEEADFY QNFIEGDLTI EAFRHLEVEP
210 220 230 240 250
MYKESDHIHI IALCTALGAG VRVEYLDRGE GGTVKAHDFP EGSEPRIYLI
260
YRPGHYDILY PN
Length:262
Mass (Da):30,372
Last modified:May 1, 2000 - v1
Checksum:i5F65662D161DFCD2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AE014134 Genomic DNA. Translation: AAF52905.1.
AY061382 mRNA. Translation: AAL28930.1.
RefSeqiNP_609375.1. NM_135531.3.
UniGeneiDm.385.

3D structure databases

ProteinModelPortaliQ9VL00.
SMRiQ9VL00. Positions 31-260.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Protein family/group databases

MEROPSiC65.001.

Proteomic databases

PaxDbiQ9VL00.
PRIDEiQ9VL00.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

FlyBaseiFBgn0032214. CG4968.

Phylogenomic databases

eggNOGiCOG5539.
GeneTreeiENSGT00390000006979.
InParanoidiQ9VL00.
KOiK09602.
OMAiRVEYMDR.
OrthoDBiEOG71K64D.
PhylomeDBiQ9VL00.

Miscellaneous databases

GenomeRNAii34384.
NextBioi788236.
PROiQ9VL00.

Gene expression databases

BgeeiQ9VL00.

Family and domain databases

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

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: April 1, 2015
This is version 94 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.