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Protein

Ubiquitin thioesterase OTU1

Gene

CG4603

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

Hydrolase that can remove conjugated ubiquitin from proteins 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 sitei158 – 1581By similarity
Active sitei161 – 1611NucleophileBy similarity
Active sitei341 – 3411By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri317 – 34125C2H2-typeAdd
BLAST

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. ubiquitin-specific protease activity Source: FlyBase

GO - Biological processi

  1. protein deubiquitination Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin thioesterase OTU1 (EC:3.4.19.12)
Gene namesi
ORF Names:CG4603
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0035593. CG4603.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 347347Ubiquitin thioesterase OTU1PRO_0000282362Add
BLAST

Proteomic databases

PaxDbiQ9VRJ9.
PRIDEiQ9VRJ9.

Expressioni

Gene expression databases

BgeeiQ9VRJ9.

Interactioni

Protein-protein interaction databases

BioGridi64071. 8 interactions.
IntActiQ9VRJ9. 1 interaction.
MINTiMINT-951773.
STRINGi7227.FBpp0076867.

Structurei

3D structure databases

ProteinModelPortaliQ9VRJ9.
SMRiQ9VRJ9. Positions 5-91, 149-308.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 8783Ubiquitin-likeAdd
BLAST
Domaini150 – 274125OTUPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 C2H2-type zinc finger.Curated
Contains 1 OTU domain.PROSITE-ProRule annotation
Contains 1 ubiquitin-like domain.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri317 – 34125C2H2-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5539.
GeneTreeiENSGT00390000009989.
InParanoidiQ9VRJ9.
KOiK13719.
OrthoDBiEOG7J1808.
PhylomeDBiQ9VRJ9.

Family and domain databases

InterProiIPR003323. OTU.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF02338. OTU. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS50802. OTU. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9VRJ9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTGSFSVKLK SKKGQFIVND LNEHTTLGEL KTKIVQATDI EATQLHVLVG
60 70 80 90 100
YPPKPLDLSQ QQEQRALKAV GINSGETLIV EEKAAPAPAA PVPGGTTVED
110 120 130 140 150
DEALARRLQA EEEAQLLQET AGGPVAQAAD YQLPVAPTES GPNGDFNGIL
160 170 180 190 200
LKKVVPADNS CLFTSIRFVL NGKVDNEGSE MMRHIIAQEV AADPQSYNDA
210 220 230 240 250
VLGKSNAEYC AWIQKADSWG GAIEVSILSN YYGIEIDVVD IQNAIINRFG
260 270 280 290 300
EDKNFGLRVF LLFDGIHYDP LYMETSPSAA PATIFPVEEL GVYQQAEQLA
310 320 330 340
NEAQSSRQYT NVDKFTLRCM QCDVRLVGQV QAQEHAKQTG HKNFGEI
Length:347
Mass (Da):37,823
Last modified:May 1, 2000 - v1
Checksum:iF8AFA9C679DD77E4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti87 – 871A → S in AAL39440 (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014296 Genomic DNA. Translation: AAF50796.1.
AY069295 mRNA. Translation: AAL39440.1.
RefSeqiNP_001261436.1. NM_001274507.1.
NP_647951.2. NM_139694.4.
UniGeneiDm.2192.

Genome annotation databases

EnsemblMetazoaiFBtr0077164; FBpp0076867; FBgn0035593.
FBtr0331804; FBpp0304189; FBgn0035593.
GeneIDi38603.
KEGGidme:Dmel_CG4603.
UCSCiCG4603-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014296 Genomic DNA. Translation: AAF50796.1.
AY069295 mRNA. Translation: AAL39440.1.
RefSeqiNP_001261436.1. NM_001274507.1.
NP_647951.2. NM_139694.4.
UniGeneiDm.2192.

3D structure databases

ProteinModelPortaliQ9VRJ9.
SMRiQ9VRJ9. Positions 5-91, 149-308.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi64071. 8 interactions.
IntActiQ9VRJ9. 1 interaction.
MINTiMINT-951773.
STRINGi7227.FBpp0076867.

Proteomic databases

PaxDbiQ9VRJ9.
PRIDEiQ9VRJ9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0077164; FBpp0076867; FBgn0035593.
FBtr0331804; FBpp0304189; FBgn0035593.
GeneIDi38603.
KEGGidme:Dmel_CG4603.
UCSCiCG4603-RA. d. melanogaster.

Organism-specific databases

FlyBaseiFBgn0035593. CG4603.

Phylogenomic databases

eggNOGiCOG5539.
GeneTreeiENSGT00390000009989.
InParanoidiQ9VRJ9.
KOiK13719.
OrthoDBiEOG7J1808.
PhylomeDBiQ9VRJ9.

Miscellaneous databases

GenomeRNAii38603.
NextBioi809477.
PROiQ9VRJ9.

Gene expression databases

BgeeiQ9VRJ9.

Family and domain databases

InterProiIPR003323. OTU.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF02338. OTU. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS50802. OTU. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 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(1999) [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: Ovary.

Entry informationi

Entry nameiOTU1_DROME
AccessioniPrimary (citable) accession number: Q9VRJ9
Secondary accession number(s): Q8T9H3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: May 1, 2000
Last modified: April 1, 2015
This is version 91 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. 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.