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Q9W422 (JOSL_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein attributes

Sequence length221 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

May act as a deubiquitinating enzyme By similarity.

Catalytic activity

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).

Sequence similarities

Contains 1 Josephin domain.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Molecular functionHydrolase
Protease
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Molecular_functionomega peptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 221221Josephin-like protein
PRO_0000053845

Regions

Domain36 – 214179Josephin

Sites

Active site491Nucleophile By similarity
Active site1521Proton acceptor By similarity

Experimental info

Sequence conflict431R → L in AAL48447. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9W422 [UniParc].

Last modified March 1, 2003. Version 3.
Checksum: 17202EB46E97EFAB

FASTA22125,656
        10         20         30         40         50         60 
MESPSARTLG NSLGDDSGNG NENGNGSGNG NTTMMPHGIY HERQTRHLCG LHALNNLFQG 

        70         80         90        100        110        120 
PDMFSKSELD DYCTTLTPRN WLNPHRSWIG WGNYDVNVIM YALQQRNCEA VWFDRRRDPH 

       130        140        150        160        170        180 
CLNLSVIFGF ILNVPAQMSL GYYIPLPFHM RHWLALRRLN GSYYNLDSKL REPKCLGTEQ 

       190        200        210        220 
QFLEFLATQL QMDHELFLVL DEETDCKDKS QQRWLLPQFR D 

« 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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 28-221.
Strain: Berkeley.
Tissue: Testis.
[4]"Structural modeling of ataxin-3 reveals distant homology to adaptins."
Albrecht M., Hoffmann D., Evert B.O., Schmitt I., Wuellner U., Lengauer T.
Proteins 50:355-370(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014298 Genomic DNA. Translation: AAF46138.3.
AY070825 mRNA. Translation: AAL48447.2.
RefSeqNP_572303.4. NM_132075.4.
UniGeneDm.5285.

3D structure databases

ProteinModelPortalQ9W422.
SMRQ9W422. Positions 39-207.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid58051. 1 interaction.
DIPDIP-23119N.
MINTMINT-966633.

Proteomic databases

PaxDbQ9W422.
PRIDEQ9W422.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0070895; FBpp0070860; FBgn0029853.
GeneID31560.
KEGGdme:Dmel_CG3781.
UCSCCG3781-RA. d. melanogaster.

Organism-specific databases

FlyBaseFBgn0029853. CG3781.

Phylogenomic databases

eggNOGNOG321724.
GeneTreeENSGT00390000009228.
InParanoidQ9W422.
KOK15235.
OMAREVGGTY.
OrthoDBEOG75B871.
PhylomeDBQ9W422.

Gene expression databases

BgeeQ9W422.

Family and domain databases

InterProIPR006155. Josephin.
[Graphical view]
PfamPF02099. Josephin. 1 hit.
[Graphical view]
PROSITEPS50957. JOSEPHIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi31560.
NextBio774203.

Entry information

Entry nameJOSL_DROME
AccessionPrimary (citable) accession number: Q9W422
Secondary accession number(s): Q8MTV0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2003
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 79 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

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