Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9W422

- JOSL_DROME

UniProt

Q9W422 - JOSL_DROME

Protein

Josephin-like protein

Gene

CG3781

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 3 (01 Mar 2003)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    May act as a deubiquitinating enzyme.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 sitei49 – 491NucleophilePROSITE-ProRule annotation
    Active sitei152 – 1521Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. omega peptidase activity Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease

    Keywords - Biological processi

    Ubl conjugation pathway

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Josephin-like protein (EC:3.4.19.12)
    Gene namesi
    ORF Names:CG3781
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome X

    Organism-specific databases

    FlyBaseiFBgn0029853. CG3781.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 221221Josephin-like proteinPRO_0000053845Add
    BLAST

    Proteomic databases

    PaxDbiQ9W422.
    PRIDEiQ9W422.

    Expressioni

    Gene expression databases

    BgeeiQ9W422.

    Interactioni

    Protein-protein interaction databases

    BioGridi58051. 1 interaction.
    DIPiDIP-23119N.
    MINTiMINT-966633.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9W422.
    SMRiQ9W422. Positions 39-207.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini36 – 214179JosephinPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 Josephin domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG321724.
    GeneTreeiENSGT00390000009228.
    InParanoidiQ9W422.
    KOiK15235.
    OMAiREVGGTY.
    OrthoDBiEOG75B871.
    PhylomeDBiQ9W422.

    Family and domain databases

    InterProiIPR006155. Josephin.
    [Graphical view]
    PfamiPF02099. Josephin. 1 hit.
    [Graphical view]
    PROSITEiPS50957. JOSEPHIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9W422-1 [UniParc]FASTAAdd to Basket

    « Hide

    MESPSARTLG NSLGDDSGNG NENGNGSGNG NTTMMPHGIY HERQTRHLCG    50
    LHALNNLFQG PDMFSKSELD DYCTTLTPRN WLNPHRSWIG WGNYDVNVIM 100
    YALQQRNCEA VWFDRRRDPH CLNLSVIFGF ILNVPAQMSL GYYIPLPFHM 150
    RHWLALRRLN GSYYNLDSKL REPKCLGTEQ QFLEFLATQL QMDHELFLVL 200
    DEETDCKDKS QQRWLLPQFR D 221
    Length:221
    Mass (Da):25,656
    Last modified:March 1, 2003 - v3
    Checksum:i17202EB46E97EFAB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti43 – 431R → L in AAL48447. (PubMed:12537569)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014298 Genomic DNA. Translation: AAF46138.3.
    AY070825 mRNA. Translation: AAL48447.2.
    RefSeqiNP_572303.4. NM_132075.4.
    UniGeneiDm.5285.

    Genome annotation databases

    EnsemblMetazoaiFBtr0070895; FBpp0070860; FBgn0029853.
    GeneIDi31560.
    KEGGidme:Dmel_CG3781.
    UCSCiCG3781-RA. d. melanogaster.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014298 Genomic DNA. Translation: AAF46138.3 .
    AY070825 mRNA. Translation: AAL48447.2 .
    RefSeqi NP_572303.4. NM_132075.4.
    UniGenei Dm.5285.

    3D structure databases

    ProteinModelPortali Q9W422.
    SMRi Q9W422. Positions 39-207.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 58051. 1 interaction.
    DIPi DIP-23119N.
    MINTi MINT-966633.

    Proteomic databases

    PaxDbi Q9W422.
    PRIDEi Q9W422.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0070895 ; FBpp0070860 ; FBgn0029853 .
    GeneIDi 31560.
    KEGGi dme:Dmel_CG3781.
    UCSCi CG3781-RA. d. melanogaster.

    Organism-specific databases

    FlyBasei FBgn0029853. CG3781.

    Phylogenomic databases

    eggNOGi NOG321724.
    GeneTreei ENSGT00390000009228.
    InParanoidi Q9W422.
    KOi K15235.
    OMAi REVGGTY.
    OrthoDBi EOG75B871.
    PhylomeDBi Q9W422.

    Miscellaneous databases

    GenomeRNAii 31560.
    NextBioi 774203.

    Gene expression databases

    Bgeei Q9W422.

    Family and domain databases

    InterProi IPR006155. Josephin.
    [Graphical view ]
    Pfami PF02099. Josephin. 1 hit.
    [Graphical view ]
    PROSITEi PS50957. JOSEPHIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] 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.

    Entry informationi

    Entry nameiJOSL_DROME
    AccessioniPrimary (citable) accession number: Q9W422
    Secondary accession number(s): Q8MTV0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2003
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 80 of the entry and version 3 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