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Q8T3Y0

- SINAL_DROME

UniProt

Q8T3Y0 - SINAL_DROME

Protein

Probable E3 ubiquitin-protein ligase sinah

Gene

sinah

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 2 (26 Apr 2004)
      Previous versions | rss
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    Functioni

    E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. The adapter phyl is required to direct the degradation of the two isoforms of the transcriptional repressor Tramtrack (Ttk). E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. It probably triggers the ubiquitin-mediated degradation of different substrates. A phyl-independent mechanism of degradation exists for isoform beta of ttk that involves motifs in the C-terminus of ttk.2 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi163 – 1631Zinc 1By similarity
    Metal bindingi170 – 1701Zinc 1By similarity
    Metal bindingi182 – 1821Zinc 1By similarity
    Metal bindingi186 – 1861Zinc 1By similarity
    Metal bindingi193 – 1931Zinc 2By similarity
    Metal bindingi200 – 2001Zinc 2By similarity
    Metal bindingi212 – 2121Zinc 2By similarity
    Metal bindingi217 – 2171Zinc 2By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri106 – 14136RING-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri158 – 21861SIAH-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. ubiquitin-protein transferase activity Source: InterPro
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. proteasomal protein catabolic process Source: FlyBase
    2. regulation of R7 cell differentiation Source: UniProtKB
    3. sensory organ development Source: UniProtKB
    4. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable E3 ubiquitin-protein ligase sinah (EC:6.3.2.-)
    Alternative name(s):
    Sina homolog
    Gene namesi
    Name:sinah
    ORF Names:CG13030
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3L

    Organism-specific databases

    FlyBaseiFBgn0259794. sinah.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: UniProtKB

    Pathology & Biotechi

    Disruption phenotypei

    Flies are viable. In combination with a mutation in ebi, flies show an extra dorsal central bristle phenotype. Flies that lack both sina and sinah show visible eye and bristle phenotypes, which can be explained by an inability to degrade the neuronal repressor, Tramtrack.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 351351Probable E3 ubiquitin-protein ligase sinahPRO_0000056178Add
    BLAST

    Expressioni

    Developmental stagei

    Expressed in pupae and in adults, with a higher expression in males than females.1 Publication

    Gene expression databases

    BgeeiQ8T3Y0.

    Interactioni

    Subunit structurei

    Interacts with ebi and phyl.2 Publications

    Protein-protein interaction databases

    BioGridi65184. 77 interactions.
    DIPiDIP-17367N.
    IntActiQ8T3Y0. 20 interactions.
    MINTiMINT-288495.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8T3Y0.
    SMRiQ8T3Y0. Positions 98-343.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni155 – 346192SBDAdd
    BLAST

    Domaini

    The RING-type zinc finger domain is essential for ubiquitin ligase activity.By similarity
    The SBD domain (substrate-binding domain) mediates the homodimerization and the interaction with substrate proteins. It is related to the TRAF family By similarity.By similarity

    Sequence similaritiesi

    Belongs to the SINA (Seven in absentia) family.Curated
    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation
    Contains 1 SIAH-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri106 – 14136RING-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri158 – 21861SIAH-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG308883.
    GeneTreeiENSGT00390000005434.
    InParanoidiQ8T3Y0.
    KOiK04506.
    OMAiLMSSHEN.
    OrthoDBiEOG7V766B.
    PhylomeDBiQ8T3Y0.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    3.90.890.10. 1 hit.
    InterProiIPR018121. 7-in-absentia-prot_TRAF-dom.
    IPR013323. SIAH-type.
    IPR004162. SINA_like.
    IPR008974. TRAF-like.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR013010. Znf_SIAH.
    [Graphical view]
    PANTHERiPTHR10315. PTHR10315. 1 hit.
    PfamiPF03145. Sina. 1 hit.
    [Graphical view]
    SMARTiSM00184. RING. 1 hit.
    [Graphical view]
    SUPFAMiSSF49599. SSF49599. 1 hit.
    PROSITEiPS50089. ZF_RING_2. 1 hit.
    PS51081. ZF_SIAH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8T3Y0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSVRNSRPQL SWPERVSPQR TIDTPTASGE MLTRRQSAPA LVVPPEETTH    50
    VVVVKRQSPD AAAAGELVPS RRKDSVAVQS GIVATGPLDT TRSGARDDFL 100
    MALLECPVCF GYIMPPIMQC PRGHLICSTC RSKLTICPVC RVFMTNIRSL 150
    AMEKVASKLI FPCKHSHFGC RARLSYAEKT KHEEDCECRP YFCPYPDDKC 200
    SWQGPLRDVY QHLMSSHENV ITMEGNDIIF LATNVNLEGA LDWTMVQSCH 250
    GRHFLLSLEK INLGEDCQQY FTACRMIGSM KDAAEFVYNI SLEAYNRTLR 300
    WQSKPRSIRE NFSSFTNADF LVLNKHTVEL FSEDGNLALN VVIRKVEERT 350
    N 351
    Length:351
    Mass (Da):39,645
    Last modified:April 26, 2004 - v2
    Checksum:i415764CBBD433331
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti351 – 3511N → Y in AAL90183. (PubMed:12537569)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014296 Genomic DNA. Translation: AAF49402.3.
    AY089445 mRNA. Translation: AAL90183.1.
    RefSeqiNP_648927.1. NM_140670.2.
    UniGeneiDm.29700.

    Genome annotation databases

    EnsemblMetazoaiFBtr0301683; FBpp0290897; FBgn0259794.
    GeneIDi39885.
    KEGGidme:Dmel_CG13030.
    UCSCiCG13030-RB. d. melanogaster.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014296 Genomic DNA. Translation: AAF49402.3 .
    AY089445 mRNA. Translation: AAL90183.1 .
    RefSeqi NP_648927.1. NM_140670.2.
    UniGenei Dm.29700.

    3D structure databases

    ProteinModelPortali Q8T3Y0.
    SMRi Q8T3Y0. Positions 98-343.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 65184. 77 interactions.
    DIPi DIP-17367N.
    IntActi Q8T3Y0. 20 interactions.
    MINTi MINT-288495.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0301683 ; FBpp0290897 ; FBgn0259794 .
    GeneIDi 39885.
    KEGGi dme:Dmel_CG13030.
    UCSCi CG13030-RB. d. melanogaster.

    Organism-specific databases

    CTDi 39885.
    FlyBasei FBgn0259794. sinah.

    Phylogenomic databases

    eggNOGi NOG308883.
    GeneTreei ENSGT00390000005434.
    InParanoidi Q8T3Y0.
    KOi K04506.
    OMAi LMSSHEN.
    OrthoDBi EOG7V766B.
    PhylomeDBi Q8T3Y0.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    GenomeRNAii 39885.
    NextBioi 815894.

    Gene expression databases

    Bgeei Q8T3Y0.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    3.90.890.10. 1 hit.
    InterProi IPR018121. 7-in-absentia-prot_TRAF-dom.
    IPR013323. SIAH-type.
    IPR004162. SINA_like.
    IPR008974. TRAF-like.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR013010. Znf_SIAH.
    [Graphical view ]
    PANTHERi PTHR10315. PTHR10315. 1 hit.
    Pfami PF03145. Sina. 1 hit.
    [Graphical view ]
    SMARTi SM00184. RING. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49599. SSF49599. 1 hit.
    PROSITEi PS50089. ZF_RING_2. 1 hit.
    PS51081. ZF_SIAH. 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].
      Strain: Berkeley.
      Tissue: Testis.
    4. "In vivo function of a novel Siah protein in Drosophila."
      Cooper S.E.
      Mech. Dev. 124:584-591(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EBI, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
    5. "Two modes of degradation of the tramtrack transcription factors by Siah homologues."
      Cooper S.E., Murawsky C.M., Lowe N., Travers A.A.
      J. Biol. Chem. 283:1076-1083(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PHYL.

    Entry informationi

    Entry nameiSINAL_DROME
    AccessioniPrimary (citable) accession number: Q8T3Y0
    Secondary accession number(s): Q9VVB1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2004
    Last sequence update: April 26, 2004
    Last modified: October 1, 2014
    This is version 95 of the entry and version 2 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3