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Q8T3Y0

- SINAL_DROME

UniProt

Q8T3Y0 - SINAL_DROME

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Protein

Probable E3 ubiquitin-protein ligase sinah

Gene
sinah, CG13030
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 1 By similarity
Metal bindingi170 – 1701Zinc 1 By similarity
Metal bindingi182 – 1821Zinc 1 By similarity
Metal bindingi186 – 1861Zinc 1 By similarity
Metal bindingi193 – 1931Zinc 2 By similarity
Metal bindingi200 – 2001Zinc 2 By similarity
Metal bindingi212 – 2121Zinc 2 By similarity
Metal bindingi217 – 2171Zinc 2 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri106 – 14136RING-typeAdd
BLAST
Zinc fingeri158 – 21861SIAH-typeAdd
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
Complete GO annotation...

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
Complete GO annotation...

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.

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.

Sequence similaritiesi

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti351 – 3511N → Y in AAL90183. 1 Publication

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

« 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: 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: September 3, 2014
This is version 94 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

Similar proteinsi