Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8T3Y0 (SINAL_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 namesRecommended name:
Probable E3 ubiquitin-protein ligase sinah

EC=6.3.2.-
Alternative name(s):
Sina homolog
Gene names
Name:sinah
ORF Names:CG13030
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length351 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 betaof ttk that involves motifs in the C-terminus of ttk. Ref.4 Ref.5

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with ebi and phyl. Ref.4 Ref.5

Developmental stage

Expressed in pupae and in adults, with a higher expression in males than females. Ref.4

Domain

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.

Disruption phenotype

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. Ref.4

Sequence similarities

Belongs to the SINA (Seven in absentia) family.

Contains 1 RING-type zinc finger.

Contains 1 SIAH-type zinc finger.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 351351Probable E3 ubiquitin-protein ligase sinah
PRO_0000056178

Regions

Zinc finger106 – 14136RING-type
Zinc finger158 – 21861SIAH-type
Region155 – 346192SBD

Sites

Metal binding1631Zinc 1 By similarity
Metal binding1701Zinc 1 By similarity
Metal binding1821Zinc 1 By similarity
Metal binding1861Zinc 1 By similarity
Metal binding1931Zinc 2 By similarity
Metal binding2001Zinc 2 By similarity
Metal binding2121Zinc 2 By similarity
Metal binding2171Zinc 2 By similarity

Experimental info

Sequence conflict3511N → Y in AAL90183. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q8T3Y0 [UniParc].

Last modified April 26, 2004. Version 2.
Checksum: 415764CBBD433331

FASTA35139,645
        10         20         30         40         50         60 
MSVRNSRPQL SWPERVSPQR TIDTPTASGE MLTRRQSAPA LVVPPEETTH VVVVKRQSPD 

        70         80         90        100        110        120 
AAAAGELVPS RRKDSVAVQS GIVATGPLDT TRSGARDDFL MALLECPVCF GYIMPPIMQC 

       130        140        150        160        170        180 
PRGHLICSTC RSKLTICPVC RVFMTNIRSL AMEKVASKLI FPCKHSHFGC RARLSYAEKT 

       190        200        210        220        230        240 
KHEEDCECRP YFCPYPDDKC SWQGPLRDVY QHLMSSHENV ITMEGNDIIF LATNVNLEGA 

       250        260        270        280        290        300 
LDWTMVQSCH GRHFLLSLEK INLGEDCQQY FTACRMIGSM KDAAEFVYNI SLEAYNRTLR 

       310        320        330        340        350 
WQSKPRSIRE NFSSFTNADF LVLNKHTVEL FSEDGNLALN VVIRKVEERT N 

« 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].
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014296 Genomic DNA. Translation: AAF49402.3.
AY089445 mRNA. Translation: AAL90183.1.
RefSeqNP_648927.1. NM_140670.2.
UniGeneDm.29700.

3D structure databases

ProteinModelPortalQ8T3Y0.
SMRQ8T3Y0. Positions 97-343.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid65184. 77 interactions.
DIPDIP-17367N.
IntActQ8T3Y0. 20 interactions.
MINTMINT-288495.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0301683; FBpp0290897; FBgn0259794.
GeneID39885.
KEGGdme:Dmel_CG13030.
UCSCCG13030-RB. d. melanogaster.

Organism-specific databases

CTD39885.
FlyBaseFBgn0259794. sinah.

Phylogenomic databases

eggNOGNOG308883.
GeneTreeENSGT00390000005434.
InParanoidQ8T3Y0.
KOK04506.
OMAHEKNCKY.
OrthoDBEOG7V766B.
PhylomeDBQ8T3Y0.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

BgeeQ8T3Y0.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
3.90.890.10. 1 hit.
InterProIPR018121. 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]
PANTHERPTHR10315. PTHR10315. 1 hit.
PfamPF03145. Sina. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
[Graphical view]
SUPFAMSSF49599. SSF49599. 1 hit.
PROSITEPS50089. ZF_RING_2. 1 hit.
PS51081. ZF_SIAH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi39885.
NextBio815894.

Entry information

Entry nameSINAL_DROME
AccessionPrimary (citable) accession number: Q8T3Y0
Secondary accession number(s): Q9VVB1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: February 19, 2014
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Drosophila

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