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Protein

Probable E3 ubiquitin-protein ligase sinah

Gene

sinah

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: 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 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. ubiquitin-protein transferase activity Source: InterPro
  3. zinc ion binding Source: FlyBase

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

ReactomeiREACT_236260. Netrin-1 signaling.
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.
ExpressionAtlasiQ8T3Y0. differential.

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 97-343.
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.
OMAiHENVITM.
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

        10         20         30         40         50
MSVRNSRPQL SWPERVSPQR TIDTPTASGE MLTRRQSAPA LVVPPEETTH
60 70 80 90 100
VVVVKRQSPD AAAAGELVPS RRKDSVAVQS GIVATGPLDT TRSGARDDFL
110 120 130 140 150
MALLECPVCF GYIMPPIMQC PRGHLICSTC RSKLTICPVC RVFMTNIRSL
160 170 180 190 200
AMEKVASKLI FPCKHSHFGC RARLSYAEKT KHEEDCECRP YFCPYPDDKC
210 220 230 240 250
SWQGPLRDVY QHLMSSHENV ITMEGNDIIF LATNVNLEGA LDWTMVQSCH
260 270 280 290 300
GRHFLLSLEK INLGEDCQQY FTACRMIGSM KDAAEFVYNI SLEAYNRTLR
310 320 330 340 350
WQSKPRSIRE NFSSFTNADF LVLNKHTVEL FSEDGNLALN VVIRKVEERT

N
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AE014296 Genomic DNA. Translation: AAF49402.3.
AY089445 mRNA. Translation: AAL90183.1.
RefSeqiNP_648927.1. NM_140670.2.
UniGeneiDm.29700.

3D structure databases

ProteinModelPortaliQ8T3Y0.
SMRiQ8T3Y0. Positions 97-343.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi39885.
FlyBaseiFBgn0259794. sinah.

Phylogenomic databases

eggNOGiNOG308883.
GeneTreeiENSGT00390000005434.
InParanoidiQ8T3Y0.
KOiK04506.
OMAiHENVITM.
OrthoDBiEOG7V766B.
PhylomeDBiQ8T3Y0.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiREACT_236260. Netrin-1 signaling.

Miscellaneous databases

GenomeRNAii39885.
NextBioi815894.

Gene expression databases

BgeeiQ8T3Y0.
ExpressionAtlasiQ8T3Y0. differential.

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]
ProtoNetiSearch...

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: February 4, 2015
This is version 99 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.