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Protein

Probable E3 ubiquitin-protein ligase sinah

Gene

sinah

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: -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

Catalytic activityi

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi163Zinc 1By similarity1
Metal bindingi170Zinc 1By similarity1
Metal bindingi182Zinc 1By similarity1
Metal bindingi186Zinc 1By similarity1
Metal bindingi193Zinc 2By similarity1
Metal bindingi200Zinc 2By similarity1
Metal bindingi212Zinc 2By similarity1
Metal bindingi217Zinc 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri106 – 141RING-typePROSITE-ProRule annotationAdd BLAST36
Zinc fingeri158 – 218SIAH-typePROSITE-ProRule annotationAdd BLAST61

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferase
Biological processUbl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-DME-373752 Netrin-1 signaling
R-DME-5689880 Ub-specific processing proteases
R-DME-983168 Antigen processing: Ubiquitination & Proteasome degradation
UniPathwayiUPA00143

Names & Taxonomyi

Protein namesi
Recommended name:
Probable E3 ubiquitin-protein ligase sinah (EC:2.3.2.27)
Alternative name(s):
RING-type E3 ubiquitin transferase sinahCurated
Sina homolog
Gene namesi
Name:sinah
ORF Names:CG13030
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0259794 sinah

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000561781 – 351Probable E3 ubiquitin-protein ligase sinahAdd BLAST351

Proteomic databases

PaxDbiQ8T3Y0
PRIDEiQ8T3Y0

Expressioni

Developmental stagei

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

Gene expression databases

BgeeiFBgn0259794
ExpressionAtlasiQ8T3Y0 differential
GenevisibleiQ8T3Y0 DM

Interactioni

Subunit structurei

Interacts with ebi and phyl.2 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi65184, 77 interactors
DIPiDIP-17367N
IntActiQ8T3Y0, 39 interactors
STRINGi7227.FBpp0290897

Structurei

3D structure databases

ProteinModelPortaliQ8T3Y0
SMRiQ8T3Y0
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni155 – 346SBDAdd BLAST192

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

Belongs to the SINA (Seven in absentia) family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri106 – 141RING-typePROSITE-ProRule annotationAdd BLAST36
Zinc fingeri158 – 218SIAH-typePROSITE-ProRule annotationAdd BLAST61

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG3002 Eukaryota
ENOG410XVP0 LUCA
GeneTreeiENSGT00390000005434
InParanoidiQ8T3Y0
KOiK04506
OMAiNVITMEG
OrthoDBiEOG091G0DK5
PhylomeDBiQ8T3Y0

Family and domain databases

Gene3Di2.60.210.10, 1 hit
3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR018121 7-in-absentia-prot_TRAF-dom
IPR004162 SINA-like
IPR008974 TRAF-like
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR013010 Znf_SIAH
PANTHERiPTHR10315 PTHR10315, 1 hit
PfamiView protein in Pfam
PF03145 Sina, 1 hit
SUPFAMiSSF49599 SSF49599, 1 hit
PROSITEiView protein in PROSITE
PS50089 ZF_RING_2, 1 hit
PS51081 ZF_SIAH, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti351N → Y in AAL90183 (PubMed:12537569).Curated1

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

Similar proteinsi

Entry informationi

Entry nameiSINAL_DROME
AccessioniPrimary (citable) accession number: Q8T3Y0
Secondary accession number(s): Q9VVB1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: May 23, 2018
This is version 130 of the entry and version 2 of the sequence. See 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
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