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Protein

E3 ubiquitin-protein ligase sina

Gene

sina

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 is required for specification of R7 photoreceptor cell fate in the eye by mediating the ubiquitination and subsequent proteasomal degradation of 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. Acts via the formation of a complex with ebi and phyl that ubiquitinates the transcription repressor ttk, a general inhibitor of photoreceptor differentiation, in a subset of photoreceptor cells in the eye, leading to the differentiation of cells into neurons. Also involved in external sensory organ development.4 Publications

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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi130 – 1301Zinc 1By similarity
Metal bindingi137 – 1371Zinc 1By similarity
Metal bindingi149 – 1491Zinc 1By similarity
Metal bindingi153 – 1531Zinc 1By similarity
Metal bindingi160 – 1601Zinc 2By similarity
Metal bindingi167 – 1671Zinc 2By similarity
Metal bindingi179 – 1791Zinc 2By similarity
Metal bindingi184 – 1841Zinc 2By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri73 – 10836RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri125 – 18561SIAH-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • ligase activity Source: UniProtKB-KW
  • protein self-association Source: FlyBase
  • ubiquitin-protein transferase activity Source: FlyBase
  • zinc ion binding Source: FlyBase

GO - Biological processi

  • proteasomal protein catabolic process Source: FlyBase
  • proteolysis Source: FlyBase
  • R7 cell fate commitment Source: FlyBase
  • regulation of R7 cell differentiation Source: UniProtKB
  • response to stimulus Source: UniProtKB-KW
  • sensory organ development Source: FlyBase
  • ubiquitin-dependent protein catabolic process Source: FlyBase
  • visual perception Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Ligase

Keywords - Biological processi

Sensory transduction, Ubl conjugation pathway, Vision

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-DME-373752. Netrin-1 signaling.
R-DME-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase sina (EC:6.3.2.-)
Alternative name(s):
Seven in absentia protein
Gene namesi
Name:sina
ORF Names:CG9949
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0003410. sina.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: FlyBase
  • nucleus Source: UniProtKB
  • ubiquitin ligase complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 314314E3 ubiquitin-protein ligase sinaPRO_0000056175Add
BLAST

Proteomic databases

PaxDbiP21461.

Expressioni

Tissue specificityi

In many ommatidial precursor cells.

Gene expression databases

BgeeiP21461.
ExpressionAtlasiP21461. differential.
GenevisibleiP21461. DM.

Interactioni

Subunit structurei

Component of some E3 complex at least composed of sina, ebi and phyl. Interacts with eff.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-77019,EBI-77019
ebiQ95RJ93EBI-77019,EBI-421390
phylQ2793411EBI-77019,EBI-77033
ttkP422824EBI-77019,EBI-77008

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein self-association Source: FlyBase

Protein-protein interaction databases

BioGridi65183. 61 interactions.
DIPiDIP-17392N.
IntActiP21461. 14 interactions.
MINTiMINT-286541.
STRINGi7227.FBpp0075091.

Structurei

3D structure databases

ProteinModelPortaliP21461.
SMRiP21461. Positions 62-126, 128-313.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni122 – 314193SBDAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi14 – 218Poly-Ala
Compositional biasi26 – 5530Ser/Thr-richAdd
BLAST
Compositional biasi46 – 5510Poly-Ser

Domaini

The RING-type zinc finger domain is essential for ubiquitin ligase activity.By similarity
The SBD domain (substrate-binding domain) mediates 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 fingeri73 – 10836RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri125 – 18561SIAH-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG3002. Eukaryota.
ENOG410XVP0. LUCA.
InParanoidiP21461.
KOiK04506.
OMAiPKANVAG.
OrthoDBiEOG7JT6XC.
PhylomeDBiP21461.

Family and domain databases

Gene3Di2.60.210.10. 1 hit.
3.30.40.10. 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]
SUPFAMiSSF49599. SSF49599. 1 hit.
PROSITEiPS50089. ZF_RING_2. 1 hit.
PS51081. ZF_SIAH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P21461-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNKINPKRR EPTAAAAGAG ATGVATNTST STGSSSAGNT SSANTSSSSS
60 70 80 90 100
SSLSSAGGGD AGMSADLTSL FECPVCFDYV LPPILQCSSG HLVCVSCRSK
110 120 130 140 150
LTCCPTCRGP LANIRNLAME KVASNVKFPC KHSGYGCTAS LVYTEKTEHE
160 170 180 190 200
ETCECRPYLC PCPGASCKWQ GPLDLVMQHL MMSHKSITTL QGEDIVFLAT
210 220 230 240 250
DINLPGAVDW VMMQSCFGHH FMLVLEKQEK YDGHQQFFAI VQLIGSRKEA
260 270 280 290 300
ENFVYRLELN GNRRRLTWEA MPRSIHEGVA SAIHNSDCLV FDTSIAQLFA
310
DNGNLGINVT ISLV
Length:314
Mass (Da):33,707
Last modified:November 1, 1995 - v2
Checksum:iB58D7D5E8DA2F958
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M38384 mRNA. Translation: AAA28901.1.
AE014296 Genomic DNA. Translation: AAF49403.1.
AE014296 Genomic DNA. Translation: AAN11744.1.
AY060358 mRNA. Translation: AAL25397.1.
PIRiA36195.
RefSeqiNP_001287089.1. NM_001300160.1.
NP_476725.1. NM_057377.4.
NP_730206.1. NM_168689.2.
UniGeneiDm.7276.

Genome annotation databases

EnsemblMetazoaiFBtr0075332; FBpp0075091; FBgn0003410.
FBtr0075333; FBpp0075092; FBgn0003410.
FBtr0344230; FBpp0310636; FBgn0003410.
GeneIDi39884.
KEGGidme:Dmel_CG9949.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M38384 mRNA. Translation: AAA28901.1.
AE014296 Genomic DNA. Translation: AAF49403.1.
AE014296 Genomic DNA. Translation: AAN11744.1.
AY060358 mRNA. Translation: AAL25397.1.
PIRiA36195.
RefSeqiNP_001287089.1. NM_001300160.1.
NP_476725.1. NM_057377.4.
NP_730206.1. NM_168689.2.
UniGeneiDm.7276.

3D structure databases

ProteinModelPortaliP21461.
SMRiP21461. Positions 62-126, 128-313.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi65183. 61 interactions.
DIPiDIP-17392N.
IntActiP21461. 14 interactions.
MINTiMINT-286541.
STRINGi7227.FBpp0075091.

Proteomic databases

PaxDbiP21461.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0075332; FBpp0075091; FBgn0003410.
FBtr0075333; FBpp0075092; FBgn0003410.
FBtr0344230; FBpp0310636; FBgn0003410.
GeneIDi39884.
KEGGidme:Dmel_CG9949.

Organism-specific databases

CTDi39884.
FlyBaseiFBgn0003410. sina.

Phylogenomic databases

eggNOGiKOG3002. Eukaryota.
ENOG410XVP0. LUCA.
InParanoidiP21461.
KOiK04506.
OMAiPKANVAG.
OrthoDBiEOG7JT6XC.
PhylomeDBiP21461.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-DME-373752. Netrin-1 signaling.
R-DME-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

GenomeRNAii39884.
PROiP21461.

Gene expression databases

BgeeiP21461.
ExpressionAtlasiP21461. differential.
GenevisibleiP21461. DM.

Family and domain databases

Gene3Di2.60.210.10. 1 hit.
3.30.40.10. 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]
SUPFAMiSSF49599. SSF49599. 1 hit.
PROSITEiPS50089. ZF_RING_2. 1 hit.
PS51081. ZF_SIAH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Seven in absentia, a gene required for specification of R7 cell fate in the Drosophila eye."
    Carthew R.W., Rubin G.M.
    Cell 63:561-577(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. "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: Head.
  5. "PHYL acts to down-regulate TTK88, a transcriptional repressor of neuronal cell fates, by a SINA-dependent mechanism."
    Tang A.H., Neufeld T.P., Kwan E., Rubin G.M.
    Cell 90:459-467(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TTK DEGRADATION, INTERACTION WITH PHYL AND EFF.
  6. "Photoreceptor cell differentiation requires regulated proteolysis of the transcriptional repressor Tramtrack."
    Li S., Li Y., Carthew R.W., Lai Z.-C.
    Cell 90:469-478(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TTK DEGRADATION, INTERACTION WITH PHYL.
  7. Cited for: COMPONENT OF A COMPLEX WITH EBI AND PHYL.
  8. "A dual function of phyllopod in Drosophila external sensory organ development: cell fate specification of sensory organ precursor and its progeny."
    Pi H., Wu H.-J., Chien C.-T.
    Development 128:2699-2710(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Phyllopod acts as an adaptor protein to link the sina ubiquitin ligase to the substrate protein tramtrack."
    Li S., Xu C., Carthew R.W.
    Mol. Cell. Biol. 22:6854-6865(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE COMPLEX.

Entry informationi

Entry nameiSINA_DROME
AccessioniPrimary (citable) accession number: P21461
Secondary accession number(s): A4V214, Q9VVB0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: November 1, 1995
Last modified: June 8, 2016
This is version 155 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

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 one 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.