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Q9STN8 (SINA4_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
E3 ubiquitin-protein ligase SINAT4
EC=6.3.2.-
Alternative name(s):
Seven in absentia homolog 4
Gene names
Name:SINAT4
Ordered Locus Names:At4g27880
ORF Names:T27E11.120
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length327 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. 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 By similarity.

Pathway

Protein modification; protein ubiquitination.

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.

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 – 327327E3 ubiquitin-protein ligase SINAT4
PRO_0000056183

Regions

Zinc finger64 – 10037RING-type
Zinc finger117 – 17761SIAH-type
Region114 – 307194SBD

Sites

Metal binding1221Zinc 1 By similarity
Metal binding1291Zinc 1 By similarity
Metal binding1411Zinc 1 By similarity
Metal binding1451Zinc 1 By similarity
Metal binding1521Zinc 2 By similarity
Metal binding1591Zinc 2 By similarity
Metal binding1711Zinc 2 By similarity
Metal binding1761Zinc 2 By similarity

Experimental info

Sequence conflict1661P → L in BX826742. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9STN8 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 0724A09157567F0C

FASTA32736,574
        10         20         30         40         50         60 
METDSMECVS STGNEIHQNG NGHQSYQFSS TKTHGGAAAA AVVTNIVGPT ATAPATSVYE 

        70         80         90        100        110        120 
LLECPVCTYS MYPPIHQCHN GHTLCSTCKV RVHNRCPTCR QELGDIRCLA LEKVAESLEL 

       130        140        150        160        170        180 
PCKFYNLGCP EIFPYYSKLK HESLCNFRPY SCPYAGSECG IVGDIPFLVA HLRDDHKVDM 

       190        200        210        220        230        240 
HAGSTFNHRY VKSNPREVEN ATWMLTVFHC FGQYFCLHFE AFQLGMGPVY MAFLRFMGDE 

       250        260        270        280        290        300 
EDARSYSYSL EVGGSGRKLT WEGTPRSIRD SHRKVRDSND GLIIQRNMAL FFSGGDRKEL 

       310        320 
KLRVTGKIWK EQHSPDSGLS IPNLSSS

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Whole genome sequence comparisons and 'full-length' cDNA sequences: a combined approach to evaluate and improve Arabidopsis genome annotation."
Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M., Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M., Weissenbach J., Salanoubat M.
Genome Res. 14:406-413(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
+Additional computationally mapped references.

Web resources

PlantsUBQ

A functional genomics database for the ubiquitin/26S proteasome proteolytic pathway in plants

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL078579 Genomic DNA. Translation: CAB43976.1.
AL161571 Genomic DNA. Translation: CAB81437.1.
CP002687 Genomic DNA. Translation: AEE85404.1.
BX826742 mRNA. No translation available.
IPIIPI00526488.
PIRT09027.
RefSeqNP_194517.1. NM_118926.2.
UniGeneAt.32065.

3D structure databases

ProteinModelPortalQ9STN8.
SMRQ9STN8. Positions 51-293.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G27880.1; AT4G27880.1; AT4G27880.
GeneID828901.
KEGGath:AT4G27880.

Organism-specific databases

TAIRAt4g27880.

Phylogenomic databases

eggNOGNOG264215.
HOGENOMHOG000231487.
InParanoidQ9STN8.
KOK04506.
OMAMETDSME.
PhylomeDBQ9STN8.
ProtClustDBCLSN2683805.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ9STN8.
GenevestigatorQ9STN8.
GermOnlineAT4G27880. Arabidopsis thaliana.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
3.90.890.10. 1 hit.
InterProIPR004162. 7-in-absentia-prot.
IPR018121. 7-in-absentia-prot_TRAF-dom.
IPR013323. SIAH-type.
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]
SUPFAMSSF49599. Traf_like. 1 hit.
PROSITEPS00518. ZF_RING_1. False negative.
PS50089. ZF_RING_2. 1 hit.
PS51081. ZF_SIAH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSINA4_ARATH
AccessionPrimary (citable) accession number: Q9STN8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: May 1, 2000
Last modified: May 1, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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