ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q9ZPE4


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name FBW2_ARATH
Primary accession number Q9ZPE4
Secondary accession numbers None
Integrated into Swiss-Prot on January 23, 2007
Sequence was last modified on May 1, 1999 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 48)
Name and origin of the protein
Protein name F-box protein FBW2
Synonyms None
Gene name
Name: FBW2
OrderedLocusNames: At4g08980
ORFNames: T3H13.1
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/47134; PubMed=10617198 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
Nature 402:769-777(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[4]
GENE FAMILY, AND NOMENCLATURE.
DOI=10.1016/S1360-1385(00)01769-6; PubMed=11077244 [NCBI, ExPASy, EBI, Israel, Japan]
Xiao W., Jang J.-C.;
"F-box proteins in Arabidopsis.";
Trends Plant Sci. 5:454-457(2000).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF128396; AAD17367.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161513; CAB78022.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT002431; AAO00791.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT008715; AAP42728.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY084585; AAM61150.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR F85090; F85090.
RefSeq NP_001078359.1; -.
NP_567343.1; -.
NP_849346.1; -.
NP_974523.1; -.
UniGene At.27697
3D structure databases
ModBase Q9ZPE4.
Protein-protein interaction databases
IntAct Q9ZPE4; -.
Organism-specific databases
TAIR At4g08980; -.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006511; Biological process: ubiquitin-dependent protein catabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001810; F-box.
Graphical view of domain structure.
Pfam PF00646; F-box; 1.
Pfam graphical view of domain structure.
PROSITE PS50181; FBOX; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q9ZPE4.
ProtoNet Q9ZPE4.
Genome annotation databases
GeneID 826476; -.
GenomeReviews CT486007_GR; AT4G08980.
KEGG ath:AT4G08980; -.
NMPDR fig|3702.1.peg.18553; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Ubl conjugation pathway.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom To Length Description FTId
CHAIN   1   317  317     F-box protein FBW2. PRO_0000272241
DOMAIN   7    54  48     F-box. 
Sequence information
Length: 317 AA [This is the length of the unprocessed precursor] Molecular weight: 36483 Da [This is the MW of the unprocessed precursor] CRC64: FB409A1EA4DAB4F2 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEEDCEFRHW DELIPDALGL IFSHLPLQEV LTVVPRVCKA WNRAVTGPYC WQEIDIELWS 

        70         80         90        100        110        120 
NRFHQSDHLD RMLEMLIPRS AGSLRKLSVT GLRNDSIFSF IAQHAGSLKT LKVPRSGLTN 

       130        140        150        160        170        180 
SGVVNVAEKL SSLTFLDLSY CCKIGPEAIQ AIGKHCKSLR EFCRNMHPLD VASVVSHDDE 

       190        200        210        220        230        240 
AYAIANTMPK LKRLEIAYHR VSTEGVLKIL SCCVFLEFLE LRGCWDVQLD NKFFKEKFPD 

       250        260        270        280        290        300 
MKVLGPRVIG FYDMINDWED CCSDYFSDGS DYLAWEFFED GVMGEFYEDE FEHGWDDNFY 

       310 
AENAVLDMEP HIWPPSP 

Q9ZPE4 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by au flag APAF Australia Mirror sites: Brazil  Canada  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!