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UniProtKB/Swiss-Prot entry Q9ZR12


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

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Entry information
Entry name GRH1_ARATH
Primary accession number Q9ZR12
Secondary accession numbers Q94AU0 Q9C5Y7
Integrated into Swiss-Prot on January 23, 2007
Sequence was last modified on May 1, 1999 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 48)
Name and origin of the protein
Protein name GRR1-like protein 1
Synonyms Protein AUXIN SIGNALING F-BOX 1
F-box/LRR-repeat protein 18
Gene name
Name: GRH1
Synonyms: AFB1, FBL18, GER1, LRF1
OrderedLocusNames: At4g03190
ORFNames: F4C21.11
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 [MRNA], FUNCTION, INTERACTION WITH SKP1A/ASK1 AND SKP1B/ASK2, AND LEUCINE-RICH REPEATS.
DOI=10.1023/A:1014440531842; PubMed=12008900 [NCBI, ExPASy, EBI, Israel, Japan]
Thelander M., Fredriksson D., Schouten J., Hoge J.H.C., Ronne H.;
"Cloning by pathway activation in yeast: identification of an Arabidopsis thaliana F-box protein that can turn on glucose repression.";
Plant Mol. Biol. 49:69-79(2002).
[2]
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).
[3]
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).
[4]
INTERACTION WITH SKP1A/ASK1 AND SKP1B/ASK2.
DOI=10.1101/gad.13.13.1678; PubMed=10398681 [NCBI, ExPASy, EBI, Israel, Japan]
Gray W.M., del Pozo J.C., Walker L., Hobbie L., Risseeuw E., Banks T., Crosby W.L., Yang M., Ma H., Estelle M.;
"Identification of an SCF ubiquitin-ligase complex required for auxin response in Arabidopsis thaliana.";
Genes Dev. 13:1678-1691(1999).
[5]
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).
[6]
FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH CUL1; IAA7; IAA12 AND SKP1A/ASK1.
DOI=10.1016/j.devcel.2005.05.014; PubMed=15992545 [NCBI, ExPASy, EBI, Israel, Japan]
Dharmasiri N., Dharmasiri S., Weijers D., Lechner E., Yamada M., Hobbie L., Ehrismann J.S., Juergens G., Estelle M.;
"Plant development is regulated by a family of auxin receptor F box proteins.";
Dev. Cell 9:109-119(2005).
[7]
FUNCTION.
DOI=10.1038/nature03543; PubMed=15917797 [NCBI, ExPASy, EBI, Israel, Japan]
Dharmasiri N., Dharmasiri S., Estelle M.;
"The F-box protein TIR1 is an auxin receptor.";
Nature 435:441-445(2005).
[8]
FUNCTION, AND INDUCTION.
DOI=10.1126/science.1126088; PubMed=16627744 [NCBI, ExPASy, EBI, Israel, Japan]
Navarro L., Dunoyer P., Jay F., Arnold B., Dharmasiri N., Estelle M., Voinnet O., Jones J.D.G.;
"A plant miRNA contributes to antibacterial resistance by repressing auxin signaling.";
Science 312:436-439(2006).
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
AF291816; AAK01147.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC005275; AAD14447.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161496; CAB77804.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY045799; AAK76473.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY150427; AAN12969.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR E85040; E85040.
RefSeq NP_567255.1; -.
UniGene At.24291
3D structure databases
SMR Q9ZR12; 6-571.
ModBase Q9ZR12.
Protein-protein interaction databases
IntAct Q9ZR12; 6.
Organism-specific databases
TAIR At4g03190; -.
Ontologies
GO
GO:0043224; Cellular component: nuclear SCF ubiquitin ligase complex (inferred from physical interaction from TAIR).
GO:0010011; Molecular function: auxin binding (inferred from genetic interaction from TAIR).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0009734; Biological process: auxin mediated signaling pathway (inferred from electronic annotation from UniProtKB-KW).
GO:0006952; Biological process: defense response (inferred from electronic annotation from UniProtKB-KW).
GO:0048589; Biological process: developmental growth (inferred from genetic interaction from TAIR).
GO:0045014; Biological process: negative regulation of transcription by glucose (traceable author statement from TAIR).
GO:0010152; Biological process: pollen maturation (inferred from genetic interaction from TAIR).
GO:0002237; Biological process: response to molecule of bacterial origin (inferred from expression pattern from TAIR).
GO:0048443; Biological process: stamen development (inferred from genetic interaction from TAIR).
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.
SMART SM00256; FBOX; 1.
SMART graphical view of domain structure.
PROSITE PS50181; FBOX; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).
Proteomics databases
PRIDE Q9ZR12; -.
Genome annotation databases
GeneID 828045; -.
GenomeReviews CT486007_GR; AT4G03190.
KEGG ath:AT4G03190; -.
NMPDR fig|3702.1.peg.18146; -.
Other
ProtoNet Q9ZR12.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Auxin signaling pathway; Complete proteome; Developmental protein; Leucine-rich repeat; Nucleus; Plant defense; Repeat; Ubl conjugation pathway.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   585  585     GRR1-like protein 1. PRO_0000272265
DOMAIN   1    48  48     F-box. 
REPEAT   92   109  18     LRR 1. 
REPEAT   110   142  33     LRR 2. 
REPEAT   143   170  28     LRR 3. 
REPEAT   171   197  27     LRR 4. 
REPEAT   198   224  27     LRR 5. 
REPEAT   225   251  27     LRR 6. 
REPEAT   252   275  24     LRR 7. 
REPEAT   276   300  25     LRR 8. 
REPEAT   301   324  24     LRR 9. 
REPEAT   325   358  34     LRR 10. 
REPEAT   359   383  25     LRR 11. 
REPEAT   384   418  35     LRR 12. 
REPEAT   419   445  27     LRR 13. 
REPEAT   446   467  22     LRR 14. 
REPEAT   468   489  22     LRR 15. 
REPEAT   490   513  24     LRR 16. 
CONFLICT   111   111        M -> I (in Ref. 3; AAK76473). 
CONFLICT   149   149        A -> S (in Ref. 1; AAK01147). 
CONFLICT   293   293        S -> T (in Ref. 1; AAK01147). 
CONFLICT   377   377        C -> S (in Ref. 3; AAK76473). 
CONFLICT   584   584        I -> M (in Ref. 3; AAK76473). 
Sequence information
Length: 585 AA [This is the length of the unprocessed precursor] Molecular weight: 65648 Da [This is the MW of the unprocessed precursor] CRC64: D39D627C82864D83 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGLRFPPKVL EHILSFIDSN EDRNSVSLVC KSWFETERKT RKRVFVGNCY AVSPAAVTRR 

        70         80         90        100        110        120 
FPEMRSLTLK GKPHFADYNL VPDGWGGYAW PWIEAMAAKS SSLEEIRMKR MVVTDECLEK 

       130        140        150        160        170        180 
IAASFKDFKV LVLTSCEGFS TDGIAAIAAT CRNLRVLELR ECIVEDLGGD WLSYFPESST 

       190        200        210        220        230        240 
SLVSLDFSCL DSEVKISDLE RLVSRSPNLK SLKLNPAVTL DGLVSLLRCA PQLTELGTGS 

       250        260        270        280        290        300 
FAAQLKPEAF SKLSEAFSNC KQLQSLSGLW DVLPEYLPAL YSVCPGLTSL NLSYATVRMP 

       310        320        330        340        350        360 
DLVELLRRCS KLQKLWVMDL IEDKGLEAVA SYCKELRELR VFPSEPDLDA TNIPLTEQGL 

       370        380        390        400        410        420 
VFVSKGCRKL ESVLYFCVQF TNAALFTIAR KRPNLKCFRL CVIEPFAPDY KTNEPLDKGF 

       430        440        450        460        470        480 
KAIAEGCRDL RRLSVSGLLS DKAFKYIGKH AKKVRMLSIA FAGDSDLMLH HLLSGCESLK 

       490        500        510        520        530        540 
KLEIRDCPFG DTALLEHAAK LETMRSLWMS SCFVSFGACK LLSQKMPRLN VEVIDEHPPE 

       550        560        570        580 
SRPESSPVER IYIYRTVAGP RMDTPEFVWT IHKNPENGVS HLAIK 

Q9ZR12 in FASTA format

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