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Q9ZR12 (GRH1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 87. Feed History...

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

Names and origin

Protein namesRecommended name:
GRR1-like protein 1
Alternative name(s):
Protein AUXIN SIGNALING F-BOX 1
Gene names
Name:GRH1
Synonyms:AFB1, FBL18, GER1, LRF1
Ordered Locus Names:At4g03190
ORF Names:F4C21.11
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length585 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Auxin receptor that mediates Aux/IAA proteins proteasomal degradation and auxin-regulated transcription. Involved in embryogenesis regulation by auxin. Confers sensitivity to the virulent bacterial pathogen P.syringae. Mediates glucose repression in yeast. Ref.1 Ref.7 Ref.8 Ref.9

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Part of a SCF (SKP1-cullin-F-box) protein ligase complex. Interacts with CUL1, SKP1A/ASK1 and SKP1B/ASK2. Interacts with Aux/IAA proteins (IAA7 and IAA12) in an auxin-dependent manner. Ref.1 Ref.5 Ref.7

Subcellular location

Nucleus Ref.7.

Tissue specificity

Ubiquitous. Ref.7

Induction

Partially repressed by miR393a (microRNA) in response to flg-22 (flagellin-derived peptide 22). Ref.9

Domain

The F-box is necessary for the interaction with SKP1 By similarity.

Sequence similarities

Contains 1 F-box domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SKP1AQ392553EBI-617479,EBI-532357

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 585585GRR1-like protein 1
PRO_0000272265

Regions

Domain1 – 4848F-box
Region77 – 782Interaction with auxin-responsive proteins By similarity
Region109 – 1102Myo-inositol hexakisphosphate binding By similarity
Region343 – 3486Interaction with auxin-responsive proteins By similarity
Region397 – 3993Myo-inositol hexakisphosphate binding By similarity
Region401 – 4055Interaction with auxin-responsive proteins By similarity
Region460 – 4612Interaction with auxin-responsive proteins By similarity
Region480 – 4812Myo-inositol hexakisphosphate binding By similarity

Sites

Binding site701Myo-inositol hexakisphosphate By similarity
Binding site3401Myo-inositol hexakisphosphate By similarity
Binding site4321Myo-inositol hexakisphosphate By similarity
Binding site5051Myo-inositol hexakisphosphate By similarity
Site1351Interaction with auxin-responsive proteins By similarity
Site1611Interaction with auxin-responsive proteins By similarity
Site3761Interaction with auxin-responsive proteins By similarity
Site4851Interaction with auxin-responsive proteins By similarity

Experimental info

Sequence conflict1111M → I in AAK76473. Ref.4
Sequence conflict1491A → S in AAK01147. Ref.1
Sequence conflict2931S → T in AAK01147. Ref.1
Sequence conflict3771C → S in AAK76473. Ref.4
Sequence conflict5841I → M in AAK76473. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9ZR12 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: D39D627C82864D83

FASTA58565,648
        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 

« Hide

References

« Hide 'large scale' references
[1]"Cloning by pathway activation in yeast: identification of an Arabidopsis thaliana F-box protein that can turn on glucose repression."
Thelander M., Fredriksson D., Schouten J., Hoge J.H.C., Ronne H.
Plant Mol. Biol. 49:69-79(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH SKP1A/ASK1 AND SKP1B/ASK2, LEUCINE-RICH REPEATS.
[2]"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.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
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. expand/collapse author list , 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.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Identification of an SCF ubiquitin-ligase complex required for auxin response in Arabidopsis thaliana."
Gray W.M., del Pozo J.C., Walker L., Hobbie L., Risseeuw E., Banks T., Crosby W.L., Yang M., Ma H., Estelle M.
Genes Dev. 13:1678-1691(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SKP1A/ASK1 AND SKP1B/ASK2.
[6]"F-box proteins in Arabidopsis."
Xiao W., Jang J.-C.
Trends Plant Sci. 5:454-457(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
[7]"Plant development is regulated by a family of auxin receptor F box proteins."
Dharmasiri N., Dharmasiri S., Weijers D., Lechner E., Yamada M., Hobbie L., Ehrismann J.S., Juergens G., Estelle M.
Dev. Cell 9:109-119(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH CUL1; IAA7; IAA12 AND SKP1A/ASK1.
[8]"The F-box protein TIR1 is an auxin receptor."
Dharmasiri N., Dharmasiri S., Estelle M.
Nature 435:441-445(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"A plant miRNA contributes to antibacterial resistance by repressing auxin signaling."
Navarro L., Dunoyer P., Jay F., Arnold B., Dharmasiri N., Estelle M., Voinnet O., Jones J.D.G.
Science 312:436-439(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.

Web resources

PlantsUBQ

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF291816 mRNA. Translation: AAK01147.1.
AC005275 Genomic DNA. Translation: AAD14447.1.
AL161496 Genomic DNA. Translation: CAB77804.1.
CP002687 Genomic DNA. Translation: AEE82287.1.
AY045799 mRNA. Translation: AAK76473.1.
AY150427 mRNA. Translation: AAN12969.1.
PIRE85040.
RefSeqNP_567255.1. NM_116555.3.
UniGeneAt.24291.
At.69891.

3D structure databases

ProteinModelPortalQ9ZR12.
SMRQ9ZR12. Positions 6-571.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid13336. 9 interactions.
DIPDIP-34607N.
IntActQ9ZR12. 6 interactions.

Proteomic databases

PaxDbQ9ZR12.
PRIDEQ9ZR12.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G03190.1; AT4G03190.1; AT4G03190.
GeneID828045.
KEGGath:AT4G03190.

Organism-specific databases

TAIRAT4G03190.

Phylogenomic databases

eggNOGNOG324137.
HOGENOMHOG000239805.
InParanoidQ9ZR12.
OMASWFETER.
PhylomeDBQ9ZR12.
ProtClustDBCLSN2689313.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ9ZR12.
GenevestigatorQ9ZR12.

Family and domain databases

InterProIPR001810. F-box_dom.
[Graphical view]
SMARTSM00256. FBOX. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGRH1_ARATH
AccessionPrimary (citable) accession number: Q9ZR12
Secondary accession number(s): Q94AU0, Q9C5Y7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names