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O22476 (BRI1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 128. 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
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:
Protein BRASSINOSTEROID INSENSITIVE 1
Short name=AtBRI1
EC=2.7.10.1
EC=2.7.11.1
Alternative name(s):
Brassinosteroid LRR receptor kinase
Gene names
Name:BRI1
Ordered Locus Names:At4g39400
ORF Names:F23K16.30
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 length1196 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor with a dual specificity kinase activity acting on both serine/threonine- and tyrosine-containing substrates. Regulates, in response to brassinosteroid binding, a signaling cascade involved in plant development, including expression of light- and stress-regulated genes, promotion of cell elongation, normal leaf and chloroplast senescence, and flowering. Binds brassinolide, and less effectively castasterone, but not 2,3,22,23-O-tetramethylbrassinolide or ecdysone. May be involved in a feedback regulation of brassinosteroid biosynthesis. Phosphorylates BRI1-associated receptor kinase 1 (BAK1), Transthyretin-Like protein (TTL) and SERK1 on 'Ser-299' and 'Thr-462' in vitro. May have a guanylyl cyclase activity. Ref.2 Ref.3 Ref.16 Ref.19 Ref.22 Ref.24

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Enzyme regulation

Activated by Ser and Thr phosphorylation.

Subunit structure

Monomer or homodimer in the plasma membrane. Heterodimer with BAK1 in the endosomes. Interacts with SERK1 and TTL in a kinase-dependent manner. Component of the SERK1 signaling complex, composed of KAPP, CDC48A, GRF6 or GRF7, SERK1, SERK2, SERK3/BAK1 and BRI1. Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.20 Ref.22

Subcellular location

Cell membrane; Single-pass type I membrane protein. Endosome membrane; Single-pass type I membrane protein Ref.3 Ref.9 Ref.10 Ref.12 Ref.17 Ref.18.

Tissue specificity

Expressed ubiquitously. Ref.1 Ref.3

Developmental stage

Expressed constitutively in either dark- or light-grown seedlings.

Domain

Contains one leucine-zipper motif and two pairs of conservatively spaced Cys (Cys pair 1 and 2) involved in forming heterodimers. Ref.19

A 70 amino acid island between the 20th and the 21th LRR is essential for the binding of brassinosteroids. Ref.19

The JM domain (815-883) is a positive regulator of kinase activity and is required for Tyr phosphorylation. Ref.19

A guanylyl cyclase domain (1021-1134) having an in vitro activity is included in the C-terminal kinase domain. Ref.19

Post-translational modification

Autophosphorylated on Tyr-831, Tyr-956 and maybe Tyr-1072. Phosphorylated on at least 12 sites, with a preference for Ser residues. Transphosphorylated on Ser-887 by SERK1 and on Ser-838, Thr-846, Ser-858 and Ser-1166 by BAK1. Phosphorylation on Ser-1166 enhances the kinase activity. Ref.7 Ref.9 Ref.10 Ref.11 Ref.14 Ref.22 Ref.23 Ref.24

Glycosylated. Ref.18

Disruption phenotype

Dwarf phenotype and aberrant leaf shape. Ref.2

Miscellaneous

Binding of brassinosteroid induces intramolecular autophosphorylation of BRI1. Interaction with BAK1 activates both receptor kinases and the full activation of either receptor kinase requires transphosphorylation by their partners. Optimum in vitro phosphorylation of the substrate requires Arg or Lys residues at P-3, P-4, and P+5 (relative to the phosphorylated amino acid at P=0). Homodimerizes in the absence of ligand and binds brassinosteroid in the absence of its coreceptor BAK1.

The bri1-9 mutation produces a fully active protein with a subtle conformational change that is recognized for reglucosylation by UGGT, resulting in its endoplasmic reticulum retention via Glc1Man9GlcNAc(2)-calreticulin/calnexin interaction (Ref.18).

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.

Contains 25 LRR (leucine-rich) repeats.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentCell membrane
Endosome
Membrane
   DomainLeucine-rich repeat
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Lipid-binding
Nucleotide-binding
Steroid-binding
   Molecular functionKinase
Receptor
Serine/threonine-protein kinase
Transferase
Tyrosine-protein kinase
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbrassinosteroid homeostasis

Inferred from expression pattern PubMed 15908602. Source: TAIR

brassinosteroid mediated signaling pathway

Inferred from mutant phenotype Ref.24. Source: TAIR

detection of brassinosteroid stimulus

Inferred from mutant phenotype Ref.1. Source: TAIR

leaf development

Inferred from mutant phenotype PubMed 20460583. Source: TAIR

microtubule bundle formation

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

negative regulation of cell death

Inferred from mutant phenotype PubMed 17600708. Source: UniProtKB

pollen exine formation

Inferred from mutant phenotype PubMed 20231470. Source: TAIR

positive regulation of flower development

Inferred from genetic interaction PubMed 17611230. Source: TAIR

regulation of seedling development

Inferred from mutant phenotype PubMed 17600708. Source: UniProtKB

response to UV-B

Inferred from genetic interaction PubMed 15474373. Source: TAIR

skotomorphogenesis

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

tapetal cell differentiation

Inferred from mutant phenotype PubMed 20231470. Source: TAIR

   Cellular_componentendosome

Inferred from direct assay Ref.12. Source: TAIR

endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from direct assay Ref.3PubMed 16618929PubMed 19004783PubMed 22923678. Source: TAIR

protein complex

Inferred from physical interaction Ref.15. Source: TAIR

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

growth hormone receptor activity

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

protein homodimerization activity

Inferred from direct assay PubMed 15650741. Source: TAIR

protein serine/threonine kinase activity

Inferred from direct assay PubMed 15935775. Source: TAIR

steroid binding

Inferred from direct assay PubMed 21666665. Source: TAIR

transmembrane receptor protein tyrosine kinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 11961173Protein BRASSINOSTEROID INSENSITIVE 1
PRO_0000024305

Regions

Transmembrane793 – 81321Helical; Potential
Repeat100 – 12223LRR 1
Repeat123 – 14523LRR 2
Repeat149 – 17022LRR 3
Repeat174 – 19522LRR 4
Repeat201 – 22222LRR 5
Repeat223 – 24523LRR 6
Repeat246 – 26823LRR 7
Repeat270 – 29122LRR 8
Repeat292 – 31423LRR 9
Repeat317 – 33923LRR 10
Repeat341 – 36323LRR 11
Repeat366 – 38924LRR 12
Repeat391 – 41121LRR 13
Repeat417 – 44024LRR 14
Repeat441 – 46323LRR 15
Repeat465 – 48723LRR 16
Repeat489 – 51224LRR 17
Repeat513 – 53523LRR 18
Repeat537 – 56024LRR 19
Repeat561 – 58323LRR 20
Repeat655 – 67723LRR 21
Repeat679 – 70123LRR 22
Repeat703 – 72523LRR 23
Repeat727 – 74923LRR 24
Domain883 – 1158276Protein kinase
Repeat1175 – 119521LRR 25
Nucleotide binding889 – 8979ATP By similarity
Motif62 – 698Cys pair 1
Motif763 – 7708Cys pair 2

Sites

Active site10091Proton acceptor By similarity
Binding site9111ATP By similarity

Amino acid modifications

Modified residue8311Phosphotyrosine Ref.24
Modified residue8381Phosphoserine Ref.22
Modified residue8421Phosphothreonine
Modified residue8461Phosphothreonine Ref.22
Modified residue8511Phosphothreonine Potential
Modified residue8581Phosphoserine Ref.22
Modified residue8721Phosphothreonine
Modified residue8801Phosphothreonine
Modified residue8871Phosphoserine Ref.23
Modified residue8911Phosphoserine Potential
Modified residue9561Phosphotyrosine Ref.24
Modified residue9811Phosphoserine Potential
Modified residue9821Phosphothreonine
Modified residue10351Phosphoserine Potential
Modified residue10391Phosphothreonine Potential
Modified residue10421Phosphoserine Potential
Modified residue10441Phosphoserine Potential
Modified residue10451Phosphothreonine Potential
Modified residue10491Phosphothreonine Potential
Modified residue10601Phosphoserine Potential
Modified residue10721Phosphotyrosine Potential
Modified residue11661Phosphoserine Ref.22
Modified residue11681Phosphoserine
Modified residue11691Phosphothreonine Potential
Modified residue11721Phosphoserine Potential
Modified residue11791Phosphoserine Potential
Modified residue11801Phosphothreonine Ref.22
Modified residue11871Phosphoserine Potential
Glycosylation1121N-linked (GlcNAc...) Potential
Glycosylation1541N-linked (GlcNAc...) Potential
Glycosylation2331N-linked (GlcNAc...) Potential
Glycosylation2751N-linked (GlcNAc...) Potential
Glycosylation3511N-linked (GlcNAc...) Potential
Glycosylation3871N-linked (GlcNAc...) Potential
Glycosylation4011N-linked (GlcNAc...) Potential
Glycosylation4381N-linked (GlcNAc...) Potential
Glycosylation5101N-linked (GlcNAc...) Potential
Glycosylation5451N-linked (GlcNAc...) Potential
Glycosylation5731N-linked (GlcNAc...) Potential
Glycosylation6361N-linked (GlcNAc...) Potential
Glycosylation6531N-linked (GlcNAc...) Potential
Glycosylation7371N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis691C → Y in bri1-5; brassinosteroid-insensitive semi-dwarf mutant.
Mutagenesis6111G → E in bri1-113; brassinosteroid-insensitive semi-dwarf mutant.
Mutagenesis6131G → S in bri1-7; brassinosteroid-insensitive semi-dwarf mutant.
Mutagenesis6441G → D in bri1-6; brassinosteroid-insensitive semi-dwarf mutant.
Mutagenesis6621S → F in bri1-9; brassinosteroid-insensitive semi-dwarf mutant.
Mutagenesis7501T → I in bri1-102; brassinosteroid-insensitive dwarf mutant.
Mutagenesis8311Y → D or E: No effect on kinase activity, flowering time or leaf size, but altered leaf shape. Ref.24
Mutagenesis8311Y → F: No effect on kinase activity but altered flowering time and leaf size and shape. Ref.24
Mutagenesis8381S → A: Decreases peptide phosphorylation, but no effect on autophosphorylation. Ref.14 Ref.22
Mutagenesis8381S → D: Increased kinase activity; when associated with D-842; D-846 and D-858. Ref.14 Ref.22
Mutagenesis8421T → A: Decreases peptide phosphorylation, but no effect on autophosphorylation. Ref.14 Ref.22
Mutagenesis8421T → D: Increased kinase activity; when associated with D-838; D-846 and D-858. Ref.14 Ref.22
Mutagenesis8461T → A: Decreases peptide phosphorylation, but no effect on autophosphorylation. Ref.14 Ref.22
Mutagenesis8461T → D: Increased kinase activity; when associated with D-838; D-842 and D-858. Ref.14 Ref.22
Mutagenesis8581S → A: Decreases peptide phosphorylation, but no effect on autophosphorylation. Ref.14 Ref.22
Mutagenesis8581S → D: Increased kinase activity; when associated with D-838; D-842 and D-846. Ref.14 Ref.22
Mutagenesis8721T → A: 10-fold increase in peptide phosphorylation. Ref.14
Mutagenesis8981Y → F: No effect on kinase activity. Ref.24
Mutagenesis9091A → T in bri1-1; brassinosteroid-insensitive dwarf mutant.
Mutagenesis9111K → E: Loss of kinase activity; dwarf mutant. Ref.7
Mutagenesis9451Y → F: No effect on kinase activity. Ref.24
Mutagenesis9561Y → F: Loss of kinase activity. Ref.24
Mutagenesis9611Y → F: No effect on kinase activity. Ref.24
Mutagenesis9831R → N in bri1-8; brassinosteroid-insensitive dwarf mutant.
Mutagenesis9831R → Q in bri1-108; brassinosteroid-insensitive dwarf mutant.
Mutagenesis9891G → I in bri1-301; impaired kinase activity and loss of autophosphorylation. Ref.21
Mutagenesis10311A → W in bri1-104; brassinosteroid-insensitive dwarf mutant, but no effect on interaction with TTL.
Mutagenesis10391T → A: Abolishes peptide phosphorylation, and to a lower level autophosphorylation. Ref.14
Mutagenesis10421S → A: Abolishes peptide phosphorylation, and to a lower level autophosphorylation.
Mutagenesis10441S → A: Abolishes peptide phosphorylation, and autophosphorylation. Ref.14
Mutagenesis10451T → A: Abolishes peptide phosphorylation, and autophosphorylation. Ref.14
Mutagenesis10481G → D in bri1-115; brassinosteroid-insensitive dwarf mutant and no interaction with TTL.
Mutagenesis10491T → A: Abolishes peptide phosphorylation, and autophosphorylation. Ref.14 Ref.22
Mutagenesis10491T → D: Loss of kinase activity and brassinosteroid signaling. Ref.14 Ref.22
Mutagenesis10521Y → F: Loss of kinase activity. Ref.24
Mutagenesis10571Y → F: Loss of kinase activity. Ref.24
Mutagenesis10581Y → F: No effect on kinase activity. Ref.24
Mutagenesis10701Y → F: No effect on kinase activity. Ref.24
Mutagenesis10721Y → F: Loss of kinase activity. Ref.24
Mutagenesis10781E → K in bri1-101; brassinosteroid-insensitive dwarf mutant and no interaction with TTL.
Mutagenesis11391D → N in bri1-117; brassinosteroid-insensitive dwarf mutant.
Mutagenesis11661S → D: Increased kinase activity; when associated with D-1168; D-1172; D-1179 and D-1180. Ref.22
Mutagenesis11681S → A: Decreases peptide phosphorylation, but no effect on autophosphorylation. Ref.14 Ref.22
Mutagenesis11681S → D: Increased kinase activity; when associated with D-1166; D-1172; D-1179 and D-1180. Ref.14 Ref.22
Mutagenesis11721S → A: Decreases peptide phosphorylation, but no effect on autophosphorylation. Ref.14 Ref.22
Mutagenesis11721S → D: Increased kinase activity; when associated with D-1166; D-1168; D-1179 and D-1180. Ref.14 Ref.22
Mutagenesis1179 – 11802ST → A: Decreases peptide phosphorylation, but no effect on autophosphorylation. Ref.22
Mutagenesis11791S → D: Increased kinase activity; when associated with D-1166; D-1168; D-1172 and D-1180. Ref.22
Mutagenesis11801T → D: Increased kinase activity; when associated with D-1166; D-1168; D-1172 and D-1179. Ref.22
Mutagenesis11871S → A: Decreases peptide phosphorylation, but no effect on autophosphorylation. Ref.14

Secondary structure

1 ........................................................................................................................................................................ 1196
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O22476 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: C7FBA1C21294E600

FASTA1,196130,543
        10         20         30         40         50         60 
MKTFSSFFLS VTTLFFFSFF SLSFQASPSQ SLYREIHQLI SFKDVLPDKN LLPDWSSNKN 

        70         80         90        100        110        120 
PCTFDGVTCR DDKVTSIDLS SKPLNVGFSA VSSSLLSLTG LESLFLSNSH INGSVSGFKC 

       130        140        150        160        170        180 
SASLTSLDLS RNSLSGPVTT LTSLGSCSGL KFLNVSSNTL DFPGKVSGGL KLNSLEVLDL 

       190        200        210        220        230        240 
SANSISGANV VGWVLSDGCG ELKHLAISGN KISGDVDVSR CVNLEFLDVS SNNFSTGIPF 

       250        260        270        280        290        300 
LGDCSALQHL DISGNKLSGD FSRAISTCTE LKLLNISSNQ FVGPIPPLPL KSLQYLSLAE 

       310        320        330        340        350        360 
NKFTGEIPDF LSGACDTLTG LDLSGNHFYG AVPPFFGSCS LLESLALSSN NFSGELPMDT 

       370        380        390        400        410        420 
LLKMRGLKVL DLSFNEFSGE LPESLTNLSA SLLTLDLSSN NFSGPILPNL CQNPKNTLQE 

       430        440        450        460        470        480 
LYLQNNGFTG KIPPTLSNCS ELVSLHLSFN YLSGTIPSSL GSLSKLRDLK LWLNMLEGEI 

       490        500        510        520        530        540 
PQELMYVKTL ETLILDFNDL TGEIPSGLSN CTNLNWISLS NNRLTGEIPK WIGRLENLAI 

       550        560        570        580        590        600 
LKLSNNSFSG NIPAELGDCR SLIWLDLNTN LFNGTIPAAM FKQSGKIAAN FIAGKRYVYI 

       610        620        630        640        650        660 
KNDGMKKECH GAGNLLEFQG IRSEQLNRLS TRNPCNITSR VYGGHTSPTF DNNGSMMFLD 

       670        680        690        700        710        720 
MSYNMLSGYI PKEIGSMPYL FILNLGHNDI SGSIPDEVGD LRGLNILDLS SNKLDGRIPQ 

       730        740        750        760        770        780 
AMSALTMLTE IDLSNNNLSG PIPEMGQFET FPPAKFLNNP GLCGYPLPRC DPSNADGYAH 

       790        800        810        820        830        840 
HQRSHGRRPA SLAGSVAMGL LFSFVCIFGL ILVGREMRKR RRKKEAELEM YAEGHGNSGD 

       850        860        870        880        890        900 
RTANNTNWKL TGVKEALSIN LAAFEKPLRK LTFADLLQAT NGFHNDSLIG SGGFGDVYKA 

       910        920        930        940        950        960 
ILKDGSAVAI KKLIHVSGQG DREFMAEMET IGKIKHRNLV PLLGYCKVGD ERLLVYEFMK 

       970        980        990       1000       1010       1020 
YGSLEDVLHD PKKAGVKLNW STRRKIAIGS ARGLAFLHHN CSPHIIHRDM KSSNVLLDEN 

      1030       1040       1050       1060       1070       1080 
LEARVSDFGM ARLMSAMDTH LSVSTLAGTP GYVPPEYYQS FRCSTKGDVY SYGVVLLELL 

      1090       1100       1110       1120       1130       1140 
TGKRPTDSPD FGDNNLVGWV KQHAKLRISD VFDPELMKED PALEIELLQH LKVAVACLDD 

      1150       1160       1170       1180       1190 
RAWRRPTMVQ VMAMFKEIQA GSGIDSQSTI RSIEDGGFST IEMVDMSIKE VPEGKL

« Hide

References

« Hide 'large scale' references
[1]"A putative leucine-rich repeat receptor kinase involved in brassinosteroid signal transduction."
Li J., Chory J.
Cell 90:929-938(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, MUTANTS BRI1-101; BRI1-104; BRI1-113 AND BRI1-115.
Strain: cv. Columbia.
[2]"Brassinosteroid-insensitive dwarf mutants of Arabidopsis accumulate brassinosteroids."
Noguchi T., Fujioka S., Choe S., Takatsuto S., Yoshida S., Yuan H., Feldmann K.A., Tax F.E.
Plant Physiol. 121:743-752(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, MUTANTS BRI1-5/DWF2-W41; BRI1-6/BRI1-119/DWF2-399; BRI1-7/DWF2-WM3-2; BRI1-8/DWF2-WM6-2 AND BRI1-9/DWF2-WMB19, DISRUPTION PHENOTYPE.
Strain: cv. En-2 and cv. Wassilewskija-2.
[3]"BRASSINOSTEROID-INSENSITIVE-1 is a ubiquitously expressed leucine-rich repeat receptor serine/threonine kinase."
Friedrichsen D.M., Joazeiro C.A.P., Li J., Hunter T., Chory J.
Plant Physiol. 123:1247-1256(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTANTS BRI1-1; BRI1-108; BRI1-117 AND BRI1-102.
Strain: cv. Columbia.
[4]"Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-like protein kinase genes in Arabidopsis thaliana."
Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.
BMC Genomics 11:19-19(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
[5]"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.
[6]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[7]"Recombinant BRASSINOSTEROID INSENSITIVE 1 receptor-like kinase autophosphorylates on serine and threonine residues and phosphorylates a conserved peptide motif in vitro."
Oh M.-H., Ray W.K., Huber S.C., Asara J.M., Gage D.A., Clouse S.D.
Plant Physiol. 124:751-766(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, MUTAGENESIS OF LYS-911.
[8]"Perception of brassinosteroids by the extracellular domain of the receptor kinase BRI1."
He Z., Wang Z.-Y., Li J., Zhu Q., Lamb C., Ronald P., Chory J.
Science 288:2360-2363(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: STEROID-BINDING.
[9]"BRI1 is a critical component of a plasma-membrane receptor for plant steroids."
Wang Z.-Y., Seto H., Fujioka S., Yoshida S., Chory J.
Nature 410:380-383(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, STEROID-BINDING, AUTOPHOSPHORYLATION.
[10]"BRI1/BAK1, a receptor kinase pair mediating brassinosteroid signaling."
Nam K.H., Li J.
Cell 110:203-212(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH BAK1.
[11]"BAK1, an Arabidopsis LRR receptor-like protein kinase, interacts with BRI1 and modulates brassinosteroid signaling."
Li J., Wen J., Lease K.A., Doke J.T., Tax F.E., Walker J.C.
Cell 110:213-222(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, INTERACTION WITH BAK1.
[12]"Heterodimerization and endocytosis of Arabidopsis brassinosteroid receptors BRI1 and AtSERK3 (BAK1)."
Russinova E., Borst J.-W., Kwaaitaal M., Cano-Delgado A., Yin Y., Chory J., de Vries S.C.
Plant Cell 16:3216-3229(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH BAK1.
[13]"The Arabidopsis transthyretin-like protein is a potential substrate of BRASSINOSTEROID-INSENSITIVE 1."
Nam K.H., Li J.
Plant Cell 16:2406-2417(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TTL.
[14]"Identification and functional analysis of in vivo phosphorylation sites of the Arabidopsis BRASSINOSTEROID-INSENSITIVE1 receptor kinase."
Wang X., Goshe M.B., Soderblom E.J., Phinney B.S., Kuchar J.A., Li J., Asami T., Yoshida S., Huber S.C., Clouse S.D.
Plant Cell 17:1685-1703(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, INTERACTION WITH BAK1, MUTAGENESIS OF SER-838; THR-842; THR-846; SER-858; THR-872; THR-1039; SER-1044; THR-1045; THR-1049; SER-1168; SER-1172; 1179-SER-THR-1180 AND SER-1187.
[15]"The Arabidopsis SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE1 protein complex includes BRASSINOSTEROID-INSENSITIVE1."
Karlova R., Boeren S., Russinova E., Aker J., Vervoort J., de Vries S.C.
Plant Cell 18:626-638(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SERK1.
[16]"Brassinosteroid signaling: a paradigm for steroid hormone signaling from the cell surface."
Belkhadir Y., Chory J.
Science 314:1410-1411(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"Endosomal signaling of plant steroid receptor kinase BRI1."
Geldner N., Hyman D.L., Wang X., Schumacher K., Chory J.
Genes Dev. 21:1598-1602(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[18]"Allele-specific suppression of a defective brassinosteroid receptor reveals a physiological role of UGGT in ER quality control."
Jin H., Yan Z., Nam K.H., Li J.
Mol. Cell 26:821-830(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION, SUBCELLULAR LOCATION.
[19]"The Arabidopsis thaliana brassinosteroid receptor (AtBRI1) contains a domain that functions as a guanylyl cyclase in vitro."
Kwezi L., Meier S., Mungur L., Ruzvidzo O., Irving H., Gehring C.
PLoS ONE 2:E449-E449(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DOMAIN.
[20]"Fluorescence fluctuation analysis of Arabidopsis thaliana somatic embryogenesis receptor-like kinase and brassinosteroid insensitive 1 receptor oligomerization."
Hink M.A., Shah K., Russinova E., de Vries S.C., Visser A.J.
Biophys. J. 94:1052-1062(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[21]"Is kinase activity essential for biological functions of BRI1?"
Xu W., Huang J., Li B., Li J., Wang Y.
Cell Res. 18:472-478(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLY-989.
[22]"Sequential transphosphorylation of the BRI1/BAK1 receptor kinase complex impacts early events in brassinosteroid signaling."
Wang X., Kota U., He K., Blackburn K., Li J., Goshe M.B., Huber S.C., Clouse S.D.
Dev. Cell 15:220-235(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT SER-838; THR-846; SER-858; SER-1166 AND THR-1180, INTERACTION WITH BAK1, MUTAGENESIS OF SER-838; THR-842; THR-846; SER-858; THR-1049; SER-1166; SER-1168; SER-1172; SER-1179 AND THR-1180.
[23]"Identification of in vitro phosphorylation sites in the Arabidopsis thaliana somatic embryogenesis receptor-like kinases."
Karlova R., Boeren S., van Dongen W., Kwaaitaal M., Aker J., Vervoort J., de Vries S.C.
Proteomics 9:368-379(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-887, PHOSPHORYLATION OF SERK1.
[24]"Tyrosine phosphorylation of the BRI1 receptor kinase emerges as a component of brassinosteroid signaling in Arabidopsis."
Oh M.-H., Wang X., Kota U., Goshe M.B., Clouse S.D., Huber S.C.
Proc. Natl. Acad. Sci. U.S.A. 106:658-663(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF TYR-831; TYR-898; TYR-945; TYR-956; TYR-961; TYR-1052; TYR-1057; TYR-1058; TYR-1070 AND TYR-1072, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT TYR-831 AND TYR-956.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF017056 Genomic DNA. Translation: AAC49810.1.
FJ708766 mRNA. Translation: ACN59359.1.
AL078620 Genomic DNA. Translation: CAB44675.1.
AL161595 Genomic DNA. Translation: CAB80603.1.
CP002687 Genomic DNA. Translation: AEE87069.1.
IPIIPI00528172.
PIRT09356.
RefSeqNP_195650.1. NM_120100.2.
UniGeneAt.27898.
At.69020.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3RGXX-ray2.47A23-785[»]
3RGZX-ray2.28A23-785[»]
3RIZX-ray2.52A29-788[»]
3RJ0X-ray2.54A29-788[»]
ProteinModelPortalO22476.
SMRO22476. Positions 30-774, 862-1158.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-45997N.
IntActO22476. 7 interactions.

Proteomic databases

PaxDbO22476.
PRIDEO22476.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G39400.1; AT4G39400.1; AT4G39400.
GeneID830095.
KEGGath:AT4G39400.

Organism-specific databases

GeneFarm612. 54.
TAIRAt4g39400.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000116551.
InParanoidO22476.
KOK13415.
OMAMSAMDTH.
PhylomeDBO22476.
ProtClustDBCLSN2682665.

Gene expression databases

GenevestigatorO22476.
GermOnlineAT4G39400. Arabidopsis thaliana.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
InterProIPR013320. ConA-like_subgrp.
IPR011009. Kinase-like_dom.
IPR001611. Leu-rich_rpt.
IPR013210. LRR-contain_N2.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00560. LRR_1. 2 hits.
PF08263. LRRNT_2. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMSSF56112. Kinase_like. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO22476.

Entry information

Entry nameBRI1_ARATH
AccessionPrimary (citable) accession number: O22476
Secondary accession number(s): C0LGS4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: January 1, 1998
Last modified: May 1, 2013
This is version 128 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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