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O22476

- BRI1_ARATH

UniProt

O22476 - BRI1_ARATH

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Protein

Protein BRASSINOSTEROID INSENSITIVE 1

Gene

BRI1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.6 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

Enzyme regulationi

Activated by Ser and Thr phosphorylation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei597 – 5971Brassinolide2 Publications
Binding sitei642 – 6421Brassinolide1 Publication
Binding sitei647 – 6471Brassinolide; via amide nitrogen3 Publications
Binding sitei705 – 7051Brassinolide1 Publication
Binding sitei911 – 9111ATP1 Publication
Active sitei1009 – 10091Proton acceptorPROSITE-ProRule annotation
Binding sitei1027 – 10271ATP1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi889 – 8979ATPPROSITE-ProRule annotation
Nucleotide bindingi957 – 9593ATP1 Publication
Nucleotide bindingi963 – 9664ATP1 Publication
Nucleotide bindingi1009 – 10146ATP1 Publication

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. identical protein binding Source: IntAct
  3. protein heterodimerization activity Source: TAIR
  4. protein homodimerization activity Source: TAIR
  5. protein kinase activity Source: TAIR
  6. protein serine/threonine kinase activity Source: TAIR
  7. steroid binding Source: TAIR
  8. transmembrane receptor protein tyrosine kinase activity Source: UniProtKB-EC

GO - Biological processi

  1. anther wall tapetum cell differentiation Source: TAIR
  2. brassinosteroid homeostasis Source: TAIR
  3. brassinosteroid mediated signaling pathway Source: TAIR
  4. detection of brassinosteroid stimulus Source: TAIR
  5. leaf development Source: TAIR
  6. negative regulation of cell death Source: UniProtKB
  7. pollen exine formation Source: TAIR
  8. positive regulation of flower development Source: TAIR
  9. regulation of seedling development Source: UniProtKB
  10. response to UV-B Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Serine/threonine-protein kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Brassinosteroid signaling pathway

Keywords - Ligandi

ATP-binding, Lipid-binding, Nucleotide-binding, Steroid-binding

Enzyme and pathway databases

BioCyciARA:AT4G39400-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein BRASSINOSTEROID INSENSITIVE 1 (EC:2.7.10.1, EC:2.7.11.1)
Short name:
AtBRI1
Alternative name(s):
Brassinosteroid LRR receptor kinase
Gene namesi
Name:BRI1
Ordered Locus Names:At4g39400
ORF Names:F23K16.30
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G39400.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei793 – 81321HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endosome Source: TAIR
  2. integral component of membrane Source: UniProtKB-KW
  3. plasma membrane Source: TAIR
  4. protein complex Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

Pathology & Biotechi

Disruption phenotypei

Dwarf phenotype and aberrant leaf shape.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi69 – 691C → Y in bri1-5; brassinosteroid-insensitive semi-dwarf mutant.
Mutagenesisi611 – 6111G → E in bri1-113; brassinosteroid-insensitive semi-dwarf mutant.
Mutagenesisi613 – 6131G → S in bri1-7; brassinosteroid-insensitive semi-dwarf mutant.
Mutagenesisi644 – 6441G → D in bri1-6; brassinosteroid-insensitive semi-dwarf mutant.
Mutagenesisi662 – 6621S → F in bri1-9; brassinosteroid-insensitive semi-dwarf mutant.
Mutagenesisi750 – 7501T → I in bri1-102; brassinosteroid-insensitive dwarf mutant.
Mutagenesisi831 – 8311Y → D or E: No effect on kinase activity, flowering time or leaf size, but altered leaf shape. 1 Publication
Mutagenesisi831 – 8311Y → F: No effect on kinase activity but altered flowering time and leaf size and shape. 1 Publication
Mutagenesisi838 – 8381S → A: Decreases peptide phosphorylation, but no effect on autophosphorylation. 2 Publications
Mutagenesisi838 – 8381S → D: Increased kinase activity; when associated with D-842; D-846 and D-858. 2 Publications
Mutagenesisi842 – 8421T → A: Decreases peptide phosphorylation, but no effect on autophosphorylation. 2 Publications
Mutagenesisi842 – 8421T → D: Increased kinase activity; when associated with D-838; D-846 and D-858. 2 Publications
Mutagenesisi846 – 8461T → A: Decreases peptide phosphorylation, but no effect on autophosphorylation. 2 Publications
Mutagenesisi846 – 8461T → D: Increased kinase activity; when associated with D-838; D-842 and D-858. 2 Publications
Mutagenesisi858 – 8581S → A: Decreases peptide phosphorylation, but no effect on autophosphorylation. 2 Publications
Mutagenesisi858 – 8581S → D: Increased kinase activity; when associated with D-838; D-842 and D-846. 2 Publications
Mutagenesisi872 – 8721T → A: 10-fold increase in peptide phosphorylation. 1 Publication
Mutagenesisi898 – 8981Y → F: No effect on kinase activity. 1 Publication
Mutagenesisi909 – 9091A → T in bri1-1; brassinosteroid-insensitive dwarf mutant.
Mutagenesisi911 – 9111K → E: Loss of kinase activity; dwarf mutant. 1 Publication
Mutagenesisi945 – 9451Y → F: No effect on kinase activity. 1 Publication
Mutagenesisi956 – 9561Y → F: Loss of kinase activity. 1 Publication
Mutagenesisi961 – 9611Y → F: No effect on kinase activity. 1 Publication
Mutagenesisi983 – 9831R → N in bri1-8; brassinosteroid-insensitive dwarf mutant.
Mutagenesisi983 – 9831R → Q in bri1-108; brassinosteroid-insensitive dwarf mutant.
Mutagenesisi989 – 9891G → I in bri1-301; impaired kinase activity and loss of autophosphorylation. 1 Publication
Mutagenesisi1031 – 10311A → W in bri1-104; brassinosteroid-insensitive dwarf mutant, but no effect on interaction with TTL.
Mutagenesisi1039 – 10391T → A: Abolishes peptide phosphorylation, and to a lower level autophosphorylation. 1 Publication
Mutagenesisi1042 – 10421S → A: Abolishes peptide phosphorylation, and to a lower level autophosphorylation.
Mutagenesisi1044 – 10441S → A: Abolishes peptide phosphorylation, and autophosphorylation. 1 Publication
Mutagenesisi1045 – 10451T → A: Abolishes peptide phosphorylation, and autophosphorylation. 1 Publication
Mutagenesisi1048 – 10481G → D in bri1-115; brassinosteroid-insensitive dwarf mutant and no interaction with TTL.
Mutagenesisi1049 – 10491T → A: Abolishes peptide phosphorylation, and autophosphorylation. 2 Publications
Mutagenesisi1049 – 10491T → D: Loss of kinase activity and brassinosteroid signaling. 2 Publications
Mutagenesisi1052 – 10521Y → F: Loss of kinase activity. 1 Publication
Mutagenesisi1057 – 10571Y → F: Loss of kinase activity. 1 Publication
Mutagenesisi1058 – 10581Y → F: No effect on kinase activity. 1 Publication
Mutagenesisi1070 – 10701Y → F: No effect on kinase activity. 1 Publication
Mutagenesisi1072 – 10721Y → F: Loss of kinase activity. 1 Publication
Mutagenesisi1078 – 10781E → K in bri1-101; brassinosteroid-insensitive dwarf mutant and no interaction with TTL.
Mutagenesisi1139 – 11391D → N in bri1-117; brassinosteroid-insensitive dwarf mutant.
Mutagenesisi1166 – 11661S → D: Increased kinase activity; when associated with D-1168; D-1172; D-1179 and D-1180. 1 Publication
Mutagenesisi1168 – 11681S → A: Decreases peptide phosphorylation, but no effect on autophosphorylation. 2 Publications
Mutagenesisi1168 – 11681S → D: Increased kinase activity; when associated with D-1166; D-1172; D-1179 and D-1180. 2 Publications
Mutagenesisi1172 – 11721S → A: Decreases peptide phosphorylation, but no effect on autophosphorylation. 2 Publications
Mutagenesisi1172 – 11721S → D: Increased kinase activity; when associated with D-1166; D-1168; D-1179 and D-1180. 2 Publications
Mutagenesisi1179 – 11802ST → A: Decreases peptide phosphorylation, but no effect on autophosphorylation. 1 Publication
Mutagenesisi1179 – 11791S → D: Increased kinase activity; when associated with D-1166; D-1168; D-1172 and D-1180. 1 Publication
Mutagenesisi1180 – 11801T → D: Increased kinase activity; when associated with D-1166; D-1168; D-1172 and D-1179. 1 Publication
Mutagenesisi1187 – 11871S → A: Decreases peptide phosphorylation, but no effect on autophosphorylation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 11961173Protein BRASSINOSTEROID INSENSITIVE 1PRO_0000024305Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi112 – 1121N-linked (GlcNAc...)3 Publications
Glycosylationi154 – 1541N-linked (GlcNAc...)4 Publications
Glycosylationi233 – 2331N-linked (GlcNAc...)3 Publications
Glycosylationi275 – 2751N-linked (GlcNAc...)4 Publications
Glycosylationi351 – 3511N-linked (GlcNAc...)3 Publications
Glycosylationi387 – 3871N-linked (GlcNAc...)Sequence Analysis
Glycosylationi401 – 4011N-linked (GlcNAc...)Sequence Analysis
Glycosylationi438 – 4381N-linked (GlcNAc...)Sequence Analysis
Glycosylationi510 – 5101N-linked (GlcNAc...)1 Publication
Glycosylationi545 – 5451N-linked (GlcNAc...)4 Publications
Glycosylationi573 – 5731N-linked (GlcNAc...)2 Publications
Glycosylationi636 – 6361N-linked (GlcNAc...)Sequence Analysis
Glycosylationi653 – 6531N-linked (GlcNAc...)Sequence Analysis
Glycosylationi737 – 7371N-linked (GlcNAc...)Sequence Analysis
Modified residuei831 – 8311Phosphotyrosine1 Publication
Modified residuei838 – 8381Phosphoserine3 Publications
Modified residuei842 – 8421Phosphothreonine1 Publication
Modified residuei846 – 8461Phosphothreonine2 Publications
Modified residuei851 – 8511PhosphothreonineSequence Analysis
Modified residuei858 – 8581Phosphoserine3 Publications
Modified residuei872 – 8721Phosphothreonine2 Publications
Modified residuei880 – 8801Phosphothreonine1 Publication
Modified residuei887 – 8871Phosphoserine1 Publication
Modified residuei891 – 8911PhosphoserineSequence Analysis
Modified residuei956 – 9561Phosphotyrosine1 Publication
Modified residuei981 – 9811PhosphoserineSequence Analysis
Modified residuei982 – 9821Phosphothreonine1 Publication
Modified residuei1035 – 10351PhosphoserineSequence Analysis
Modified residuei1039 – 10391PhosphothreonineSequence Analysis
Modified residuei1042 – 10421PhosphoserineSequence Analysis
Modified residuei1044 – 10441PhosphoserineSequence Analysis
Modified residuei1045 – 10451PhosphothreonineSequence Analysis
Modified residuei1049 – 10491PhosphothreonineSequence Analysis
Modified residuei1060 – 10601PhosphoserineSequence Analysis
Modified residuei1072 – 10721PhosphotyrosineSequence Analysis
Modified residuei1166 – 11661Phosphoserine1 Publication
Modified residuei1168 – 11681Phosphoserine1 Publication
Modified residuei1169 – 11691PhosphothreonineSequence Analysis
Modified residuei1172 – 11721PhosphoserineSequence Analysis
Modified residuei1179 – 11791PhosphoserineSequence Analysis
Modified residuei1180 – 11801Phosphothreonine1 Publication
Modified residuei1187 – 11871PhosphoserineSequence Analysis

Post-translational modificationi

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.7 Publications
Glycosylated.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiO22476.
PRIDEiO22476.

Expressioni

Tissue specificityi

Expressed ubiquitously.2 Publications

Developmental stagei

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

Gene expression databases

GenevestigatoriO22476.

Interactioni

Subunit structurei

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. Interacts with CDG1 (PubMed:21855796).9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-1797828,EBI-1797828
At4g35230Q944A74EBI-1797828,EBI-1797846
BAK1Q94F625EBI-1797828,EBI-617138
F6N23.9O652802EBI-1797828,EBI-1797930
SERK1Q94AG25EBI-1797828,EBI-1555537
TTLQ9LVM53EBI-1797828,EBI-1803584

Protein-protein interaction databases

BioGridi15375. 18 interactions.
DIPiDIP-45997N.
IntActiO22476. 7 interactions.

Structurei

Secondary structure

1
1196
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi32 – 4312Combined sources
Helixi49 – 513Combined sources
Beta strandi57 – 593Combined sources
Helixi61 – 633Combined sources
Beta strandi67 – 704Combined sources
Beta strandi73 – 786Combined sources
Helixi88 – 947Combined sources
Turni95 – 973Combined sources
Beta strandi103 – 1053Combined sources
Beta strandi111 – 1133Combined sources
Beta strandi126 – 1283Combined sources
Beta strandi131 – 1377Combined sources
Helixi138 – 1469Combined sources
Beta strandi152 – 1543Combined sources
Beta strandi157 – 1615Combined sources
Beta strandi176 – 1794Combined sources
Beta strandi182 – 1843Combined sources
Beta strandi186 – 1883Combined sources
Helixi190 – 1956Combined sources
Beta strandi204 – 2063Combined sources
Beta strandi209 – 2146Combined sources
Beta strandi226 – 2283Combined sources
Beta strandi249 – 2513Combined sources
Helixi261 – 2644Combined sources
Turni265 – 2673Combined sources
Beta strandi273 – 2753Combined sources
Beta strandi282 – 2843Combined sources
Beta strandi295 – 2973Combined sources
Beta strandi300 – 3067Combined sources
Helixi309 – 3146Combined sources
Turni315 – 3173Combined sources
Beta strandi319 – 3224Combined sources
Beta strandi325 – 3306Combined sources
Helixi334 – 3385Combined sources
Beta strandi344 – 3463Combined sources
Beta strandi349 – 3557Combined sources
Helixi358 – 3614Combined sources
Beta strandi369 – 3713Combined sources
Beta strandi374 – 3796Combined sources
Helixi385 – 3884Combined sources
Turni389 – 3913Combined sources
Beta strandi393 – 3964Combined sources
Beta strandi399 – 4057Combined sources
Turni408 – 4114Combined sources
Beta strandi413 – 4153Combined sources
Beta strandi420 – 4223Combined sources
Beta strandi425 – 4317Combined sources
Helixi434 – 4385Combined sources
Beta strandi444 – 4463Combined sources
Beta strandi449 – 4546Combined sources
Helixi458 – 4625Combined sources
Beta strandi468 – 4703Combined sources
Helixi482 – 4865Combined sources
Beta strandi492 – 4943Combined sources
Beta strandi497 – 5004Combined sources
Helixi506 – 5105Combined sources
Beta strandi516 – 5183Combined sources
Beta strandi525 – 5273Combined sources
Helixi530 – 5345Combined sources
Beta strandi540 – 5423Combined sources
Beta strandi549 – 5513Combined sources
Helixi554 – 5585Combined sources
Beta strandi564 – 5663Combined sources
Beta strandi569 – 5757Combined sources
Helixi578 – 5814Combined sources
Turni582 – 5854Combined sources
Turni591 – 5944Combined sources
Beta strandi596 – 6016Combined sources
Beta strandi611 – 6177Combined sources
Helixi623 – 6319Combined sources
Beta strandi641 – 6455Combined sources
Beta strandi651 – 6544Combined sources
Beta strandi658 – 6603Combined sources
Beta strandi663 – 6686Combined sources
Helixi672 – 6765Combined sources
Beta strandi682 – 6843Combined sources
Beta strandi687 – 6937Combined sources
Helixi696 – 7005Combined sources
Beta strandi706 – 7083Combined sources
Beta strandi715 – 7173Combined sources
Helixi720 – 7245Combined sources
Beta strandi729 – 7324Combined sources
Beta strandi735 – 7417Combined sources
Beta strandi744 – 7474Combined sources
Helixi748 – 7503Combined sources
Helixi753 – 7564Combined sources
Beta strandi761 – 7644Combined sources
Helixi873 – 8797Combined sources
Turni880 – 8834Combined sources
Helixi885 – 8873Combined sources
Beta strandi888 – 8925Combined sources
Beta strandi895 – 9017Combined sources
Beta strandi907 – 9137Combined sources
Turni916 – 9183Combined sources
Helixi919 – 92911Combined sources
Helixi931 – 9333Combined sources
Beta strandi942 – 9487Combined sources
Beta strandi951 – 9577Combined sources
Helixi964 – 9685Combined sources
Helixi971 – 9733Combined sources
Helixi980 – 99920Combined sources
Beta strandi1001 – 10066Combined sources
Helixi1012 – 10143Combined sources
Beta strandi1015 – 10173Combined sources
Beta strandi1023 – 10253Combined sources
Beta strandi1032 – 10343Combined sources
Turni1050 – 10523Combined sources
Helixi1055 – 10584Combined sources
Beta strandi1060 – 10634Combined sources
Helixi1065 – 108117Combined sources
Helixi1102 – 11087Combined sources
Helixi1109 – 11113Combined sources
Helixi1113 – 11164Combined sources
Helixi1126 – 113712Combined sources
Helixi1142 – 11443Combined sources
Helixi1148 – 115912Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3RGXX-ray2.47A23-784[»]
3RGZX-ray2.28A23-784[»]
3RIZX-ray2.52A29-788[»]
3RJ0X-ray2.54A29-788[»]
4LSAX-ray2.50A29-788[»]
4LSXX-ray3.30A/B29-788[»]
4M7EX-ray3.60A/B24-784[»]
4OA2X-ray2.48A865-1196[»]
4OA6X-ray2.43A865-1160[»]
4OA9X-ray2.70A865-1160[»]
4OABX-ray2.30A865-1160[»]
4OACX-ray1.98A865-1160[»]
ProteinModelPortaliO22476.
SMRiO22476. Positions 30-774, 866-1160.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO22476.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati71 – 9828LRR 1Sequence AnalysisAdd
BLAST
Repeati99 – 12123LRR 2Sequence AnalysisAdd
BLAST
Repeati122 – 14625LRR 3Sequence AnalysisAdd
BLAST
Repeati148 – 16922LRR 4Sequence AnalysisAdd
BLAST
Repeati172 – 19726LRR 5Sequence AnalysisAdd
BLAST
Repeati199 – 22123LRR 6Sequence AnalysisAdd
BLAST
Repeati222 – 24423LRR 7Sequence AnalysisAdd
BLAST
Repeati245 – 26824LRR 8Sequence AnalysisAdd
BLAST
Repeati269 – 29022LRR 9Sequence AnalysisAdd
BLAST
Repeati291 – 31424LRR 10Sequence AnalysisAdd
BLAST
Repeati316 – 33823LRR 11Sequence AnalysisAdd
BLAST
Repeati339 – 36325LRR 12Sequence AnalysisAdd
BLAST
Repeati364 – 38825LRR 13Sequence AnalysisAdd
BLAST
Repeati390 – 41324LRR 14Sequence AnalysisAdd
BLAST
Repeati415 – 43925LRR 15Sequence AnalysisAdd
BLAST
Repeati441 – 46323LRR 16Sequence AnalysisAdd
BLAST
Repeati464 – 48724LRR 17Sequence AnalysisAdd
BLAST
Repeati488 – 51124LRR 18Sequence AnalysisAdd
BLAST
Repeati513 – 53523LRR 19Sequence AnalysisAdd
BLAST
Repeati536 – 55924LRR 20Sequence AnalysisAdd
BLAST
Repeati561 – 58323LRR 21Sequence AnalysisAdd
BLAST
Repeati653 – 67725LRR 22Sequence AnalysisAdd
BLAST
Repeati678 – 70124LRR 23Sequence AnalysisAdd
BLAST
Repeati702 – 72524LRR 24Sequence AnalysisAdd
BLAST
Repeati727 – 75024LRR 25Sequence AnalysisAdd
BLAST
Domaini883 – 1158276Protein kinasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi62 – 698Cys pair 1
Motifi763 – 7708Cys pair 2

Domaini

Contains one leucine-zipper motif and two pairs of conservatively spaced Cys (Cys pair 1 and 2) involved in forming heterodimers.1 Publication
A 70 amino acid island between the 20th and the 21th LRR is essential for the binding of brassinosteroids.1 Publication
The JM domain (815-883) is a positive regulator of kinase activity and is required for Tyr phosphorylation.1 Publication
A guanylyl cyclase domain (1021-1134) having an in vitro activity is included in the C-terminal kinase domain.1 Publication

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
Contains 25 LRR (leucine-rich) repeats.Curated
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000116551.
InParanoidiO22476.
KOiK13415.
OMAiKSQYENN.
PhylomeDBiO22476.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR011009. Kinase-like_dom.
IPR001611. Leu-rich_rpt.
IPR013210. LRR-contain_N2.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00560. LRR_1. 2 hits.
PF13855. LRR_8. 2 hits.
PF08263. LRRNT_2. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O22476-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKTFSSFFLS VTTLFFFSFF SLSFQASPSQ SLYREIHQLI SFKDVLPDKN
60 70 80 90 100
LLPDWSSNKN PCTFDGVTCR DDKVTSIDLS SKPLNVGFSA VSSSLLSLTG
110 120 130 140 150
LESLFLSNSH INGSVSGFKC SASLTSLDLS RNSLSGPVTT LTSLGSCSGL
160 170 180 190 200
KFLNVSSNTL DFPGKVSGGL KLNSLEVLDL SANSISGANV VGWVLSDGCG
210 220 230 240 250
ELKHLAISGN KISGDVDVSR CVNLEFLDVS SNNFSTGIPF LGDCSALQHL
260 270 280 290 300
DISGNKLSGD FSRAISTCTE LKLLNISSNQ FVGPIPPLPL KSLQYLSLAE
310 320 330 340 350
NKFTGEIPDF LSGACDTLTG LDLSGNHFYG AVPPFFGSCS LLESLALSSN
360 370 380 390 400
NFSGELPMDT LLKMRGLKVL DLSFNEFSGE LPESLTNLSA SLLTLDLSSN
410 420 430 440 450
NFSGPILPNL CQNPKNTLQE LYLQNNGFTG KIPPTLSNCS ELVSLHLSFN
460 470 480 490 500
YLSGTIPSSL GSLSKLRDLK LWLNMLEGEI PQELMYVKTL ETLILDFNDL
510 520 530 540 550
TGEIPSGLSN CTNLNWISLS NNRLTGEIPK WIGRLENLAI LKLSNNSFSG
560 570 580 590 600
NIPAELGDCR SLIWLDLNTN LFNGTIPAAM FKQSGKIAAN FIAGKRYVYI
610 620 630 640 650
KNDGMKKECH GAGNLLEFQG IRSEQLNRLS TRNPCNITSR VYGGHTSPTF
660 670 680 690 700
DNNGSMMFLD MSYNMLSGYI PKEIGSMPYL FILNLGHNDI SGSIPDEVGD
710 720 730 740 750
LRGLNILDLS SNKLDGRIPQ AMSALTMLTE IDLSNNNLSG PIPEMGQFET
760 770 780 790 800
FPPAKFLNNP GLCGYPLPRC DPSNADGYAH HQRSHGRRPA SLAGSVAMGL
810 820 830 840 850
LFSFVCIFGL ILVGREMRKR RRKKEAELEM YAEGHGNSGD RTANNTNWKL
860 870 880 890 900
TGVKEALSIN LAAFEKPLRK LTFADLLQAT NGFHNDSLIG SGGFGDVYKA
910 920 930 940 950
ILKDGSAVAI KKLIHVSGQG DREFMAEMET IGKIKHRNLV PLLGYCKVGD
960 970 980 990 1000
ERLLVYEFMK YGSLEDVLHD PKKAGVKLNW STRRKIAIGS ARGLAFLHHN
1010 1020 1030 1040 1050
CSPHIIHRDM KSSNVLLDEN LEARVSDFGM ARLMSAMDTH LSVSTLAGTP
1060 1070 1080 1090 1100
GYVPPEYYQS FRCSTKGDVY SYGVVLLELL TGKRPTDSPD FGDNNLVGWV
1110 1120 1130 1140 1150
KQHAKLRISD VFDPELMKED PALEIELLQH LKVAVACLDD RAWRRPTMVQ
1160 1170 1180 1190
VMAMFKEIQA GSGIDSQSTI RSIEDGGFST IEMVDMSIKE VPEGKL
Length:1,196
Mass (Da):130,543
Last modified:January 1, 1998 - v1
Checksum:iC7FBA1C21294E600
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiT09356.
RefSeqiNP_195650.1. NM_120100.2.
UniGeneiAt.27898.
At.69020.

Genome annotation databases

EnsemblPlantsiAT4G39400.1; AT4G39400.1; AT4G39400.
GeneIDi830095.
KEGGiath:AT4G39400.

Cross-referencesi

Web resourcesi

PlantP kinase Classification PPC

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
PIRi T09356.
RefSeqi NP_195650.1. NM_120100.2.
UniGenei At.27898.
At.69020.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3RGX X-ray 2.47 A 23-784 [» ]
3RGZ X-ray 2.28 A 23-784 [» ]
3RIZ X-ray 2.52 A 29-788 [» ]
3RJ0 X-ray 2.54 A 29-788 [» ]
4LSA X-ray 2.50 A 29-788 [» ]
4LSX X-ray 3.30 A/B 29-788 [» ]
4M7E X-ray 3.60 A/B 24-784 [» ]
4OA2 X-ray 2.48 A 865-1196 [» ]
4OA6 X-ray 2.43 A 865-1160 [» ]
4OA9 X-ray 2.70 A 865-1160 [» ]
4OAB X-ray 2.30 A 865-1160 [» ]
4OAC X-ray 1.98 A 865-1160 [» ]
ProteinModelPortali O22476.
SMRi O22476. Positions 30-774, 866-1160.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 15375. 18 interactions.
DIPi DIP-45997N.
IntActi O22476. 7 interactions.

Proteomic databases

PaxDbi O22476.
PRIDEi O22476.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G39400.1 ; AT4G39400.1 ; AT4G39400 .
GeneIDi 830095.
KEGGi ath:AT4G39400.

Organism-specific databases

GeneFarmi 612. 54.
TAIRi AT4G39400.

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000116551.
InParanoidi O22476.
KOi K13415.
OMAi KSQYENN.
PhylomeDBi O22476.

Enzyme and pathway databases

BioCyci ARA:AT4G39400-MONOMER.

Miscellaneous databases

EvolutionaryTracei O22476.
PROi O22476.

Gene expression databases

Genevestigatori O22476.

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
InterProi IPR013320. ConA-like_dom.
IPR011009. Kinase-like_dom.
IPR001611. Leu-rich_rpt.
IPR013210. LRR-contain_N2.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00560. LRR_1. 2 hits.
PF13855. LRR_8. 2 hits.
PF08263. LRRNT_2. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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 AT SER-838; THR-842; THR-846; SER-858 AND THR-872, 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 AT SER-838; SER-858; THR-872; THR-880; THR-982 AND SER-1168, 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.
  25. "The CDG1 kinase mediates brassinosteroid signal transduction from BRI1 receptor kinase to BSU1 phosphatase and GSK3-like kinase BIN2."
    Kim T.W., Guan S., Burlingame A.L., Wang Z.Y.
    Mol. Cell 43:561-571(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDG1.
  26. "Structural basis of steroid hormone perception by the receptor kinase BRI1."
    Hothorn M., Belkhadir Y., Dreux M., Dabi T., Noel J.P., Wilson I.A., Chory J.
    Nature 474:467-471(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) OF 29-788 IN COMPLEX WITH BRASSINOLIDE, GLYCOSYLATION AT ASN-112; ASN-154; ASN-233; ASN-275; ASN-351 AND ASN-545.
  27. "Structural insight into brassinosteroid perception by BRI1."
    She J., Han Z., Kim T.W., Wang J., Cheng W., Chang J., Shi S., Wang J., Yang M., Wang Z.Y., Chai J.
    Nature 474:472-476(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 23-784 IN COMPLEX WITH BRASSINOLIDE, GLYCOSYLATION AT ASN-112; ASN-154; ASN-233; ASN-275; ASN-351; ASN-510; ASN-545 AND ASN-573.
  28. "Molecular mechanism for plant steroid receptor activation by somatic embryogenesis co-receptor kinases."
    Santiago J., Henzler C., Hothorn M.
    Science 341:889-892(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 29-788 IN COMPLEX WITH BRASSINOLIDE, GLYCOSYLATION AT ASN-112; ASN-154; ASN-233; ASN-275; ASN-351; ASN-545 AND ASN-573.
  29. "Crystal structures of the phosphorylated BRI1 kinase domain and implications for brassinosteroid signal initiation."
    Bojar D., Martinez J., Santiago J., Rybin V., Bayliss R., Hothorn M.
    Plant J. 78:31-43(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 865-1160 IN COMPLEX WITH ATP, GLYCOSYLATION AT ASN-154; ASN-275 AND ASN-545.

Entry informationi

Entry nameiBRI1_ARATH
AccessioniPrimary (citable) accession number: O22476
Secondary accession number(s): C0LGS4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: January 1, 1998
Last modified: November 26, 2014
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3