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O22476

- BRI1_ARATH

UniProt

O22476 - BRI1_ARATH

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
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    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 sitei911 – 9111ATPPROSITE-ProRule annotation
    Active sitei1009 – 10091Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi889 – 8979ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. identical protein binding Source: IntAct
    3. protein binding Source: IntAct
    4. protein heterodimerization activity Source: TAIR
    5. protein homodimerization activity Source: TAIR
    6. protein kinase activity Source: TAIR
    7. protein serine/threonine kinase activity Source: TAIR
    8. steroid binding Source: TAIR
    9. 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

    Keywords - Molecular functioni

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

    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

    GO - Cellular componenti

    1. endosome Source: TAIR
    2. endosome membrane Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW
    4. plasma membrane Source: TAIR
    5. protein complex Source: TAIR

    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...)Sequence Analysis
    Glycosylationi154 – 1541N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi233 – 2331N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi275 – 2751N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi351 – 3511N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi387 – 3871N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi401 – 4011N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi438 – 4381N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi510 – 5101N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi545 – 5451N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi573 – 5731N-linked (GlcNAc...)Sequence Analysis
    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 BRI1.8 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 – 4312
    Helixi49 – 513
    Beta strandi57 – 593
    Helixi61 – 633
    Beta strandi67 – 704
    Beta strandi73 – 786
    Helixi88 – 947
    Turni95 – 973
    Beta strandi103 – 1053
    Beta strandi111 – 1133
    Beta strandi126 – 1283
    Beta strandi131 – 1377
    Helixi138 – 1469
    Beta strandi152 – 1543
    Beta strandi157 – 1615
    Beta strandi176 – 1794
    Beta strandi182 – 1843
    Beta strandi186 – 1883
    Helixi190 – 1956
    Beta strandi204 – 2063
    Beta strandi209 – 2146
    Beta strandi226 – 2283
    Beta strandi249 – 2513
    Helixi261 – 2644
    Turni265 – 2673
    Beta strandi273 – 2753
    Beta strandi282 – 2843
    Beta strandi295 – 2973
    Beta strandi300 – 3067
    Helixi309 – 3146
    Turni315 – 3173
    Beta strandi319 – 3224
    Beta strandi325 – 3306
    Helixi334 – 3385
    Beta strandi344 – 3463
    Beta strandi349 – 3557
    Helixi358 – 3614
    Beta strandi369 – 3713
    Beta strandi374 – 3796
    Helixi385 – 3884
    Turni389 – 3913
    Beta strandi393 – 3964
    Beta strandi399 – 4057
    Turni408 – 4114
    Beta strandi413 – 4153
    Beta strandi420 – 4223
    Beta strandi425 – 4317
    Helixi434 – 4385
    Beta strandi444 – 4463
    Beta strandi449 – 4546
    Helixi458 – 4625
    Beta strandi468 – 4703
    Helixi482 – 4865
    Beta strandi492 – 4943
    Beta strandi497 – 5004
    Helixi506 – 5105
    Beta strandi516 – 5183
    Beta strandi525 – 5273
    Helixi530 – 5345
    Beta strandi540 – 5423
    Beta strandi549 – 5513
    Helixi554 – 5585
    Beta strandi564 – 5663
    Beta strandi569 – 5757
    Helixi578 – 5814
    Turni582 – 5854
    Turni591 – 5944
    Beta strandi596 – 6016
    Beta strandi611 – 6177
    Helixi623 – 6319
    Beta strandi641 – 6455
    Beta strandi651 – 6544
    Beta strandi658 – 6603
    Beta strandi663 – 6686
    Helixi672 – 6765
    Beta strandi682 – 6843
    Beta strandi687 – 6937
    Helixi696 – 7005
    Beta strandi706 – 7083
    Beta strandi715 – 7173
    Helixi720 – 7245
    Beta strandi729 – 7324
    Beta strandi735 – 7417
    Beta strandi744 – 7474
    Helixi748 – 7503
    Helixi753 – 7564
    Beta strandi761 – 7644
    Helixi873 – 8797
    Turni880 – 8834
    Helixi885 – 8873
    Beta strandi888 – 8925
    Beta strandi895 – 9017
    Beta strandi907 – 9137
    Turni916 – 9183
    Helixi919 – 92911
    Helixi931 – 9333
    Beta strandi942 – 9487
    Beta strandi951 – 9577
    Helixi964 – 9685
    Helixi971 – 9733
    Helixi980 – 99920
    Beta strandi1001 – 10066
    Helixi1012 – 10143
    Beta strandi1015 – 10173
    Beta strandi1023 – 10253
    Beta strandi1032 – 10343
    Turni1050 – 10523
    Helixi1055 – 10584
    Beta strandi1060 – 10634
    Helixi1065 – 108117
    Helixi1102 – 11087
    Helixi1109 – 11113
    Helixi1113 – 11164
    Helixi1126 – 113712
    Helixi1142 – 11443
    Helixi1148 – 115912

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.

    Transmembrane

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

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati100 – 12223LRR 1Add
    BLAST
    Repeati123 – 14523LRR 2Add
    BLAST
    Repeati149 – 17022LRR 3Add
    BLAST
    Repeati174 – 19522LRR 4Add
    BLAST
    Repeati201 – 22222LRR 5Add
    BLAST
    Repeati223 – 24523LRR 6Add
    BLAST
    Repeati246 – 26823LRR 7Add
    BLAST
    Repeati270 – 29122LRR 8Add
    BLAST
    Repeati292 – 31423LRR 9Add
    BLAST
    Repeati317 – 33923LRR 10Add
    BLAST
    Repeati341 – 36323LRR 11Add
    BLAST
    Repeati366 – 38924LRR 12Add
    BLAST
    Repeati391 – 41121LRR 13Add
    BLAST
    Repeati417 – 44024LRR 14Add
    BLAST
    Repeati441 – 46323LRR 15Add
    BLAST
    Repeati465 – 48723LRR 16Add
    BLAST
    Repeati489 – 51224LRR 17Add
    BLAST
    Repeati513 – 53523LRR 18Add
    BLAST
    Repeati537 – 56024LRR 19Add
    BLAST
    Repeati561 – 58323LRR 20Add
    BLAST
    Repeati655 – 67723LRR 21Add
    BLAST
    Repeati679 – 70123LRR 22Add
    BLAST
    Repeati703 – 72523LRR 23Add
    BLAST
    Repeati727 – 74923LRR 24Add
    BLAST
    Domaini883 – 1158276Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Repeati1175 – 119521LRR 25Add
    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_subgrp.
    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

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    MKTFSSFFLS VTTLFFFSFF SLSFQASPSQ SLYREIHQLI SFKDVLPDKN     50
    LLPDWSSNKN PCTFDGVTCR DDKVTSIDLS SKPLNVGFSA VSSSLLSLTG 100
    LESLFLSNSH INGSVSGFKC SASLTSLDLS RNSLSGPVTT LTSLGSCSGL 150
    KFLNVSSNTL DFPGKVSGGL KLNSLEVLDL SANSISGANV VGWVLSDGCG 200
    ELKHLAISGN KISGDVDVSR CVNLEFLDVS SNNFSTGIPF LGDCSALQHL 250
    DISGNKLSGD FSRAISTCTE LKLLNISSNQ FVGPIPPLPL KSLQYLSLAE 300
    NKFTGEIPDF LSGACDTLTG LDLSGNHFYG AVPPFFGSCS LLESLALSSN 350
    NFSGELPMDT LLKMRGLKVL DLSFNEFSGE LPESLTNLSA SLLTLDLSSN 400
    NFSGPILPNL CQNPKNTLQE LYLQNNGFTG KIPPTLSNCS ELVSLHLSFN 450
    YLSGTIPSSL GSLSKLRDLK LWLNMLEGEI PQELMYVKTL ETLILDFNDL 500
    TGEIPSGLSN CTNLNWISLS NNRLTGEIPK WIGRLENLAI LKLSNNSFSG 550
    NIPAELGDCR SLIWLDLNTN LFNGTIPAAM FKQSGKIAAN FIAGKRYVYI 600
    KNDGMKKECH GAGNLLEFQG IRSEQLNRLS TRNPCNITSR VYGGHTSPTF 650
    DNNGSMMFLD MSYNMLSGYI PKEIGSMPYL FILNLGHNDI SGSIPDEVGD 700
    LRGLNILDLS SNKLDGRIPQ AMSALTMLTE IDLSNNNLSG PIPEMGQFET 750
    FPPAKFLNNP GLCGYPLPRC DPSNADGYAH HQRSHGRRPA SLAGSVAMGL 800
    LFSFVCIFGL ILVGREMRKR RRKKEAELEM YAEGHGNSGD RTANNTNWKL 850
    TGVKEALSIN LAAFEKPLRK LTFADLLQAT NGFHNDSLIG SGGFGDVYKA 900
    ILKDGSAVAI KKLIHVSGQG DREFMAEMET IGKIKHRNLV PLLGYCKVGD 950
    ERLLVYEFMK YGSLEDVLHD PKKAGVKLNW STRRKIAIGS ARGLAFLHHN 1000
    CSPHIIHRDM KSSNVLLDEN LEARVSDFGM ARLMSAMDTH LSVSTLAGTP 1050
    GYVPPEYYQS FRCSTKGDVY SYGVVLLELL TGKRPTDSPD FGDNNLVGWV 1100
    KQHAKLRISD VFDPELMKED PALEIELLQH LKVAVACLDD RAWRRPTMVQ 1150
    VMAMFKEIQA GSGIDSQSTI RSIEDGGFST IEMVDMSIKE VPEGKL 1196
    Length:1,196
    Mass (Da):130,543
    Last modified:January 1, 1998 - v1
    Checksum:iC7FBA1C21294E600
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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_subgrp.
    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

    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.

    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: October 1, 2014
    This is version 140 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