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O22476

- BRI1_ARATH

UniProt

O22476 - BRI1_ARATH

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Protein
Protein BRASSINOSTEROID INSENSITIVE 1
Gene
BRI1, At4g39400, F23K16.30
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.

Enzyme regulationi

Activated by Ser and Thr phosphorylation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei911 – 9111ATP By similarity
Active sitei1009 – 10091Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi889 – 8979ATP By similarity

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
Complete GO annotation...

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

Cell membrane; Single-pass type I membrane protein. Endosome membrane; Single-pass type I membrane protein 6 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei793 – 81321Helical; Reviewed prediction
Add
BLAST

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
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 – 2323 Reviewed prediction
Add
BLAST
Chaini24 – 11961173Protein BRASSINOSTEROID INSENSITIVE 1
PRO_0000024305Add
BLAST

Amino acid modifications

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

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.8 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

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.

Miscellaneous databases

EvolutionaryTraceiO22476.

Family & Domainsi

Domains and Repeats

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

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

« 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.

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: June 11, 2014
This is version 139 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

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