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Protein

Protein BRASSINOSTEROID INSENSITIVE 1

Gene

BRI1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: 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.Curated
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)DescriptionActionsGraphical viewLength
Binding sitei597Brassinolide2 Publications1
Binding sitei642Brassinolide1 Publication1
Binding sitei647Brassinolide; via amide nitrogen3 Publications1
Binding sitei705Brassinolide1 Publication1
Binding sitei911ATP1 Publication1
Active sitei1009Proton acceptorPROSITE-ProRule annotation1
Binding sitei1027ATP1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi889 – 897ATPPROSITE-ProRule annotation9
Nucleotide bindingi957 – 959ATP1 Publication3
Nucleotide bindingi963 – 966ATP1 Publication4
Nucleotide bindingi1009 – 1014ATP1 Publication6

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • protein heterodimerization activity Source: TAIR
  • protein homodimerization activity Source: TAIR
  • protein kinase activity Source: TAIR
  • protein serine/threonine kinase activity Source: TAIR
  • steroid binding Source: TAIR
  • transmembrane receptor protein tyrosine kinase activity Source: UniProtKB-EC

GO - Biological processi

  • anther wall tapetum cell differentiation Source: TAIR
  • brassinosteroid homeostasis Source: TAIR
  • brassinosteroid mediated signaling pathway Source: TAIR
  • detection of brassinosteroid stimulus Source: TAIR
  • leaf development Source: TAIR
  • microtubule bundle formation Source: EnsemblPlants
  • negative regulation of cell death Source: UniProtKB
  • pollen exine formation Source: TAIR
  • positive regulation of flower development Source: TAIR
  • regulation of seedling development Source: UniProtKB
  • response to UV-B Source: TAIR
  • skotomorphogenesis Source: EnsemblPlants
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

Names & Taxonomyi

Protein namesi
Recommended name:
Protein BRASSINOSTEROID INSENSITIVE 11 Publication (EC:2.7.10.1Curated, EC:2.7.11.1Curated)
Short name:
AtBRI11 Publication
Alternative name(s):
Brassinosteroid LRR receptor kinase1 Publication
Gene namesi
Name:BRI11 Publication
Ordered Locus Names:At4g39400
ORF Names:F23K16.30
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G39400.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei793 – 813HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

  • endosome Source: TAIR
  • endosome membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane 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)DescriptionActionsGraphical viewLength
Mutagenesisi69C → Y in bri1-5; brassinosteroid-insensitive semi-dwarf mutant. 1
Mutagenesisi611G → E in bri1-113; brassinosteroid-insensitive semi-dwarf mutant. 1
Mutagenesisi613G → S in bri1-7; brassinosteroid-insensitive semi-dwarf mutant. 1
Mutagenesisi644G → D in bri1-6; brassinosteroid-insensitive semi-dwarf mutant. 1
Mutagenesisi662S → F in bri1-9; brassinosteroid-insensitive semi-dwarf mutant. 1
Mutagenesisi750T → I in bri1-102; brassinosteroid-insensitive dwarf mutant. 1
Mutagenesisi831Y → D or E: No effect on kinase activity, flowering time or leaf size, but altered leaf shape. 1 Publication1
Mutagenesisi831Y → F: No effect on kinase activity but altered flowering time and leaf size and shape. 1 Publication1
Mutagenesisi838S → A: Decreases peptide phosphorylation, but no effect on autophosphorylation. 2 Publications1
Mutagenesisi838S → D: Increased kinase activity; when associated with D-842; D-846 and D-858. 2 Publications1
Mutagenesisi842T → A: Decreases peptide phosphorylation, but no effect on autophosphorylation. 2 Publications1
Mutagenesisi842T → D: Increased kinase activity; when associated with D-838; D-846 and D-858. 2 Publications1
Mutagenesisi846T → A: Decreases peptide phosphorylation, but no effect on autophosphorylation. 2 Publications1
Mutagenesisi846T → D: Increased kinase activity; when associated with D-838; D-842 and D-858. 2 Publications1
Mutagenesisi858S → A: Decreases peptide phosphorylation, but no effect on autophosphorylation. 2 Publications1
Mutagenesisi858S → D: Increased kinase activity; when associated with D-838; D-842 and D-846. 2 Publications1
Mutagenesisi872T → A: 10-fold increase in peptide phosphorylation. 1 Publication1
Mutagenesisi898Y → F: No effect on kinase activity. 1 Publication1
Mutagenesisi909A → T in bri1-1; brassinosteroid-insensitive dwarf mutant. 1
Mutagenesisi911K → E: Loss of kinase activity; dwarf mutant. 1 Publication1
Mutagenesisi945Y → F: No effect on kinase activity. 1 Publication1
Mutagenesisi956Y → F: Loss of kinase activity. 1 Publication1
Mutagenesisi961Y → F: No effect on kinase activity. 1 Publication1
Mutagenesisi983R → N in bri1-8; brassinosteroid-insensitive dwarf mutant. 1
Mutagenesisi983R → Q in bri1-108; brassinosteroid-insensitive dwarf mutant. 1
Mutagenesisi989G → I in bri1-301; impaired kinase activity and loss of autophosphorylation. 1 Publication1
Mutagenesisi1031A → W in bri1-104; brassinosteroid-insensitive dwarf mutant, but no effect on interaction with TTL. 1
Mutagenesisi1039T → A: Abolishes peptide phosphorylation, and to a lower level autophosphorylation. 1 Publication1
Mutagenesisi1042S → A: Abolishes peptide phosphorylation, and to a lower level autophosphorylation. 1
Mutagenesisi1044S → A: Abolishes peptide phosphorylation, and autophosphorylation. 1 Publication1
Mutagenesisi1045T → A: Abolishes peptide phosphorylation, and autophosphorylation. 1 Publication1
Mutagenesisi1048G → D in bri1-115; brassinosteroid-insensitive dwarf mutant and no interaction with TTL. 1
Mutagenesisi1049T → A: Abolishes peptide phosphorylation, and autophosphorylation. 2 Publications1
Mutagenesisi1049T → D: Loss of kinase activity and brassinosteroid signaling. 2 Publications1
Mutagenesisi1052Y → F: Loss of kinase activity. 1 Publication1
Mutagenesisi1057Y → F: Loss of kinase activity. 1 Publication1
Mutagenesisi1058Y → F: No effect on kinase activity. 1 Publication1
Mutagenesisi1070Y → F: No effect on kinase activity. 1 Publication1
Mutagenesisi1072Y → F: Loss of kinase activity. 1 Publication1
Mutagenesisi1078E → K in bri1-101; brassinosteroid-insensitive dwarf mutant and no interaction with TTL. 1
Mutagenesisi1139D → N in bri1-117; brassinosteroid-insensitive dwarf mutant. 1
Mutagenesisi1166S → D: Increased kinase activity; when associated with D-1168; D-1172; D-1179 and D-1180. 1 Publication1
Mutagenesisi1168S → A: Decreases peptide phosphorylation, but no effect on autophosphorylation. 2 Publications1
Mutagenesisi1168S → D: Increased kinase activity; when associated with D-1166; D-1172; D-1179 and D-1180. 2 Publications1
Mutagenesisi1172S → A: Decreases peptide phosphorylation, but no effect on autophosphorylation. 2 Publications1
Mutagenesisi1172S → D: Increased kinase activity; when associated with D-1166; D-1168; D-1179 and D-1180. 2 Publications1
Mutagenesisi1179 – 1180ST → A: Decreases peptide phosphorylation, but no effect on autophosphorylation. 1 Publication2
Mutagenesisi1179S → D: Increased kinase activity; when associated with D-1166; D-1168; D-1172 and D-1180. 1 Publication1
Mutagenesisi1180T → D: Increased kinase activity; when associated with D-1166; D-1168; D-1172 and D-1179. 1 Publication1
Mutagenesisi1187S → A: Decreases peptide phosphorylation, but no effect on autophosphorylation. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
ChainiPRO_000002430524 – 1196Protein BRASSINOSTEROID INSENSITIVE 1Add BLAST1173

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi112N-linked (GlcNAc...)3 Publications1
Glycosylationi154N-linked (GlcNAc...)4 Publications1
Glycosylationi233N-linked (GlcNAc...)3 Publications1
Glycosylationi275N-linked (GlcNAc...)4 Publications1
Glycosylationi351N-linked (GlcNAc...)3 Publications1
Glycosylationi387N-linked (GlcNAc...)Sequence analysis1
Glycosylationi401N-linked (GlcNAc...)Sequence analysis1
Glycosylationi438N-linked (GlcNAc...)Sequence analysis1
Glycosylationi510N-linked (GlcNAc...)1 Publication1
Glycosylationi545N-linked (GlcNAc...)4 Publications1
Glycosylationi573N-linked (GlcNAc...)2 Publications1
Glycosylationi636N-linked (GlcNAc...)Sequence analysis1
Glycosylationi653N-linked (GlcNAc...)Sequence analysis1
Glycosylationi737N-linked (GlcNAc...)Sequence analysis1
Modified residuei831Phosphotyrosine1 Publication1
Modified residuei838Phosphoserine3 Publications1
Modified residuei842Phosphothreonine1 Publication1
Modified residuei846Phosphothreonine2 Publications1
Modified residuei851PhosphothreonineSequence analysis1
Modified residuei858Phosphoserine3 Publications1
Modified residuei872Phosphothreonine2 Publications1
Modified residuei880Phosphothreonine1 Publication1
Modified residuei887Phosphoserine1 Publication1
Modified residuei891PhosphoserineSequence analysis1
Modified residuei956Phosphotyrosine1 Publication1
Modified residuei981PhosphoserineSequence analysis1
Modified residuei982Phosphothreonine1 Publication1
Modified residuei1035PhosphoserineSequence analysis1
Modified residuei1039PhosphothreonineSequence analysis1
Modified residuei1042PhosphoserineSequence analysis1
Modified residuei1044PhosphoserineSequence analysisBy similarity1
Modified residuei1045PhosphothreonineSequence analysis1
Modified residuei1049PhosphothreonineSequence analysis1
Modified residuei1052PhosphotyrosineBy similarity1
Modified residuei1060PhosphoserineSequence analysis1
Modified residuei1072PhosphotyrosineSequence analysis1
Modified residuei1166Phosphoserine1 Publication1
Modified residuei1168Phosphoserine1 Publication1
Modified residuei1169PhosphothreonineSequence analysis1
Modified residuei1172PhosphoserineSequence analysis1
Modified residuei1179PhosphoserineSequence analysis1
Modified residuei1180Phosphothreonine1 Publication1
Modified residuei1187PhosphoserineSequence analysis1

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.

PTM databases

iPTMnetiO22476.

Expressioni

Tissue specificityi

Expressed ubiquitously.2 Publications

Developmental stagei

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

Gene expression databases

GenevisibleiO22476. AT.

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). No interactions with PSKR1 or CNGC17 (PubMed:26071421). Interacts with BIK1 (PubMed:23818580).11 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

GO - Molecular functioni

  • protein heterodimerization activity Source: TAIR
  • protein homodimerization activity Source: TAIR

Protein-protein interaction databases

BioGridi15375. 26 interactors.
DIPiDIP-45997N.
IntActiO22476. 7 interactors.
STRINGi3702.AT4G39400.1.

Structurei

Secondary structure

11196
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi32 – 43Combined sources12
Helixi49 – 51Combined sources3
Beta strandi57 – 59Combined sources3
Helixi61 – 63Combined sources3
Beta strandi67 – 70Combined sources4
Beta strandi73 – 78Combined sources6
Helixi88 – 94Combined sources7
Turni95 – 97Combined sources3
Beta strandi103 – 105Combined sources3
Beta strandi111 – 113Combined sources3
Beta strandi126 – 128Combined sources3
Beta strandi131 – 137Combined sources7
Helixi138 – 146Combined sources9
Beta strandi152 – 154Combined sources3
Beta strandi157 – 161Combined sources5
Beta strandi176 – 179Combined sources4
Beta strandi182 – 184Combined sources3
Beta strandi186 – 188Combined sources3
Helixi190 – 195Combined sources6
Beta strandi204 – 206Combined sources3
Beta strandi209 – 214Combined sources6
Beta strandi226 – 228Combined sources3
Beta strandi249 – 251Combined sources3
Helixi261 – 264Combined sources4
Turni265 – 267Combined sources3
Beta strandi273 – 275Combined sources3
Beta strandi282 – 284Combined sources3
Beta strandi295 – 297Combined sources3
Beta strandi300 – 306Combined sources7
Helixi309 – 314Combined sources6
Turni315 – 317Combined sources3
Beta strandi319 – 322Combined sources4
Beta strandi325 – 330Combined sources6
Helixi334 – 338Combined sources5
Beta strandi344 – 346Combined sources3
Beta strandi349 – 355Combined sources7
Helixi358 – 361Combined sources4
Beta strandi369 – 371Combined sources3
Beta strandi374 – 379Combined sources6
Helixi385 – 388Combined sources4
Turni389 – 391Combined sources3
Beta strandi393 – 396Combined sources4
Beta strandi399 – 405Combined sources7
Turni408 – 411Combined sources4
Beta strandi413 – 415Combined sources3
Beta strandi420 – 422Combined sources3
Beta strandi425 – 431Combined sources7
Helixi434 – 438Combined sources5
Beta strandi444 – 446Combined sources3
Beta strandi449 – 454Combined sources6
Helixi458 – 462Combined sources5
Beta strandi468 – 470Combined sources3
Helixi482 – 486Combined sources5
Beta strandi492 – 494Combined sources3
Beta strandi497 – 500Combined sources4
Helixi506 – 510Combined sources5
Beta strandi516 – 518Combined sources3
Beta strandi525 – 527Combined sources3
Helixi530 – 534Combined sources5
Beta strandi540 – 542Combined sources3
Beta strandi549 – 551Combined sources3
Helixi554 – 558Combined sources5
Beta strandi564 – 566Combined sources3
Beta strandi569 – 575Combined sources7
Helixi578 – 581Combined sources4
Turni582 – 585Combined sources4
Turni591 – 594Combined sources4
Beta strandi596 – 601Combined sources6
Beta strandi611 – 617Combined sources7
Helixi623 – 631Combined sources9
Beta strandi641 – 645Combined sources5
Beta strandi651 – 654Combined sources4
Beta strandi658 – 660Combined sources3
Beta strandi663 – 668Combined sources6
Helixi672 – 676Combined sources5
Beta strandi682 – 684Combined sources3
Beta strandi687 – 693Combined sources7
Helixi696 – 700Combined sources5
Beta strandi706 – 708Combined sources3
Beta strandi715 – 717Combined sources3
Helixi720 – 724Combined sources5
Beta strandi729 – 732Combined sources4
Beta strandi735 – 741Combined sources7
Beta strandi744 – 747Combined sources4
Helixi748 – 750Combined sources3
Helixi753 – 756Combined sources4
Beta strandi761 – 764Combined sources4
Helixi873 – 879Combined sources7
Turni880 – 883Combined sources4
Helixi885 – 887Combined sources3
Beta strandi888 – 892Combined sources5
Beta strandi895 – 901Combined sources7
Beta strandi907 – 913Combined sources7
Turni916 – 918Combined sources3
Helixi919 – 929Combined sources11
Helixi931 – 933Combined sources3
Beta strandi942 – 948Combined sources7
Beta strandi951 – 957Combined sources7
Helixi964 – 969Combined sources6
Helixi971 – 973Combined sources3
Helixi980 – 999Combined sources20
Beta strandi1001 – 1006Combined sources6
Helixi1012 – 1014Combined sources3
Beta strandi1015 – 1017Combined sources3
Beta strandi1023 – 1025Combined sources3
Beta strandi1032 – 1034Combined sources3
Turni1050 – 1052Combined sources3
Helixi1055 – 1058Combined sources4
Beta strandi1060 – 1063Combined sources4
Helixi1065 – 1081Combined sources17
Turni1089 – 1093Combined sources5
Helixi1096 – 1103Combined sources8
Helixi1108 – 1110Combined sources3
Helixi1114 – 1117Combined sources4
Helixi1121 – 1123Combined sources3
Helixi1124 – 1137Combined sources14
Helixi1142 – 1144Combined sources3
Helixi1148 – 1159Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4OH4X-ray2.25A/B863-1172[»]
4Q5JX-ray2.77A/B863-1180[»]
5LPBX-ray1.98A865-1160[»]
5LPVX-ray2.70A865-1160[»]
5LPWX-ray2.43A865-1160[»]
5LPYX-ray2.30A865-1160[»]
5LPZX-ray2.48A865-1196[»]
ProteinModelPortaliO22476.
SMRiO22476.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO22476.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati71 – 98LRR 1Sequence analysisAdd BLAST28
Repeati99 – 121LRR 2Sequence analysisAdd BLAST23
Repeati122 – 146LRR 3Sequence analysisAdd BLAST25
Repeati148 – 169LRR 4Sequence analysisAdd BLAST22
Repeati172 – 197LRR 5Sequence analysisAdd BLAST26
Repeati199 – 221LRR 6Sequence analysisAdd BLAST23
Repeati222 – 244LRR 7Sequence analysisAdd BLAST23
Repeati245 – 268LRR 8Sequence analysisAdd BLAST24
Repeati269 – 290LRR 9Sequence analysisAdd BLAST22
Repeati291 – 314LRR 10Sequence analysisAdd BLAST24
Repeati316 – 338LRR 11Sequence analysisAdd BLAST23
Repeati339 – 363LRR 12Sequence analysisAdd BLAST25
Repeati364 – 388LRR 13Sequence analysisAdd BLAST25
Repeati390 – 413LRR 14Sequence analysisAdd BLAST24
Repeati415 – 439LRR 15Sequence analysisAdd BLAST25
Repeati441 – 463LRR 16Sequence analysisAdd BLAST23
Repeati464 – 487LRR 17Sequence analysisAdd BLAST24
Repeati488 – 511LRR 18Sequence analysisAdd BLAST24
Repeati513 – 535LRR 19Sequence analysisAdd BLAST23
Repeati536 – 559LRR 20Sequence analysisAdd BLAST24
Repeati561 – 583LRR 21Sequence analysisAdd BLAST23
Repeati653 – 677LRR 22Sequence analysisAdd BLAST25
Repeati678 – 701LRR 23Sequence analysisAdd BLAST24
Repeati702 – 725LRR 24Sequence analysisAdd BLAST24
Repeati727 – 750LRR 25Sequence analysisAdd BLAST24
Domaini883 – 1158Protein kinasePROSITE-ProRule annotationAdd BLAST276

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi62 – 69Cys pair 18
Motifi763 – 770Cys pair 28

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 21th and the 22th 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

eggNOGiENOG410IF0B. Eukaryota.
COG0515. LUCA.
COG4886. LUCA.
HOGENOMiHOG000116551.
InParanoidiO22476.
KOiK13415.
OMAiQPTDSAD.
OrthoDBiEOG093600TU.
PhylomeDBiO22476.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
3.80.10.10. 4 hits.
InterProiIPR013320. ConA-like_dom.
IPR011009. Kinase-like_dom.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR025875. Leu-rich_rpt_4.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR013210. LRR_N_plant-typ.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00560. LRR_1. 1 hit.
PF12799. LRR_4. 1 hit.
PF13855. LRR_8. 2 hits.
PF08263. LRRNT_2. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 7 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 2 hits.
SSF56112. 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_120100.3.
UniGeneiAt.27898.
At.69020.

Genome annotation databases

EnsemblPlantsiAT4G39400.1; AT4G39400.1; AT4G39400.
GeneIDi830095.
GrameneiAT4G39400.1; AT4G39400.1; AT4G39400.
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.
PIRiT09356.
RefSeqiNP_195650.1. NM_120100.3.
UniGeneiAt.27898.
At.69020.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4OH4X-ray2.25A/B863-1172[»]
4Q5JX-ray2.77A/B863-1180[»]
5LPBX-ray1.98A865-1160[»]
5LPVX-ray2.70A865-1160[»]
5LPWX-ray2.43A865-1160[»]
5LPYX-ray2.30A865-1160[»]
5LPZX-ray2.48A865-1196[»]
ProteinModelPortaliO22476.
SMRiO22476.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi15375. 26 interactors.
DIPiDIP-45997N.
IntActiO22476. 7 interactors.
STRINGi3702.AT4G39400.1.

PTM databases

iPTMnetiO22476.

Proteomic databases

PaxDbiO22476.
PRIDEiO22476.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G39400.1; AT4G39400.1; AT4G39400.
GeneIDi830095.
GrameneiAT4G39400.1; AT4G39400.1; AT4G39400.
KEGGiath:AT4G39400.

Organism-specific databases

TAIRiAT4G39400.

Phylogenomic databases

eggNOGiENOG410IF0B. Eukaryota.
COG0515. LUCA.
COG4886. LUCA.
HOGENOMiHOG000116551.
InParanoidiO22476.
KOiK13415.
OMAiQPTDSAD.
OrthoDBiEOG093600TU.
PhylomeDBiO22476.

Miscellaneous databases

EvolutionaryTraceiO22476.
PROiO22476.

Gene expression databases

GenevisibleiO22476. AT.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
3.80.10.10. 4 hits.
InterProiIPR013320. ConA-like_dom.
IPR011009. Kinase-like_dom.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR025875. Leu-rich_rpt_4.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR013210. LRR_N_plant-typ.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00560. LRR_1. 1 hit.
PF12799. LRR_4. 1 hit.
PF13855. LRR_8. 2 hits.
PF08263. LRRNT_2. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 7 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 30, 2016
This is version 159 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.