Reviewed, UniProtKB/Swiss-Prot O22476 (BRI1_ARATH)

Names and origin

Protein names

Recommended name:
    Protein BRASSINOSTEROID INSENSITIVE 1
      Short name=AtBRI1
    EC=2.7.11.1
Alternative name(s):
    Brassinosteroid LRR receptor kinase

Gene names

Name:	BRI1
Ordered Locus Names:	At4g39400
ORF Names:	F23K16.30

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	1196 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Receptor with a serine/threonine-protein kinase activity. 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) and Transthyretin-Like protein (TTL) in vitro. Ref.2 Ref.3
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Activated by Ser and Thr phosphorylation.
Subunit structure	Homodimer in the plasma membrane Probable. Heterodimer with BAK1 in the endosomes. Interacts with TTL in a kinase-dependent manner.
Subcellular location	Cell membrane; Single-pass type I membrane protein. Endosome membrane; Single-pass type I membrane protein. Ref.3 Ref.7 Ref.8 Ref.10
Tissue specificity	Expressed ubiquitously. Ref.3 Ref.1
Developmental stage	Expressed constitutively in either dark- or light-grown seedlings.
Domain	Contains one leucine-zipper motif and two pairs of conservatively spaced Cys (Cys pair 1 and 2) involved in forming heterodimers. A 70 amino acid island between the 20th and the 21th LRR is essential for the binding of brassinosteroids.
Post-translational modification	Phosphorylated on at least 12 sites, with a preference for Ser residues. Ref.7 Ref.8 Ref.5 Ref.9 Ref.12
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).
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Contains 25 LRR (leucine-rich) repeats. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Cell membrane Endosome Membrane
Domain	Leucine-rich repeat Repeat Signal Transmembrane
Ligand	ATP-binding Lipid-binding Nucleotide-binding Steroid-binding
Molecular function	Kinase Receptor Serine/threonine-protein kinase Transferase
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	brassinosteroid homeostasis Inferred from expression pattern. Source: TAIR brassinosteroid mediated signaling Inferred from mutant phenotype. Source: TAIR detection of brassinosteroid stimulus Ref.1 Inferred from mutant phenotype. Source: TAIR positive regulation of flower development Inferred from genetic interaction. Source: TAIR protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro response to UV-B Inferred from genetic interaction. Source: TAIR
Cellular component	endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Ref.3 Inferred from direct assay. Source: TAIR protein complex Inferred from physical interaction. Source: TAIR
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein heterodimerization activity Ref.10 Inferred from physical interaction. Source: TAIR protein homodimerization activity Inferred from direct assay. Source: TAIR protein serine/threonine kinase activity Inferred from direct assay. Source: TAIR receptor activity Inferred from electronic annotation. Source: UniProtKB-KW steroid binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-1797828,EBI-1797828
	Q94AG2	2	EBI-1797828,EBI-1555537
At4g35230	Q944A7	4	EBI-1797828,EBI-1797846
BAK1	Q94F62	4	EBI-1797828,EBI-617138
F6N23.9	O65280	2	EBI-1797828,EBI-1797930
TTL	Q9LVM5	3	EBI-1797828,EBI-1803584

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Potential
	Chain	24 – 1196	1173	Protein BRASSINOSTEROID INSENSITIVE 1		PRO_0000024305
Regions
	Transmembrane	793 – 813	21	Potential
	Repeat	98 – 121	24	LRR 1
	Repeat	122 – 146	25	LRR 2
	Repeat	148 – 169	22	LRR 3
	Repeat	172 – 197	26	LRR 4
	Repeat	199 – 221	23	LRR 5
	Repeat	222 – 244	23	LRR 6
	Repeat	245 – 268	24	LRR 7
	Repeat	269 – 290	22	LRR 8
	Repeat	291 – 314	24	LRR 9
	Repeat	316 – 338	23	LRR 10
	Repeat	339 – 363	25	LRR 11
	Repeat	364 – 388	25	LRR 12
	Repeat	390 – 413	24	LRR 13
	Repeat	415 – 439	25	LRR 14
	Repeat	441 – 463	23	LRR 15
	Repeat	464 – 487	24	LRR 16
	Repeat	488 – 511	24	LRR 17
	Repeat	513 – 535	23	LRR 18
	Repeat	536 – 559	24	LRR 19
	Repeat	561 – 583	23	LRR 20
	Repeat	653 – 677	25	LRR 21
	Repeat	678 – 701	24	LRR 22
	Repeat	702 – 725	24	LRR 23
	Repeat	727 – 750	24	LRR 24
	Domain	883 – 1158	276	Protein kinase
	Repeat	1175 – 1195	21	LRR 25
	Nucleotide binding	889 – 897	9	ATP By similarity
	Motif	62 – 69	8	Cys pair 1
	Motif	763 – 770	8	Cys pair 2
Sites
	Active site	1009	1	Proton acceptor By similarity
	Binding site	911	1	ATP By similarity
Amino acid modifications
	Modified residue	838	1	Phosphoserine
	Modified residue	842	1	Phosphothreonine
	Modified residue	846	1	Phosphothreonine
	Modified residue	851	1	Phosphothreonine Potential
	Modified residue	858	1	Phosphoserine
	Modified residue	872	1	Phosphothreonine
	Modified residue	880	1	Phosphothreonine
	Modified residue	887	1	Phosphoserine Potential
	Modified residue	891	1	Phosphoserine Potential
	Modified residue	981	1	Phosphoserine Potential
	Modified residue	982	1	Phosphothreonine
	Modified residue	1035	1	Phosphoserine Potential
	Modified residue	1039	1	Phosphothreonine Potential
	Modified residue	1042	1	Phosphoserine Potential
	Modified residue	1044	1	Phosphoserine Potential
	Modified residue	1045	1	Phosphothreonine Potential
	Modified residue	1049	1	Phosphothreonine Potential
	Modified residue	1060	1	Phosphoserine Potential
	Modified residue	1166	1	Phosphoserine Potential
	Modified residue	1168	1	Phosphoserine
	Modified residue	1169	1	Phosphothreonine Potential
	Modified residue	1172	1	Phosphoserine Potential
	Modified residue	1179	1	Phosphoserine Potential
	Modified residue	1180	1	Phosphothreonine Potential
	Modified residue	1187	1	Phosphoserine Potential
	Glycosylation	112	1	N-linked (GlcNAc...) Potential
	Glycosylation	154	1	N-linked (GlcNAc...) Potential
	Glycosylation	233	1	N-linked (GlcNAc...) Potential
	Glycosylation	275	1	N-linked (GlcNAc...) Potential
	Glycosylation	351	1	N-linked (GlcNAc...) Potential
	Glycosylation	387	1	N-linked (GlcNAc...) Potential
	Glycosylation	401	1	N-linked (GlcNAc...) Potential
	Glycosylation	438	1	N-linked (GlcNAc...) Potential
	Glycosylation	510	1	N-linked (GlcNAc...) Potential
	Glycosylation	545	1	N-linked (GlcNAc...) Potential
	Glycosylation	573	1	N-linked (GlcNAc...) Potential
	Glycosylation	636	1	N-linked (GlcNAc...) Potential
	Glycosylation	653	1	N-linked (GlcNAc...) Potential
	Glycosylation	737	1	N-linked (GlcNAc...) Potential
Experimental info
	Mutagenesis	69	1	C → Y in bri1-5; brassinosteroid-insensitive semi-dwarf mutant.
	Mutagenesis	611	1	G → E in bri1-113; brassinosteroid-insensitive semi-dwarf mutant.
	Mutagenesis	613	1	G → S in bri1-7; brassinosteroid-insensitive semi-dwarf mutant.
	Mutagenesis	644	1	G → D in bri1-6; brassinosteroid-insensitive semi-dwarf mutant.
	Mutagenesis	662	1	S → F in bri1-9; brassinosteroid-insensitive semi-dwarf mutant.
	Mutagenesis	750	1	T → I in bri1-102; brassinosteroid-insensitive dwarf mutant.
	Mutagenesis	838	1	S → A: Decreases peptide phosphorylation, but no effect on autophosphorylation. Ref.12
	Mutagenesis	842	1	T → A: Decreases peptide phosphorylation, but no effect on autophosphorylation. Ref.12
	Mutagenesis	846	1	T → A: Decreases peptide phosphorylation, but no effect on autophosphorylation. Ref.12
	Mutagenesis	858	1	S → A: Decreases peptide phosphorylation, but no effect on autophosphorylation. Ref.12
	Mutagenesis	872	1	T → A: 10-fold increase in peptide phosphorylation. Ref.12
	Mutagenesis	909	1	A → T in bri1-1; brassinosteroid-insensitive dwarf mutant.
	Mutagenesis	911	1	K → E: Loss of kinase activity; dwarf mutant. Ref.5
	Mutagenesis	983	1	R → N in bri1-8; brassinosteroid-insensitive dwarf mutant.
	Mutagenesis	983	1	R → Q in bri1-108; brassinosteroid-insensitive dwarf mutant.
	Mutagenesis	1031	1	A → W in bri1-104; brassinosteroid-insensitive dwarf mutant, but no effect on interaction with TTL.
	Mutagenesis	1039	1	T → A: Abolishes peptide phosphorylation, and to a lower level autophosphorylation. Ref.12
	Mutagenesis	1042	1	S → A: Abolishes peptide phosphorylation, and to a lower level autophosphorylation.
	Mutagenesis	1044	1	S → A: Abolishes peptide phosphorylation, and autophosphorylation. Ref.12
	Mutagenesis	1045	1	T → A: Abolishes peptide phosphorylation, and autophosphorylation. Ref.12
	Mutagenesis	1048	1	G → D in bri1-115; brassinosteroid-insensitive dwarf mutant and no interaction with TTL.
	Mutagenesis	1049	1	T → A: Abolishes peptide phosphorylation, and autophosphorylation. Ref.12
	Mutagenesis	1078	1	E → K in bri1-101; brassinosteroid-insensitive dwarf mutant and no interaction with TTL.
	Mutagenesis	1139	1	D → N in bri1-117; brassinosteroid-insensitive dwarf mutant.
	Mutagenesis	1168	1	S → A: Decreases peptide phosphorylation, but no effect on autophosphorylation. Ref.12
	Mutagenesis	1172	1	S → A: Decreases peptide phosphorylation, but no effect on autophosphorylation. Ref.12
	Mutagenesis	1179 – 1180	2	ST → A: Decreases peptide phosphorylation, but no effect on autophosphorylation.
	Mutagenesis	1187	1	S → A: Decreases peptide phosphorylation, but no effect on autophosphorylation. Ref.12

Sequences

	Sequence		Length	Mass (Da)
	O22476-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: C7FBA1C21294E600	FASTA	1,196	130,543
	10 20 30 40 50 60 MKTFSSFFLS VTTLFFFSFF SLSFQASPSQ SLYREIHQLI SFKDVLPDKN LLPDWSSNKN 70 80 90 100 110 120 PCTFDGVTCR DDKVTSIDLS SKPLNVGFSA VSSSLLSLTG LESLFLSNSH INGSVSGFKC 130 140 150 160 170 180 SASLTSLDLS RNSLSGPVTT LTSLGSCSGL KFLNVSSNTL DFPGKVSGGL KLNSLEVLDL 190 200 210 220 230 240 SANSISGANV VGWVLSDGCG ELKHLAISGN KISGDVDVSR CVNLEFLDVS SNNFSTGIPF 250 260 270 280 290 300 LGDCSALQHL DISGNKLSGD FSRAISTCTE LKLLNISSNQ FVGPIPPLPL KSLQYLSLAE 310 320 330 340 350 360 NKFTGEIPDF LSGACDTLTG LDLSGNHFYG AVPPFFGSCS LLESLALSSN NFSGELPMDT 370 380 390 400 410 420 LLKMRGLKVL DLSFNEFSGE LPESLTNLSA SLLTLDLSSN NFSGPILPNL CQNPKNTLQE 430 440 450 460 470 480 LYLQNNGFTG KIPPTLSNCS ELVSLHLSFN YLSGTIPSSL GSLSKLRDLK LWLNMLEGEI 490 500 510 520 530 540 PQELMYVKTL ETLILDFNDL TGEIPSGLSN CTNLNWISLS NNRLTGEIPK WIGRLENLAI 550 560 570 580 590 600 LKLSNNSFSG NIPAELGDCR SLIWLDLNTN LFNGTIPAAM FKQSGKIAAN FIAGKRYVYI 610 620 630 640 650 660 KNDGMKKECH GAGNLLEFQG IRSEQLNRLS TRNPCNITSR VYGGHTSPTF DNNGSMMFLD 670 680 690 700 710 720 MSYNMLSGYI PKEIGSMPYL FILNLGHNDI SGSIPDEVGD LRGLNILDLS SNKLDGRIPQ 730 740 750 760 770 780 AMSALTMLTE IDLSNNNLSG PIPEMGQFET FPPAKFLNNP GLCGYPLPRC DPSNADGYAH 790 800 810 820 830 840 HQRSHGRRPA SLAGSVAMGL LFSFVCIFGL ILVGREMRKR RRKKEAELEM YAEGHGNSGD 850 860 870 880 890 900 RTANNTNWKL TGVKEALSIN LAAFEKPLRK LTFADLLQAT NGFHNDSLIG SGGFGDVYKA 910 920 930 940 950 960 ILKDGSAVAI KKLIHVSGQG DREFMAEMET IGKIKHRNLV PLLGYCKVGD ERLLVYEFMK 970 980 990 1000 1010 1020 YGSLEDVLHD PKKAGVKLNW STRRKIAIGS ARGLAFLHHN CSPHIIHRDM KSSNVLLDEN 1030 1040 1050 1060 1070 1080 LEARVSDFGM ARLMSAMDTH LSVSTLAGTP GYVPPEYYQS FRCSTKGDVY SYGVVLLELL 1090 1100 1110 1120 1130 1140 TGKRPTDSPD FGDNNLVGWV KQHAKLRISD VFDPELMKED PALEIELLQH LKVAVACLDD 1150 1160 1170 1180 1190 RAWRRPTMVQ VMAMFKEIQA GSGIDSQSTI RSIEDGGFST IEMVDMSIKE VPEGKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A putative leucine-rich repeat receptor kinase involved in brassinosteroid signal transduction." Li J., Chory J. Cell 90:929-938(1997) [PubMed: 9298904] [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: 10557222] [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. 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: 10938344] [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]	"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: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[5]	"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: 11027724] [Abstract] Cited for: PHOSPHORYLATION, MUTAGENESIS OF LYS-911.
[6]	"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: 10875920] [Abstract] Cited for: STEROID-BINDING.
[7]	"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: 11268216] [Abstract] Cited for: SUBCELLULAR LOCATION, STEROID-BINDING, AUTOPHOSPHORYLATION.
[8]	"BRI1/BAK1, a receptor kinase pair mediating brassinosteroid signaling." Nam K.H., Li J. Cell 110:203-212(2002) [PubMed: 12150928] [Abstract] Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH BAK1.
[9]	"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: 12150929] [Abstract] Cited for: PHOSPHORYLATION, INTERACTION WITH BAK1.
[10]	"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: 15548744] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH BAK1.
[11]	"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: 15319482] [Abstract] Cited for: INTERACTION WITH TTL.
[12]	"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: 15894717] [Abstract] Cited for: PHOSPHORYLATION, INTERACTION WITH BAK1, MUTAGENESIS OF SER-838; THR-842; THR-846; SER-858; THR-872; THR-1039; SER-1044; THR-1045; THR-1049; SER-1168; SER-1172; 1179-SER-THR-1180 AND SER-1187.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF017056 Genomic DNA. Translation: AAC49810.1. AL078620 Genomic DNA. Translation: CAB44675.1. AL161595 Genomic DNA. Translation: CAB80603.1.
IPI	IPI00528172.
PIR	T09356.
RefSeq	NP_195650.1.
UniGene	At.27898 At.69020
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	O22476. 7 interactions.
Proteomic databases
PRIDE	O22476.
Genome annotation databases
GeneID	830095.
GenomeReviews	Gene locus AT4G39400 in contig CT486007_GR.
KEGG	ath:AT4G39400.
NMPDR	fig|3702.1.peg.22077.
Organism-specific databases
GeneFarm	612. 54.
TAIR	At4g39400.
Phylogenomic databases
OMA	O22476. DCRSLIW.
Enzyme and pathway databases
BRENDA	2.7.11.1. 302.
Gene expression databases
ArrayExpress	O22476.
GermOnline	AT4G39400. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR001611. Leu-rich_rpt. IPR013210. Leu-rich_rpt_N. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. [Graphical view]
Pfam	PF00560. LRR_1. 12 hits. PF08263. LRRNT_2. 1 hit. PF00069. Pkinase. 1 hit. [Graphical view]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BRI1_ARATH

Accession

Primary (citable) accession number: O22476

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 28, 2003
Last sequence update:	January 1, 1998
Last modified:	June 16, 2009
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)