Q94F62 (BAK1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1
Short name=AtBAK1
Short name=BRI1-associated receptor kinase 1
EC=2.7.10.1
EC=2.7.11.1

Alternative name(s):
Protein ELONGATED
Somatic embryogenesis receptor kinase 3
Short name=AtSERK3
Somatic embryogenesis receptor-like kinase 3

Gene names

Name:	BAK1
Synonyms:	ELG, SERK3
Ordered Locus Names:	At4g33430
ORF Names:	F17M5.190

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	615 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	Dual specificity kinase acting on both serine/threonine- and tyrosine-containing substrates. Controls the expression of genes associated with innate immunity in the absence of pathogens or elicitors. Involved in brassinosteroid (BR) signal transduction. Phosphorylates BRI1. May be involved in changing the equilibrium between plasma membrane-located BRI1 homodimers and endocytosed BRI1-BAK1 heterodimers. Interaction with MSBP1 stimulates the endocytosis of BAK1 and suppresses brassinosteroid signaling. Acts in pathogen-associated molecular pattern (PAMP)-triggered immunity (PTI) via its interaction with FLS2 and the phosphorylation of BIK1. Involved in programmed cell death (PCD) control. Positively regulates the BR-dependent plant growth pathway and negatively regulates the BR-independent cell-death pathway. Ref.14 Ref.15 Ref.20 Ref.21 Ref.26 Ref.27 Ref.29 Ref.31
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Subunit structure	Monomer. Heterodimer with BRI1 in the endosomes. Component of the SERK1 signaling complex, composed of KAPP, CDC48A, GRF6 or GRF7, SERK1, SERK2, SERK3/BAK1 and BRI1. Interacts with FLS2, the P.syringae AvrPto and hopAB2/AvrPtoB, ERD13, PEPR1 and PEPR2. Interacts (via extracellular region) with MSBP1. Interacts probably with the EF-Tu receptor EFR. Ref.2 Ref.7 Ref.9 Ref.10 Ref.13 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.22 Ref.23 Ref.27 Ref.28 Ref.31
Subcellular location	Cell membrane; Single-pass type I membrane protein. Endosome membrane; Single-pass type I membrane protein. Note: Endocytosis enhanced upon interaction with MSBP1. Ref.2 Ref.7 Ref.9
Tissue specificity	Expressed ubiquitously. Ref.2
Induction	Up-regulated by flagellin and harpin. Ref.27
Domain	Contains one leucine-zipper motif and one pair of conservatively spaced Cys (Cys pair) involved in forming heterodimers. Ref.17
Post-translational modification	Autophosphorylated on Ser-290, Thr-312, Thr-446, Thr-449, Thr-455 and Tyr-610. Probable autophosphorylation on additional Tyr residues. Transphosphorylated by BRI1. It is not sure whether Thr-589 or Ser-595 is the target of the phosphorylation. The phosphorylations on Thr and Tyr are induced by brassinolide. Phosphorylation on Tyr-610 is required for brassinolide signaling, but not for falgellin signaling. Phosphorylation at Ser-286, Ser-290 Thr-446 or Thr-449 is not critical for flagellin signaling. Ref.2 Ref.7 Ref.8 Ref.10 Ref.20 Ref.24 Ref.26 Ref.28 Ref.30 Ref.31
Disruption phenotype	Semidwarfed phenotype, altered leaf morphology and reduced sensitivity to brassinolide and flagellin. Enhanced chlorosis and lesion formation upon pathogen infection. Double mutants bak1-bkk1 are seedling lethal. Ref.2 Ref.14 Ref.16 Ref.27
Miscellaneous	Interaction with BRI1 activates both receptor kinases and the full activation of either receptor kinase requires transphosphorylation by their partners. This interaction in vitro is magnesium dependent. Instantaneous heteromeric complex formation between FLS2 and BAK1 and reciprocal transphosphorylation after binding of the flagellin flg22 ligand to FLS2. The kinase activity is not required for the complex formation. The interaction with the bacterial effectors AvrPto and AvrPtoB/hopAB2 interfers with FLS2 binding and plant immunity.
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Contains 4 LRR (leucine-rich) repeats. Contains 1 protein kinase domain.
Sequence caution	The sequence CAB38801.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB80060.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Cell membrane Endosome Membrane
Coding sequence diversity	Alternative splicing
Domain	Leucine-rich repeat Repeat Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Receptor Serine/threonine-protein kinase Transferase Tyrosine-protein kinase
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	brassinosteroid mediated signaling pathway Inferred from mutant phenotype Ref.21. Source: TAIR cell death Inferred from mutant phenotype Ref.21. Source: TAIR cell growth Inferred from mutant phenotype. Source: TAIR defense response to bacterium Inferred from mutant phenotype Ref.15. Source: TAIR defense response to fungus Inferred from mutant phenotype Ref.15. Source: TAIR defense response to oomycetes Inferred from mutant phenotype Ref.15. 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 Inferred from direct assay. Source: UniProtKB protein complex Inferred from physical interaction Ref.12. Source: TAIR
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein heterodimerization activity Inferred from physical interaction Ref.9. Source: TAIR protein serine/threonine kinase activity Inferred from direct assay Ref.2. Source: TAIR receptor serine/threonine kinase binding Inferred from physical interaction. Source: UniProtKB transmembrane receptor protein tyrosine kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BRI1	O22476	5	EBI-617138,EBI-1797828
BRL1	Q9ZWC8	5	EBI-617138,EBI-590903
FLS2	Q9FL28	3	EBI-617138,EBI-1799448

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q94F62-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 25	25	Potential
	Chain	26 – 615	590	BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1		PRO_0000024304
Regions
	Topological domain	26 – 225	200	Extracellular Potential
	Transmembrane	226 – 246	21	Helical; Potential
	Topological domain	247 – 615	369	Cytoplasmic Potential
	Repeat	93 – 116	24	LRR 1
	Repeat	117 – 140	24	LRR 2
	Repeat	141 – 163	23	LRR 3
	Repeat	165 – 187	23	LRR 4
	Domain	289 – 576	288	Protein kinase
	Nucleotide binding	295 – 303	9	ATP By similarity
	Motif	57 – 64	8	Cys pair
	Compositional bias	191 – 217	27	Pro-rich
Sites
	Active site	416	1	Proton acceptor By similarity
	Binding site	317	1	ATP By similarity
Amino acid modifications
	Modified residue	290	1	Phosphoserine Ref.10 Ref.20 Ref.24
	Modified residue	312	1	Phosphothreonine Ref.20
	Modified residue	446	1	Phosphothreonine Ref.10 Ref.20 Ref.24
	Modified residue	449	1	Phosphothreonine Ref.8 Ref.10 Ref.20 Ref.24
	Modified residue	450	1	Phosphothreonine Ref.8 Ref.20 Ref.24
	Modified residue	455	1	Phosphothreonine Ref.10 Ref.20 Ref.24
	Modified residue	546	1	Phosphothreonine Probable
	Modified residue	589	1	Phosphothreonine Ref.24
	Modified residue	595	1	Phosphoserine Ref.24
	Modified residue	604	1	Phosphoserine Ref.24
	Modified residue	610	1	Phosphotyrosine Ref.30
	Modified residue	612	1	Phosphoserine Ref.24
	Glycosylation	79	1	N-linked (GlcNAc...) Potential
	Glycosylation	103	1	N-linked (GlcNAc...) Potential
	Glycosylation	114	1	N-linked (GlcNAc...) Potential
	Glycosylation	127	1	N-linked (GlcNAc...) Potential
	Glycosylation	149	1	N-linked (GlcNAc...) Potential
	Glycosylation	183	1	N-linked (GlcNAc...) Potential
Experimental info
	Mutagenesis	32	1	L → E: Loss of binding to BRI1, but no effect on kinase activity. Ref.25
	Mutagenesis	46	1	L → E: Loss of binding to BRI1 and loss of kinase activity. Ref.25
	Mutagenesis	64	1	C → Y: No effect. Ref.25
	Mutagenesis	94	1	L → E: No effect. Ref.25
	Mutagenesis	121	1	L → E: No effect. Ref.25
	Mutagenesis	122	1	D → N: Hypersensitivity to brassinosteroids and enhanced high-light phototropism. Ref.11
	Mutagenesis	172	1	S → F: No effect. Ref.25
	Mutagenesis	286	1	S → A: No effect.
	Mutagenesis	286	1	S → D: Loss of kinase activity.
	Mutagenesis	290	1	S → A: No effect.
	Mutagenesis	304	1	Y → F: No effect on autophosphorylation. Ref.30
	Mutagenesis	312	1	T → A: No effect on the kinase activity or on the binding to the FHA domain of KAPP. Ref.17
	Mutagenesis	317	1	K → E: Loss of kinase activity, but no effect on the binding to the FHA domain of KAPP. Ref.2 Ref.17 Ref.25
	Mutagenesis	363	1	Y → F: No effect on autophosphorylation. Ref.30
	Mutagenesis	365	1	Y → F: No effect on autophosphorylation. Ref.30
	Mutagenesis	403	1	Y → F: No effect on autophosphorylation. Ref.30
	Mutagenesis	443	1	Y → F: No effect on autophosphorylation. Ref.30
	Mutagenesis	446	1	T → A or D: No effect. Loss of kinase activity; when associated with D-449 and D-450. Ref.25
	Mutagenesis	449	1	T → A or D: Slight decrease of kinase activity. Loss of kinase activity; when associated with A-446 and D-450. Ref.25
	Mutagenesis	450	1	T → A or D: No effect. Loss of kinase activity; when associated with A-446 and D-449. Ref.25
	Mutagenesis	455	1	T → A, D or E: Loss of kinase activity. Ref.20 Ref.25
	Mutagenesis	463	1	Y → F: Loss of kinase activity. Ref.30
	Mutagenesis	478	1	Y → F: No effect on autophosphorylation. Ref.30
	Mutagenesis	530	1	Y → F: No effect on autophosphorylation. Ref.30
	Mutagenesis	546	1	T → A: 60% decrease of binding to the FHA domain of KAPP. Ref.17
	Mutagenesis	587	1	Y → F: No effect on autophosphorylation. Ref.30
	Mutagenesis	610	1	Y → E: Loss of brassinosteroid signaling but no effect on programmed cell death inhibition. Ref.30
	Mutagenesis	610	1	Y → F: Decreased autophosphorylation on tyrosine, loss of transphosphorylation and activation of BRI1 but no effect on the binding to BRI1. Ref.30
	Sequence conflict	12	1	W → G in AAK68074. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 28, 2003. Version 2. Checksum: 547B3F38FB46E1DD	FASTA	615	68,161
	10 20 30 40 50 60 MERRLMIPCF FWLILVLDLV LRVSGNAEGD ALSALKNSLA DPNKVLQSWD ATLVTPCTWF 70 80 90 100 110 120 HVTCNSDNSV TRVDLGNANL SGQLVMQLGQ LPNLQYLELY SNNITGTIPE QLGNLTELVS 130 140 150 160 170 180 LDLYLNNLSG PIPSTLGRLK KLRFLRLNNN SLSGEIPRSL TAVLTLQVLD LSNNPLTGDI 190 200 210 220 230 240 PVNGSFSLFT PISFANTKLT PLPASPPPPI SPTPPSPAGS NRITGAIAGG VAAGAALLFA 250 260 270 280 290 300 VPAIALAWWR RKKPQDHFFD VPAEEDPEVH LGQLKRFSLR ELQVASDNFS NKNILGRGGF 310 320 330 340 350 360 GKVYKGRLAD GTLVAVKRLK EERTQGGELQ FQTEVEMISM AVHRNLLRLR GFCMTPTERL 370 380 390 400 410 420 LVYPYMANGS VASCLRERPE SQPPLDWPKR QRIALGSARG LAYLHDHCDP KIIHRDVKAA 430 440 450 460 470 480 NILLDEEFEA VVGDFGLAKL MDYKDTHVTT AVRGTIGHIA PEYLSTGKSS EKTDVFGYGV 490 500 510 520 530 540 MLLELITGQR AFDLARLAND DDVMLLDWVK GLLKEKKLEA LVDVDLQGNY KDEEVEQLIQ 550 560 570 580 590 600 VALLCTQSSP MERPKMSEVV RMLEGDGLAE RWEEWQKEEM FRQDFNYPTH HPAVSGWIIG 610 DSTSQIENEY PSGPR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Arabidopsis SOMATIC EMBRYOGENESIS RECEPTOR KINASE 1 gene is expressed in developing ovules and embryos and enhances embryogenic competence in culture." Hecht V.F.G., Vielle-Calzada J.-P., Hartog M.V., Schmidt E.D.L., Boutilier K., Grossniklaus U., de Vries S.C. Plant Physiol. 127:803-816(2001) [PubMed: 11706164] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Landsberg erecta.
[2]	"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: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF LYS-317, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH BRI1, DISRUPTION PHENOTYPE.
[3]	"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: 20064227] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[6]	"Molecular characterisation of two novel maize LRR receptor-like kinases, which belong to the SERK gene family." Baudino S., Hansen S., Brettschneider R., Hecht V.F.G., Dresselhaus T., Loerz H., Dumas C., Rogowsky P.M. Planta 213:1-10(2001) [PubMed: 11523644] [Abstract] Cited for: IDENTIFICATION.
[7]	"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 BRI1.
[8]	"Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database." Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C. Plant Cell 16:2394-2405(2004) [PubMed: 15308754] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-449 AND THR-450, MASS SPECTROMETRY.
[9]	"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 BRI1.
[10]	"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 AT SER-290; THR-446; THR-449 AND THR-455, INTERACTION WITH BRI1.
[11]	"A brassinosteroid-hypersensitive mutant of BAK1 indicates that a convergence of photomorphogenic and hormonal signaling modulates phototropism." Whippo C.W., Hangarter R.P. Plant Physiol. 139:448-457(2005) [PubMed: 16126860] [Abstract] Cited for: MUTAGENESIS OF ASP-122.
[12]	"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: 16473966] [Abstract] Cited for: IDENTIFICATION IN THE SERK1 COMPLEX.
[13]	"The receptor-like kinase SERK3/BAK1 is a central regulator of innate immunity in plants." Heese A., Hann D.R., Gimenez-Ibanez S., Jones A.M.E., He K., Li J., Schroeder J.I., Peck S.C., Rathjen J.P. Proc. Natl. Acad. Sci. U.S.A. 104:12217-12222(2007) [PubMed: 17626179] [Abstract] Cited for: INTERACTION WITH FLS2.
[14]	"BAK1 and BKK1 regulate brassinosteroid-dependent growth and brassinosteroid-independent cell-death pathways." He K., Gou X., Yuan T., Lin H., Asami T., Yoshida S., Russell S.D., Li J. Curr. Biol. 17:1109-1115(2007) [PubMed: 17600708] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[15]	"The BRI1-associated kinase 1, BAK1, has a brassinolide-independent role in plant cell-death control." Kemmerling B., Schwedt A., Rodriguez P., Mazzotta S., Frank M., Qamar S.A., Mengiste T., Betsuyaku S., Parker J.E., Mussig C., Thomma B.P., Albrecht C., de Vries S.C., Hirt H., Nurnberger T. Curr. Biol. 17:1116-1122(2007) [PubMed: 17583510] [Abstract] Cited for: FUNCTION.
[16]	"A flagellin-induced complex of the receptor FLS2 and BAK1 initiates plant defence." Chinchilla D., Zipfel C., Robatzek S., Kemmerling B., Nuernberger T., Jones J.D.G., Felix G., Boller T. Nature 448:497-500(2007) [PubMed: 17625569] [Abstract] Cited for: INTERACTION WITH FLS2, DISRUPTION PHENOTYPE.
[17]	"Phosphoprotein and phosphopeptide interactions with the FHA domain from Arabidopsis kinase-associated protein phosphatase." Ding Z., Wang H., Liang X., Morris E.R., Gallazzi F., Pandit S., Skolnick J., Walker J.C., Van Doren S.R. Biochemistry 46:2684-2696(2007) [PubMed: 17302430] [Abstract] Cited for: MUTAGENESIS OF THR-312; LYS-317 AND THR-546, INTERACTION WITH THE KINASE-INTERACTING FHA DOMAIN OF KAPP.
[18]	"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: 17905839] [Abstract] Cited for: SUBUNIT.
[19]	"Bacterial effectors target the common signaling partner BAK1 to disrupt multiple MAMP receptor-signaling complexes and impede plant immunity." Shan L., He P., Li J., Heese A., Peck S.C., Nurnberger T., Martin G.B., Sheen J. Cell Host Microbe 4:17-27(2008) [PubMed: 18621007] [Abstract] Cited for: INTERACTION WITH PSEUDOMONAS SYRINGAE AVRPTO AND AVRPTOB/HOPAB2.
[20]	"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: 18694562] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION AT SER-286; SER-290; THR-312; THR-446; THR-449; THR-450 AND THR-455, INTERACTION WITH BRI1, MUTAGENESIS OF THR-455.
[21]	"Arabidopsis SOMATIC EMBRYOGENESIS RECEPTOR KINASE proteins serve brassinosteroid-dependent and -independent signaling pathways." Albrecht C., Russinova E., Kemmerling B., Kwaaitaal M., de Vries S.C. Plant Physiol. 148:611-619(2008) [PubMed: 18667726] [Abstract] Cited for: FUNCTION.
[22]	"Modulations of AtGSTF10 expression induce stress tolerance and BAK1-mediated cell death." Ryu H.Y., Kim S.Y., Park H.M., You J.Y., Kim B.H., Lee J.S., Nam K.H. Biochem. Biophys. Res. Commun. 379:417-422(2009) [PubMed: 19118534] [Abstract] Cited for: INTERACTION WITH ERD13.
[23]	"Membrane steroid-binding protein 1 (MSBP1) negatively regulates brassinosteroid signaling by enhancing the endocytosis of BAK1." Song L., Shi Q.M., Yang X.H., Xu Z.H., Xue H.W. Cell Res. 19:864-876(2009) [PubMed: 19532123] [Abstract] Cited for: INTERACTION WITH MSBP1.
[24]	"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: 19105183] [Abstract] Cited for: AUTOPHOSPHORYLATION, PHOSPHORYLATION AT SER-290; THR-446; THR-449; THR-450; THR-455; THR-589; SER-595; SER-604 AND SER-612.
[25]	"Analysis of phosphorylation of the BRI1/BAK1 complex in arabidopsis reveals amino acid residues critical for receptor formation and activation of BR signaling." Yun H.S., Bae Y.H., Lee Y.J., Chang S.C., Kim S.-K., Li J., Nam K.H. Mol. Cells 27:183-190(2009) [PubMed: 19277500] [Abstract] Cited for: MUTAGENESIS OF LEU-32; LEU-46; CYS-64; LEU-94; LEU-121; SER-172; LYS-317; THR-446; THR-449; THR-450 AND THR-455.
[26]	"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: 19124768] [Abstract] Cited for: FUNCTION, AUTOPHOSPHORYLATION.
[27]	"The multifunctional leucine-rich repeat receptor kinase BAK1 is implicated in Arabidopsis development and immunity." Postel S., Kuefner I., Beuter C., Mazzotta S., Schwedt A., Borlotti A., Halter T., Kemmerling B., Nuernberger T. Eur. J. Cell Biol. 89:169-174(2010) [PubMed: 20018402] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY FLAGELLIN AND HARPIN, INTERACTION WITH PEPR1 AND PEPR2.
[28]	"Rapid heteromerization and phosphorylation of ligand-activated plant transmembrane receptors and their associated kinase BAK1." Schulze B., Mentzel T., Jehle A.K., Mueller K., Beeler S., Boller T., Felix G., Chinchilla D. J. Biol. Chem. 285:9444-9451(2010) [PubMed: 20103591] [Abstract] Cited for: INTERACTION WITH FLS2, PHOSPHORYLATION.
[29]	"Phosphorylation of receptor-like cytoplasmic kinases by bacterial flagellin." Lu D., Wu S., He P., Shan L. Plant Signal. Behav. 5:598-600(2010) [PubMed: 20404519] [Abstract] Cited for: FUNCTION.
[30]	"Autophosphorylation of Tyr-610 in the receptor kinase BAK1 plays a role in brassinosteroid signaling and basal defense gene expression." Oh M.H., Wang X., Wu X., Zhao Y., Clouse S.D., Huber S.C. Proc. Natl. Acad. Sci. U.S.A. 107:17827-17832(2010) [PubMed: 20876109] [Abstract] Cited for: MUTAGENESIS OF TYR-304; TYR-363; TYR-365; TYR-403; TYR-443; TYR-463; TYR-478; TYR-530; TYR-587 AND TYR-610, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT TYR-610.
[31]	"Functional importance of BAK1 tyrosine phosphorylation in vivo." Oh M.H., Wu X., Clouse S.D., Huber S.C. Plant Signal. Behav. 6:400-405(2011) [PubMed: 21350342] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH BRI1.
+	Additional computationally mapped references.

Web resources

PlantP kinase Classification PPC

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF384970 mRNA. Translation: AAK68074.1. FJ708762 mRNA. Translation: ACN59355.1. AL035678 Genomic DNA. Translation: CAB38801.1. Sequence problems. AL161583 Genomic DNA. Translation: CAB80060.1. Sequence problems. CP002687 Genomic DNA. Translation: AEE86223.1.
IPI	IPI00519519.
PIR	T05994.
RefSeq	NP_567920.1. NM_119497.4.
UniGene	At.376.
3D structure databases
ProteinModelPortal	Q94F62.
SMR	Q94F62. Positions 25-202, 279-566.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-34976N.
IntAct	Q94F62. 7 interactions.
STRING	Q94F62.
Proteomic databases
PRIDE	Q94F62.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G33430.1; AT4G33430.1; AT4G33430.
GeneID	829480.
GenomeReviews	Gene locus AT4G33430 in contig CT486007_GR.
KEGG	ath:AT4G33430.
NMPDR	fig|3702.1.peg.21385.
Organism-specific databases
GeneFarm	511. 46.
TAIR	At4g33430.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	EPGT00070000028183.
HOGENOM	HBG755340.
InParanoid	Q94F62.
OMA	LKEERTQ.
PhylomeDB	Q94F62.
ProtClustDB	CLSN2689734.
Gene expression databases
ArrayExpress	Q94F62.
Genevestigator	Q94F62.
GermOnline	AT4G33430. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR013320. ConA-like_subgrp. IPR011009. Kinase-like_dom. IPR001611. Leu-rich_rpt. IPR013210. LRR-contain_N2. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_kinase-like_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Gene3D	G3DSA:2.60.120.200. ConA_like_subgrp. 1 hit.
KO	K13416.
Pfam	PF00560. LRR_1. 3 hits. PF08263. LRRNT_2. 1 hit. PF00069. Pkinase. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
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

BAK1_ARATH

Accession

Primary (citable) accession number: Q94F62
Secondary accession number(s): C0LGS0, Q9SZC0

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 28, 2003
Last sequence update:	March 28, 2003
Last modified:	December 14, 2011
This is version 106 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program