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BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1BAK1Arabidopsis thaliana (Mouse-ear cress)-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveliFunctioniDual 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 interactions with FLS2 and EFR, 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 (PubMed:, PubMed:, PubMed:, PubMed:, PubMed:, PubMed:, PubMed:, PubMed:, PubMed:). Phosphorylates BIR2 and thus promotes interaction with BIR2 (PubMed:, PubMed:). This interaction prevents interaction with FLS2 in the absence of pathogen-associated molecular patterns (PAMP) (PubMed:, PubMed:). Required for PSK promotion of seedling growth and protoplast expansion (PubMed:). CNGC17 and AHAs form a functional cation-translocating unit that is activated by PSKR1/BAK1 and possibly other BAK1/RLK complexes (PubMed:).Manual assertion based on experiment ini"BAK1 and BKK1 regulate brassinosteroid-dependent growth and brassinosteroid-independent cell-death pathways.", , , , , , ,
[] [] []Cited for: FUNCTION, DISRUPTION PHENOTYPE."The BRI1-associated kinase 1, BAK1, has a brassinolide-independent role in plant cell-death control.", , , , , , , , , , , , , ,
[] [] []Cited for: FUNCTION."Sequential transphosphorylation of the BRI1/BAK1 receptor kinase complex impacts early events in brassinosteroid signaling.", , , , , , ,
[] [] []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."Arabidopsis SOMATIC EMBRYOGENESIS RECEPTOR KINASE proteins serve brassinosteroid-dependent and -independent signaling pathways.", , , ,
[] [] []Cited for: FUNCTION."Tyrosine phosphorylation of the BRI1 receptor kinase emerges as a component of brassinosteroid signaling in Arabidopsis.", , , , ,
[] [] []Cited for: FUNCTION, AUTOPHOSPHORYLATION."The multifunctional leucine-rich repeat receptor kinase BAK1 is implicated in Arabidopsis development and immunity.", , , , , , , ,
[] [] []Cited for: FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY FLAGELLIN AND HARPIN, INTERACTION WITH PEPR1 AND PEPR2."Phosphorylation of receptor-like cytoplasmic kinases by bacterial flagellin.", , ,
[] [] []Cited for: FUNCTION."The Arabidopsis leucine-rich repeat receptor-like kinases BAK1/SERK3 and BKK1/SERK4 are required for innate immunity to hemibiotrophic and biotrophic pathogens.", , , , , , , , ,
[] [] []Cited for: FUNCTION, INTERACTION WITH EFR AND FLS2."Functional importance of BAK1 tyrosine phosphorylation in vivo.", , ,
[] [] []Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH BRI1."The leucine-rich repeat receptor kinase BIR2 is a negative regulator of BAK1 in plant immunity.", , , , , , , , , , , , , , , , ,
[] [] []Cited for: FUNCTION, MUTAGENESIS OF SER-290; THR-312; LYS-317; THR-446; THR-449; THR-450 AND THR-455, INTERACTION WITH BIR2, AUTOPHOSPHORYLATION."Structure of the pseudokinase domain of BIR2, a regulator of BAK1-mediated immune signaling in Arabidopsis.", , , , , ,
[] [] []Cited for: FUNCTION, INTERACTION WITH BIR2."Phytosulfokine regulates growth in Arabidopsis through a response module at the plasma membrane that includes CYCLIC NUCLEOTIDE-GATED CHANNEL17, H+-ATPase, and BAK1.", , , , ,
[] [] []Cited for: FUNCTION, INTERACTION WITH CNGC17 AND PSKR1, SUBCELLULAR LOCATION.MiscellaneousInteraction 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.Phosphorylated residues T-450 and T-455 have stronger functional effects than other phosphorylated residues by interacting with both the catalytic and activation loops to achieve a conformational stability, locking BAK1 kinase in the active conformation.Manual assertion inferred by curator fromi"Structural basis for the impact of phosphorylation on the activation of plant receptor-like kinase BAK1.", , , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF
IN COMPLEX WITH ATP ANALOG, PHOSPHORYLATION AT SER-290; THR-312; THR-446; THR-449; THR-450 AND THR-455, MUTAGENESIS OF TYR-363; ASP-416; ASN-421; LYS-439; THR-450; ARG-453 AND HIS-458.Catalytic activityiATP + a protein = ADP + a phosphoprotein.ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.Manual assertion according to rulesiSitesFeature keyPosition(s)DescriptionActionsGraphical viewLengthBinding siteiflg22Manual assertion based on experiment ini"Structural basis for flg22-induced activation of the Arabidopsis FLS2-BAK1 immune complex.", , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (3.06 ANGSTROMS) OF
IN COMPLEX WITH FLS2 AND FLG22, DISULFIDE BONDS, SUBUNIT, MUTAGENESIS OF ASP-30; PHE-60; TYR-96 AND PHE-144.1Binding siteiflg22; via amide nitrogenManual assertion based on experiment ini"Structural basis for flg22-induced activation of the Arabidopsis FLS2-BAK1 immune complex.", , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (3.06 ANGSTROMS) OF
IN COMPLEX WITH FLS2 AND FLG22, DISULFIDE BONDS, SUBUNIT, MUTAGENESIS OF ASP-30; PHE-60; TYR-96 AND PHE-144.1Binding siteiATP; via carbonyl oxygenManual assertion based on experiment ini"Structural basis for the impact of phosphorylation on the activation of plant receptor-like kinase BAK1.", , , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF
IN COMPLEX WITH ATP ANALOG, PHOSPHORYLATION AT SER-290; THR-312; THR-446; THR-449; THR-450 AND THR-455, MUTAGENESIS OF TYR-363; ASP-416; ASN-421; LYS-439; THR-450; ARG-453 AND HIS-458.1Binding siteiATPManual assertion according to rulesi1Active siteiProton acceptorManual assertion according to rulesi1Binding siteiATPManual assertion based on experiment ini"Structural basis for the impact of phosphorylation on the activation of plant receptor-like kinase BAK1.", , , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF
IN COMPLEX WITH ATP ANALOG, PHOSPHORYLATION AT SER-290; THR-312; THR-446; THR-449; THR-450 AND THR-455, MUTAGENESIS OF TYR-363; ASP-416; ASN-421; LYS-439; THR-450; ARG-453 AND HIS-458.1RegionsFeature keyPosition(s)DescriptionActionsGraphical viewLengthNucleotide bindingiATPManual assertion according to rulesi9Nucleotide bindingiATPManual assertion based on experiment ini"Structural basis for the impact of phosphorylation on the activation of plant receptor-like kinase BAK1.", , , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF
IN COMPLEX WITH ATP ANALOG, PHOSPHORYLATION AT SER-290; THR-312; THR-446; THR-449; THR-450 AND THR-455, MUTAGENESIS OF TYR-363; ASP-416; ASN-421; LYS-439; THR-450; ARG-453 AND HIS-458.3GO - Molecular functioniInferred from physical interactioniGO - Biological processiKeywordsiMolecular function, , , , Ligand, Names & TaxonomyiProtein namesiRecommended name:BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1Manual assertion based on opinion ini"BAK1, an Arabidopsis LRR receptor-like protein kinase, interacts with BRI1 and modulates brassinosteroid signaling.", , , , ,
[] [] []Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF LYS-317, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH BRI1, DISRUPTION PHENOTYPE. (EC:, EC:)Short name: AtBAK1Manual assertion based on opinion ini"BAK1, an Arabidopsis LRR receptor-like protein kinase, interacts with BRI1 and modulates brassinosteroid signaling.", , , , ,
[] [] []Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF LYS-317, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH BRI1, DISRUPTION PHENOTYPE.Short name: BRI1-associated receptor kinase 1Manual assertion based on opinion ini"BAK1, an Arabidopsis LRR receptor-like protein kinase, interacts with BRI1 and modulates brassinosteroid signaling.", , , , ,
[] [] []Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF LYS-317, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH BRI1, DISRUPTION PHENOTYPE.Alternative name(s):Protein ELONGATEDSomatic embryogenesis receptor kinase 3Manual assertion based on opinion ini"The Arabidopsis SOMATIC EMBRYOGENESIS RECEPTOR KINASE 1 gene is expressed in developing ovules and embryos and enhances embryogenic competence in culture.", , , , , ,
[] [] []Cited for: NUCLEOTIDE SEQUENCE [MRNA].Short name: AtSERK3Manual assertion based on opinion ini"The Arabidopsis SOMATIC EMBRYOGENESIS RECEPTOR KINASE 1 gene is expressed in developing ovules and embryos and enhances embryogenic competence in culture.", , , , , ,
[] [] []Cited for: NUCLEOTIDE SEQUENCE [MRNA].Somatic embryogenesis receptor-like kinase 3Manual assertion based on opinion ini"The Arabidopsis SOMATIC EMBRYOGENESIS RECEPTOR KINASE 1 gene is expressed in developing ovules and embryos and enhances embryogenic competence in culture.", , , , , ,
[] [] []Cited for: NUCLEOTIDE SEQUENCE [MRNA].Gene namesiName:BAK1Manual assertion based on opinion ini"BAK1, an Arabidopsis LRR receptor-like protein kinase, interacts with BRI1 and modulates brassinosteroid signaling.", , , , ,
[] [] []Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF LYS-317, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH BRI1, DISRUPTION PHENOTYPE.Synonyms:ELG, SERK3Manual assertion based on opinion ini"The Arabidopsis SOMATIC EMBRYOGENESIS RECEPTOR KINASE 1 gene is expressed in developing ovules and embryos and enhances embryogenic competence in culture.", , , , , ,
[] [] []Cited for: NUCLEOTIDE SEQUENCE [MRNA].Ordered Locus Names:At4g33430Manual assertion inferred from database entriesiORF Names:F17M5.190Manual assertion inferred from database entriesiOrganismiTaxonomic identifieri
[]Taxonomic lineagei >
Proteomesi Componenti: Chromosome 4 Organism-specific databasesAraporti Subcellular locationi
Extracellular region or secreted
Plasma membrane
Cytoskeleton
Chloroplast
Peroxisome
Golgi apparatus
Mitochondrion
Manual annotation
Automatic computational assertion
Graphics by Christian S Source:
"Phytosulfokine regulates growth in Arabidopsis through a response module at the plasma membrane that includes CYCLIC NUCLEOTIDE-GATED CHANNEL17, H+-ATPase, and BAK1.", , , , ,
[] [] []Cited for: FUNCTION, INTERACTION WITH CNGC17 AND PSKR1, SUBCELLULAR LOCATION.; Note: Endocytosis enhanced upon interaction with MSBP1.TopologyFeature keyPosition(s)DescriptionActionsGraphical viewLengthTopological domainiExtracellular 200TransmembraneiHelical 21Topological domainiCytoplasmic 369Keywords - Cellular componenti, , Pathology & BiotechiDisruption phenotypeiSemi-dwarfed phenotype, altered leaf morphology and reduced sensitivity to brassinolide and flagellin. Enhanced chlorosis and lesion formation upon pathogen infection. Bak1 and bkk1 double mutants are seedling lethal.Manual assertion based on experiment ini"BAK1, an Arabidopsis LRR receptor-like protein kinase, interacts with BRI1 and modulates brassinosteroid signaling.", , , , ,
[] [] []Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF LYS-317, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH BRI1, DISRUPTION PHENOTYPE."BAK1 and BKK1 regulate brassinosteroid-dependent growth and brassinosteroid-independent cell-death pathways.", , , , , , ,
[] [] []Cited for: FUNCTION, DISRUPTION PHENOTYPE."A flagellin-induced complex of the receptor FLS2 and BAK1 initiates plant defence.", , , , , , ,
[] [] []Cited for: INTERACTION WITH FLS2, DISRUPTION PHENOTYPE."The multifunctional leucine-rich repeat receptor kinase BAK1 is implicated in Arabidopsis development and immunity.", , , , , , , ,
[] [] []Cited for: FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY FLAGELLIN AND HARPIN, INTERACTION WITH PEPR1 AND PEPR2.MutagenesisPTM / ProcessingiMolecule processingFeature keyPosition(s)DescriptionActionsGraphical viewLengthSignal peptidei 25ChainiPRO_BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1 590Amino acid modificationsFeature keyPosition(s)DescriptionActionsGraphical viewLengthDisulfide bondiManual assertion based on experiment ini"Structural basis for flg22-induced activation of the Arabidopsis FLS2-BAK1 immune complex.", , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (3.06 ANGSTROMS) OF
IN COMPLEX WITH FLS2 AND FLG22, DISULFIDE BONDS, SUBUNIT, MUTAGENESIS OF ASP-30; PHE-60; TYR-96 AND PHE-144."Structural insight into BL-induced activation of the BRI1-BAK1 complex.", , Submitted (AUG-2013) to the PDB data bankCited for: X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) OF
IN COMPLEX WITH BRASSINOLIDE, DISULFIDE BONDS.GlycosylationiN-linked (GlcNAc...) asparagine1GlycosylationiN-linked (GlcNAc...) asparagine1GlycosylationiN-linked (GlcNAc...) asparagine1GlycosylationiN-linked (GlcNAc...) asparagine1GlycosylationiN-linked (GlcNAc...) asparagine1GlycosylationiN-linked (GlcNAc...) asparagine1Modified residueiPhosphoserineManual assertion based on experiment ini"Sequential transphosphorylation of the BRI1/BAK1 receptor kinase complex impacts early events in brassinosteroid signaling.", , , , , , ,
[] [] []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-455.1Modified residueiPhosphoserineManual assertion based on experiment ini"Identification and functional analysis of in vivo phosphorylation sites of the Arabidopsis BRASSINOSTEROID-INSENSITIVE1 receptor kinase.", , , , , , , , ,
[] [] []Cited for: PHOSPHORYLATION AT SER-290; THR-446; THR-449 AND THR-455, INTERACTION WITH BRI1."Sequential transphosphorylation of the BRI1/BAK1 receptor kinase complex impacts early events in brassinosteroid signaling.", , , , , , ,
[] [] []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."Identification of in vitro phosphorylation sites in the Arabidopsis thaliana somatic embryogenesis receptor-like kinases.", , , , , ,
[] [] []Cited for: AUTOPHOSPHORYLATION, PHOSPHORYLATION AT SER-290; THR-446; THR-449; THR-450; THR-455; THR-589; SER-595; SER-604 AND SER-612."Structural basis for the impact of phosphorylation on the activation of plant receptor-like kinase BAK1.", , , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF
IN COMPLEX WITH ATP ANALOG, PHOSPHORYLATION AT SER-290; THR-312; THR-446; THR-449; THR-450 AND THR-455, MUTAGENESIS OF TYR-363; ASP-416; ASN-421; LYS-439; THR-450; ARG-453 AND HIS-458.1Modified residueiPhosphothreonineManual assertion based on experiment ini"Sequential transphosphorylation of the BRI1/BAK1 receptor kinase complex impacts early events in brassinosteroid signaling.", , , , , , ,
[] [] []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."Structural basis for the impact of phosphorylation on the activation of plant receptor-like kinase BAK1.", , , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF
IN COMPLEX WITH ATP ANALOG, PHOSPHORYLATION AT SER-290; THR-312; THR-446; THR-449; THR-450 AND THR-455, MUTAGENESIS OF TYR-363; ASP-416; ASN-421; LYS-439; THR-450; ARG-453 AND HIS-458.1Modified residueiPhosphoserineManual assertion inferred from sequence similarity toi1Modified residueiPhosphoserineManual assertion inferred from sequence similarity toi1Modified residueiPhosphothreonineManual assertion based on experiment ini"Identification and functional analysis of in vivo phosphorylation sites of the Arabidopsis BRASSINOSTEROID-INSENSITIVE1 receptor kinase.", , , , , , , , ,
[] [] []Cited for: PHOSPHORYLATION AT SER-290; THR-446; THR-449 AND THR-455, INTERACTION WITH BRI1."Sequential transphosphorylation of the BRI1/BAK1 receptor kinase complex impacts early events in brassinosteroid signaling.", , , , , , ,
[] [] []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."Identification of in vitro phosphorylation sites in the Arabidopsis thaliana somatic embryogenesis receptor-like kinases.", , , , , ,
[] [] []Cited for: AUTOPHOSPHORYLATION, PHOSPHORYLATION AT SER-290; THR-446; THR-449; THR-450; THR-455; THR-589; SER-595; SER-604 AND SER-612."Structural analysis of Pseudomonas syringae AvrPtoB bound to host BAK1 reveals two similar kinase-interacting domains in a type III Effector.", , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF
IN COMPLEX WITH HOPAB2/AVRPTOB, PHOSPHORYLATION AT THR-446; THR-449 AND THR-450, MUTAGENESIS OF LYS-317; THR-449; THR-450; ALA-451; VAL-452; THR-455; ILE-456; HIS-458; LEU-464 AND ALA-495."Structural basis for the impact of phosphorylation on the activation of plant receptor-like kinase BAK1.", , , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF
IN COMPLEX WITH ATP ANALOG, PHOSPHORYLATION AT SER-290; THR-312; THR-446; THR-449; THR-450 AND THR-455, MUTAGENESIS OF TYR-363; ASP-416; ASN-421; LYS-439; THR-450; ARG-453 AND HIS-458.1Modified residueiPhosphothreonineManual assertion based on experiment ini"Identification and functional analysis of in vivo phosphorylation sites of the Arabidopsis BRASSINOSTEROID-INSENSITIVE1 receptor kinase.", , , , , , , , ,
[] [] []Cited for: PHOSPHORYLATION AT SER-290; THR-446; THR-449 AND THR-455, INTERACTION WITH BRI1."Sequential transphosphorylation of the BRI1/BAK1 receptor kinase complex impacts early events in brassinosteroid signaling.", , , , , , ,
[] [] []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."Identification of in vitro phosphorylation sites in the Arabidopsis thaliana somatic embryogenesis receptor-like kinases.", , , , , ,
[] [] []Cited for: AUTOPHOSPHORYLATION, PHOSPHORYLATION AT SER-290; THR-446; THR-449; THR-450; THR-455; THR-589; SER-595; SER-604 AND SER-612."Structural analysis of Pseudomonas syringae AvrPtoB bound to host BAK1 reveals two similar kinase-interacting domains in a type III Effector.", , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF
IN COMPLEX WITH HOPAB2/AVRPTOB, PHOSPHORYLATION AT THR-446; THR-449 AND THR-450, MUTAGENESIS OF LYS-317; THR-449; THR-450; ALA-451; VAL-452; THR-455; ILE-456; HIS-458; LEU-464 AND ALA-495."Structural basis for the impact of phosphorylation on the activation of plant receptor-like kinase BAK1.", , , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF
IN COMPLEX WITH ATP ANALOG, PHOSPHORYLATION AT SER-290; THR-312; THR-446; THR-449; THR-450 AND THR-455, MUTAGENESIS OF TYR-363; ASP-416; ASN-421; LYS-439; THR-450; ARG-453 AND HIS-458.1Modified residueiPhosphothreonineManual assertion based on experiment ini"Sequential transphosphorylation of the BRI1/BAK1 receptor kinase complex impacts early events in brassinosteroid signaling.", , , , , , ,
[] [] []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."Identification of in vitro phosphorylation sites in the Arabidopsis thaliana somatic embryogenesis receptor-like kinases.", , , , , ,
[] [] []Cited for: AUTOPHOSPHORYLATION, PHOSPHORYLATION AT SER-290; THR-446; THR-449; THR-450; THR-455; THR-589; SER-595; SER-604 AND SER-612."Structural analysis of Pseudomonas syringae AvrPtoB bound to host BAK1 reveals two similar kinase-interacting domains in a type III Effector.", , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF
IN COMPLEX WITH HOPAB2/AVRPTOB, PHOSPHORYLATION AT THR-446; THR-449 AND THR-450, MUTAGENESIS OF LYS-317; THR-449; THR-450; ALA-451; VAL-452; THR-455; ILE-456; HIS-458; LEU-464 AND ALA-495."Structural basis for the impact of phosphorylation on the activation of plant receptor-like kinase BAK1.", , , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF
IN COMPLEX WITH ATP ANALOG, PHOSPHORYLATION AT SER-290; THR-312; THR-446; THR-449; THR-450 AND THR-455, MUTAGENESIS OF TYR-363; ASP-416; ASN-421; LYS-439; THR-450; ARG-453 AND HIS-458.1Modified residueiPhosphothreonineManual assertion based on experiment ini"Identification and functional analysis of in vivo phosphorylation sites of the Arabidopsis BRASSINOSTEROID-INSENSITIVE1 receptor kinase.", , , , , , , , ,
[] [] []Cited for: PHOSPHORYLATION AT SER-290; THR-446; THR-449 AND THR-455, INTERACTION WITH BRI1."Sequential transphosphorylation of the BRI1/BAK1 receptor kinase complex impacts early events in brassinosteroid signaling.", , , , , , ,
[] [] []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."Identification of in vitro phosphorylation sites in the Arabidopsis thaliana somatic embryogenesis receptor-like kinases.", , , , , ,
[] [] []Cited for: AUTOPHOSPHORYLATION, PHOSPHORYLATION AT SER-290; THR-446; THR-449; THR-450; THR-455; THR-589; SER-595; SER-604 AND SER-612."Structural basis for the impact of phosphorylation on the activation of plant receptor-like kinase BAK1.", , , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF
IN COMPLEX WITH ATP ANALOG, PHOSPHORYLATION AT SER-290; THR-312; THR-446; THR-449; THR-450 AND THR-455, MUTAGENESIS OF TYR-363; ASP-416; ASN-421; LYS-439; THR-450; ARG-453 AND HIS-458.1Modified residueiPhosphotyrosineManual assertion inferred from sequence similarity toi1Modified residueiPhosphoserineManual assertion inferred from sequence similarity toi1Modified residueiPhosphothreonineManual assertion inferred from sequence similarity toi1Modified residueiPhosphoserineManual assertion inferred from sequence similarity toi1Modified residueiPhosphothreonineManual assertion inferred from sequence similarity toi1Modified residueiPhosphothreonineManual assertion based on experiment ini"Identification of in vitro phosphorylation sites in the Arabidopsis thaliana somatic embryogenesis receptor-like kinases.", , , , , ,
[] [] []Cited for: AUTOPHOSPHORYLATION, PHOSPHORYLATION AT SER-290; THR-446; THR-449; THR-450; THR-455; THR-589; SER-595; SER-604 AND SER-612.1Modified residueiPhosphoserineManual assertion based on experiment ini"Identification of in vitro phosphorylation sites in the Arabidopsis thaliana somatic embryogenesis receptor-like kinases.", , , , , ,
[] [] []Cited for: AUTOPHOSPHORYLATION, PHOSPHORYLATION AT SER-290; THR-446; THR-449; THR-450; THR-455; THR-589; SER-595; SER-604 AND SER-612.1Modified residueiPhosphoserineManual assertion based on experiment ini"Identification of in vitro phosphorylation sites in the Arabidopsis thaliana somatic embryogenesis receptor-like kinases.", , , , , ,
[] [] []Cited for: AUTOPHOSPHORYLATION, PHOSPHORYLATION AT SER-290; THR-446; THR-449; THR-450; THR-455; THR-589; SER-595; SER-604 AND SER-612.1Modified residueiPhosphotyrosineManual assertion based on experiment ini"Autophosphorylation of Tyr-610 in the receptor kinase BAK1 plays a role in brassinosteroid signaling and basal defense gene expression.", , , , ,
[] [] []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-610.1Modified residueiPhosphoserineManual assertion based on experiment ini"Identification of in vitro phosphorylation sites in the Arabidopsis thaliana somatic embryogenesis receptor-like kinases.", , , , , ,
[] [] []Cited for: AUTOPHOSPHORYLATION, PHOSPHORYLATION AT SER-290; THR-446; THR-449; THR-450; THR-455; THR-589; SER-595; SER-604 AND SER-612.1Post-translational modificationiAutophosphorylated 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 flagellin signaling. Phosphorylation at Ser-286, Ser-290 Thr-446 or Thr-449 is not critical for flagellin signaling.Manual assertion based on experiment ini"BAK1, an Arabidopsis LRR receptor-like protein kinase, interacts with BRI1 and modulates brassinosteroid signaling.", , , , ,
[] [] []Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF LYS-317, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH BRI1, DISRUPTION PHENOTYPE."BRI1/BAK1, a receptor kinase pair mediating brassinosteroid signaling.",
[] [] []Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH BRI1."Identification and functional analysis of in vivo phosphorylation sites of the Arabidopsis BRASSINOSTEROID-INSENSITIVE1 receptor kinase.", , , , , , , , ,
[] [] []Cited for: PHOSPHORYLATION AT SER-290; THR-446; THR-449 AND THR-455, INTERACTION WITH BRI1."Sequential transphosphorylation of the BRI1/BAK1 receptor kinase complex impacts early events in brassinosteroid signaling.", , , , , , ,
[] [] []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."Identification of in vitro phosphorylation sites in the Arabidopsis thaliana somatic embryogenesis receptor-like kinases.", , , , , ,
[] [] []Cited for: AUTOPHOSPHORYLATION, PHOSPHORYLATION AT SER-290; THR-446; THR-449; THR-450; THR-455; THR-589; SER-595; SER-604 AND SER-612."Rapid heteromerization and phosphorylation of ligand-activated plant transmembrane receptors and their associated kinase BAK1.", , , , , , ,
[] [] []Cited for: INTERACTION WITH FLS2, PHOSPHORYLATION."Autophosphorylation of Tyr-610 in the receptor kinase BAK1 plays a role in brassinosteroid signaling and basal defense gene expression.", , , , ,
[] [] []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."Functional importance of BAK1 tyrosine phosphorylation in vivo.", , ,
[] [] []Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH BRI1."The leucine-rich repeat receptor kinase BIR2 is a negative regulator of BAK1 in plant immunity.", , , , , , , , , , , , , , , , ,
[] [] []Cited for: FUNCTION, MUTAGENESIS OF SER-290; THR-312; LYS-317; THR-446; THR-449; THR-450 AND THR-455, INTERACTION WITH BIR2, AUTOPHOSPHORYLATION.Keywords - PTMi, , Proteomic databasesPRIDEi PTM databasesiPTMneti ExpressioniTissue specificityiExpressed ubiquitously.Manual assertion based on experiment ini"BAK1, an Arabidopsis LRR receptor-like protein kinase, interacts with BRI1 and modulates brassinosteroid signaling.", , , , ,
[] [] []Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF LYS-317, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH BRI1, DISRUPTION PHENOTYPE.InductioniUp-regulated by flagellin and harpin.Manual assertion based on experiment ini"The multifunctional leucine-rich repeat receptor kinase BAK1 is implicated in Arabidopsis development and immunity.", , , , , , , ,
[] [] []Cited for: FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY FLAGELLIN AND HARPIN, INTERACTION WITH PEPR1 AND PEPR2.Gene expression databasesExpressionAtlasi baseline and differential. Genevisiblei AT. InteractioniSubunit structureiInteracts constitutively with BIR2, thereby preventing interaction with the ligand-binding LRR-RLK FLS2. Upon infection, pathogen-associated molecular patterns (PAMP) perception leads to BIR2 release from the BAK1 complex and enables the recruitment of BAK1 into the FLS2 complex (PubMed:, PubMed:). Heterodimer with FLS2 (PubMed:). 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 the P.syringae AvrPto and hopAB2/AvrPtoB, ERD13, PEPR1 and PEPR2. Interacts (via extracellular region) with MSBP1. Interacts with the EF-Tu receptor EFR and FLS2 in a specific ligand-induced manner. Interacts with TMK4/BARK1. Part of a functional complex containing PSKR1, BAK1, CNGC17, and AHA (PubMed:). Interacts with CNGC17 and PSKR1 (PubMed:). Binds to IOS1 which triggers FLS2-BAK1 complex formation upon microbe-associated molecular patterns (MAMPs) treatment (PubMed:).Manual assertion based on experiment ini"BAK1, an Arabidopsis LRR receptor-like protein kinase, interacts with BRI1 and modulates brassinosteroid signaling.", , , , ,
[] [] []Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF LYS-317, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH BRI1, DISRUPTION PHENOTYPE."BRI1/BAK1, a receptor kinase pair mediating brassinosteroid signaling.",
[] [] []Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH BRI1."Heterodimerization and endocytosis of Arabidopsis brassinosteroid receptors BRI1 and AtSERK3 (BAK1).", , , , , ,
[] [] []Cited for: SUBCELLULAR LOCATION, INTERACTION WITH BRI1."Identification and functional analysis of in vivo phosphorylation sites of the Arabidopsis BRASSINOSTEROID-INSENSITIVE1 receptor kinase.", , , , , , , , ,
[] [] []Cited for: PHOSPHORYLATION AT SER-290; THR-446; THR-449 AND THR-455, INTERACTION WITH BRI1."The Arabidopsis SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE1 protein complex includes BRASSINOSTEROID-INSENSITIVE1.", , , , ,
[] [] []Cited for: IDENTIFICATION IN THE SERK1 COMPLEX."The receptor-like kinase SERK3/BAK1 is a central regulator of innate immunity in plants.", , , , , , , ,
[] [] []Cited for: INTERACTION WITH FLS2."A flagellin-induced complex of the receptor FLS2 and BAK1 initiates plant defence.", , , , , , ,
[] [] []Cited for: INTERACTION WITH FLS2, DISRUPTION PHENOTYPE."Phosphoprotein and phosphopeptide interactions with the FHA domain from Arabidopsis kinase-associated protein phosphatase.", , , , , , , ,
[] [] []Cited for: MUTAGENESIS OF THR-312; LYS-317 AND THR-546, INTERACTION WITH THE KINASE-INTERACTING FHA DOMAIN OF KAPP."Fluorescence fluctuation analysis of Arabidopsis thaliana somatic embryogenesis receptor-like kinase and brassinosteroid insensitive 1 receptor oligomerization.", , , ,
[] [] []Cited for: SUBUNIT."Bacterial effectors target the common signaling partner BAK1 to disrupt multiple MAMP receptor-signaling complexes and impede plant immunity.", , , , , , ,
[] [] []Cited for: INTERACTION WITH PSEUDOMONAS SYRINGAE AVRPTO AND AVRPTOB/HOPAB2."Sequential transphosphorylation of the BRI1/BAK1 receptor kinase complex impacts early events in brassinosteroid signaling.", , , , , , ,
[] [] []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."Modulations of AtGSTF10 expression induce stress tolerance and BAK1-mediated cell death.", , , , , ,
[] [] []Cited for: INTERACTION WITH ERD13."Membrane steroid-binding protein 1 (MSBP1) negatively regulates brassinosteroid signaling by enhancing the endocytosis of BAK1.", , , ,
[] [] []Cited for: INTERACTION WITH MSBP1."The multifunctional leucine-rich repeat receptor kinase BAK1 is implicated in Arabidopsis development and immunity.", , , , , , , ,
[] [] []Cited for: FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY FLAGELLIN AND HARPIN, INTERACTION WITH PEPR1 AND PEPR2."Rapid heteromerization and phosphorylation of ligand-activated plant transmembrane receptors and their associated kinase BAK1.", , , , , , ,
[] [] []Cited for: INTERACTION WITH FLS2, PHOSPHORYLATION."The Arabidopsis leucine-rich repeat receptor-like kinases BAK1/SERK3 and BKK1/SERK4 are required for innate immunity to hemibiotrophic and biotrophic pathogens.", , , , , , , , ,
[] [] []Cited for: FUNCTION, INTERACTION WITH EFR AND FLS2."Functional importance of BAK1 tyrosine phosphorylation in vivo.", , ,
[] [] []Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH BRI1."Identification of Arabidopsis BAK1-associating receptor-like kinase 1 (BARK1) and characterization of its gene expression and brassinosteroid-regulated root phenotypes.", , , , , , ,
[] [] []Cited for: INTERACTION WITH TMK4/BARK1."The leucine-rich repeat receptor kinase BIR2 is a negative regulator of BAK1 in plant immunity.", , , , , , , , , , , , , , , , ,
[] [] []Cited for: FUNCTION, MUTAGENESIS OF SER-290; THR-312; LYS-317; THR-446; THR-449; THR-450 AND THR-455, INTERACTION WITH BIR2, AUTOPHOSPHORYLATION."Structure of the pseudokinase domain of BIR2, a regulator of BAK1-mediated immune signaling in Arabidopsis.", , , , , ,
[] [] []Cited for: FUNCTION, INTERACTION WITH BIR2."Phytosulfokine regulates growth in Arabidopsis through a response module at the plasma membrane that includes CYCLIC NUCLEOTIDE-GATED CHANNEL17, H+-ATPase, and BAK1.", , , , ,
[] [] []Cited for: FUNCTION, INTERACTION WITH CNGC17 AND PSKR1, SUBCELLULAR LOCATION."The Arabidopsis malectin-like/LRR-RLK IOS1 is critical for BAK1-dependent and BAK1-independent pattern-triggered immunity.", , , , , , , , , , ,
[] [] []Cited for: INTERACTION WITH IOS1."Structural basis for flg22-induced activation of the Arabidopsis FLS2-BAK1 immune complex.", , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (3.06 ANGSTROMS) OF
IN COMPLEX WITH FLS2 AND FLG22, DISULFIDE BONDS, SUBUNIT, MUTAGENESIS OF ASP-30; PHE-60; TYR-96 AND PHE-144.Binary interactionsiGO - Molecular functioniInferred from physical interactioniProtein-protein interaction databasesBioGridi 29 interactors.DIPi IntActi 11 interactors.StructureiSecondary structure1615Legend: HelixTurnBeta strandPDB Structure known for this areaFeature keyPosition(s)DescriptionActionsGraphical viewLengthHelixiManual assertion inferred from combination of experimental and computational evidencei11HelixiManual assertion inferred from combination of experimental and computational evidencei4Beta strandiManual assertion inferred from combination of experimental and computational evidencei7Beta strandiManual assertion inferred from combination of experimental and computational evidencei3Beta strandiManual assertion inferred from combination of experimental and computational evidencei5Beta strandiManual assertion inferred from combination of experimental and computational evidencei3HelixiManual assertion inferred from combination of experimental and computational evidencei5Beta strandiManual assertion inferred from combination of experimental and computational evidencei3HelixiManual assertion inferred from combination of experimental and computational evidencei5Beta strandiManual assertion inferred from combination of experimental and computational evidencei3HelixiManual assertion inferred from combination of experimental and computational evidencei4Beta strandiManual assertion inferred from combination of experimental and computational evidencei3HelixiManual assertion inferred from combination of experimental and computational evidencei4Beta strandiManual assertion inferred from combination of experimental and computational evidencei3Beta strandiManual assertion inferred from combination of experimental and computational evidencei4TurniManual assertion inferred from combination of experimental and computational evidencei3Beta strandiManual assertion inferred from combination of experimental and computational evidencei4HelixiManual assertion inferred from combination of experimental and computational evidencei4TurniManual assertion inferred from combination of experimental and computational evidencei4HelixiManual assertion inferred from combination of experimental and computational evidencei3Beta strandiManual assertion inferred from combination of experimental and computational evidencei3Beta strandiManual assertion inferred from combination of experimental and computational evidencei8Beta strandiManual assertion inferred from combination of experimental and computational evidencei3Beta strandiManual assertion inferred from combination of experimental and computational evidencei5HelixiManual assertion inferred from combination of experimental and computational evidencei7HelixiManual assertion inferred from combination of experimental and computational evidencei3Beta strandiManual assertion inferred from combination of experimental and computational evidencei3Beta strandiManual assertion inferred from combination of experimental and computational evidencei5HelixiManual assertion inferred from combination of experimental and computational evidencei6HelixiManual assertion inferred from combination of experimental and computational evidencei20Beta strandiManual assertion inferred from combination of experimental and computational evidencei4Beta strandiManual assertion inferred from combination of experimental and computational evidencei4Beta strandiManual assertion inferred from combination of experimental and computational evidencei3Beta strandiManual assertion inferred from combination of experimental and computational evidencei3Beta strandiManual assertion inferred from combination of experimental and computational evidencei4HelixiManual assertion inferred from combination of experimental and computational evidencei3HelixiManual assertion inferred from combination of experimental and computational evidencei6Beta strandiManual assertion inferred from combination of experimental and computational evidencei3HelixiManual assertion inferred from combination of experimental and computational evidencei17HelixiManual assertion inferred from combination of experimental and computational evidencei4TurniManual assertion inferred from combination of experimental and computational evidencei3HelixiManual assertion inferred from combination of experimental and computational evidencei5TurniManual assertion inferred from combination of experimental and computational evidencei4HelixiManual assertion inferred from combination of experimental and computational evidencei3HelixiManual assertion inferred from combination of experimental and computational evidencei3Beta strandiManual assertion inferred from combination of experimental and computational evidencei4HelixiManual assertion inferred from combination of experimental and computational evidencei14HelixiManual assertion inferred from combination of experimental and computational evidencei3HelixiManual assertion inferred from combination of experimental and computational evidencei9Beta strandiManual assertion inferred from combination of experimental and computational evidencei3HelixiManual assertion inferred from combination of experimental and computational evidencei53D structure databasesSelect the link destinations:PDBeiRCSB PDBiPDBjiPDB entryMethodResolution (?)ChainPositionsPDBsumX-ray2.50A/D/G/H[]X-ray2.20A[]X-ray2.60A[]X-ray3.60C/D[]X-ray3.06B[]ProteinModelPortali SMRi ModBaseiMobiDBiFamily & DomainsiDomains and RepeatsFeature keyPosition(s)DescriptionActionsGraphical viewLengthRepeatiLRR 1 24RepeatiLRR 2 24RepeatiLRR 3 23RepeatiLRR 4 23DomainiProtein kinaseManual assertion according to rulesi 288RegionFeature keyPosition(s)DescriptionActionsGraphical viewLengthRegioniBrassinolide bindingManual assertion based on experiment ini"Structural insight into BL-induced activation of the BRI1-BAK1 complex.", , Submitted (AUG-2013) to the PDB data bankCited for: X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) OF
IN COMPLEX WITH BRASSINOLIDE, DISULFIDE BONDS.4MotifFeature keyPosition(s)DescriptionActionsGraphical viewLengthMotifiCys pair8Compositional biasFeature keyPosition(s)DescriptionActionsGraphical viewLengthCompositional biasiPro-rich 27DomainiContains one leucine-zipper motif and one pair of conservatively spaced Cys (Cys pair) involved in forming heterodimers.Sequence similaritiesiBelongs to the . .Manual assertion according to rulesiKeywords - Domaini, , , , Phylogenomic databasesHOGENOMi InParanoidi KOi PhylomeDBi Family and domain databasesGene3Di 1 hit. InterProi Kinase-like_dom_sf.
Leu-rich_rpt.
LRR_dom_sf.
LRR_N_plant-typ.
Prot_kinase_dom.
Protein_kinase_ATP_BS.
Ser/Thr_kinase_AS.
SERK. PANTHERi PTHR27001:SF1. 1 hit. Pfami LRR_1. 1 hit.
LRR_8. 1 hit.
LRRNT_2. 1 hit.
Pkinase. 1 hit. SMARTi S_TKc. 1 hit. SUPFAMi SSF52058. 1 hit.
SSF56112. 1 hit. PROSITEi PROTEIN_KINASE_ATP. 1 hit.
PROTEIN_KINASE_DOM. 1 hit.
PROTEIN_KINASE_ST. 1 hit. SequenceiSequence statusi: Complete.Sequence processingi: The displayed sequence is further processed into a mature form.This entry describes 1 isoform i produced by alternative splicing. Note: A number of isoforms are produced. According to EST sequences. (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.
50MERRLMIPCF FWLILVLDLV LRVSGNAEGD ALSALKNSLA DPNKVLQSWD
100ATLVTPCTWF HVTCNSDNSV TRVDLGNANL SGQLVMQLGQ LPNLQYLELY
150SNNITGTIPE QLGNLTELVS LDLYLNNLSG PIPSTLGRLK KLRFLRLNNN
200SLSGEIPRSL TAVLTLQVLD LSNNPLTGDI PVNGSFSLFT PISFANTKLT
250PLPASPPPPI SPTPPSPAGS NRITGAIAGG VAAGAALLFA VPAIALAWWR
300RKKPQDHFFD VPAEEDPEVH LGQLKRFSLR ELQVASDNFS NKNILGRGGF
350GKVYKGRLAD GTLVAVKRLK EERTQGGELQ FQTEVEMISM AVHRNLLRLR
400GFCMTPTERL LVYPYMANGS VASCLRERPE SQPPLDWPKR QRIALGSARG
450LAYLHDHCDP KIIHRDVKAA NILLDEEFEA VVGDFGLAKL MDYKDTHVTT
500AVRGTIGHIA PEYLSTGKSS EKTDVFGYGV MLLELITGQR AFDLARLAND
550DDVMLLDWVK GLLKEKKLEA LVDVDLQGNY KDEEVEQLIQ VALLCTQSSP
600MERPKMSEVV RMLEGDGLAE RWEEWQKEEM FRQDFNYPTH HPAVSGWIIG
610 DSTSQIENEY PSGPR
61568,161March 28, 2003 - v2Checksum:i547B3F38FB46E1DDBLASTProtParamProtScaleCompute pI/MWPeptideMassPeptideCutterSequence cautioniThe sequence
differs from that shown. Reason: Erroneous gene model prediction.The sequence
differs from that shown. Reason: Erroneous gene model prediction.Experimental InfoFeature keyPosition(s)DescriptionActionsGraphical viewLengthSequence conflictiW → G in
(PubMed:).1Sequence databasesSelect the link destinations:EMBLiGenBankiDDBJi mRNA. Translation: . mRNA. Translation: . Genomic DNA. Translation: .
Sequence problems. Genomic DNA. Translation: .
Sequence problems. Genomic DNA. Translation: .PIRi RefSeqi
[]UniGenei Genome annotation databasesEnsemblPlantsi; ; .
[]GeneIDi Gramenei; ; .
[]KEGGi Keywords - Coding sequence diversityiSimilar proteinsi mRNA. Translation: . mRNA. Translation: . Genomic DNA. Translation: .
Sequence problems. Genomic DNA. Translation: .
Sequence problems. Genomic DNA. Translation: .PIRi RefSeqi
[]UniGenei 3D structure databasesSelect the link destinations:PDBeiRCSB PDBiPDBjiPDB entryMethodResolution (?)ChainPositionsPDBsumX-ray2.50A/D/G/H[]X-ray2.20A[]X-ray2.60A[]X-ray3.60C/D[]X-ray3.06B[]ProteinModelPortali SMRi ModBaseiMobiDBiProtein-protein interaction databasesBioGridi 29 interactors.DIPi IntActi 11 interactors.PTM databasesiPTMneti Proteomic databasesPRIDEi Protocols and materials databasesStructural Biology KnowledgebaseGenome annotation databasesEnsemblPlantsi; ; .
[]GeneIDi Gramenei; ; .
[]KEGGi Organism-specific databasesAraporti Phylogenomic databasesHOGENOMi InParanoidi KOi PhylomeDBi Miscellaneous databasesPROi Gene expression databasesExpressionAtlasi baseline and differential. Genevisiblei AT. Family and domain databasesGene3Di 1 hit. InterProi Kinase-like_dom_sf.
Leu-rich_rpt.
LRR_dom_sf.
LRR_N_plant-typ.
Prot_kinase_dom.
Protein_kinase_ATP_BS.
Ser/Thr_kinase_AS.
SERK. PANTHERi PTHR27001:SF1. 1 hit. Pfami LRR_1. 1 hit.
LRR_8. 1 hit.
LRRNT_2. 1 hit.
Pkinase. 1 hit. SMARTi S_TKc. 1 hit. SUPFAMi SSF52058. 1 hit.
SSF56112. 1 hit. PROSITEi PROTEIN_KINASE_ATP. 1 hit.
PROTEIN_KINASE_DOM. 1 hit.
PROTEIN_KINASE_ST. 1 hit. ProtoNetiMiscellaneousiKeywords - Technical termi, , Documents
Arabidopsis thaliana: entries and gene names
Index of Protein Data Bank (PDB) cross-references
Index of protein domains and families