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Entry version 174 (18 Sep 2019)
Sequence version 2 (28 Mar 2003)
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Protein

BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1

Gene

BAK1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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 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:17583510, PubMed:17600708, PubMed:18667726, PubMed:18694562, PubMed:19124768, PubMed:20018402, PubMed:20404519, PubMed:21350342, PubMed:21693696). Phosphorylates BIR2 and thus promotes interaction with BIR2 (PubMed:24388849, PubMed:24556575). This interaction prevents interaction with FLS2 in the absence of pathogen-associated molecular patterns (PAMP) (PubMed:24388849, PubMed:24556575). Component of the RLP23-SOBIR1-BAK1 complex that mediates NLP-triggered immunity (PubMed:27251392). Required for PSK promotion of seedling growth and protoplast expansion (PubMed:26071421). CNGC17 and AHAs form a functional cation-translocating unit that is activated by PSKR1/BAK1 and possibly other BAK1/RLK complexes (PubMed:26071421).13 Publications

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.
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.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei52flg221 Publication1
Binding sitei54flg22; via amide nitrogen1 Publication1
Binding sitei297ATP; via carbonyl oxygen1 Publication1
Binding sitei317ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei416Proton acceptorPROSITE-ProRule annotation1
Binding sitei418ATP1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi295 – 303ATPPROSITE-ProRule annotation9
Nucleotide bindingi364 – 366ATP1 Publication3

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionKinase, Receptor, Serine/threonine-protein kinase, Transferase, Tyrosine-protein kinase
Biological processPlant defense
LigandATP-binding, Nucleotide-binding

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 11 Publication (EC:2.7.10.1Curated, EC:2.7.11.1Curated)
Short name:
AtBAK11 Publication
Short name:
BRI1-associated receptor kinase 11 Publication
Alternative name(s):
Protein ELONGATED
Somatic embryogenesis receptor kinase 31 Publication
Short name:
AtSERK31 Publication
Somatic embryogenesis receptor-like kinase 31 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:BAK11 Publication
Synonyms:ELG, SERK31 Publication
Ordered Locus Names:At4g33430Imported
ORF Names:F17M5.190Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiArabidopsis thaliana (Mouse-ear cress)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri3702 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000006548 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 4

Organism-specific databases

Arabidopsis Information Portal

More...
Araporti
AT4G33430

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini26 – 225ExtracellularSequence analysisAdd BLAST200
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei226 – 246HelicalSequence analysisAdd BLAST21
Topological domaini247 – 615CytoplasmicSequence analysisAdd BLAST369

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Semi-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.4 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi30D → Y: No effect on flg22 induced FLS2-BAK1 heterodimerization. 1 Publication1
Mutagenesisi32L → E: Loss of binding to BRI1, but no effect on kinase activity. 1 Publication1
Mutagenesisi46L → E: Loss of binding to BRI1 and loss of kinase activity. 1 Publication1
Mutagenesisi60F → A: Loss of flg22 induced FLS2-BAK1 heterodimerization. 1 Publication1
Mutagenesisi64C → Y: No effect. 1 Publication1
Mutagenesisi94L → E: No effect. 1 Publication1
Mutagenesisi96Y → A: Loss of flg22 induced FLS2-BAK1 heterodimerization. 1 Publication1
Mutagenesisi121L → E: No effect. 1 Publication1
Mutagenesisi122D → N: Hypersensitivity to brassinosteroids and enhanced high-light phototropism. 1 Publication1
Mutagenesisi144F → A: Loss of flg22 induced FLS2-BAK1 heterodimerization. 1 Publication1
Mutagenesisi172S → F: No effect. 1 Publication1
Mutagenesisi286S → A: No effect. 1
Mutagenesisi286S → D: Loss of kinase activity. 1
Mutagenesisi290S → A: Reduced kinase activity. Reduced interaction with BIR2. 1 Publication1
Mutagenesisi290S → D: Normal interaction with BIR2. 1 Publication1
Mutagenesisi304Y → F: No effect on autophosphorylation. 1 Publication1
Mutagenesisi312T → A: No effect on the kinase activity or on the binding to the FHA domain of KAPP. Reduced interaction with BIR2. 2 Publications1
Mutagenesisi312T → D: Reduced interaction with BIR2. 1 Publication1
Mutagenesisi317K → E: Loss of kinase activity and loss of interaction with hopAB2/AvrPtoB, but no effect on the binding to the FHA domain of KAPP. Reduced interaction with BIR2. 5 Publications1
Mutagenesisi363Y → F: No effect on autophosphorylation. 1 Publication1
Mutagenesisi363Y → G or A: Loss of autophosphorylation. 1 Publication1
Mutagenesisi365Y → F: No effect on autophosphorylation. 1 Publication1
Mutagenesisi403Y → F: No effect on autophosphorylation. 1 Publication1
Mutagenesisi416D → A: Loss of phosphorylation. 1 Publication1
Mutagenesisi421N → A: Loss of phosphorylation. 1 Publication1
Mutagenesisi439K → A: No effect on some phosphorylation sites. 1 Publication1
Mutagenesisi443Y → F: No effect on autophosphorylation. 1 Publication1
Mutagenesisi446T → A or D: No effect. Reduced interaction with BIR2. Loss of kinase activity; when associated with D-449 and D-450. 2 Publications1
Mutagenesisi449T → A or D: Slight decrease of kinase activity but loss of interaction with hopAB2/AvrPtoB. Reduced interaction with BIR2. Loss of kinase activity; when associated with A-446 and D-450. 3 Publications1
Mutagenesisi450T → A or D: Loss of interaction with hopAB2/AvrPtoB and loss of phosphorylation. Reduced interaction with BIR2. Loss of kinase activity; when associated with A-446 and D-449. 4 Publications1
Mutagenesisi451A → E: Loss of kinase activity and loss of interaction with hopAB2/AvrPtoB. Reduced interaction with BIR2. 2 Publications1
Mutagenesisi452V → D: Strongly decreased kinase activity and loss of interaction with hopAB2/AvrPtoB. 1 Publication1
Mutagenesisi453R → A: No effect on some phosphorylation sites. 1 Publication1
Mutagenesisi455T → A, D or E: Loss of kinase activity. 2 Publications1
Mutagenesisi455T → N: Loss of kinase activity and loss of interaction with hopAB2/AvrPtoB. 1 Publication1
Mutagenesisi456I → D: Loss of kinase activity and loss of interaction with hopAB2/AvrPtoB. 1 Publication1
Mutagenesisi458H → D: Loss of kinase activity, loss of phosphorylation and loss of interaction with hopAB2/AvrPtoB. 2 Publications1
Mutagenesisi463Y → F: Loss of kinase activity and loss of autophosphorylation. 1 Publication1
Mutagenesisi464L → D: Loss of kinase activity and loss of interaction with hopAB2/AvrPtoB. 1 Publication1
Mutagenesisi478Y → F: No effect on autophosphorylation. 1 Publication1
Mutagenesisi495A → E: Loss of kinase activity and loss of interaction with hopAB2/AvrPtoB. 1 Publication1
Mutagenesisi530Y → F: No effect on autophosphorylation. 1 Publication1
Mutagenesisi546T → A: 60% decrease of binding to the FHA domain of KAPP. 1 Publication1
Mutagenesisi587Y → F: No effect on autophosphorylation. 1 Publication1
Mutagenesisi610Y → E: Loss of brassinosteroid signaling but no effect on programmed cell death inhibition. 1 Publication1
Mutagenesisi610Y → F: Decreased autophosphorylation on tyrosine, loss of transphosphorylation and activation of BRI1 but no effect on the binding to BRI1. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 25Sequence analysisAdd BLAST25
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000002430426 – 615BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1Add BLAST590

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi57 ↔ 642 Publications
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi79N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi103N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi114N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi127N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi149N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi183N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei286Phosphoserine1 Publication1
Modified residuei290Phosphoserine4 Publications1
Modified residuei312Phosphothreonine2 Publications1
Modified residuei370PhosphoserineBy similarity1
Modified residuei373PhosphoserineBy similarity1
Modified residuei446Phosphothreonine5 Publications1
Modified residuei449Phosphothreonine5 Publications1
Modified residuei450Phosphothreonine4 Publications1
Modified residuei455Phosphothreonine4 Publications1
Modified residuei463PhosphotyrosineBy similarity1
Modified residuei465PhosphoserineBy similarity1
Modified residuei466PhosphothreonineBy similarity1
Modified residuei470PhosphoserineBy similarity1
Modified residuei546PhosphothreonineBy similarityCurated1
Modified residuei589Phosphothreonine1 Publication1
Modified residuei595Phosphoserine1 Publication1
Modified residuei604Phosphoserine1 Publication1
Modified residuei610Phosphotyrosine1 Publication1
Modified residuei612Phosphoserine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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 flagellin signaling. Phosphorylation at Ser-286, Ser-290 Thr-446 or Thr-449 is not critical for flagellin signaling.9 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

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PRIDEi
Q94F62

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q94F62

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed ubiquitously.1 Publication

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated by flagellin and harpin.1 Publication

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q94F62 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q94F62 AT

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts 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:24388849, PubMed:24556575). Heterodimer with FLS2 (PubMed:24114786). 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:26071421).

Interacts with CNGC17 and PSKR1 (PubMed:26071421). Binds to IOS1 which triggers FLS2-BAK1 complex formation upon microbe-associated molecular patterns (MAMPs) treatment (PubMed:27317676).

Interacts with ERECTA in a EPF2-induced manner.

Interacts with ERL1 in a EPF1-induced manner.

Interacts with TMM (PubMed:26320950).

Component of a trimeric complex composed of RLP23, SOBIR1 and BAK1. BAK1 is recruited into a pre-formed RLP23-SOBIR1 complex in a ligand-dependent manner (PubMed:27251392).

25 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
14764, 69 interactors

Database of interacting proteins

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DIPi
DIP-34976N

Protein interaction database and analysis system

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IntActi
Q94F62, 76 interactors

STRING: functional protein association networks

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STRINGi
3702.AT4G33430.2

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1615
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q94F62

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati93 – 116LRR 1Add BLAST24
Repeati117 – 140LRR 2Add BLAST24
Repeati141 – 163LRR 3Add BLAST23
Repeati165 – 187LRR 4Add BLAST23
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini289 – 576Protein kinasePROSITE-ProRule annotationAdd BLAST288

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni59 – 62Brassinolide binding1 Publication4

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi57 – 64Cys pair8

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi191 – 217Pro-richAdd BLAST27

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Contains one leucine-zipper motif and one pair of conservatively spaced Cys (Cys pair) involved in forming heterodimers.

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000116554

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q94F62

KEGG Orthology (KO)

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KOi
K13416

Database of Orthologous Groups

More...
OrthoDBi
684563at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q94F62

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.80.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR001611 Leu-rich_rpt
IPR032675 LRR_dom_sf
IPR013210 LRR_N_plant-typ
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
IPR031048 SERK

The PANTHER Classification System

More...
PANTHERi
PTHR27001:SF70 PTHR27001:SF70, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00560 LRR_1, 1 hit
PF13855 LRR_8, 1 hit
PF08263 LRRNT_2, 1 hit
PF00069 Pkinase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00220 S_TKc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 1 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoform i produced by alternative splicing. AlignAdd to basket
Note: A number of isoforms are produced. According to EST sequences.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: Q94F62-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MERRLMIPCF FWLILVLDLV LRVSGNAEGD ALSALKNSLA DPNKVLQSWD
60 70 80 90 100
ATLVTPCTWF HVTCNSDNSV TRVDLGNANL SGQLVMQLGQ LPNLQYLELY
110 120 130 140 150
SNNITGTIPE QLGNLTELVS LDLYLNNLSG PIPSTLGRLK KLRFLRLNNN
160 170 180 190 200
SLSGEIPRSL TAVLTLQVLD LSNNPLTGDI PVNGSFSLFT PISFANTKLT
210 220 230 240 250
PLPASPPPPI SPTPPSPAGS NRITGAIAGG VAAGAALLFA VPAIALAWWR
260 270 280 290 300
RKKPQDHFFD VPAEEDPEVH LGQLKRFSLR ELQVASDNFS NKNILGRGGF
310 320 330 340 350
GKVYKGRLAD GTLVAVKRLK EERTQGGELQ FQTEVEMISM AVHRNLLRLR
360 370 380 390 400
GFCMTPTERL LVYPYMANGS VASCLRERPE SQPPLDWPKR QRIALGSARG
410 420 430 440 450
LAYLHDHCDP KIIHRDVKAA NILLDEEFEA VVGDFGLAKL MDYKDTHVTT
460 470 480 490 500
AVRGTIGHIA PEYLSTGKSS EKTDVFGYGV MLLELITGQR AFDLARLAND
510 520 530 540 550
DDVMLLDWVK GLLKEKKLEA LVDVDLQGNY KDEEVEQLIQ VALLCTQSSP
560 570 580 590 600
MERPKMSEVV RMLEGDGLAE RWEEWQKEEM FRQDFNYPTH HPAVSGWIIG
610
DSTSQIENEY PSGPR
Length:615
Mass (Da):68,161
Last modified:March 28, 2003 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i547B3F38FB46E1DD
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F4JIX9F4JIX9_ARATH
BRI1-associated receptor kinase
BAK1 ATBAK1, ATSERK3, ELG, ELONGATED, RECEPTOR KINASES LIKE SERK 10
662Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence CAB38801 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence CAB80060 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti12W → G in AAK68074 (PubMed:11706164).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
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

Protein sequence database of the Protein Information Resource

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PIRi
T05994

NCBI Reference Sequences

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RefSeqi
NP_567920.1, NM_119497.5 [Q94F62-1]

Genome annotation databases

Ensembl plant genome annotation project

More...
EnsemblPlantsi
AT4G33430.1; AT4G33430.1; AT4G33430 [Q94F62-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
829480

Gramene; a comparative resource for plants

More...
Gramenei
AT4G33430.1; AT4G33430.1; AT4G33430 [Q94F62-1]

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ath:AT4G33430

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

PlantP kinase Classification PPC

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
PIRiT05994
RefSeqiNP_567920.1, NM_119497.5 [Q94F62-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3TL8X-ray2.50A/D/G/H250-590[»]
3UIMX-ray2.20A258-583[»]
3ULZX-ray2.60A258-583[»]
4M7EX-ray3.60C/D26-220[»]
4MN8X-ray3.06B1-220[»]
SMRiQ94F62
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi14764, 69 interactors
DIPiDIP-34976N
IntActiQ94F62, 76 interactors
STRINGi3702.AT4G33430.2

PTM databases

iPTMnetiQ94F62

Proteomic databases

PRIDEiQ94F62

Genome annotation databases

EnsemblPlantsiAT4G33430.1; AT4G33430.1; AT4G33430 [Q94F62-1]
GeneIDi829480
GrameneiAT4G33430.1; AT4G33430.1; AT4G33430 [Q94F62-1]
KEGGiath:AT4G33430

Organism-specific databases

AraportiAT4G33430

Phylogenomic databases

HOGENOMiHOG000116554
InParanoidiQ94F62
KOiK13416
OrthoDBi684563at2759
PhylomeDBiQ94F62

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q94F62

Gene expression databases

ExpressionAtlasiQ94F62 baseline and differential
GenevisibleiQ94F62 AT

Family and domain databases

Gene3Di3.80.10.10, 1 hit
InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR001611 Leu-rich_rpt
IPR032675 LRR_dom_sf
IPR013210 LRR_N_plant-typ
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
IPR031048 SERK
PANTHERiPTHR27001:SF70 PTHR27001:SF70, 1 hit
PfamiView protein in Pfam
PF00560 LRR_1, 1 hit
PF13855 LRR_8, 1 hit
PF08263 LRRNT_2, 1 hit
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiBAK1_ARATH
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q94F62
Secondary accession number(s): C0LGS0, Q9SZC0
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: March 28, 2003
Last modified: September 18, 2019
This is version 174 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
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