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Entry version 160 (07 Apr 2021)
Sequence version 1 (01 Jun 1998)
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Protein

Serine/threonine-protein kinase BIK1

Gene

BIK1

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

Plays a central role in immune responses (PubMed:20413097, PubMed:29649442). Required to activate the resistance responses to necrotrophic pathogens, including the regulation of defense hormone expression (e.g. jasmonic acid (JA) and salicylic acid (SA)) (PubMed:16339855, PubMed:29649442). Phosphorylates FLS2 and BAK1 (PubMed:20404519, PubMed:24104392). Involved in pathogen-associated molecular pattern (PAMP)-triggered immunity (PTI) signaling, including calcium signaling, and defense responses downstream of FLS2; upon PAMP recognition, first phosphorylated by FLS2 prior to being monoubiquitinated by ATL44/RHA3A and ATL45/RHA3B at the plasma membrane, then internalized dynamically into endocytic compartments together with FLS2 (PubMed:20413097, PubMed:25522736, Ref. 19). Acts additively with PBL1 in PTI defenses (PubMed:20413097). Acts as positive regulator of the PAMP flg22-induced increase of cytosolic calcium. Binds directly and phosphorylates the NADPH oxidase RBOHD at specific sites in a calcium-independent manner to enhance reactive oxygen species (ROS) generation upon flg22 perception. ROS production in response to flg22 controls stomatal movement and restriction of bacterial entry into leaf tissues (PubMed:24629339). Seems not required for flg22-induced MAPK activation (Probable). Required for Pep1-induced defenses. Pep1 is an endogenous elicitor that potentiates PAMP-inducible plant responses. In association with PEPR1, acts downstream of the canonical ethylene signaling cascade to regulate ethylene responses (PubMed:23431184). Involved in ethylene signaling. Destabilizes EIN3, the key transcription activator in ethylene signaling, and represses EIN3-dependent transcription (PubMed:26021844). Acts as a negative regulator in brassinosteroid (BR) signaling. Functions in BR signaling by direct interaction with the BR receptor BRI1 cytosolic kinase domain (PubMed:23818580).Curated11 Publications
(Microbial infection) Xanthomonas campestris effector AvrAC/XopAC-mediated uridylylation prevents activation by phosphorylation at the same residues, thus affecting immune responses and reducing defense responses toward X.campestris, mediating avrAC/XopAC virulence functions.1 Publication

Miscellaneous

The association with FLS2 and BAK1 is reduced after flagellin perception, BIK1 being probably released from the receptor complex upon phosphorylation.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Kinase activation is repressed by the phosphatase PP2C38.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei105ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei202Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi73 – 81ATPPROSITE-ProRule annotation9

<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, Serine/threonine-protein kinase, Transferase
Biological processImmunity, Innate immunity, Plant 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%5Fand%5Ftaxonomy%5Fsection">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:
Serine/threonine-protein kinase BIK1Curated (EC:2.7.11.11 Publication)
Alternative name(s):
Protein BOTRYTIS-INDUCED KINASE 11 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:BIK11 Publication
Ordered Locus Names:At2g39660Imported
ORF Names:F12L6.32Imported, F17A14.3Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 2

Organism-specific databases

Arabidopsis Information Portal

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Araporti
AT2G39660

The Arabidopsis Information Resource

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TAIRi
locus:2039772, AT2G39660

<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

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane, Nucleus

<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

Altered growth traits, early flowering, weak stems, small siliques and reduced fertility. Mutant plants have a severely impaired resistance to Botrytis and A.brassicicola (PubMed:16339855). Reduced plant size (PubMed:20413097, PubMed:27679580). Enhanced resistance to Plasmodiophora brassicae, a soil-borne obligate pathogen that causes clubroot disease (PubMed:27679580). Hypersensitivity to the plant hormone brassinolide (PubMed:23818580). Reduced calcium levels after elicitation with peptides representing bacteria-derived microbe- and damage-associated molecular patterns (MAMPs, flg22 and elf18, and the endogenous DAMP AtPep1) (PubMed:25522736).5 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi2G → A: Mis-localization and impaired phosphorylation and ubiquitination upon flagellin (flg22) treatment, but conserved kinase activity and autophosphorylation. 2 Publications1
Mutagenesisi2G → S: Drastic reduction of plasma membrane localization and strong increase of cytoplasmic localization. 1 Publication1
Mutagenesisi31K → R: Impaired flg22-induced ubiquination, internalization of BIK1 and FLS2 from the plasma membrane and reactive oxygen species (ROS) production, as well as enhanced susceptibilitye to the bacterial pathogen Pseudomonas syringae pv. tomato (Pst) DC3000 and to the fungal pathogen Botrytis cinerea, but normal phosphorylation; when associated with R-41, R-95, R-170, R-186, R-286, R-337, R-358 and R-366. 1 Publication1
Mutagenesisi41K → R: Impaired flg22-induced ubiquination, internalization of BIK1 and FLS2 from the plasma membrane and reactive oxygen species (ROS) production, as well as enhanced susceptibilitye to the bacterial pathogen Pseudomonas syringae pv. tomato (Pst) DC3000 and to the fungal pathogen Botrytis cinerea, but normal phosphorylation; when associated with R-31, R-95, R-170, R-186, R-286, R-337, R-358 and R-366. 1 Publication1
Mutagenesisi89 – 90ST → AA: Impaired sensitivity toward elf18-mediated growth inhibition and increased sensitivity to Pseudomonas syringae pv. tomato (Pst) DC3000 bacteria, but no growth defect in normal conditions and normal mitogen-activated protein kinases (MAPKs) activation during EFR-mediated signaling. Enhanced interaction with the WRKY transcription factors WRKY33, WRKY50, WRKY51 and WRKY57 involved in the regulation of jasmonic acid (JA) and salicylic acid (SA) biosynthesis. 1 Publication2
Mutagenesisi89 – 90ST → DD: Phosphomimetic, associated with an increased sensitivity toward elf18-mediated growth inhibition and an enhanced resistance to Pseudomonas syringae pv. tomato (Pst) DC3000 bacteria despite a normal mitogen-activated protein kinases (MAPKs) activation during EFR-mediated signaling. Growth defect in normal conditions. Reduced interaction with EFR. Increased jasmonic acid (JA) and salicylic acid (SA) levels. Reduced interaction with and phosphorylation of the WRKY transcription factors WRKY33, WRKY50, WRKY51 and WRKY57 involved in the regulation of jasmonic acid (JA) and salicylic acid (SA) biosynthesis. 1 Publication2
Mutagenesisi95K → R: Impaired flg22-induced ubiquination, internalization of BIK1 and FLS2 from the plasma membrane and reactive oxygen species (ROS) production, as well as enhanced susceptibilitye to the bacterial pathogen Pseudomonas syringae pv. tomato (Pst) DC3000 and to the fungal pathogen Botrytis cinerea, but normal phosphorylation; when associated with R-31, R-41, R-170, R-186, R-286, R-337, R-358 and R-366. 1 Publication1
Mutagenesisi105K → E: Loss of autophosphorylation. 1 Publication1
Mutagenesisi106K → R: Impaired kinase activity. 1 Publication1
Mutagenesisi120T → A: Normal sensitivity toward elf18-mediated growth inhibition. Normal sensitivity toward elf18-mediated growth inhibition; when associated with A-129. 1 Publication1
Mutagenesisi129S → A: Normal sensitivity toward elf18-mediated growth inhibition. Normal sensitivity toward elf18-mediated growth inhibition; when associated with A-120. 1 Publication1
Mutagenesisi150Y → F: Loss of function in innate immunity. 1 Publication1
Mutagenesisi170K → R: Impaired flg22-induced ubiquination, internalization of BIK1 and FLS2 from the plasma membrane and reactive oxygen species (ROS) production, as well as enhanced susceptibilitye to the bacterial pathogen Pseudomonas syringae pv. tomato (Pst) DC3000 and to the fungal pathogen Botrytis cinerea, but normal phosphorylation; when associated with R-31, R-41, R-95, R-186, R-286, R-337, R-358 and R-366. 1 Publication1
Mutagenesisi186K → R: Impaired flg22-induced ubiquination, internalization of BIK1 and FLS2 from the plasma membrane and reactive oxygen species (ROS) production, as well as enhanced susceptibilitye to the bacterial pathogen Pseudomonas syringae pv. tomato (Pst) DC3000 and to the fungal pathogen Botrytis cinerea, but normal phosphorylation; when associated with R-31, R-41, R-95, R-170, R-286, R-337, R-358 and R-366. 1 Publication1
Mutagenesisi202D → A: Abolishes kinase activity. 1 Publication1
Mutagenesisi204K → R: Compromised flg22-induced ubiquitination and reduced phosphorylation. 1 Publication1
Mutagenesisi237T → A: Compromised flg22-induced ubiquitination. 1 Publication1
Mutagenesisi243Y → F: Loss of function in innate immunity. 1 Publication1
Mutagenesisi250Y → A: Compromised flg22-induced ubiquitination. 1 Publication1
Mutagenesisi250Y → F: Loss of function in innate immunity. 1 Publication1
Mutagenesisi286K → R: Impaired flg22-induced ubiquination, internalization of BIK1 and FLS2 from the plasma membrane and reactive oxygen species (ROS) production, as well as enhanced susceptibilitye to the bacterial pathogen Pseudomonas syringae pv. tomato (Pst) DC3000 and to the fungal pathogen Botrytis cinerea, but normal phosphorylation; when associated with R-31, R-41, R-95, R-170, R-186, R-337, R-358 and R-366. 1 Publication1
Mutagenesisi337K → R: Impaired flg22-induced ubiquination, internalization of BIK1 and FLS2 from the plasma membrane and reactive oxygen species (ROS) production, as well as enhanced susceptibilitye to the bacterial pathogen Pseudomonas syringae pv. tomato (Pst) DC3000 and to the fungal pathogen Botrytis cinerea, but normal phosphorylation; when associated with R-31, R-41, R-95, R-170, R-186, R-286, R-358 and R-366. 1 Publication1
Mutagenesisi358K → R: Impaired flg22-induced ubiquination, internalization of BIK1 and FLS2 from the plasma membrane and reactive oxygen species (ROS) production, as well as enhanced susceptibilitye to the bacterial pathogen Pseudomonas syringae pv. tomato (Pst) DC3000 and to the fungal pathogen Botrytis cinerea, but normal phosphorylation; when associated with R-31, R-41, R-95, R-170, R-186, R-286, R-337 and R-366. 1 Publication1
Mutagenesisi366K → R: Impaired flg22-induced ubiquination, internalization of BIK1 and FLS2 from the plasma membrane and reactive oxygen species (ROS) production, as well as enhanced susceptibilitye to the bacterial pathogen Pseudomonas syringae pv. tomato (Pst) DC3000 and to the fungal pathogen Botrytis cinerea, but normal phosphorylation; when associated with R-31, R-41, R-95, R-170, R-186, R-286, R-337 and R-358. 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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003111182 – 395Serine/threonine-protein kinase BIK1Add BLAST394

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi2N-myristoyl glycine1 Publication1
Lipidationi4S-palmitoyl cysteineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki31Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki41Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
<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 residuei48Phosphoserine; by autocatalysis and BAK11 Publication1
Modified residuei54Phosphoserine; by autocatalysis1 Publication1
Modified residuei56Phosphothreonine; by autocatalysis1 Publication1
Modified residuei71Phosphoserine; by autocatalysis and BAK11 Publication1
Modified residuei89Phosphoserine; by EFR1 Publication1
Modified residuei90Phosphothreonine; by EFR1 Publication1
Cross-linki95Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei120Phosphothreonine; by EFR1 Publication1
Modified residuei129Phosphoserine; by autocatalysis1 Publication1
Modified residuei129Phosphoserine; by EFR1 Publication1
Modified residuei150Phosphotyrosine1 Publication1
Modified residuei168Phosphotyrosine; by autocatalysis1 Publication1
Cross-linki170Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki186Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei206Phosphoserine; by autocatalysis and BAK11 Publication1
Modified residuei214Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei233Phosphoserine; by autocatalysis2 Publications1
Modified residuei236O-UMP-serine; by Xanthomonas campestris effector XopAC/AvrAC; alternate1 Publication1
Modified residuei236Phosphoserine; by autocatalysis and BAK1; alternate3 Publications1
Modified residuei237O-UMP-threonine; by Xanthomonas campestris effector XopAC/AvrAC; alternate1 Publication1
Modified residuei237Phosphothreonine; by autocatalysis and BAK1; alternate3 Publications1
Modified residuei242Phosphothreonine; by autocatalysis and BAK11 Publication1
Modified residuei243Phosphotyrosine1 Publication1
Modified residuei250Phosphotyrosine; by autocatalysis2 Publications1
Modified residuei252Phosphoserine; by autocatalysis1 Publication1
Modified residuei253Phosphoserine; by autocatalysis1 Publication1
Cross-linki286Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei314Phosphothreonine; by autocatalysis1 Publication1
Cross-linki337Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki358Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei360Phosphoserine; by autocatalysis and BAK11 Publication1
Modified residuei362Phosphothreonine; by autocatalysis and BAK11 Publication1
Cross-linki366Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei368Phosphothreonine; by autocatalysis and BAK11 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Phosphorylated by FLS2 and BAK1 (PubMed:20404519, Ref. 19). Autophosphorylated (PubMed:22504181, PubMed:23431184, PubMed:24104392, PubMed:26021844). Autophosphorylation is reduced in presence of the Xanthomonas campestris effector XopAC/AvrAC (PubMed:22504181, Ref. 19). Phosphorylated, especially by EFR at Ser-89 and Thr-90, in response to the microbe-associated molecular pattern (MAMP) flg22 (PubMed:20413097, PubMed:22504181, PubMed:25522736, PubMed:29649442, Ref. 19). Phosphorylation in response to flg22 is abolished in presence of the Xanthomonas campestris effector XopAC/AvrAC (PubMed:22504181). Phosphorylated at Ser-233, Ser-236 and THR-237 by PEPR1 (PubMed:23431184). Phosphorylated at Tyr-150, Tyr-243 and Tyr-250. Tyrosine phosphorylation is required for BIK1 function in plant innate immunity (PubMed:24532660).10 Publications
Uridylylated at Ser-236 and Thr-237 by the Xanthomonas campestris effector XopAC/AvrAC. This conceals conserved phosphorylation sites in the activation loop, reducing BIK1 kinase activity and consequently inhibiting downstream signaling.1 Publication
Monoubiquitinated by ATL44/RHA3A and ATL45/RHA3B following phosphorylation upon the recognition of microbe-associated molecular patterns (MAMPs, e.g. flg22) by pattern recognition receptors (PRRs), then released from the FLS2/BAK1 complex and internalized dynamically into endocytic compartments followed by the activation of immune signaling.1 Publication

Keywords - PTMi

Isopeptide bond, Lipoprotein, Myristate, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
O48814

PRoteomics IDEntifications database

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PRIDEi
O48814

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
240422

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
O48814

<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 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

By infection with necrotrophic pathogens and by paraquat. Not induced by salicylic acid, jasmonate or 1-aminocyclopropane-1-carboxylate (ACC) (PubMed:16339855). Induced by flagellin (flg22) (PubMed:20413097).2 Publications

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
O48814, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O48814, 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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with FLS2 (PubMed:20413097, PubMed:20404519). Activation of FLS2 by flagellin (flg22) induces the dissociation of the complex (PubMed:20413097, Ref. 19).

Interacts with BAK1 (PubMed:20404519).

Interacts with the Xanthomonas campestris effector XopAC/AvrAC (PubMed:22504181).

Interacts with CPK28 (PubMed:25525792).

Interacts with PEPR1 (PubMed:23431184).

Interacts with PP2C38 (PubMed:27494702).

Interacts with BRI1 (PubMed:23818580).

Interacts with RBOHD (PubMed:24629339). Binds to EFR when not phosphorylated at Ser-89 and Thr-90, in the absence of pathogen elicitor; dissociates upon pathogen-associated molecular pattern (PAMP)-triggered activation by EFR-mediated phosphorylation (PubMed:29649442).

Interacts directly with and phosphorylates WRKY transcription factors in the nucleus involved in the jasmonic acid (JA) and salicylic acid (SA) regulation (e.g. WRKY33, WRKY50, WRKY51 and WRKY57) to modulate defense hormones during plant immunity (PubMed:29649442). Binds to ATL44/RHA3A and ATL45/RHA3B (Ref. 19).

10 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

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Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
3887, 7 interactors

Database of interacting proteins

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DIPi
DIP-51510N

Protein interaction database and analysis system

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IntActi
O48814, 4 interactors

STRING: functional protein association networks

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STRINGi
3702.AT2G39660.1

<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

1395
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
O48814

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 <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">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>Domaini67 – 356Protein kinasePROSITE-ProRule annotationAdd BLAST290

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>Motifi89 – 90Required for physical interaction with and phosphorylation of downstream signaling proteins (e.g. WRKY33, WRKY50, WRKY51 and WRKY57) to activate EFR-mediated immune signaling1 Publication2

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1187, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_000288_21_1_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O48814

Identification of Orthologs from Complete Genome Data

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OMAi
FQIMDAR

Database of Orthologous Groups

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OrthoDBi
684563at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
O48814

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011009, Kinase-like_dom_sf
IPR000719, Prot_kinase_dom
IPR017441, Protein_kinase_ATP_BS
IPR001245, Ser-Thr/Tyr_kinase_cat_dom
IPR008271, Ser/Thr_kinase_AS

Pfam protein domain database

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Pfami
View protein in Pfam
PF07714, PK_Tyr_Ser-Thr, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00220, S_TKc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF56112, SSF56112, 1 hit

PROSITE; a protein domain and family database

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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%5Flength">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>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

O48814-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGSCFSSRVK ADIFHNGKSS DLYGLSLSSR KSSSTVAAAQ KTEGEILSST
60 70 80 90 100
PVKSFTFNEL KLATRNFRPD SVIGEGGFGC VFKGWLDEST LTPTKPGTGL
110 120 130 140 150
VIAVKKLNQE GFQGHREWLT EINYLGQLSH PNLVKLIGYC LEDEHRLLVY
160 170 180 190 200
EFMQKGSLEN HLFRRGAYFK PLPWFLRVNV ALDAAKGLAF LHSDPVKVIY
210 220 230 240 250
RDIKASNILL DADYNAKLSD FGLARDGPMG DLSYVSTRVM GTYGYAAPEY
260 270 280 290 300
MSSGHLNARS DVYSFGVLLL EILSGKRALD HNRPAKEENL VDWARPYLTS
310 320 330 340 350
KRKVLLIVDN RLDTQYLPEE AVRMASVAVQ CLSFEPKSRP TMDQVVRALQ
360 370 380 390
QLQDNLGKPS QTNPVKDTKK LGFKTGTTKS SEKRFTQKPF GRHLV
Length:395
Mass (Da):44,097
Last modified:June 1, 1998 - v1
<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:i4C06B1FD01889440
GO

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

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DDBJi
Links Updated
AC003674 Genomic DNA Translation: AAB97121.1
AC004218 Genomic DNA Translation: AAM14921.1
CP002685 Genomic DNA Translation: AEC09703.1
AF325086 mRNA Translation: AAK17154.1
AY062493 mRNA Translation: AAL32571.1
AY065029 mRNA Translation: AAL57667.1
AY093278 mRNA Translation: AAM13277.1
AY093997 mRNA Translation: AAM16258.1

Protein sequence database of the Protein Information Resource

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PIRi
T00574

NCBI Reference Sequences

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RefSeqi
NP_181496.1, NM_129522.5

Genome annotation databases

Ensembl plant genome annotation project

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EnsemblPlantsi
AT2G39660.1; AT2G39660.1; AT2G39660

Database of genes from NCBI RefSeq genomes

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GeneIDi
818549

Gramene; a comparative resource for plants

More...
Gramenei
AT2G39660.1; AT2G39660.1; AT2G39660

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
ath:AT2G39660

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC003674 Genomic DNA Translation: AAB97121.1
AC004218 Genomic DNA Translation: AAM14921.1
CP002685 Genomic DNA Translation: AEC09703.1
AF325086 mRNA Translation: AAK17154.1
AY062493 mRNA Translation: AAL32571.1
AY065029 mRNA Translation: AAL57667.1
AY093278 mRNA Translation: AAM13277.1
AY093997 mRNA Translation: AAM16258.1
PIRiT00574
RefSeqiNP_181496.1, NM_129522.5

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5TOSX-ray2.35A/B1-395[»]
SMRiO48814
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi3887, 7 interactors
DIPiDIP-51510N
IntActiO48814, 4 interactors
STRINGi3702.AT2G39660.1

PTM databases

iPTMnetiO48814

Proteomic databases

PaxDbiO48814
PRIDEiO48814
ProteomicsDBi240422

Genome annotation databases

EnsemblPlantsiAT2G39660.1; AT2G39660.1; AT2G39660
GeneIDi818549
GrameneiAT2G39660.1; AT2G39660.1; AT2G39660
KEGGiath:AT2G39660

Organism-specific databases

AraportiAT2G39660
TAIRilocus:2039772, AT2G39660

Phylogenomic databases

eggNOGiKOG1187, Eukaryota
HOGENOMiCLU_000288_21_1_1
InParanoidiO48814
OMAiFQIMDAR
OrthoDBi684563at2759
PhylomeDBiO48814

Miscellaneous databases

Protein Ontology

More...
PROi
PR:O48814

Gene expression databases

ExpressionAtlasiO48814, baseline and differential
GenevisibleiO48814, AT

Family and domain databases

InterProiView protein in InterPro
IPR011009, Kinase-like_dom_sf
IPR000719, Prot_kinase_dom
IPR017441, Protein_kinase_ATP_BS
IPR001245, Ser-Thr/Tyr_kinase_cat_dom
IPR008271, Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF07714, PK_Tyr_Ser-Thr, 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

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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 nameiBIK1_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: O48814
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: June 1, 1998
Last modified: April 7, 2021
This is version 160 of the entry and version 1 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, Reference proteome

Documents

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