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Entry version 160 (07 Oct 2020)
Sequence version 1 (01 Mar 2001)
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Protein

LRR receptor-like serine/threonine-protein kinase FLS2

Gene

FLS2

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

Constitutes the pattern-recognition receptor (PPR) that determines the specific perception of flagellin (flg22), a potent elicitor of the defense response to pathogen-associated molecular patterns (PAMPs). Flagellin-binding to the receptor is the first step to initiate the innate immune MAP kinase signaling cascade (MEKK1, MKK4/MKK5 and MPK3/MPK6), resulting in enhanced resistance against pathogens. Binding to the effector AvrPto1 or to the phosphatase hopD2 from Pseudomonas syringae blocks the downstream plant immune response.7 Publications

Miscellaneous

After flg22-binding, forms instantaneously a heteromeric complex with BAK1 and is transphosphorylated within 15 seconds. After activation, the receptor is internalized by endocytosis and subject to degradation.

<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

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 sitei148flg221 Publication1
Binding sitei152flg221 Publication1
Binding sitei272flg221 Publication1
Binding sitei296flg221 Publication1
Binding sitei898ATPPROSITE-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 sitei997Proton 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 bindingi876 – 884ATPPROSITE-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, Receptor, Serine/threonine-protein kinase, Transferase
Biological processPlant defense, Ubl conjugation pathway
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:
LRR receptor-like serine/threonine-protein kinase FLS2 (EC:2.7.11.1)
Alternative name(s):
Protein FLAGELLIN-SENSING 21 Publication
Protein FLAGELLIN-SENSITIVE 21 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:FLS21 Publication
Ordered Locus Names:At5g46330Imported
ORF Names:MPL12.13Imported, MPL12.8Imported
<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 5

Organism-specific databases

Arabidopsis Information Portal

More...
Araporti
AT5G46330

The Arabidopsis Information Resource

More...
TAIRi
locus:2170483, AT5G46330

<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%5Flocation%5Fsection">'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 domaini24 – 806ExtracellularSequence analysisAdd BLAST783
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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>Transmembranei807 – 827HelicalSequence analysisAdd BLAST21
Topological domaini828 – 1173CytoplasmicSequence analysisAdd BLAST346

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

Impaired BIK1 pathogen-associated molecular patterns (PAMPs e.g. flg22)-induced ubiquitination.1 Publication

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>Mutagenesisi294R → A: Abolishes flagellin-binding. 1 Publication1
Mutagenesisi316H → A: Abolishes flagellin-binding. 1 Publication1
Mutagenesisi318G → R in fls2-24; abolishes flagellin-binding. 2 Publications1
Mutagenesisi342T → Y: Abolishes flagellin-binding. 1 Publication1
Mutagenesisi434T → Y: No effect on flagellin-binding. 1 Publication1
Mutagenesisi867T → V: Abolishes flagellin-dependent signaling and reduces ligand-receptor internalization. 1
Mutagenesisi898K → H: Loss of binding with avrPto. 1 Publication1
Mutagenesisi1040T → A: Abolishes flagellin-dependent signaling. 1
Mutagenesisi1064G → R in fls2-17; abolishes kinase activity and strongly reduces flagellin-binding. 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 – 23Sequence analysisAdd BLAST23
<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_000032372024 – 1173LRR receptor-like serine/threonine-protein kinase FLS2Add BLAST1150

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 bondi61 ↔ 681 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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>Glycosylationi62N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi94N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Disulfide bondi165 ↔ 1871 Publication
Glycosylationi179N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi217N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi262N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi347N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi361N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi371N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi388N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi406N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi432N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi453N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi466N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi525N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi588N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi631N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi684N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi704N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi720N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi733N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi744N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi772N-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 residuei867Phosphothreonine1 Publication1
Modified residuei869Phosphoserine; by BAK11 Publication1
Modified residuei906Phosphoserine; by BAK11 Publication1
Modified residuei938Phosphoserine1 Publication1
Modified residuei941Phosphothreonine1 Publication1
Modified residuei961Phosphoserine; by BAK11 Publication1
Modified residuei984PhosphotyrosineBy similarity1
Modified residuei1035PhosphoserineBy similarity1
Modified residuei1043PhosphotyrosineBy similarity1
Modified residuei1050PhosphotyrosineBy similarity1
Modified residuei1084Phosphoserine1 Publication1
Modified residuei1115Phosphoserine; by 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

Autophosphorylated. The phosphorylated form is essential in the perception of flagellin. Dephosphorylated by KAPP. Autophosphorylation is inhibited by the binding with avrPto1.1 Publication
Polyubiquitinated at the kinase domain mediated by P.syringae AvrPtoB.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

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

More...
PaxDbi
Q9FL28

PRoteomics IDEntifications database

More...
PRIDEi
Q9FL28

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
230627

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9FL28

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q9FL28

<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

Ubiquitously expressed.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

Repressed upon infection with the P.syringae virulent DC3000 strain, in a flg22- and avrPtoB-dependent manner (at protein level).1 Publication

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q9FL28, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9FL28, 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

Heterodimer with SERK3/BAK1 (PubMed:24114786, PubMed:17626179, PubMed:20103591, PubMed:21693696, Ref. 32). The activation by flagellin (flg22) induces the dissociation of the complex with SERK3/BAK1 (Ref. 32, PubMed:20413097).

Interacts with KAPP. Does not form homodimer.

Interacts with SERK3/BAK1, SERK4/BKK1, SERK1 and SERK2 in a specific ligand-induced manner.

Interacts with P.syringae AvrPto1, AvrPtoB and (via the kinase and cytoplasmic domains) hopD2.

Component of large complexes containing, at least, FLS2 and ACD6 in endoplasmic reticulum and plasma membrane (PubMed:24923602).

Interacts with MORC1/CRT1 (PubMed:23250427).

Interacts with PBS1, BIK1, PBL1 and PBL2 (PubMed:20413097).

Interacts with RBOHD (PubMed:24629339). Binds to IOS1 which triggers FLS2-BAK1 complex formation upon microbe-associated molecular patterns (MAMPs) treatment (PubMed:27317676).

Interacts with PCRK1 AND PCRK2 (PubMed:27208222).

Interacts with BSK1 (PubMed:23532072). Interaction with BSK8 (PubMed:21726371).

19 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

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
19925, 54 interactors

Database of interacting proteins

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DIPi
DIP-46004N

Protein interaction database and analysis system

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IntActi
Q9FL28, 45 interactors

Molecular INTeraction database

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MINTi
Q9FL28

STRING: functional protein association networks

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STRINGi
3702.AT5G46330.1

<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

11173
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
Q9FL28

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>Repeati97 – 119LRR 1Add BLAST23
Repeati121 – 143LRR 2Add BLAST23
Repeati145 – 167LRR 3Add BLAST23
Repeati169 – 192LRR 4Add BLAST24
Repeati193 – 215LRR 5Add BLAST23
Repeati217 – 240LRR 6Add BLAST24
Repeati241 – 263LRR 7Add BLAST23
Repeati265 – 288LRR 8Add BLAST24
Repeati289 – 311LRR 9Add BLAST23
Repeati313 – 335LRR 10Add BLAST23
Repeati337 – 359LRR 11Add BLAST23
Repeati361 – 383LRR 12Add BLAST23
Repeati385 – 407LRR 13Add BLAST23
Repeati409 – 431LRR 14Add BLAST23
Repeati432 – 454LRR 15Add BLAST23
Repeati456 – 478LRR 16Add BLAST23
Repeati480 – 503LRR 17Add BLAST24
Repeati504 – 527LRR 18Add BLAST24
Repeati528 – 550LRR 19Add BLAST23
Repeati552 – 574LRR 20Add BLAST23
Repeati576 – 599LRR 21Add BLAST24
Repeati600 – 621LRR 22Add BLAST22
Repeati627 – 649LRR 23Add BLAST23
Repeati650 – 673LRR 24Add BLAST24
Repeati674 – 696LRR 25Add BLAST23
Repeati699 – 721LRR 26Add BLAST23
Repeati723 – 746LRR 27Add BLAST24
Repeati747 – 769LRR 28Add BLAST23
<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>Domaini870 – 1155Protein kinasePROSITE-ProRule annotationAdd BLAST286

<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

Both extracellular leucine-rich repeats and protein kinase domains are required for flg22-binding. The LRR 9 to LRR 15 domains are involved in flg22-binding.1 Publication

<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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG502QPYS, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_000288_22_1_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9FL28

KEGG Orthology (KO)

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KOi
K13420

Identification of Orthologs from Complete Genome Data

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OMAi
GALPRHC

Database of Orthologous Groups

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OrthoDBi
826997at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9FL28

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.80.10.10, 6 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011009, Kinase-like_dom_sf
IPR001611, Leu-rich_rpt
IPR003591, Leu-rich_rpt_typical-subtyp
IPR032675, LRR_dom_sf
IPR013210, LRR_N_plant-typ
IPR000719, Prot_kinase_dom
IPR008271, Ser/Thr_kinase_AS

Pfam protein domain database

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Pfami
View protein in Pfam
PF00560, LRR_1, 2 hits
PF13855, LRR_8, 2 hits
PF08263, LRRNT_2, 1 hit
PF00069, Pkinase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00369, LRR_TYP, 13 hits
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
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.

Q9FL28-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKLLSKTFLI LTLTFFFFGI ALAKQSFEPE IEALKSFKNG ISNDPLGVLS
60 70 80 90 100
DWTIIGSLRH CNWTGITCDS TGHVVSVSLL EKQLEGVLSP AIANLTYLQV
110 120 130 140 150
LDLTSNSFTG KIPAEIGKLT ELNQLILYLN YFSGSIPSGI WELKNIFYLD
160 170 180 190 200
LRNNLLSGDV PEEICKTSSL VLIGFDYNNL TGKIPECLGD LVHLQMFVAA
210 220 230 240 250
GNHLTGSIPV SIGTLANLTD LDLSGNQLTG KIPRDFGNLL NLQSLVLTEN
260 270 280 290 300
LLEGDIPAEI GNCSSLVQLE LYDNQLTGKI PAELGNLVQL QALRIYKNKL
310 320 330 340 350
TSSIPSSLFR LTQLTHLGLS ENHLVGPISE EIGFLESLEV LTLHSNNFTG
360 370 380 390 400
EFPQSITNLR NLTVLTVGFN NISGELPADL GLLTNLRNLS AHDNLLTGPI
410 420 430 440 450
PSSISNCTGL KLLDLSHNQM TGEIPRGFGR MNLTFISIGR NHFTGEIPDD
460 470 480 490 500
IFNCSNLETL SVADNNLTGT LKPLIGKLQK LRILQVSYNS LTGPIPREIG
510 520 530 540 550
NLKDLNILYL HSNGFTGRIP REMSNLTLLQ GLRMYSNDLE GPIPEEMFDM
560 570 580 590 600
KLLSVLDLSN NKFSGQIPAL FSKLESLTYL SLQGNKFNGS IPASLKSLSL
610 620 630 640 650
LNTFDISDNL LTGTIPGELL ASLKNMQLYL NFSNNLLTGT IPKELGKLEM
660 670 680 690 700
VQEIDLSNNL FSGSIPRSLQ ACKNVFTLDF SQNNLSGHIP DEVFQGMDMI
710 720 730 740 750
ISLNLSRNSF SGEIPQSFGN MTHLVSLDLS SNNLTGEIPE SLANLSTLKH
760 770 780 790 800
LKLASNNLKG HVPESGVFKN INASDLMGNT DLCGSKKPLK PCTIKQKSSH
810 820 830 840 850
FSKRTRVILI ILGSAAALLL VLLLVLILTC CKKKEKKIEN SSESSLPDLD
860 870 880 890 900
SALKLKRFEP KELEQATDSF NSANIIGSSS LSTVYKGQLE DGTVIAVKVL
910 920 930 940 950
NLKEFSAESD KWFYTEAKTL SQLKHRNLVK ILGFAWESGK TKALVLPFME
960 970 980 990 1000
NGNLEDTIHG SAAPIGSLLE KIDLCVHIAS GIDYLHSGYG FPIVHCDLKP
1010 1020 1030 1040 1050
ANILLDSDRV AHVSDFGTAR ILGFREDGST TASTSAFEGT IGYLAPEFAY
1060 1070 1080 1090 1100
MRKVTTKADV FSFGIIMMEL MTKQRPTSLN DEDSQDMTLR QLVEKSIGNG
1110 1120 1130 1140 1150
RKGMVRVLDM ELGDSIVSLK QEEAIEDFLK LCLFCTSSRP EDRPDMNEIL
1160 1170
THLMKLRGKA NSFREDRNED REV
Length:1,173
Mass (Da):128,824
Last modified:March 1, 2001 - 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:i6AF93B467A339359
GO

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 conflicti652Q → K in AAO41929 (PubMed:14593172).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AB010698 Genomic DNA Translation: BAB11088.1
CP002688 Genomic DNA Translation: AED95370.1
CP002688 Genomic DNA Translation: ANM68238.1
BT003880 mRNA Translation: AAO41929.1
AK226709 mRNA Translation: BAE98815.1

NCBI Reference Sequences

More...
RefSeqi
NP_001330009.1, NM_001344672.1
NP_199445.1, NM_124003.4

Genome annotation databases

Ensembl plant genome annotation project

More...
EnsemblPlantsi
AT5G46330.1; AT5G46330.1; AT5G46330
AT5G46330.2; AT5G46330.2; AT5G46330

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
834676

Gramene; a comparative resource for plants

More...
Gramenei
AT5G46330.1; AT5G46330.1; AT5G46330
AT5G46330.2; AT5G46330.2; AT5G46330

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ath:AT5G46330

<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%5Freferences%5Fsection">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
AB010698 Genomic DNA Translation: BAB11088.1
CP002688 Genomic DNA Translation: AED95370.1
CP002688 Genomic DNA Translation: ANM68238.1
BT003880 mRNA Translation: AAO41929.1
AK226709 mRNA Translation: BAE98815.1
RefSeqiNP_001330009.1, NM_001344672.1
NP_199445.1, NM_124003.4

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4MN8X-ray3.06A25-800[»]
4MNAX-ray4.00A25-800[»]
SMRiQ9FL28
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi19925, 54 interactors
DIPiDIP-46004N
IntActiQ9FL28, 45 interactors
MINTiQ9FL28
STRINGi3702.AT5G46330.1

PTM databases

iPTMnetiQ9FL28
SwissPalmiQ9FL28

Proteomic databases

PaxDbiQ9FL28
PRIDEiQ9FL28
ProteomicsDBi230627

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
834676

Genome annotation databases

EnsemblPlantsiAT5G46330.1; AT5G46330.1; AT5G46330
AT5G46330.2; AT5G46330.2; AT5G46330
GeneIDi834676
GrameneiAT5G46330.1; AT5G46330.1; AT5G46330
AT5G46330.2; AT5G46330.2; AT5G46330
KEGGiath:AT5G46330

Organism-specific databases

AraportiAT5G46330
TAIRilocus:2170483, AT5G46330

Phylogenomic databases

eggNOGiENOG502QPYS, Eukaryota
HOGENOMiCLU_000288_22_1_1
InParanoidiQ9FL28
KOiK13420
OMAiGALPRHC
OrthoDBi826997at2759
PhylomeDBiQ9FL28

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q9FL28

Gene expression databases

ExpressionAtlasiQ9FL28, baseline and differential
GenevisibleiQ9FL28, AT

Family and domain databases

Gene3Di3.80.10.10, 6 hits
InterProiView protein in InterPro
IPR011009, Kinase-like_dom_sf
IPR001611, Leu-rich_rpt
IPR003591, Leu-rich_rpt_typical-subtyp
IPR032675, LRR_dom_sf
IPR013210, LRR_N_plant-typ
IPR000719, Prot_kinase_dom
IPR008271, Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF00560, LRR_1, 2 hits
PF13855, LRR_8, 2 hits
PF08263, LRRNT_2, 1 hit
PF00069, Pkinase, 1 hit
SMARTiView protein in SMART
SM00369, LRR_TYP, 13 hits
SM00220, S_TKc, 1 hit
SUPFAMiSSF56112, SSF56112, 1 hit
PROSITEiView protein in PROSITE
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 nameiFLS2_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: Q9FL28
Secondary accession number(s): Q0WVN3, Q84WF4
<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: March 18, 2008
Last sequence update: March 1, 2001
Last modified: October 7, 2020
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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