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Entry version 157 (07 Apr 2021)
Sequence version 2 (28 Jul 2009)
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Protein

Somatic embryogenesis receptor kinase 1

Gene

SERK1

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. Phosphorylates BRI1 on 'Ser-887' and CDC48 on at least one threonine residue and on 'Ser-41'. Confers embryogenic competence. Acts redundantly with SERK2 as a control point for sporophytic development controlling male gametophyte production. Involved in the brassinolide signaling pathway. Probably required during small peptide (e.g. RGF1) signaling (Probable). Involved in the perception of phytosulfokine and subsequent signal transduction (PubMed:26308901). Acts as a RLK5 coreceptor and promotes high-affinity IDA sensing, thus being a positive regulator of floral abscission (PubMed:27058169).1 Publication4 Publications

Miscellaneous

Seems to be related with early development of tissues in general rather than with embryogenesis.

<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 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+

<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

Inhibited by manganese.

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=4 µM for ATP1 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 sitei330ATPPROSITE-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 sitei429Proton 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 bindingi308 – 316ATPPROSITE-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, Tyrosine-protein kinase
    LigandATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    Q94AG2

    <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:
    Somatic embryogenesis receptor kinase 11 Publication (EC:2.7.10.1PROSITE-ProRule annotation, EC:2.7.11.1PROSITE-ProRule annotation)
    Short name:
    AtSERK11 Publication
    Alternative name(s):
    Somatic embryogenesis receptor-like 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:SERK11 Publication
    Ordered Locus Names:At1g71830Imported
    ORF Names:F14O23.21Imported, F14O23_24Imported
    <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 1

    Organism-specific databases

    Arabidopsis Information Portal

    More...
    Araporti
    AT1G71830

    The Arabidopsis Information Resource

    More...
    TAIRi
    locus:2013021, AT1G71830

    <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

    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 domaini27 – 238ExtracellularSequence analysisAdd BLAST212
    <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>Transmembranei239 – 259HelicalSequence analysisAdd BLAST21
    Topological domaini260 – 625CytoplasmicSequence analysisAdd BLAST366

    Keywords - Cellular componenti

    Cell membrane, Endoplasmic reticulum, 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

    No visible phenotype. Serk1 and serk2 double mutants are completely male sterile due to a failure in tapetum specification. Delayed floral abscission (PubMed:27058169).3 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>Mutagenesisi330K → E: Loss of kinase activity. 1 Publication1
    Mutagenesisi459T → A or E: No effect. 1 Publication1
    Mutagenesisi462T → A or E: Decreased kinase activity. Loss of kinase activity; when associated with A,E-463 and A,E-468. 1 Publication1
    Mutagenesisi463T → A or E: Loss of autophosphorylation. Loss of kinase activity; when associated with A,E-462 and A,E-468. 1 Publication1
    Mutagenesisi468T → A or E: Loss of kinase activity. Loss of kinase activity; when associated with A,E-462 and A,E-463. 1 Publication1
    Mutagenesisi541T → A: No effect. Reduction of autophosphorylation; when associated with A-570. 1 Publication1
    Mutagenesisi562S → A: Loss of autophosphorylation. 1 Publication1
    Mutagenesisi570S → A: No effect. Reduction of autophosphorylation; when associated with A-541. 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 – 26Sequence analysisAdd BLAST26
    <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_000037959627 – 625Somatic embryogenesis receptor kinase 1Add BLAST599

    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 bondi58 ↔ 65Combined sources4 Publications
    <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>Glycosylationi104N-linked (GlcNAc...) asparaginePROSITE-ProRule annotationCombined sources1 Publication1
    Glycosylationi115N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
    Glycosylationi150N-linked (GlcNAc...) asparaginePROSITE-ProRule annotationCombined sources3 Publications1
    Glycosylationi163N-linked (GlcNAc...) asparaginePROSITE-ProRule annotationCombined sources1 Publication1
    Glycosylationi184N-linked (GlcNAc...) asparaginePROSITE-ProRule annotationCombined sources2 Publications1
    Disulfide bondi202 ↔ 210Combined sources4 Publications
    <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 residuei291Phosphoserine1 Publication1
    Modified residuei299Phosphoserine1 Publication1
    Modified residuei303Phosphoserine1 Publication1
    Modified residuei325Phosphothreonine1 Publication1
    Modified residuei337Phosphothreonine1 Publication1
    Modified residuei346Phosphothreonine1 Publication1
    Modified residuei352Phosphoserine1 Publication1
    Modified residuei383Phosphoserine1 Publication1
    Modified residuei386PhosphoserineBy similarity1
    Modified residuei394Phosphoserine1 Publication1
    Modified residuei402Phosphothreonine1 Publication1
    Modified residuei415Phosphoserine1 Publication1
    Modified residuei456Phosphotyrosine1 Publication1
    Modified residuei459Phosphothreonine1 Publication1
    Modified residuei462Phosphothreonine1 Publication1
    Modified residuei463Phosphothreonine1 Publication1
    Modified residuei468Phosphothreonine1 Publication1
    Modified residuei476Phosphotyrosine1 Publication1
    Modified residuei478Phosphoserine1 Publication1
    Modified residuei479Phosphothreonine1 Publication1
    Modified residuei483Phosphoserine1 Publication1
    Modified residuei541Phosphothreonine1 Publication1
    Modified residuei543Phosphotyrosine1 Publication1
    Modified residuei559Phosphothreonine1 Publication1
    Modified residuei606Phosphoserine1 Publication1
    Modified residuei612Phosphoserine1 Publication1
    Modified residuei613Phosphothreonine1 Publication1
    Modified residuei614Phosphotyrosine1 Publication1
    Modified residuei622Phosphoserine1 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

    Glycosylated. Important for targeting to the plasma membrane.
    Intermolecular autophosphorylation. The catalytic activity of SERK1 depends on the presence of a phosphorylated Thr residue in SERK1. The phosphorylation is induced by brassinosteroids. Transphosphorylation by BRI1 occurs only on Ser-299 and Thr-462. Dephosphorylation of threonine residues by the kinase-associated protein phosphatase (KAPP) is involved in SERK1 endocytosis.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

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

    More...
    PaxDbi
    Q94AG2

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q94AG2

    ProteomicsDB: a multi-organism proteome resource

    More...
    ProteomicsDBi
    232575

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    Q94AG2

    <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 in flowers, tapetum, developing microspores, all cells of the embryo sac, provascular strands and developing vascular bundles. Low expression in adult vascular tissue. Detected in root meristem.4 Publications

    <p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

    Expressed during pollen development and megasporogenesis in the nucellus of developing ovules, in all cells of the embryo sac up to fertilization and in all cells of the developing embryo until the heart-shaped stage. Found in epidermal and vascular cells of the late torpedo and cotyledon stages embryos.3 Publications

    Gene expression databases

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    Q94AG2, baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    Q94AG2, 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

    Monomer, homo- and heterodimer.

    Interacts with KAPP, CDC48A, GRF6 or GRF7, SERK2, BRI1 and SERK3/BAK1 to form the SERK1 signaling complex. Bind to BRI1 in a brassinolide-dependent manner (PubMed:23929946). Heterodimer with PSKR1 (PubMed:26308901).

    Interacts with the EF-Tu receptor EFR and FLS2 in a specific ligand-induced manner.

    Interacts with ERECTA in a EPF2-induced manner.

    Interacts with ERL1 in a EPF1-induced manner.

    Interacts with TMM (PubMed:26320950). In the presence of the signal peptide RGF1, interacts with RGI1/RGFR4/RCH2, RGI2/RGFR3/RCH1, RGI3/RGFR1, RGI4/RGFR2/SKM2 and RGI5/RGFR5 (PubMed:27229311).

    13 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)

    More...
    BioGRIDi
    28733, 30 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-38028N

    Protein interaction database and analysis system

    More...
    IntActi
    Q94AG2, 34 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    3702.AT1G71830.1

    <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

    1625
    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

    More...
    SMRi
    Q94AG2

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    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>Repeati92 – 116LRR 1Sequence analysisAdd BLAST25
    Repeati118 – 140LRR 2Sequence analysisAdd BLAST23
    Repeati141 – 164LRR 3Sequence analysisAdd BLAST24
    Repeati165 – 189LRR 4Sequence analysisAdd BLAST25
    <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>Domaini302 – 589Protein 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 – 78Leucine-rich repeat receptor-like protein kinase bindingCombined sources2 PublicationsAdd BLAST20
    Regioni61 – 62Brassinolide bindingCombined sources1 Publication2
    Regioni97 – 102Leucine-rich repeat receptor-like protein kinase bindingCombined sources2 Publications6
    Regioni123 – 126Leucine-rich repeat receptor-like protein kinase bindingCombined sources2 Publications4
    Regioni145 – 147Leucine-rich repeat receptor-like protein kinase bindingCombined sources2 Publications3
    Regioni171 – 194Leucine-rich repeat receptor-like protein kinase bindingCombined sources1 PublicationAdd BLAST24

    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 biasi204 – 231Pro-richPROSITE-ProRule annotationAdd BLAST28
    Compositional biasi239 – 260Ala-richPROSITE-ProRule annotationAdd BLAST22

    <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

    The extracellular domain (26-234) is required for dimerization.

    <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

    More...
    eggNOGi
    ENOG502QQ7B, Eukaryota

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_000288_92_7_1

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q94AG2

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    TIHVAFI

    Database of Orthologous Groups

    More...
    OrthoDBi
    684563at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    Q94AG2

    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
    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
    PTHR47988:SF34, PTHR47988:SF34, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    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%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.

    Q94AG2-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MESSYVVFIL LSLILLPNHS LWLASANLEG DALHTLRVTL VDPNNVLQSW
    60 70 80 90 100
    DPTLVNPCTW FHVTCNNENS VIRVDLGNAE LSGHLVPELG VLKNLQYLEL
    110 120 130 140 150
    YSNNITGPIP SNLGNLTNLV SLDLYLNSFS GPIPESLGKL SKLRFLRLNN
    160 170 180 190 200
    NSLTGSIPMS LTNITTLQVL DLSNNRLSGS VPDNGSFSLF TPISFANNLD
    210 220 230 240 250
    LCGPVTSHPC PGSPPFSPPP PFIQPPPVST PSGYGITGAI AGGVAAGAAL
    260 270 280 290 300
    LFAAPAIAFA WWRRRKPLDI FFDVPAEEDP EVHLGQLKRF SLRELQVASD
    310 320 330 340 350
    GFSNKNILGR GGFGKVYKGR LADGTLVAVK RLKEERTPGG ELQFQTEVEM
    360 370 380 390 400
    ISMAVHRNLL RLRGFCMTPT ERLLVYPYMA NGSVASCLRE RPPSQPPLDW
    410 420 430 440 450
    PTRKRIALGS ARGLSYLHDH CDPKIIHRDV KAANILLDEE FEAVVGDFGL
    460 470 480 490 500
    AKLMDYKDTH VTTAVRGTIG HIAPEYLSTG KSSEKTDVFG YGIMLLELIT
    510 520 530 540 550
    GQRAFDLARL ANDDDVMLLD WVKGLLKEKK LEMLVDPDLQ TNYEERELEQ
    560 570 580 590 600
    VIQVALLCTQ GSPMERPKMS EVVRMLEGDG LAEKWDEWQK VEILREEIDL
    610 620
    SPNPNSDWIL DSTYNLHAVE LSGPR
    Length:625
    Mass (Da):69,022
    Last modified:July 28, 2009 - 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:i98F6B69126DB664A
    GO

    <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 AAF43236 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 conflicti53T → R in AAK82463 (PubMed:14593172).Curated1
    Sequence conflicti53T → R in AAN72307 (PubMed:14593172).Curated1
    Sequence conflicti251L → P in CAB42254 (PubMed:11706164).Curated1
    Sequence conflicti266K → S in CAB42254 (PubMed:11706164).Curated1
    Sequence conflicti327V → I in AAK82463 (PubMed:14593172).Curated1
    Sequence conflicti327V → I in AAN72307 (PubMed:14593172).Curated1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    A67827 Unassigned DNA Translation: CAB42254.1
    A67815 Unassigned DNA No translation available.
    FJ708676 mRNA Translation: ACN59271.1
    AC012654 Genomic DNA Translation: AAF43236.1 Sequence problems.
    CP002684 Genomic DNA Translation: AEE35238.1
    AY048200 mRNA Translation: AAK82463.1
    BT002217 mRNA Translation: AAN72307.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    H96740

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_177328.1, NM_105841.4

    Genome annotation databases

    Ensembl plant genome annotation project

    More...
    EnsemblPlantsi
    AT1G71830.1; AT1G71830.1; AT1G71830

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    843513

    Gramene; a comparative resource for plants

    More...
    Gramenei
    AT1G71830.1; AT1G71830.1; AT1G71830

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ath:AT1G71830

    <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
    A67827 Unassigned DNA Translation: CAB42254.1
    A67815 Unassigned DNA No translation available.
    FJ708676 mRNA Translation: ACN59271.1
    AC012654 Genomic DNA Translation: AAF43236.1 Sequence problems.
    CP002684 Genomic DNA Translation: AEE35238.1
    AY048200 mRNA Translation: AAK82463.1
    BT002217 mRNA Translation: AAN72307.1
    PIRiH96740
    RefSeqiNP_177328.1, NM_105841.4

    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
    4LSCX-ray1.53A24-213[»]
    4LSXX-ray3.30C/D24-213[»]
    4Z64X-ray2.66C1-213[»]
    5IYXX-ray2.43C24-213[»]
    6FG8X-ray1.25A24-208[»]
    SMRiQ94AG2
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi28733, 30 interactors
    DIPiDIP-38028N
    IntActiQ94AG2, 34 interactors
    STRINGi3702.AT1G71830.1

    PTM databases

    iPTMnetiQ94AG2

    Proteomic databases

    PaxDbiQ94AG2
    PRIDEiQ94AG2
    ProteomicsDBi232575

    Genome annotation databases

    EnsemblPlantsiAT1G71830.1; AT1G71830.1; AT1G71830
    GeneIDi843513
    GrameneiAT1G71830.1; AT1G71830.1; AT1G71830
    KEGGiath:AT1G71830

    Organism-specific databases

    AraportiAT1G71830
    TAIRilocus:2013021, AT1G71830

    Phylogenomic databases

    eggNOGiENOG502QQ7B, Eukaryota
    HOGENOMiCLU_000288_92_7_1
    InParanoidiQ94AG2
    OMAiTIHVAFI
    OrthoDBi684563at2759
    PhylomeDBiQ94AG2

    Enzyme and pathway databases

    SABIO-RKiQ94AG2

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:Q94AG2

    Gene expression databases

    ExpressionAtlasiQ94AG2, baseline and differential
    GenevisibleiQ94AG2, AT

    Family and domain databases

    Gene3Di3.80.10.10, 1 hit
    InterProiView protein in InterPro
    IPR011009, Kinase-like_dom_sf
    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
    PANTHERiPTHR47988:SF34, PTHR47988:SF34, 1 hit
    PfamiView protein in Pfam
    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 nameiSERK1_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: Q94AG2
    Secondary accession number(s): C0LGI6, Q9M9G3
    <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: July 28, 2009
    Last sequence update: July 28, 2009
    Last modified: April 7, 2021
    This is version 157 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, 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
    UniProt is an ELIXIR core data resource
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