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Entry version 81 (16 Oct 2019)
Sequence version 2 (13 Feb 2019)
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Protein

LRR receptor-like serine/threonine-protein kinase GHR1

Gene

GHR1

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

Receptor kinase acting as an early component in abscisic acid (ABA) signaling (PubMed:22730405). Required for darkness, ABA, high CO2 and hydrogen peroxide (H2O2) induction of S-type anion currents in guard cells leading to stomatal closure, possibly via the phosphorylation and activation of the anion channel SLAC1 and as a scaffolding component (PubMed:22730405, PubMed:27694184, PubMed:30361234). Seems to act in parallel with SRK2E/OST1 in the ABA signaling pathway which regulates stomatal movement (PubMed:22730405). Binds ATP (PubMed:30361234). Involved in the local and/or systemic stomatal responses (e.g. stomatal closure) to light stress (PubMed:29463779).4 Publications

Caution

Exhibits protein kinase activity according to PubMed:22730405, but in contradiction, described as an inactive pseudokinase by PubMed:30361234.2 Publications

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

Negatively regulated by ABI2.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei798ATPPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi776 – 784ATPPROSITE-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

  • ATP binding Source: UniProtKB-KW
  • protein kinase activity Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB-KW

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 processAbscisic acid signaling pathway, Stress response
LigandATP-binding, Nucleotide-binding

Protein family/group databases

Transport Classification Database

More...
TCDBi
1.A.87.2.4 the mechanosensitive calcium channel (mca) family

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

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
LRR receptor-like serine/threonine-protein kinase GHR11 Publication (EC:2.7.11.11 Publication)
Alternative name(s):
Protein GUARD CELL HYDROGEN PEROXIDE-RESISTANT 11 Publication
Short name:
AtGHR11 Publication
Protein RADICAL-INDUCED CELL DEATH 71 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:GHR11 Publication
Synonyms:RCD71 Publication
Ordered Locus Names:At4g20940Imported
ORF Names:T13K14.100Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiArabidopsis thaliana (Mouse-ear cress)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri3702 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000006548 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 4

Organism-specific databases

Arabidopsis Information Portal

More...
Araporti
AT4G20940

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

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini19 – 630ExtracellularCuratedAdd BLAST612
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei631 – 651HelicalSequence analysisAdd BLAST21
Topological domaini652 – 1053CytoplasmicCuratedAdd BLAST402

Keywords - Cellular componenti

Cell membrane, 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 under normal growth conditions but early wilting (PubMed:22730405). Increased sensitivity to drought stress due to impaired stomatal closure and increased water loss (PubMed:22730405). Abolished CO2-mediated and darkness-induced stomatal closure (PubMed:27694184). Defective abscisic acid (ABA) and hydrogen peroxide (H2O2) induction of stomatal closure associated with an impaired activation of S-type anion currents in guard cells (PubMed:22730405). Impaired stomatal closure after treatment with methyl jasmonate (MeJA), salicylic acid (SA) and flagellin 22 (Flg22) (PubMed:29463779). Altered ABA-mediated inhibition of light-induced stomatal opening (PubMed:22730405). Apoplastic ROS-sensitive plants exhibiting severe tissue damage when exposed to ozone (O3) (PubMed:30361234).4 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi56G → D in ghr1-13; apoplastic ROS-sensitive plants exhibiting increased tissue damage when exposed to ozone (O3) and slightly higher steady-state stomatal conductance; when associated with N-220. 1 Publication1
Mutagenesisi57C → A: Abolishes the capacity to complement the water loss phenotype of the ghr1 mutant. 1 Publication1
Mutagenesisi63G → D in ghr1-12; apoplastic ROS-sensitive plants exhibiting increased tissue damage when exposed to ozone (O3). Slightly higher steady-state stomatal conductance. 1 Publication1
Mutagenesisi66C → A: Abolishes the capacity to complement the water loss phenotype of the ghr1 mutant. 1 Publication1
Mutagenesisi108G → D in ghr1-7; apoplastic ROS-sensitive plants exhibiting increased tissue damage when exposed to ozone (O3). Slightly higher steady-state stomatal conductance. 1 Publication1
Mutagenesisi220D → N in ghr1-13; apoplastic ROS-sensitive plants exhibiting increased tissue damage when exposed to ozone (O3) and slightly higher steady-state stomatal conductance; when associated with D-56. 1 Publication1
Mutagenesisi293D → N in ghr1-8; apoplastic ROS-sensitive plants exhibiting increased tissue damage when exposed to ozone (O3). Slightly higher steady-state stomatal conductance. 1 Publication1
Mutagenesisi381C → A: No effect on the capacity to complement the water loss phenotype of the ghr1 mutant. 1 Publication1
Mutagenesisi618A → T in ghr1-2/rcd7 and ghr1-10; apoplastic ROS-sensitive plants exhibiting increased tissue damage when exposed to ozone (O3). Slightly higher steady-state stomatal conductance. 1 Publication1
Mutagenesisi637A → V in ghr1-15; apoplastic ROS-sensitive plants exhibiting increased tissue damage when exposed to ozone (O3). Slightly higher steady-state stomatal conductance. 1 Publication1
Mutagenesisi680S → N in ghr1-16; apoplastic ROS-sensitive plants exhibiting increased tissue damage when exposed to ozone (O3). Slightly higher steady-state stomatal conductance. 1 Publication1
Mutagenesisi798K → E: Loss of phosphorylation activity on SLAC1. 1 Publication1
Mutagenesisi798K → W: Impaired ATP 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 – 18Sequence analysisAdd BLAST18
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000038755519 – 1053LRR receptor-like serine/threonine-protein kinase GHR1Add BLAST1035

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi92N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
<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 residuei100Phosphoserine; by HT11 Publication1
Modified residuei102Phosphoserine; by HT11 Publication1
Glycosylationi103N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Modified residuei105Phosphoserine; by HT11 Publication1
Modified residuei126Phosphoserine; by HT11 Publication1
Glycosylationi146N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi153N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi196N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi239N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Modified residuei262Phosphoserine; by HT11 Publication1
Glycosylationi269N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Modified residuei278Phosphoserine; by HT11 Publication1
Modified residuei280Phosphothreonine; by HT11 Publication1
Modified residuei281Phosphoserine; by HT11 Publication1
Modified residuei325Phosphoserine; by HT11 Publication1
Glycosylationi347N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi394N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Modified residuei406Phosphotyrosine; by HT11 Publication1
Modified residuei410Phosphoserine; by HT11 Publication1
Modified residuei415Phosphothreonine; by HT11 Publication1
Modified residuei417Phosphoserine; by HT11 Publication1
Glycosylationi432N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Modified residuei434Phosphoserine; by HT11 Publication1
Glycosylationi534N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi566N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi575N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Modified residuei613Phosphoserine; by HT11 Publication1
Modified residuei614Phosphoserine; by HT11 Publication1
Modified residuei616Phosphoserine; by HT11 Publication1
Glycosylationi621N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Modified residuei669Phosphothreonine; by HT11 Publication1
Modified residuei675Phosphothreonine; by HT11 Publication1
Modified residuei678Phosphoserine; by HT11 Publication1
Modified residuei680Phosphoserine; by HT11 Publication1
Modified residuei698Phosphoserine; by HT11 Publication1
Modified residuei699Phosphoserine; by HT11 Publication1
Modified residuei700Phosphoserine; by HT11 Publication1
Modified residuei704Phosphoserine1 Publication1
Modified residuei713Phosphothreonine; by HT11 Publication1
Modified residuei716Phosphoserine; by HT11 Publication1
Modified residuei718Phosphoserine; by HT11 Publication1
Modified residuei720Phosphothreonine; by HT11 Publication1
Modified residuei721Phosphoserine; by HT11 Publication1
Modified residuei724Phosphoserine; by HT11 Publication1
Modified residuei760Phosphoserine; by HT11 Publication1
Modified residuei764Phosphothreonine; by HT11 Publication1
Modified residuei769Phosphoserine; by HT11 Publication1
Modified residuei928Phosphothreonine; by HT11 Publication1
Modified residuei1010Phosphothreonine; by HT11 Publication1
Modified residuei1015Phosphoserine; by HT11 Publication1
Modified residuei1045Phosphothreonine; by HT11 Publication1
Modified residuei1047Phosphotyrosine; by HT11 Publication1
Modified residuei1051Phosphoserine; by HT11 Publication1
Modified residuei1052Phosphoserine; by HT11 Publication1

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

Phosphorylated by HT1; this phosphorylation is inhibited by MPK12 and MPK4.2 Publications

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

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

More...
PaxDbi
C0LGQ9

PRoteomics IDEntifications database

More...
PRIDEi
C0LGQ9

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
C0LGQ9

<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 guard cells and in the vasculature of roots and leaves.2 Publications

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
C0LGQ9 baseline and differential

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

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

Interacts with SLAC1 (via N-terminus) (PubMed:22730405, PubMed:30361234). Binds to ABI2, but not ABI1 (PubMed:22730405).

Interacts with CPK3 (PubMed:30361234).

2 Publications

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

WithEntry#Exp.IntActNotes
At2g28960C0LGL42EBI-16939160,EBI-16946048

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
13133, 47 interactors

Protein interaction database and analysis system

More...
IntActi
C0LGQ9, 48 interactors

STRING: functional protein association networks

More...
STRINGi
3702.AT4G20940.1

<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

3D structure databases

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

More...
SMRi
C0LGQ9

Database of comparative protein structure models

More...
ModBasei
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>Repeati73 – 93LRR 1Sequence analysisAdd BLAST21
Repeati94 – 119LRR 2Sequence analysisAdd BLAST26
Repeati121 – 141LRR 3Sequence analysisAdd BLAST21
Repeati142 – 165LRR 4Sequence analysisAdd BLAST24
Repeati166 – 189LRR 5Sequence analysisAdd BLAST24
Repeati191 – 212LRR 6Sequence analysisAdd BLAST22
Repeati213 – 237LRR 7Sequence analysisAdd BLAST25
Repeati239 – 260LRR 8Sequence analysisAdd BLAST22
Repeati262 – 285LRR 9Sequence analysisAdd BLAST24
Repeati286 – 309LRR 10Sequence analysisAdd BLAST24
Repeati310 – 333LRR 11Sequence analysisAdd BLAST24
Repeati335 – 357LRR 12Sequence analysisAdd BLAST23
Repeati358 – 384LRR 13Sequence analysisAdd BLAST27
Repeati401 – 425LRR 14Sequence analysisAdd BLAST25
Repeati426 – 449LRR 15Sequence analysisAdd BLAST24
Repeati450 – 474LRR 16Sequence analysisAdd BLAST25
Repeati476 – 498LRR 17Sequence analysisAdd BLAST23
Repeati499 – 521LRR 18Sequence analysisAdd BLAST23
Repeati522 – 546LRR 19Sequence analysisAdd BLAST25
Repeati548 – 570LRR 20Sequence analysisAdd BLAST23
Repeati572 – 592LRR 21Sequence analysisAdd BLAST21
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini770 – 1053Protein kinasePROSITE-ProRule annotationAdd BLAST284

<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 protein kinase domain is predicted to be catalytically inactive.1 PublicationPROSITE-ProRule annotation

<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
ENOG410ITA6 Eukaryota
COG4886 LUCA

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
C0LGQ9

Database of Orthologous Groups

More...
OrthoDBi
826997at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
C0LGQ9

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.80.10.10, 3 hits

Integrated resource of protein families, domains and functional sites

More...
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
IPR001245 Ser-Thr/Tyr_kinase_cat_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF13516 LRR_6, 2 hits
PF13855 LRR_8, 3 hits
PF08263 LRRNT_2, 1 hit
PF07714 Pkinase_Tyr, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00369 LRR_TYP, 8 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50011 PROTEIN_KINASE_DOM, 1 hit

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

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

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

C0LGQ9-1 [UniParc]FASTAAdd to basket
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        10         20         30         40         50
MNLSRILLLS MFFLSAMGQL PSQDIMALLE FKKGIKHDPT GFVLNSWNDE
60 70 80 90 100
SIDFNGCPSS WNGIVCNGGN VAGVVLDNLG LTADADFSLF SNLTKLVKLS
110 120 130 140 150
MSNNSLSGVL PNDLGSFKSL QFLDLSDNLF SSSLPKEIGR SVSLRNLSLS
160 170 180 190 200
GNNFSGEIPE SMGGLISLQS LDMSSNSLSG PLPKSLTRLN DLLYLNLSSN
210 220 230 240 250
GFTGKMPRGF ELISSLEVLD LHGNSIDGNL DGEFFLLTNA SYVDISGNRL
260 270 280 290 300
VTTSGKLLPG VSESIKHLNL SHNQLEGSLT SGFQLFQNLK VLDLSYNMLS
310 320 330 340 350
GELPGFNYVY DLEVLKLSNN RFSGSLPNNL LKGDSLLLTT LDLSGNNLSG
360 370 380 390 400
PVSSIMSTTL HTLDLSSNSL TGELPLLTGG CVLLDLSNNQ FEGNLTRWSK
410 420 430 440 450
WENIEYLDLS QNHFTGSFPD ATPQLLRANH LNLSYNKLTG SLPERIPTHY
460 470 480 490 500
PKLRVLDISS NSLEGPIPGA LLSMPTLEEI HLQNNGMTGN IGPLPSSGSR
510 520 530 540 550
IRLLDLSHNR FDGDLPGVFG SLTNLQVLNL AANNLSGSLP SSMNDIVSLS
560 570 580 590 600
SLDVSQNHFT GPLPSNLSSN IMAFNVSYND LSGTVPENLK NFPPPSFYPG
610 620 630 640 650
NSKLVLPAGS PGSSASEASK NKSTNKLVKV VIIVSCAVAL IILILVAILL
660 670 680 690 700
FCICKSRRRE ERSITGKETN RRAQTIPSGS GGGMVVSAED LVASRKGSSS
710 720 730 740 750
EILSPDEKLA VATGFSPSKT SNLSWSPGSG DSFPADQQLA RLDVRSPDRL
760 770 780 790 800
VGELHFLDDS IKLTPEELSR APAEVLGRSS HGTSYRATLD NGVFLTVKWL
810 820 830 840 850
REGVAKQRKE FAKEVKKFSN IRHPNVVTLR GYYWGPTQHE KLILSDYISP
860 870 880 890 900
GSLASFLYDR PGRKGPPLAW TQRLKIAVDV ARGLNYLHFD RAVPHGNLKA
910 920 930 940 950
TNILLDGAEL NARVADYCLH RLMTQAGTVE QILDAGILGY RAPELAASRK
960 970 980 990 1000
PLPSFKSDVY AFGVILLEIL TGRCAGDVIT GEQEGVDLTD WVRLRVAEGR
1010 1020 1030 1040 1050
GAECFDSVLT QEMGSDPVTE KGMKEVLGIA LRCIRSVSER PGIKTIYEDL

SSI
Length:1,053
Mass (Da):113,881
Last modified:February 13, 2019 - 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:i9A714A3EC89C02AB
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 AEE84378 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence CAB45889 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence CAB79094 differs from that shown. Reason: Erroneous gene model prediction.Curated

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
KF531634 mRNA Translation: AGT59499.1
AL080282 Genomic DNA Translation: CAB45889.1 Sequence problems.
AL161554 Genomic DNA Translation: CAB79094.1 Sequence problems.
CP002687 Genomic DNA Translation: AEE84378.2 Different initiation.
FJ708750 mRNA Translation: ACN59344.1

Protein sequence database of the Protein Information Resource

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PIRi
T10636

NCBI Reference Sequences

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RefSeqi
NP_001320016.1, NM_001341467.1

Genome annotation databases

Ensembl plant genome annotation project

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EnsemblPlantsi
AT4G20940.1; AT4G20940.1; AT4G20940

Database of genes from NCBI RefSeq genomes

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GeneIDi
827842

Gramene; a comparative resource for plants

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Gramenei
AT4G20940.1; AT4G20940.1; AT4G20940

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
ath:AT4G20940

<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
KF531634 mRNA Translation: AGT59499.1
AL080282 Genomic DNA Translation: CAB45889.1 Sequence problems.
AL161554 Genomic DNA Translation: CAB79094.1 Sequence problems.
CP002687 Genomic DNA Translation: AEE84378.2 Different initiation.
FJ708750 mRNA Translation: ACN59344.1
PIRiT10636
RefSeqiNP_001320016.1, NM_001341467.1

3D structure databases

SMRiC0LGQ9
ModBaseiSearch...

Protein-protein interaction databases

BioGridi13133, 47 interactors
IntActiC0LGQ9, 48 interactors
STRINGi3702.AT4G20940.1

Protein family/group databases

TCDBi1.A.87.2.4 the mechanosensitive calcium channel (mca) family

PTM databases

iPTMnetiC0LGQ9

Proteomic databases

PaxDbiC0LGQ9
PRIDEiC0LGQ9

Genome annotation databases

EnsemblPlantsiAT4G20940.1; AT4G20940.1; AT4G20940
GeneIDi827842
GrameneiAT4G20940.1; AT4G20940.1; AT4G20940
KEGGiath:AT4G20940

Organism-specific databases

AraportiAT4G20940

Phylogenomic databases

eggNOGiENOG410ITA6 Eukaryota
COG4886 LUCA
InParanoidiC0LGQ9
OrthoDBi826997at2759
PhylomeDBiC0LGQ9

Miscellaneous databases

Protein Ontology

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PROi
PR:C0LGQ9

Gene expression databases

ExpressionAtlasiC0LGQ9 baseline and differential

Family and domain databases

Gene3Di3.80.10.10, 3 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
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
PfamiView protein in Pfam
PF13516 LRR_6, 2 hits
PF13855 LRR_8, 3 hits
PF08263 LRRNT_2, 1 hit
PF07714 Pkinase_Tyr, 1 hit
SMARTiView protein in SMART
SM00369 LRR_TYP, 8 hits
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS50011 PROTEIN_KINASE_DOM, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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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 nameiGHR1_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: C0LGQ9
Secondary accession number(s): F4JIJ5, Q9SUB9, T1T4Z8
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: February 13, 2019
Last modified: October 16, 2019
This is version 81 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
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