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Entry version 182 (16 Oct 2019)
Sequence version 3 (10 Oct 2018)
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Protein

SNF1-related protein kinase catalytic subunit alpha KIN10

Gene

KIN10

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

Catalytic subunit of the probable trimeric SNF1-related protein kinase (SnRK) complex, a central regulator of cellular energy homeostasis, which, in response to seemingly unrelated darkness, sugar and stress conditions, activates energy-producing pathways and inhibits energy-consuming processes. May play a role in a signal transduction cascade regulating gene expression and carbohydrate metabolism in higher plants. The SnRK complex may also be involved in the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase and in assimilation of nitrogen by phosphorylating nitrate reductase (PubMed:17671505). In vitro, KIN10 exhibits kinase activity on sucrose phosphate synthase and the kinase activity is inhibited by PRL1 (PubMed:10220464). May be a subunit of a SCF ubiquitin ligase complex and thus be involved in proteasomal ubiquitination (PubMed:11387208). Phosphorylates GRIK1/SNAK2 and GRIK2/SNAK1 in vitro (PubMed:20164192). Cooperates with FUS3 to regulate developmental phase transitions and lateral organ development and act both as positive regulators of abscisic acid (ABA) signaling during germination (PubMed:22026387, PubMed:22902692). Phosphorylates FUS3 in embryo (PubMed:28922765). Negatively modulates MYC2 accumulation through its protein phosphorylation (PubMed:24890857). Phosphorylates geminivirus (CaLCuV, TGMV, ToMoV) AL2 protein resulting in a delay in the viral DNA accumulation and symptom appearance during infection (PubMed:24990996). Regulates bZIP63 activity to alter metabolism in response to starvation through its protein phosphorylation (PubMed:26263501). Under sugar deprivation conditions, antagonizes the IDD8 function in flowering time control by its protein phosphorylation (PubMed:25929516). Plays a cardinal role in the control of cell proliferation through inhibition of KRP6 activity by its protein phosphorylation (PubMed:23617622). Under submergence, phosphorylates PTP1, leading to the release of the MPK6 signaling pathway inhibition (PubMed:27029354). Triggers its own SUMO-mediated proteasomal degradation, establishing a negative feedback loop that attenuates SnRK1 signaling and prevents detrimental hyperactivation of stress responses (PubMed:26662259). Phosphorylates RAPTOR1B in vitro (PubMed:27545962). Phosphorylates and down-regulates HMGR1S in vitro (PubMed:28263378). Kinase activity is redox-sensitive (PubMed:28940407). Acts upstream of TOR in the regulation of autophagy. Required for the activation of autophagy by many abiotic stresses (PubMed:28783755). Involved in positive regulation of autophagy, possibly by affecting the phosphorylation of ATG1 proteins (PubMed:28740502). Negatively modulates WRI1 accumulation through its protein phosphorylation (PubMed:28314829). Modulates leaf senescence progression by the negative regulation of EIN3 accumulation through its protein phosphorylation (PubMed:28600557). Under extended darkness, C/S1-bZIP-SnRK1 complex interacts with the histone acetylation machinery to remodel chromatin and facilitate transcription. BZIP2-BZIP63-KIN10 complex binds to the ETFQO promoter to up-regulate its transcription (PubMed:29348240). Phosphorylates and down-regulates IPK2b in vitro (PubMed:29216370). Involved in the regulation of sucrose-induced hypocotyl elongation under light/dark cycles (PubMed:29114081, PubMed:29584583).25 Publications

Miscellaneous

Overexpressing plants show delayed leaf senescence, enhanced tolerance to nutrient starvation dependent on a functional autophagy pathway, enhanced formation of autophagosomes, and tolerance to drought and submergence (PubMed:28740502). Overexpression of KIN10 leads to increased autophagy (PubMed:28783755). Overexpression inhibits sucrose-induced hypocotyl elongation (PubMed:29114081).3 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

Activated by phosphorylation at Thr-175 by GRIK1/SNAK2 and GRIK2/SNAK1 (PubMed:19339507). Inactivated by dephosphorylation at Thr-175 (PubMed:24179127). Inhibited by trehalose-6-phosphate (PubMed:19193861). Down-regulated by SR45 by affecting its stability (PubMed:27436712). Reduced kinase activity in response to H2O2 treatment. The redox-state of Cys-177 seems to directly influence its kinase activity (PubMed:28940407). Down-regulated by FLZ6 and FLZ10 (PubMed:29406622).6 Publications

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 sitei48ATPPROSITE-ProRule annotation2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei142Proton acceptorPROSITE-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 bindingi25 – 33ATPPROSITE-ProRule annotation9

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

GO - Biological processi

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

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processCarbohydrate metabolism, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Nitrate assimilation, Ubl conjugation pathway
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.11.1 399

<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:
SNF1-related protein kinase catalytic subunit alpha KIN10Curated (EC:2.7.11.12 Publications)
Short name:
AKIN10Imported
Alternative name(s):
AKIN alpha-2
Short name:
AKINalpha2
SNF1-related kinase 1.11 Publication
Short name:
SnRK1.11 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:KIN10Curated
Synonyms:AK21Imported, AKIN10Imported, SKIN10Imported, SNR2Imported, SNRK1.11 Publication
Ordered Locus Names:At3g01090Imported
ORF Names:T4P13.22Imported
<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 3

Organism-specific databases

Arabidopsis Information Portal

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Araporti
AT3G01090

The Arabidopsis Information Resource

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TAIRi
locus:2102132 AT3G01090

<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

Keywords - Cellular componenti

Chloroplast, Cytoplasm, Endoplasmic reticulum, Golgi apparatus, Nucleus, Plastid

<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

Anthocyanin accumulation and accelerated senescence (PubMed:17671505). Starch accumulation during phosphate deficiency (PubMed:19211700). Reduced sensitivity to glucose during early development (PubMed:27436712). Increased seed abortion (PubMed:28922765). Blocked autophagy during abiotic stresses but not under control conditions (PubMed:28783755). Enhanced sucrose-induced hypocotyl elongation (PubMed:29584583).6 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>Mutagenesisi34K → R: Abolishes sumoylation. When associated with R-63 and R-390. 1 Publication1
Mutagenesisi48K → M: Abolishes kinase activity. Enhances sensitivity to submergence. 2 Publications1
Mutagenesisi63K → R: Abolishes sumoylation. When associated with R-34 and R-390. 1 Publication1
Mutagenesisi133C → S: Reduced kinase activity and retained redox sensitivity. 1 Publication1
Mutagenesisi175T → A: Abolishes phosphorylation by GRIK1 or GRIK2 leading to inactivation of the protein. Enhances sensitivity to submergence. 4 Publications1
Mutagenesisi175T → D: Enhances tolerance to submergence. 1 Publication1
Mutagenesisi177C → S: Retained kinase activity and abolished redox sensitivity. 1 Publication1
Mutagenesisi390K → R: Abolishes sumoylation. When associated with R-34 and R-63. 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 describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000861281 – 512SNF1-related protein kinase catalytic subunit alpha KIN10Add BLAST512

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 describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki20Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki34Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Cross-linki63Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei164PhosphoserineBy similarity1
Modified residuei175Phosphothreonine; by GRIK1 or GRIK25 Publications1
Modified residuei364Phosphoserine1 Publication1
Cross-linki390Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication

<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 at Thr-175 in response to glucose (PubMed:19302419). Phosphorylated at Thr-175 under submergence (PubMed:27029354). Autophosphorylated (PubMed:10220464, PubMed:24179127, PubMed:25929516). Dephosphorylated at Thr-175 by ABI1 and PP2CA (PubMed:24179127).5 Publications
Ubiquitinated (PubMed:26662259). Degradation is mediated by a CUL4-based E3 ligase that uses PRL1 as a substrate receptor (PubMed:18223036).2 Publications
Sumoylated by SIZ1 (PubMed:20855607, PubMed:26662259). Sumoylated SnRK1 is ubiquitinated and degraded by the proteasome (PubMed:26662259).2 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

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

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PaxDbi
Q38997

PRoteomics IDEntifications database

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PRIDEi
Q38997

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q38997

<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

Isoform 2 is widely expressed, especially in newly developing tissues (PubMed:25697797). Isoform 2 is expressed throughout the seedling, with highest expression in leaf primordia and vascular tissue, and the seedling root tip. Isoform 2 is later expressed in developing lateral root primordia and developing embryos within siliques (PubMed:25071807). Isoform 1 is widely expressed but at very low levels (PubMed:25071807).2 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 throughout embryo development from the heart to mature embryo stages.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

Induced by sucrose (PubMed:10220464). Induced by DCMU herbicide (PubMed:17671505). Induced by glucose (PubMed:19302419). Up-regulated by beta-aminobutyric acid (BABA) (PubMed:20484986). Induced by hypoxia following submergence (PubMed:22232383). Induced by salt and oxidative stresses (at the protein level) (PubMed:26471895).6 Publications

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q38997 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q38997 AT

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

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

Subunit of a probable heterotrimeric complex consisting of an alpha catalytic (KIN10 or KIN11) subunit, and a beta (KINB) and a gamma (KING or SNF4) non-catalytic regulatory subunits (PubMed:17028154, PubMed:25736509).

Interacts with KINB2, KINB3, SNF4 and probably with KINB1 and KING1 (PubMed:10929106, PubMed:11522840, PubMed:15803412, PubMed:17028154, PubMed:21235649).

Interacts with SKP1/ASK1, PAD1, the N-terminus of PRL1 and the WD40 domain of 5PTase13 (PubMed:10220464, PubMed:11387208, PubMed:18931139). Potential subunit of a SCF ubiquitin ligase complex consisting of a SNF1-related protein kinase, SKP1 and CUL1. The association of the SCF complex with the proteasome may be mediated by PAD1 and seems to be inhibited by the interaction with PRL1 (PubMed:11387208).

Interacts with ATAF1 (Ref. 26).

Interacts with ESD4 (PubMed:20855607).

Interacts with SCE1 (PubMed:20855607, PubMed:26662259).

Interacts with FUS3 (PubMed:22026387).

Interacts with PP2C74 (PubMed:22449965).

Interacts with CDKE1 (PubMed:23229550).

Interacts with ABI1 and PP2CA (PubMed:24179127).

Interacts with KRP6 (PubMed:23617622).

Interacts with CIPK14 (PubMed:25058458).

Interacts with FLZ proteins through their FLZ-type zinc finger domains (PubMed:24600465, PubMed:29945970).

Interacts with GEBP/STKR1 (PubMed:24600465, PubMed:29192025).

Interacts with MYC2 (PubMed:24890857).

Interacts with IDD8 (PubMed:25929516).

Interacts with BZIP63 (PubMed:26263501).

Interacts with PTL (PubMed:25697797).

Interacts with FLZ3, FLZ9, TCP3, TCP13, HB21/ZHD3 and HB23/ZHD10 (Ref. 50).

Interacts with PTP1 (PubMed:27029354).

Interacts with RAPTOR1B (PubMed:27545962). Forms oligomers in vitro under strongly reducing conditions (PubMed:28940407).

Interacts with WRI1 (PubMed:28314829).

Interacts with EIN3 (PubMed:28600557).

Component of a ternary complex composed of BZIP2-BZIP63 heterodimer and KIN10 (PubMed:29348240).

Interacts with IPK2b (PubMed:29216370).

Interacts with FLZ6 and FLZ10 (PubMed:29406622).

34 Publications

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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
6592, 36 interactors

Protein interaction database and analysis system

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IntActi
Q38997, 11 interactors

STRING: functional protein association networks

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STRINGi
3702.AT3G01090.2

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

3D structure databases

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

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SMRi
Q38997

Database of comparative protein structure models

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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 <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>Domaini19 – 271Protein kinasePROSITE-ProRule annotationAdd BLAST253
Domaini292 – 332UBAPROSITE-ProRule annotationAdd BLAST41
Domaini463 – 511KA1PROSITE-ProRule annotationAdd BLAST49

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>Regioni290 – 389Auto-inhibitory domain (AID)1 PublicationAdd BLAST100
Regioni294 – 512Regulatory domain (RD)1 PublicationAdd BLAST219
Regioni390 – 512PPI1 PublicationAdd BLAST123

<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 regulatory domain (RD) contains the auto-inhibitory domain (AID) that inhibits kinase activity of the protein kinase domain (KD).1 Publication
The PPI motif mediates the interaction with the ABI (abscisic acid-insensitive) phosphatases.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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0583 Eukaryota
COG0515 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000233016

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q38997

KEGG Orthology (KO)

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KOi
K07198

Identification of Orthologs from Complete Genome Data

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OMAi
TAHEINE

Database of Orthologous Groups

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OrthoDBi
1127668at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q38997

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR028375 KA1/Ssp2_C
IPR001772 KA1_dom
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
IPR015940 UBA
IPR009060 UBA-like_sf

Pfam protein domain database

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Pfami
View protein in Pfam
PF02149 KA1, 1 hit
PF00069 Pkinase, 1 hit
PF00627 UBA, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00220 S_TKc, 1 hit
SM00165 UBA, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF103243 SSF103243, 1 hit
SSF46934 SSF46934, 1 hit
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50032 KA1, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit
PS50030 UBA, 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>Sequences (2)i

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

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 2 (identifier: Q38997-2) [UniParc]FASTAAdd to basket

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

« Hide
        10         20         30         40         50
MDGSGTGSRS GVESILPNYK LGRTLGIGSF GRVKIAEHAL TGHKVAIKIL
60 70 80 90 100
NRRKIKNMEM EEKVRREIKI LRLFMHPHII RLYEVIETPT DIYLVMEYVN
110 120 130 140 150
SGELFDYIVE KGRLQEDEAR NFFQQIISGV EYCHRNMVVH RDLKPENLLL
160 170 180 190 200
DSKCNVKIAD FGLSNIMRDG HFLKTSCGSP NYAAPEVISG KLYAGPEVDV
210 220 230 240 250
WSCGVILYAL LCGTLPFDDE NIPNLFKKIK GGIYTLPSHL SPGARDLIPR
260 270 280 290 300
MLVVDPMKRV TIPEIRQHPW FQAHLPRYLA VPPPDTVQQA KKIDEEILQE
310 320 330 340 350
VINMGFDRNH LIESLRNRTQ NDGTVTYYLI LDNRFRASSG YLGAEFQETM
360 370 380 390 400
EGTPRMHPAE SVASPVSHRL PGLMEYQGVG LRSQYPVERK WALGLQSRAH
410 420 430 440 450
PREIMTEVLK ALQDLNVCWK KIGHYNMKCR WVPNSSADGM LSNSMHDNNY
460 470 480 490 500
FGDESSIIEN EAAVKSPNVV KFEIQLYKTR DDKYLLDLQR VQGPQFLFLD
510
LCAAFLAQLR VL
Length:512
Mass (Da):58,373
Last modified:October 10, 2018 - v3
<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:i5A18655A0AA506DF
GO
Isoform 1 (identifier: Q38997-1) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MFKRVDEFNLVSSTIDHRIFKSRM

Note: No experimental confirmation available.1 Publication
Show »
Length:535
Mass (Da):61,182
Checksum:iFFFC383223FD8317
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0598901M → MFKRVDEFNLVSSTIDHRIF KSRM in isoform 1. 1

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
M93023 Genomic DNA Translation: AAA32736.1
X94757 mRNA Translation: CAA64384.1
DQ778957 mRNA Translation: ABH11527.1
AC008261 Genomic DNA Translation: AAF26165.1
CP002686 Genomic DNA Translation: AEE73607.1
CP002686 Genomic DNA Translation: AEE73608.1
CP002686 Genomic DNA Translation: AEE73609.1
AY093170 mRNA Translation: AAM13169.1
BT010386 mRNA Translation: AAQ56829.1
X79707 Genomic DNA Translation: CAA56146.1
X86966 Genomic DNA Translation: CAA60529.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JC1446

NCBI Reference Sequences

More...
RefSeqi
NP_001118546.1, NM_001125074.2 [Q38997-2]
NP_566130.1, NM_110974.5 [Q38997-2]
NP_850488.1, NM_180157.1 [Q38997-1]

Genome annotation databases

Ensembl plant genome annotation project

More...
EnsemblPlantsi
AT3G01090.1; AT3G01090.1; AT3G01090 [Q38997-2]
AT3G01090.2; AT3G01090.2; AT3G01090 [Q38997-1]
AT3G01090.3; AT3G01090.3; AT3G01090 [Q38997-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
821259

Gramene; a comparative resource for plants

More...
Gramenei
AT3G01090.1; AT3G01090.1; AT3G01090 [Q38997-2]
AT3G01090.2; AT3G01090.2; AT3G01090 [Q38997-1]
AT3G01090.3; AT3G01090.3; AT3G01090 [Q38997-2]

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ath:AT3G01090

Keywords - Coding sequence diversityi

Alternative splicing

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

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

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

PlantP kinase Classification PPC

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M93023 Genomic DNA Translation: AAA32736.1
X94757 mRNA Translation: CAA64384.1
DQ778957 mRNA Translation: ABH11527.1
AC008261 Genomic DNA Translation: AAF26165.1
CP002686 Genomic DNA Translation: AEE73607.1
CP002686 Genomic DNA Translation: AEE73608.1
CP002686 Genomic DNA Translation: AEE73609.1
AY093170 mRNA Translation: AAM13169.1
BT010386 mRNA Translation: AAQ56829.1
X79707 Genomic DNA Translation: CAA56146.1
X86966 Genomic DNA Translation: CAA60529.1
PIRiJC1446
RefSeqiNP_001118546.1, NM_001125074.2 [Q38997-2]
NP_566130.1, NM_110974.5 [Q38997-2]
NP_850488.1, NM_180157.1 [Q38997-1]

3D structure databases

SMRiQ38997
ModBaseiSearch...

Protein-protein interaction databases

BioGridi6592, 36 interactors
IntActiQ38997, 11 interactors
STRINGi3702.AT3G01090.2

PTM databases

iPTMnetiQ38997

Proteomic databases

PaxDbiQ38997
PRIDEiQ38997

Genome annotation databases

EnsemblPlantsiAT3G01090.1; AT3G01090.1; AT3G01090 [Q38997-2]
AT3G01090.2; AT3G01090.2; AT3G01090 [Q38997-1]
AT3G01090.3; AT3G01090.3; AT3G01090 [Q38997-2]
GeneIDi821259
GrameneiAT3G01090.1; AT3G01090.1; AT3G01090 [Q38997-2]
AT3G01090.2; AT3G01090.2; AT3G01090 [Q38997-1]
AT3G01090.3; AT3G01090.3; AT3G01090 [Q38997-2]
KEGGiath:AT3G01090

Organism-specific databases

AraportiAT3G01090
TAIRilocus:2102132 AT3G01090

Phylogenomic databases

eggNOGiKOG0583 Eukaryota
COG0515 LUCA
HOGENOMiHOG000233016
InParanoidiQ38997
KOiK07198
OMAiTAHEINE
OrthoDBi1127668at2759
PhylomeDBiQ38997

Enzyme and pathway databases

BRENDAi2.7.11.1 399

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q38997

Gene expression databases

ExpressionAtlasiQ38997 baseline and differential
GenevisibleiQ38997 AT

Family and domain databases

InterProiView protein in InterPro
IPR028375 KA1/Ssp2_C
IPR001772 KA1_dom
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
IPR015940 UBA
IPR009060 UBA-like_sf
PfamiView protein in Pfam
PF02149 KA1, 1 hit
PF00069 Pkinase, 1 hit
PF00627 UBA, 1 hit
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SM00165 UBA, 1 hit
SUPFAMiSSF103243 SSF103243, 1 hit
SSF46934 SSF46934, 1 hit
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS50032 KA1, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit
PS50030 UBA, 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 nameiKIN10_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: Q38997
Secondary accession number(s): A6XGR0
, O04728, Q38987, Q39076, Q8RWD2
<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: July 15, 1999
Last sequence update: October 10, 2018
Last modified: October 16, 2019
This is version 182 of the entry and version 3 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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