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Entry version 152 (17 Jun 2020)
Sequence version 1 (01 Dec 2001)
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Protein

Serine/threonine-protein kinase SRK2E

Gene

SRK2E

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

Activator of the abscisic acid (ABA) signaling pathway that regulates numerous ABA responses, such as stomata closure in response to drought, darkness, high CO2, plant pathogens, or decreases in atmospheric relative humidity (RH) (PubMed:30361234). Involved in the resistance to drought by avoiding water loss. Required for the stomata closure mediated by pathogen-associated molecular pattern (PAMPs) (e.g. flg22 and LPS) of pathogenic bacteria such as P.syringae pv. tomato (Pst) and E.coli O157:H7. As a plant defense process, stomata are closed transiently in order to limit invaders, but actively reopened by bacteria after a few hours; virulent strains (e.g. Pst DC3000) are more efficient than avirulent strains (e.g. Pst DC3000 AvrRpt2) in reopening stomata. Mediates the phosphorylation and activation of the S-type anion efflux channel SLAC1, and thus promotes stomata closure. Essential for stomatal closure in response to reactive oxygen species (ROS). Promotes MAPKKK18 activity upon abscisic acid (ABA) treatment (PubMed:26443375).14 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

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

Kinase activity enhanced by ABA and low humidity. Repressed by PP2CA independently of its phosphatase activity. Probably inactivated by ABI1 (PubMed:12468729, PubMed:12514244, PubMed:19955427). Repressed by TOPP1 (PubMed:26943172). Negatively regulated by ABI2 (PubMed:22730405).5 Publications

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 sitei50ATPPROSITE-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 sitei140Proton 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 bindingi27 – 35ATPPROSITE-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 processAbscisic acid signaling pathway, Plant defense
LigandATP-binding, Nucleotide-binding

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

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Serine/threonine-protein kinase SRK2E1 Publication (EC:2.7.11.15 Publications)
Alternative name(s):
Protein OPEN STOMATA 11 Publication
SNF1-related kinase 2.61 Publication
Short name:
SnRK2.61 Publication
Serine/threonine-protein kinase OST11 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:SRK2E1 Publication
Synonyms:OST11 Publication, SNRK2.61 Publication
Ordered Locus Names:At4g33950Imported
ORF Names:F17I5.140Imported
<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 4

Organism-specific databases

Arabidopsis Information Portal

More...
Araporti
AT4G33950

The Arabidopsis Information Resource

More...
TAIRi
locus:2118929 AT4G33950

<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

Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Impaired ozone-triggered rapid transient decrease (RTD) in stomatal conductance (PubMed:20128877). Impaired induction of MKKK18 activity after 90 minutes of abscisic acid (ABA) treatment (PubMed:26443375). Delayed CO2-mediated and darkness-induced and reduced abscisic acid (ABA)-triggered stomatal closure (PubMed:30361234).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>Mutagenesisi1 – 12Missing : Reduced kinase activity in response to ABA and osmotic stress. 1 PublicationAdd BLAST12
Mutagenesisi7S → A or D: Normal kinase activity, but loss of ABA signaling pathway positive regulation. 1 Publication1
Mutagenesisi18S → A or D: Normal kinase activity, but loss of ABA signaling pathway positive regulation. 1 Publication1
Mutagenesisi29S → A or D: Normal kinase activity, but loss of ABA signaling pathway positive regulation. 1 Publication1
Mutagenesisi33G → R in ost1-2; loss of kinase activity, and insensitivity to ABA during the stomatal aperture regulation. 3 Publications1
Mutagenesisi43S → A or D: Normal kinase activity, but constitutive ABA signaling pathway activation. 1 Publication1
Mutagenesisi50K → N: Loss of kinase activity. 1 Publication1
Mutagenesisi140D → A: Loss of kinase activity. 1 Publication1
Mutagenesisi175S → A or D: Loss of kinase activity, and loss of ABA signaling pathway positive regulation. 1 Publication1
Mutagenesisi176T → A: Normal kinase activity, and normal regulation of the ABA signaling pathway. 1 Publication1
Mutagenesisi176T → D: Reduced kinase activity, but normal regulation of the ABA signaling pathway. 1 Publication1
Mutagenesisi178G → Q in ost1-4; no stomatal closure when RH decreases, and insensitivity to ABA. 1 Publication1
Mutagenesisi280 – 362Missing : Loss of kinase activity, and loss of ABA signaling pathway positive regulation. 1 PublicationAdd BLAST83
Mutagenesisi283 – 362Missing : Loss of kinase activity in response to ABA and osmotic stress. 1 PublicationAdd BLAST80
Mutagenesisi302 – 362Missing : Loss of kinase activity, and loss of ABA signaling pathway positive regulation. 1 PublicationAdd BLAST61
Mutagenesisi319 – 362Missing : Loss of kinase activity specifically in response to ABA, and impaired interaction with ABI1. 1 PublicationAdd BLAST44
Mutagenesisi320 – 362Missing : Normal kinase activity, but loss of ABA signaling pathway positive regulation. 1 PublicationAdd BLAST43
Mutagenesisi331 – 362Missing : Normal kinase activity, but loss of ABA signaling pathway positive regulation. 1 PublicationAdd BLAST32
Mutagenesisi348 – 362Missing : Normal kinase activity, and normal regulation of the ABA signaling pathway. 1 PublicationAdd BLAST15

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003451601 – 362Serine/threonine-protein kinase SRK2EAdd BLAST362

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei7Phosphoserine; by autocatalysis1 Publication1
Modified residuei18Phosphoserine; by autocatalysis1 Publication1
Modified residuei29Phosphoserine; by autocatalysis1 Publication1
Modified residuei43Phosphoserine; by autocatalysis1 Publication1
Modified residuei175Phosphoserine1 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

Autophosphorylation on residues Ser-7, Ser-18, Ser-29, Ser-43, Ser-175 and/or Thr-176 (PubMed:30361234). Only the phosphorylation of Ser-175 is crucial for the kinase activity. The phosphorylation of Ser-43 may repress the ABA signaling pathway in absence of ABA.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

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

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PaxDbi
Q940H6

PRoteomics IDEntifications database

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PRIDEi
Q940H6

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
226874 [Q940H6-1]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q940H6

<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 seedlings, leaves, flowers, stems, and roots, but restricted to guard cells and vascular tissue.4 Publications

<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

In roots by ABA in an ABI1-dependent manner and by osmotic stress (e.g. sorbitol) in an ABI1-independent manner, but in leaves by low humidity (at protein level). Also induced by salt stress.2 Publications

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q940H6 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q940H6 AT

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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with ABI1, PP2CA and SLAC1 (PubMed:16365038, PubMed:19874541, PubMed:19955405, PubMed:19955427).

Interacts with B'ALPHA, B'BETA, B'DELTA, PP2AA2, PP2AA3, PP2A1 and PP2A2 (PubMed:26175513). Associates with MAPKKK18 within the nucleus (PubMed:26852793).

Interacts with I-2, TOPP1 and TOPP2 (PubMed:26943172).

Interacts with ABI2 (PubMed:22730405).

8 Publications

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

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
14823, 51 interactors

Database of interacting proteins

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DIPi
DIP-36705N

Protein interaction database and analysis system

More...
IntActi
Q940H6, 12 interactors

Molecular INTeraction database

More...
MINTi
Q940H6

STRING: functional protein association networks

More...
STRINGi
3702.AT4G33950.1

<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

1362
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
Q940H6

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini21 – 277Protein kinasePROSITE-ProRule annotationAdd BLAST257

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>Regioni160 – 186Activation loop1 PublicationAdd BLAST27
Regioni283 – 318Domain I; osmotic stress response, required for the kinase activity1 PublicationAdd BLAST36
Regioni319 – 362Domain II; ABA response and ABI1 binding1 PublicationAdd BLAST44

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0583 Eukaryota
COG0515 LUCA

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q940H6

KEGG Orthology (KO)

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KOi
K14498

Database for complete collections of gene phylogenies

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PhylomeDBi
Q940H6

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS

Pfam protein domain database

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Pfami
View protein in Pfam
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

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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>Sequences (2+)i

<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.

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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: Q940H6-1) [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
MDRPAVSGPM DLPIMHDSDR YELVKDIGSG NFGVARLMRD KQSNELVAVK
60 70 80 90 100
YIERGEKIDE NVKREIINHR SLRHPNIVRF KEVILTPTHL AIVMEYASGG
110 120 130 140 150
ELFERICNAG RFSEDEARFF FQQLISGVSY CHAMQVCHRD LKLENTLLDG
160 170 180 190 200
SPAPRLKICD FGYSKSSVLH SQPKSTVGTP AYIAPEVLLK KEYDGKVADV
210 220 230 240 250
WSCGVTLYVM LVGAYPFEDP EEPKNFRKTI HRILNVQYAI PDYVHISPEC
260 270 280 290 300
RHLISRIFVA DPAKRISIPE IRNHEWFLKN LPADLMNDNT MTTQFDESDQ
310 320 330 340 350
PGQSIEEIMQ IIAEATVPPA GTQNLNHYLT GSLDIDDDME EDLESDLDDL
360
DIDSSGEIVY AM
Length:362
Mass (Da):41,048
Last modified:December 1, 2001 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iFFBCCA1474839B88
GO
Isoform 2 (identifier: Q940H6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     26-57: DIGSGNFGVARLMRDKQSNELVAVKYIERGEK → MVGLFVFVQ

Show »
Length:339
Mass (Da):38,506
Checksum:iFC8BC24717DF022E
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B3H6F9B3H6F9_ARATH
Protein kinase superfamily protein
OST1 ATOST1, OPEN STOMATA 1, P44, SNRK2-6, SNRK2.6
345Annotation score:

Annotation score:2 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>

<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 CAA19877 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence CAB80112 differs from that shown. Reason: Erroneous gene model prediction.Curated

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_03492326 – 57DIGSG…ERGEK → MVGLFVFVQ in isoform 2. CuratedAdd BLAST32

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
AJ316009 Genomic DNA Translation: CAC87047.1
AL031032 Genomic DNA Translation: CAA19877.1 Sequence problems.
AL161584 Genomic DNA Translation: CAB80112.1 Sequence problems.
CP002687 Genomic DNA Translation: AEE86299.1
AY054624 mRNA Translation: AAK96815.1
AY081538 mRNA Translation: AAM10100.1

Protein sequence database of the Protein Information Resource

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PIRi
T05223

NCBI Reference Sequences

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RefSeqi
NP_567945.1, NM_119556.3 [Q940H6-1]

Genome annotation databases

Ensembl plant genome annotation project

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EnsemblPlantsi
AT4G33950.1; AT4G33950.1; AT4G33950 [Q940H6-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
829541

Gramene; a comparative resource for plants

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Gramenei
AT4G33950.1; AT4G33950.1; AT4G33950 [Q940H6-1]

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
ath:AT4G33950

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ316009 Genomic DNA Translation: CAC87047.1
AL031032 Genomic DNA Translation: CAA19877.1 Sequence problems.
AL161584 Genomic DNA Translation: CAB80112.1 Sequence problems.
CP002687 Genomic DNA Translation: AEE86299.1
AY054624 mRNA Translation: AAK96815.1
AY081538 mRNA Translation: AAM10100.1
PIRiT05223
RefSeqiNP_567945.1, NM_119556.3 [Q940H6-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3UC4X-ray2.30A/B1-362[»]
3UDBX-ray2.57A/B/C/D/E/F1-317[»]
3UJGX-ray2.60A11-362[»]
3ZUTX-ray2.50A/B1-362[»]
3ZUUX-ray2.70A/B1-362[»]
SMRiQ940H6
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi14823, 51 interactors
DIPiDIP-36705N
IntActiQ940H6, 12 interactors
MINTiQ940H6
STRINGi3702.AT4G33950.1

PTM databases

iPTMnetiQ940H6

Proteomic databases

PaxDbiQ940H6
PRIDEiQ940H6
ProteomicsDBi226874 [Q940H6-1]

Genome annotation databases

EnsemblPlantsiAT4G33950.1; AT4G33950.1; AT4G33950 [Q940H6-1]
GeneIDi829541
GrameneiAT4G33950.1; AT4G33950.1; AT4G33950 [Q940H6-1]
KEGGiath:AT4G33950

Organism-specific databases

AraportiAT4G33950
TAIRilocus:2118929 AT4G33950

Phylogenomic databases

eggNOGiKOG0583 Eukaryota
COG0515 LUCA
InParanoidiQ940H6
KOiK14498
PhylomeDBiQ940H6

Miscellaneous databases

Protein Ontology

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PROi
PR:Q940H6

Gene expression databases

ExpressionAtlasiQ940H6 baseline and differential
GenevisibleiQ940H6 AT

Family and domain databases

InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
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

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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 nameiSRK2E_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: Q940H6
Secondary accession number(s): O81763
<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 22, 2008
Last sequence update: December 1, 2001
Last modified: June 17, 2020
This is version 152 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

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