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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-Experimental evidence at protein leveli

Functioni

Activator of the abscisic acid (ABA) signaling pathway that regulates numerous ABA responses, such as stomata closure in response to drought, plant pathogens, or decreases in atmospheric relative humidity (RH). 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).12 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Kinase activity enhanced by ABA and low humidity. Repressed by PP2CA independently of its phosphatase activity. Probably inactivated by ABI1.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei50ATPPROSITE-ProRule annotation1
Active sitei140Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi27 – 35ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • calcium-dependent protein serine/threonine kinase activity Source: TAIR
  • kinase activity Source: TAIR
  • protein kinase activity Source: TAIR
  • protein phosphatase binding Source: UniProtKB
  • protein serine/threonine kinase activity Source: GO_Central

GO - Biological processi

  • abscisic acid-activated signaling pathway Source: TAIR
  • defense response to bacterium Source: TAIR
  • growth Source: TAIR
  • intracellular signal transduction Source: GO_Central
  • leaf development Source: TAIR
  • protein autophosphorylation Source: CACAO
  • regulation of anion channel activity Source: UniProtKB
  • regulation of reactive oxygen species metabolic process Source: TAIR
  • regulation of stomatal movement Source: TAIR
  • regulation of stomatal opening Source: TAIR
  • response to abscisic acid Source: TAIR
  • response to osmotic stress Source: TAIR
  • response to salt stress Source: TAIR
  • response to water deprivation Source: TAIR
  • stomatal movement Source: TAIR
  • sucrose metabolic process Source: TAIR
  • triglyceride biosynthetic process Source: TAIR
  • unsaturated fatty acid biosynthetic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Abscisic acid signaling pathway, Plant defense

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-ATH-163680. AMPK inhibits chREBP transcriptional activation activity.
R-ATH-200425. Import of palmitoyl-CoA into the mitochondrial matrix.
R-ATH-380972. Energy dependent regulation of mTOR by LKB1-AMPK.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase SRK2E (EC:2.7.11.1)
Alternative name(s):
Protein OPEN STOMATA 1
SNF1-related kinase 2.6
Short name:
SnRK2.6
Serine/threonine-protein kinase OST1
Gene namesi
Name:SRK2E
Synonyms:OST1, SNRK2.6
Ordered Locus Names:At4g33950
ORF Names:F17I5.140
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G33950.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: TAIR
  • cytosol Source: TAIR
  • nucleus Source: TAIR
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Impaired ozone-triggered rapid transient decrease (RTD) in stomatal conductance.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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 ok kinase activity. 1 Publication1
Mutagenesisi140D → A: Loss ok 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 – 357Missing : Loss of kinase activity in response to ABA and osmotic stress. 1 PublicationAdd BLAST75
Mutagenesisi302 – 362Missing : Loss of kinase activity, and loss of ABA signaling pathway positive regulation. 1 PublicationAdd BLAST61
Mutagenesisi318 – 357Missing : Loss of kinase activity specifically in response to ABA, and impaired interaction with ABI1. Add BLAST40
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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003451601 – 362Serine/threonine-protein kinase SRK2EAdd BLAST362

Amino acid modifications

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

Post-translational modificationi

Autophosphorylation on residues Ser-7, Ser-18, Ser-29, Ser-43, Ser-175 and/or Thr-176. 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.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ940H6.

PTM databases

iPTMnetiQ940H6.

Expressioni

Tissue specificityi

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

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

ExpressionAtlasiQ940H6. baseline and differential.
GenevisibleiQ940H6. AT.

Interactioni

Subunit structurei

Interacts with ABI1, PP2CA and SLAC1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABI1P495974EBI-782514,EBI-782526
HT1Q2MHE42EBI-782514,EBI-11174828
RBOHFO485384EBI-782514,EBI-7197253

GO - Molecular functioni

  • protein phosphatase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi14823. 29 interactors.
DIPiDIP-36705N.
IntActiQ940H6. 6 interactors.
MINTiMINT-7260107.
STRINGi3702.AT4G33950.1.

Structurei

Secondary structure

1362
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni18 – 20Combined sources3
Beta strandi21 – 27Combined sources7
Beta strandi30 – 32Combined sources3
Beta strandi34 – 40Combined sources7
Turni41 – 43Combined sources3
Beta strandi46 – 53Combined sources8
Turni54 – 56Combined sources3
Helixi60 – 70Combined sources11
Beta strandi80 – 85Combined sources6
Beta strandi87 – 95Combined sources9
Helixi102 – 109Combined sources8
Helixi114 – 134Combined sources21
Helixi138 – 140Combined sources3
Helixi143 – 145Combined sources3
Beta strandi147 – 149Combined sources3
Beta strandi150 – 153Combined sources4
Beta strandi156 – 158Combined sources3
Helixi161 – 163Combined sources3
Helixi180 – 182Combined sources3
Helixi185 – 189Combined sources5
Helixi195 – 212Combined sources18
Beta strandi216 – 218Combined sources3
Beta strandi220 – 222Combined sources3
Helixi226 – 234Combined sources9
Helixi248 – 257Combined sources10
Helixi262 – 264Combined sources3
Helixi268 – 272Combined sources5
Helixi275 – 278Combined sources4
Helixi291 – 296Combined sources6
Helixi297 – 299Combined sources3
Helixi305 – 314Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliQ940H6.
SMRiQ940H6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini21 – 277Protein kinasePROSITE-ProRule annotationAdd BLAST257

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni160 – 186Activation loopAdd BLAST27
Regioni283 – 317Domain I; osmotic stress response, required for the kinase activityAdd BLAST35
Regioni318 – 357Domain II; ABA response and ABI1 bindingAdd BLAST40

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0583. Eukaryota.
COG0515. LUCA.
HOGENOMiHOG000233016.
InParanoidiQ940H6.
KOiK14498.
OMAiLMRDKQS.
OrthoDBiEOG09360FEU.
PhylomeDBiQ940H6.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q940H6-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' 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
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

Note: Derived from EST data. No experimental confirmation available.
Show »
Length:339
Mass (Da):38,506
Checksum:iFC8BC24717DF022E
GO

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
Alternative sequenceiVSP_03492326 – 57DIGSG…ERGEK → MVGLFVFVQ in isoform 2. CuratedAdd BLAST32

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]
UniGeneiAt.2399.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing

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]
UniGeneiAt.2399.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliQ940H6.
SMRiQ940H6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi14823. 29 interactors.
DIPiDIP-36705N.
IntActiQ940H6. 6 interactors.
MINTiMINT-7260107.
STRINGi3702.AT4G33950.1.

PTM databases

iPTMnetiQ940H6.

Proteomic databases

PaxDbiQ940H6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

TAIRiAT4G33950.

Phylogenomic databases

eggNOGiKOG0583. Eukaryota.
COG0515. LUCA.
HOGENOMiHOG000233016.
InParanoidiQ940H6.
KOiK14498.
OMAiLMRDKQS.
OrthoDBiEOG09360FEU.
PhylomeDBiQ940H6.

Enzyme and pathway databases

ReactomeiR-ATH-163680. AMPK inhibits chREBP transcriptional activation activity.
R-ATH-200425. Import of palmitoyl-CoA into the mitochondrial matrix.
R-ATH-380972. Energy dependent regulation of mTOR by LKB1-AMPK.

Miscellaneous databases

PROiQ940H6.

Gene expression databases

ExpressionAtlasiQ940H6. baseline and differential.
GenevisibleiQ940H6. AT.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSRK2E_ARATH
AccessioniPrimary (citable) accession number: Q940H6
Secondary accession number(s): O81763
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: December 1, 2001
Last modified: November 30, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.