Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei50 – 501ATPPROSITE-ProRule annotation
Active sitei140 – 1401Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi27 – 359ATPPROSITE-ProRule annotation

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

BioCyciARA:AT4G33950-MONOMER.
ARA:GQT-701-MONOMER.
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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1 – 1212Missing : Reduced kinase activity in response to ABA and osmotic stress. 1 PublicationAdd
BLAST
Mutagenesisi7 – 71S → A or D: Normal kinase activity, but loss of ABA signaling pathway positive regulation. 1 Publication
Mutagenesisi18 – 181S → A or D: Normal kinase activity, but loss of ABA signaling pathway positive regulation. 1 Publication
Mutagenesisi29 – 291S → A or D: Normal kinase activity, but loss of ABA signaling pathway positive regulation. 1 Publication
Mutagenesisi33 – 331G → R in ost1-2; loss of kinase activity, and insensitivity to ABA during the stomatal aperture regulation. 3 Publications
Mutagenesisi43 – 431S → A or D: Normal kinase activity, but constitutive ABA signaling pathway activation. 1 Publication
Mutagenesisi50 – 501K → N: Loss ok kinase activity. 1 Publication
Mutagenesisi140 – 1401D → A: Loss ok kinase activity. 1 Publication
Mutagenesisi175 – 1751S → A or D: Loss of kinase activity, and loss of ABA signaling pathway positive regulation. 1 Publication
Mutagenesisi176 – 1761T → A: Normal kinase activity, and normal regulation of the ABA signaling pathway. 1 Publication
Mutagenesisi176 – 1761T → D: Reduced kinase activity, but normal regulation of the ABA signaling pathway. 1 Publication
Mutagenesisi178 – 1781G → Q in ost1-4; no stomatal closure when RH decreases, and insensitivity to ABA. 1 Publication
Mutagenesisi280 – 36283Missing : Loss of kinase activity, and loss of ABA signaling pathway positive regulation. 1 PublicationAdd
BLAST
Mutagenesisi283 – 35775Missing : Loss of kinase activity in response to ABA and osmotic stress. 1 PublicationAdd
BLAST
Mutagenesisi302 – 36261Missing : Loss of kinase activity, and loss of ABA signaling pathway positive regulation. 1 PublicationAdd
BLAST
Mutagenesisi318 – 35740Missing : Loss of kinase activity specifically in response to ABA, and impaired interaction with ABI1. Add
BLAST
Mutagenesisi320 – 36243Missing : Normal kinase activity, but loss of ABA signaling pathway positive regulation. 1 PublicationAdd
BLAST
Mutagenesisi331 – 36232Missing : Normal kinase activity, but loss of ABA signaling pathway positive regulation. 1 PublicationAdd
BLAST
Mutagenesisi348 – 36215Missing : Normal kinase activity, and normal regulation of the ABA signaling pathway. 1 PublicationAdd
BLAST

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 362362Serine/threonine-protein kinase SRK2EPRO_0000345160Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei7 – 71Phosphoserine; by autocatalysis1 Publication
Modified residuei18 – 181Phosphoserine; by autocatalysis1 Publication
Modified residuei29 – 291Phosphoserine; by autocatalysis1 Publication
Modified residuei43 – 431Phosphoserine; by autocatalysis1 Publication
Modified residuei175 – 1751Phosphoserine1 Publication

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.
PRIDEiQ940H6.

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 interactions.
DIPiDIP-36705N.
IntActiQ940H6. 6 interactions.
MINTiMINT-7260107.
STRINGi3702.AT4G33950.1.

Structurei

Secondary structure

1
362
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni18 – 203Combined sources
Beta strandi21 – 277Combined sources
Beta strandi30 – 323Combined sources
Beta strandi34 – 407Combined sources
Turni41 – 433Combined sources
Beta strandi46 – 538Combined sources
Turni54 – 563Combined sources
Helixi60 – 7011Combined sources
Beta strandi80 – 856Combined sources
Beta strandi87 – 959Combined sources
Helixi102 – 1098Combined sources
Helixi114 – 13421Combined sources
Helixi138 – 1403Combined sources
Helixi143 – 1453Combined sources
Beta strandi147 – 1493Combined sources
Beta strandi150 – 1534Combined sources
Beta strandi156 – 1583Combined sources
Helixi161 – 1633Combined sources
Helixi180 – 1823Combined sources
Helixi185 – 1895Combined sources
Helixi195 – 21218Combined sources
Beta strandi216 – 2183Combined sources
Beta strandi220 – 2223Combined sources
Helixi226 – 2349Combined sources
Helixi248 – 25710Combined sources
Helixi262 – 2643Combined sources
Helixi268 – 2725Combined sources
Helixi275 – 2784Combined sources
Helixi291 – 2966Combined sources
Helixi297 – 2993Combined sources
Helixi305 – 31410Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 20-318.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 277257Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni160 – 18627Activation loopAdd
BLAST
Regioni283 – 31735Domain I; osmotic stress response, required for the kinase activityAdd
BLAST
Regioni318 – 35740Domain II; ABA response and ABI1 bindingAdd
BLAST

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.
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 CAA19877.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAB80112.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei26 – 5732DIGSG…ERGEK → MVGLFVFVQ in isoform 2. CuratedVSP_034923Add
BLAST

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_119556.2. [Q940H6-1]
UniGeneiAt.2399.

Genome annotation databases

EnsemblPlantsiAT4G33950.1; AT4G33950.1; AT4G33950. [Q940H6-1]
GeneIDi829541.
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_119556.2. [Q940H6-1]
UniGeneiAt.2399.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 20-318.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiQ940H6.

Proteomic databases

PaxDbiQ940H6.
PRIDEiQ940H6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

TAIRiAT4G33950.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciARA:AT4G33950-MONOMER.
ARA:GQT-701-MONOMER.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Arabidopsis OST1 protein kinase mediates the regulation of stomatal aperture by abscisic acid and acts upstream of reactive oxygen species production."
    Mustilli A.-C., Merlot S., Vavasseur A., Fenzi F., Giraudat J.
    Plant Cell 14:3089-3099(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), FUNCTION, MUTAGENESIS OF GLY-33, ENZYME REGULATION, TISSUE SPECIFICITY.
    Strain: cv. Landsberg erecta.
  2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: cv. Columbia.
  5. "ABA-activated SnRK2 protein kinase is required for dehydration stress signaling in Arabidopsis."
    Yoshida R., Hobo T., Ichimura K., Mizoguchi T., Takahashi F., Aronso J., Ecker J.R., Shinozaki K.
    Plant Cell Physiol. 43:1473-1483(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION.
  6. "Use of infrared thermal imaging to isolate Arabidopsis mutants defective in stomatal regulation."
    Merlot S., Mustilli A.-C., Genty B., North H., Lefebvre V., Sotta B., Vavasseur A., Giraudat J.
    Plant J. 30:601-609(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLY-33.
  7. Cited for: GENE FAMILY, NOMENCLATURE.
  8. "OPEN STOMATA1 opens the door to ABA signaling in Arabidopsis guard cells."
    Assmann S.M.
    Trends Plant Sci. 8:151-153(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  9. "Identification of nine sucrose nonfermenting 1-related protein kinases 2 activated by hyperosmotic and saline stresses in Arabidopsis thaliana."
    Boudsocq M., Barbier-Brygoo H., Lauriere C.
    J. Biol. Chem. 279:41758-41766(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INDUCTION.
  10. "Cytoplasmic alkalization precedes reactive oxygen species production during methyl jasmonate- and abscisic acid-induced stomatal closure."
    Suhita D., Raghavendra A.S., Kwak J.M., Vavasseur A.
    Plant Physiol. 134:1536-1545(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Plant stomata function in innate immunity against bacterial invasion."
    Melotto M., Underwood W., Koczan J., Nomura K., He S.Y.
    Cell 126:969-980(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "The identification of genes involved in the stomatal response to reduced atmospheric relative humidity."
    Xie X., Wang Y., Williamson L., Holroyd G.H., Tagliavia C., Murchie E., Theobald J., Knight M.R., Davies W.J., Leyser H.M.O., Hetherington A.M.
    Curr. Biol. 16:882-887(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLY-178.
  13. "The regulatory domain of SRK2E/OST1/SnRK2.6 interacts with ABI1 and integrates abscisic acid (ABA) and osmotic stress signals controlling stomatal closure in Arabidopsis."
    Yoshida R., Umezawa T., Mizoguchi T., Takahashi S., Takahashi F., Shinozaki K.
    J. Biol. Chem. 281:5310-5318(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF 1-MET--LEU-12; 283-ALA--GLU-357 AND 318-PRO--GLU-358, GENE FAMILY, INTERACTION WITH ABI1, INDUCTION.
  14. "Identification of features regulating OST1 kinase activity and OST1 function in guard cells."
    Belin C., de Franco P.-O., Bourbousse C., Chaignepain S., Schmitter J.-M., Vavasseur A., Giraudat J., Barbier-Brygoo H., Thomine S.
    Plant Physiol. 141:1316-1327(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF SER-7; SER-18; SER-29; GLY-33; SER-43; SER-175; THR-176; 280-ASN--MET-362; 302-GLY--MET-362; 320-ALA--MET-362; 331-GLY--MET-362 AND 348-ASP--MET-362, PHOSPHORYLATION AT SER-7; SER-18; SER-29; SER-43 AND SER-175, TISSUE SPECIFICITY.
  15. "Identification of two protein kinases required for abscisic acid regulation of seed germination, root growth, and gene expression in Arabidopsis."
    Fujii H., Verslues P.E., Zhu J.-K.
    Plant Cell 19:485-494(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  16. "PYR/PYL/RCAR family members are major in-vivo ABI1 protein phosphatase 2C-interacting proteins in Arabidopsis."
    Nishimura N., Sarkeshik A., Nito K., Park S.-Y., Wang A., Carvalho P.C., Lee S., Caddell D.F., Cutler S.R., Chory J., Yates J.R., Schroeder J.I.
    Plant J. 61:290-299(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ABI1.
  17. "A protein kinase-phosphatase pair interacts with an ion channel to regulate ABA signaling in plant guard cells."
    Lee S.C., Lan W., Buchanan B.B., Luan S.
    Proc. Natl. Acad. Sci. U.S.A. 106:21419-21424(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, AUTOPHOSPHORYLATION, INTERACTION WITH SLAC1 AND PP2CA, ENZYME REGULATION, MUTAGENESIS OF LYS-50.
  18. "Activity of guard cell anion channel SLAC1 is controlled by drought-stress signaling kinase-phosphatase pair."
    Geiger D., Scherzer S., Mumm P., Stange A., Marten I., Bauer H., Ache P., Matschi S., Liese A., Al-Rasheid K.A.S., Romeis T., Hedrich R.
    Proc. Natl. Acad. Sci. U.S.A. 106:21425-21430(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ABI1, MUTAGENESIS OF ASP-140.
  19. "Ozone-triggered rapid stomatal response involves the production of reactive oxygen species, and is controlled by SLAC1 and OST1."
    Vahisalu T., Puzorjova I., Brosche M., Valk E., Lepiku M., Moldau H., Pechter P., Wang Y.-S., Lindgren O., Salojaervi J., Loog M., Kangasjaervi J., Kollist H.
    Plant J. 62:442-453(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, AUTOPHOSPHORYLATION.
    Strain: cv. Columbia.

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: June 8, 2016
This is version 120 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.