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UniProtKB/Swiss-Prot entry P43292


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SRK2G_ARATH
Primary accession number P43292
Secondary accession numbers Q24JK3 Q9FNM9
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on December 6, 2002 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 64)
Name and origin of the protein
Protein name Serine/threonine-protein kinase SRK2G
Synonyms EC 2.7.11.1
Arabidopsis protein SK1
OST1-kinase-like 8
SNF1-related kinase 2.1
SnRK2.1
Gene name
Name: SRK2G
Synonyms: ASK2, OSKL8, SNRK2.1
OrderedLocusNames: At5g08590
ORFNames: MAH20.15
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
TISSUE=Leaf;
DOI=10.1007/BF00047402; PubMed=8393717 [NCBI, ExPASy, EBI, Israel, Japan]
Park Y.S., Hong S.W., Oh S.A., Kwak J.M., Lee H.H., Nam H.G.;
"Two putative protein kinases from Arabidopsis thaliana contain highly acidic domains.";
Plant Mol. Biol. 22:615-624(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1093/dnares/4.4.291; PubMed=9405937 [NCBI, ExPASy, EBI, Israel, Japan]
Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence features of the regions of 1,044,062 bp covered by thirteen physically assigned P1 clones.";
DNA Res. 4:291-300(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Shinn P., Chen H., Kim C.J., Ecker J.R.;
"Arabidopsis ORF clones.";
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
[4]
PROTEIN SEQUENCE OF 148-174, PHOSPHORYLATION, SUBCELLULAR LOCALIZATION, AND IDENTIFICATION BY MASS-SPECTROMETRY.
DOI=10.1021/pr8000173; PubMed=18433157 [NCBI, ExPASy, EBI, Israel, Japan]
de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E., Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
"Site-specific phosphorylation profiling of Arabidopsis proteins by mass spectrometry and peptide chip analysis.";
J. Proteome Res. 7:2458-2470(2008).
[5]
GENE FAMILY, AND NOMENCLATURE.
DOI=10.1104/pp.102.011999; PubMed=12805596 [NCBI, ExPASy, EBI, Israel, Japan]
Hrabak E.M., Chan C.W.M., Gribskov M., Harper J.F., Choi J.H., Halford N., Kudla J., Luan S., Nimmo H.G., Sussman M.R., Thomas M., Walker-Simmons K., Zhu J.-K., Harmon A.C.;
"The Arabidopsis CDPK-SnRK superfamily of protein kinases.";
Plant Physiol. 132:666-680(2003).
[6]
TISSUE SPECIFICITY, AND INDUCTION.
DOI=10.1074/jbc.M405259200; PubMed=15292193 [NCBI, ExPASy, EBI, Israel, Japan]
Boudsocq M., Barbier-Brygoo H., Lauriere C.;
"Identification of nine sucrose nonfermenting 1-related protein kinases 2 activated by hyperosmotic and saline stresses in Arabidopsis thaliana.";
J. Biol. Chem. 279:41758-41766(2004).
[7]
GENE FAMILY, AND INDUCTION.
DOI=10.1074/jbc.M509820200; PubMed=16365038 [NCBI, ExPASy, EBI, Israel, Japan]
Yoshida R., Umezawa T., Mizoguchi T., Takahashi S., Takahashi F., Shinozaki K.;
"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.";
J. Biol. Chem. 281:5310-5318(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Z12120; CAA78106.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB006697; BAB10008.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT024886; ABD85157.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S24586; S24586.
RefSeq NP_196476.1; -.
UniGene At.23718
3D structure databases
HSSP O14757; 1IA8. [HSSP ENTRY / PDB]
ModBase P43292.
Protein-protein interaction databases
IntAct P43292; -.
Organism-specific databases
TAIR At5g08590; -.
Gene expression databases
ArrayExpress P43292; -.
GermOnline AT5G08590; Arabidopsis thaliana.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR015740; S/T_plantPK.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.
PANTHER PTHR22982:SF58; S/T_plantPK; 1.
Pfam PF00069; Pkinase; 1.
Pfam graphical view of domain structure.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00220; S_TKc; 1.
SMART graphical view of domain structure.
PROSITE PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P43292.
Genome annotation databases
GeneID 830760; -.
GenomeReviews BA000015_GR; AT5G08590.
KEGG ath:AT5G08590; -.
NMPDR fig|3702.1.peg.23012; -.
Other
ProtoNet P43292.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Complete proteome; Direct protein sequencing; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Serine/threonine-protein kinase; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   353  353     Serine/threonine-protein kinase SRK2G. PRO_0000085637
DOMAIN   4   260  257     Protein kinase. 
NP_BIND   10    18  9     ATP (By similarity). 
COMPBIAS   319   343  25     Asp/Glu-rich (acidic). 
ACT_SITE   123   123        Proton acceptor (By similarity). 
BINDING   33    33        ATP (By similarity). 
MOD_RES   149   149        Phosphoserine. 
MOD_RES   150   150        Phosphoserine. 
MOD_RES   154   154        Phosphoserine. 
MOD_RES   158   158        Phosphoserine. 
MOD_RES   159   159        Phosphothreonine. 
CONFLICT   55    55        L -> F (in Ref. 1; CAA78106). 
CONFLICT   134   134        S -> A (in Ref. 1; CAA78106). 
Sequence information
Length: 353 AA [This is the length of the unprocessed precursor] Molecular weight: 40198 Da [This is the MW of the unprocessed precursor] CRC64: 7176CE43659FCCA4 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MDKYDVVKDL GAGNFGVARL LRHKDTKELV AMKYIERGRK IDENVAREII NHRSLKHPNI 

        70         80         90        100        110        120 
IRFKEVILTP THLAIVMEYA SGGELFDRIC TAGRFSEAEA RYFFQQLICG VDYCHSLQIC 

       130        140        150        160        170        180 
HRDLKLENTL LDGSPAPLLK ICDFGYSKSS ILHSRPKSTV GTPAYIAPEV LSRREYDGKH 

       190        200        210        220        230        240 
ADVWSCGVTL YVMLVGAYPF EDPNDPKNFR KTIQRIMAVQ YKIPDYVHIS QECKHLLSRI 

       250        260        270        280        290        300 
FVTNSAKRIT LKEIKNHPWY LKNLPKELLE SAQAAYYKRD TSFSLQSVED IMKIVGEARN 

       310        320        330        340        350 
PAPSTSAVKS SGSGADEEEE EDVEAEVEEE EDDEDEYEKH VKEAQSCQES DKA 

P43292 in FASTA format

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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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