Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot P43291 (SRK2A_ARATH)

Last modified November 25, 2008. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Serine/threonine-protein kinase SRK2A
    EC=2.7.11.1
Alternative name(s):
    Arabidopsis protein SK1
    OST1-kinase-like 7
    SNF1-related kinase 2.4
      Short name=SnRK2.4
Gene names
Name: SRK2A
Synonyms: ASK1, OSKL7, SNRK2.4
Ordered Locus Names: At1g10940
ORF Names: T19D16.14
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length363 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Tissue specificity

Expressed in seedlings.

Induction

By abscisic acid (ABA), salt, and osmotic stress (at protein level).

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.

Contains 1 protein kinase domain.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 363363Serine/threonine-protein kinase SRK2A
PRO_0000085636

Regions

Domain4 – 260257Protein kinase
Nucleotide binding10 – 189ATP By similarity
Compositional bias319 – 34830Asp/Glu-rich (acidic)

Sites

Active site1231Proton acceptor By similarity
Binding site331ATP By similarity

Amino acid modifications

Modified residue1491Phosphoserine By similarity
Modified residue1501Phosphoserine By similarity
Modified residue1541Phosphoserine By similarity
Modified residue1581Phosphoserine By similarity
Modified residue1591Phosphothreonine By similarity

Sequences

Sequence LengthMass (Da)Tools
P43291-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 89C31C87AB6C6E78

FASTA36341,169
        10         20         30         40         50         60 
MDKYELVKDI GAGNFGVARL MKVKNSKELV AMKYIERGPK IDENVAREII NHRSLRHPNI 

        70         80         90        100        110        120 
IRFKEVVLTP THLAIAMEYA AGGELFERIC SAGRFSEDEA RYFFQQLISG VSYCHAMQIC 

       130        140        150        160        170        180 
HRDLKLENTL LDGSPAPRLK ICDFGYSKSS LLHSRPKSTV GTPAYIAPEV LSRREYDGKM 

       190        200        210        220        230        240 
ADVWSCGVTL YVMLVGAYPF EDQEDPKNFR KTIQKIMAVQ YKIPDYVHIS QDCKNLLSRI 

       250        260        270        280        290        300 
FVANSLKRIT IAEIKKHSWF LKNLPRELTE TAQAAYFKKE NPTFSLQTVE EIMKIVADAK 

       310        320        330        340        350        360 
TPPPVSRSIG GFGWGGNGDA DGKEEDAEDV EEEEEEVEEE EDDEDEYDKT VKEVHASGEV 


RIS 

« Hide

References

« Hide 'large scale' references
[1]"Two putative protein kinases from Arabidopsis thaliana contain highly acidic domains."
Park Y.S., Hong S.W., Oh S.A., Kwak J.M., Lee H.H., Nam H.G.
Plant Mol. Biol. 22:615-624(1993) [PubMed: 8393717] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
Tissue: Leaf.
[2]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed: 11130712] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]"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. expand/collapse author list , 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: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"The Arabidopsis CDPK-SnRK superfamily of protein kinases."
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.
Plant Physiol. 132:666-680(2003) [PubMed: 12805596] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
[6]"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: 15292193] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION.
[7]"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: 16365038] [Abstract]
Cited for: GENE FAMILY.

Cross-references

Sequence databases

M91548 mRNA. Translation: AAA02840.1.
U95973 Genomic DNA. Translation: AAB65483.1.
AY093130 mRNA. Translation: AAM13129.1.
BT008850 mRNA. Translation: AAP68289.1.
AY084221 mRNA. Translation: AAM60822.1.
PIRS36944.
RefSeqNP_172563.1.
UniGeneAt.23750

3D structure databases

HSSPHSSP built from PDB template 1GZK based on UniProtKB P31751.
ModBaseSearch...

Protein-protein interaction databases

IntActP43291.

Proteomic databases

ProMEXP43291.

Genome annotation databases

GeneID837637.
GenomeReviewsGene locus AT1G10940 in contig CT485782_GR.
KEGGath:AT1G10940.
NMPDRfig|3702.1.peg.1343.

Organism-specific databases

TAIRAt1g10940.

Gene expression databases

ArrayExpressP43291.
GermOnlineAT1G10940. Arabidopsis thaliana.

Family and domain databases

InterProIPR000719. 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]
PANTHERPTHR22982:SF58. S/T_plantPK. 1 hit.
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
ProDomPD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSRK2A_ARATH
AccessionPrimary (citable) accession number: P43291
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 25, 2008
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents