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O49339 (PTI12_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
PTI1-like tyrosine-protein kinase 2

Short name=PTI1-2
EC=2.7.10.2
Gene names
Name:PTI12
Ordered Locus Names:At2g30740
ORF Names:T11J7.13
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length366 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probable tyrosine-protein kinase involved in oxidative burst-mediated signaling leading to specific genes expression. Ref.6

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Enzyme regulation

Strongly activated in response to phosphatidic acid (PA) and xylanase in a OXI1- and PDK1-dependent manner, and, to a lesser extent, by hydrogen peroxide and flagellin in a OXI1-dependent manner. Ref.6

Subunit structure

Interacts with OXI1. Ref.6

Post-translational modification

Autophosphorylated and phosphorylated by OXI1. Ref.6

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family.

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 366366PTI1-like tyrosine-protein kinase 2
PRO_0000403323

Regions

Domain71 – 353283Protein kinase
Nucleotide binding77 – 859ATP By similarity

Sites

Active site2031Proton acceptor By similarity
Binding site991ATP Probable

Experimental info

Mutagenesis991K → N: Reduced phosphorylation and impaired kinase activity. No phosphorylation; when associated with A-238. Ref.6
Mutagenesis2381T → A: No phosphorylation; when associated with N-99. Ref.6

Sequences

Sequence LengthMass (Da)Tools
O49339 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: E9A0450069D35C72

FASTA36640,500
        10         20         30         40         50         60 
MRRWICCGDK KGDSDLSNEE VHLKSPWQNS EANQKNQKPQ AVVKPEAQKE ALPIEVPPLS 

        70         80         90        100        110        120 
VDEVKEKTDN FGSKSLIGEG SYGRVYYATL NDGKAVALKK LDVAPEAETN TEFLNQVSMV 

       130        140        150        160        170        180 
SRLKHENLIQ LVGYCVDENL RVLAYEFATM GSLHDILHGR KGVQGAQPGP TLDWLTRVKI 

       190        200        210        220        230        240 
AVEAARGLEY LHEKVQPPVI HRDIRSSNVL LFEDYQAKVA DFNLSNQAPD NAARLHSTRV 

       250        260        270        280        290        300 
LGTFGYHAPE YAMTGQLTQK SDVYSFGVVL LELLTGRKPV DHTMPRGQQS LVTWATPRLS 

       310        320        330        340        350        360 
EDKVKQCVDP KLKGEYPPKS VAKLAAVAAL CVQYESEFRP NMSIVVKALQ PLLKPPAPAP 


APVPES 

« Hide

References

« Hide 'large scale' references
[1]"Comparative proteome bioinformatics: identification of a whole complement of putative protein tyrosine kinases in the model flowering plant Arabidopsis thaliana."
Carpi A., Di Maira G., Vedovato M., Rossi V., Naccari T., Floriduz M., Terzi M., Filippini F.
Proteomics 2:1494-1503(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
[2]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(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]"Arabidopsis ORF clones."
Shinn P., Chen H., Kim C.J., Ecker J.R.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[6]"The Arabidopsis protein kinase PTI1-2 is activated by convergent phosphatidic acid and oxidative stress signaling pathways downstream of PDK1 and OXI1."
Anthony R.G., Khan S., Costa J., Pais M.S., Boegre L.
J. Biol. Chem. 281:37536-37546(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH OXI1, AUTOPHOSPHORYLATION, PHOSPHORYLATION BY OXI1, MUTAGENESIS OF LYS-99 AND THR-238, ENZYME REGULATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ303007 mRNA. Translation: CAC34450.1.
AC002340 Genomic DNA. Translation: AAC02745.1.
CP002685 Genomic DNA. Translation: AEC08434.1.
BT024893 mRNA. Translation: ABD85164.1.
AK230305 mRNA. Translation: BAF02106.1.
PIRB84712.
RefSeqNP_180632.1. NM_128627.2.
UniGeneAt.20728.

3D structure databases

ProteinModelPortalO49339.
SMRO49339. Positions 59-355.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid2974. 2 interactions.
STRING3702.AT2G30740.1-P.

Proteomic databases

PaxDbO49339.
PRIDEO49339.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G30740.1; AT2G30740.1; AT2G30740.
GeneID817625.
KEGGath:AT2G30740.

Organism-specific databases

GeneFarm1792. 139.
TAIRAT2G30740.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000116550.
InParanoidO49339.
OMAPYLENEN.
PhylomeDBO49339.
ProtClustDBCLSN2682494.

Enzyme and pathway databases

BioCycARA:AT2G30740-MONOMER.

Gene expression databases

GenevestigatorO49339.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
[Graphical view]
PfamPF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePTI12_ARATH
AccessionPrimary (citable) accession number: O49339
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2011
Last sequence update: June 1, 1998
Last modified: April 16, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names