High impact information on ATPK1

• The first intron of atpk1 functions as an enhancer in atpk1 expression [1].
• Other motifs found in the Atpk1 protein include two putative autophosphorylation sites, a pseudosubstrate site, two acidic domains, a lysine-rich domain, and two putative PEST sequences, which may contribute to the regulation of protein kinase activity [1].
• A 60-kDa form of Atpk1 derived from the insect cell-expressed p70 was more highly phosphorylated than p70 in in vitro kinase assays, suggesting a negative regulatory domain can be removed by proteolysis [2].
• These findings indicate that PK1 is regulated by two functionally distinct phosphorylations [3].
• The transcription levels of the ATPK19 and ATPK6 genes rapidly and markedly increased when plants were subjected to cold or high-salt stresses [4].

Biological context of ATPK1

• These observations suggest that ATPK19 and ATPK6 may function in the adaptation of plant cells to cold or high-salt conditions, providing an understanding of the role of protein phosphorylation in plant responses to environmental stresses [4].
• The deduced amino acid sequences of the ATPK19 and ATPK6 contain all 11 conserved regions of the catalytic domain of protein kinases, and have homology to p70 ribosomal S6 kinases (52%) [4].

Associations of ATPK1 with chemical compounds

• ATPK19 and ATPK6 have putative PEST regions in their N- and C-terminal regions, and these regions also contain putative phosphorylation sites that are recognized by casein kinases or proline-directed protein kinases such as cdc2, MAP kinase, and p54 MAP-2 kinase (SAPK) [4].

References