EC Number |
General Information |
Reference |
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2.7.1.158 | evolution |
differential spatial and temporal expression profiling of gene GmIpk1 and its two homologues Glyma06g03310 and Glyma04g03310 in Glycine max |
760240 |
2.7.1.158 | evolution |
most residues involved in substrate binding and catalysis are conserved between mammal and plant IP5 2-Ks, but some differences in the inositide P1 and P3 coordination are observed. InmIP5 2-K, additional interactions with P1 are produced through the side chain of Lys173, a residue non-conserved with the plant IP5 2-Ks but absolutely conserved in mammal enzymes, whereas conservative substitutions can be observed in other vertebrates |
761460 |
2.7.1.158 | evolution |
the amino acid sequence of GmIPK1 shows much similarity with that of Phaseolus vulgaris and Cicer arietinum. It also shows the presence of the characteristic Ins_P5_2-kinase domain required for catalytic activity |
761238 |
2.7.1.158 | malfunction |
a functional Asp1 kinase domain abolishes invasive growth which is monopolar |
723173 |
2.7.1.158 | malfunction |
a loss-of-function mutant exhibits disturbed phosphate homeostasis and overaccumulated phosphate as a consequence of increased phosphate uptake activity and root-to-shoot phosphate translocation. The mutant also shows a phosphate deficiency-like root system architecture with reduced primary root and enhanced lateral root growth |
739312 |
2.7.1.158 | malfunction |
a mutant of inositol pentakisphosphate 2-kinase displays hypersensitivity to arsenate stress and less arsenate uptake when compared to the wild type enzyme |
739275 |
2.7.1.158 | malfunction |
cells lacking the enzyme display defects in dynein-dependent trafficking pathways including endosomal sorting, vesicle movement and Golgi maintenance |
-, 737654 |
2.7.1.158 | malfunction |
disruption of inositol pentakisphosphate 2-kinase profoundly influences cellular processes |
761678 |
2.7.1.158 | malfunction |
in contrast to wild-type IPK1, which is able to restore the phosphate content of the ipk1-1 mutant to wild-type level, both kinase-inactive IPK1 forms fail to complement excessive phosphate accumulation and PSR gene activation in ipk1-1. Although both ipk1-1 and itpk1 mutants exhibit decreased levels of InsP6 (phytate) and diphosphoinositol pentakisphosphate (PP-InsP5; InsP7), disruption of another ITPK family enzyme, ITPK4, which correspondingly causes depletion of InsP6 and InsP7, does not display similar phosphate-related phenotypes, which precludes these InsP species from being effectors. Notably, the level of D/L-Ins(3,4,5,6)P4 is concurrently elevated in both ipk1-1 and itpk1 mutants, which demonstrates a specific correlation with the misregulated phosphate phenotypes. The level of D/L-Ins(3,4,5,6)P4 is not responsive to phosphate starvation that instead manifests a shoot-specific increase in the InsP7 level. Misregulation of phosphate homeostasis in ipk1-1 is not caused by defective InsP6-mediated mRNA export. Neither of the kinase-inactive IPK1 mutants K168A and D368A complement the PSR-like RSA phenotypes (i.e. reduced primary root and enhanced lateral root growth) of ipk1-1 mutant. In addition to the decreased InsP6 level, levels of InsP7 and InsP8 are also reduced in ipk1-1 mutants |
762144 |
2.7.1.158 | malfunction |
urine inositol pentakisphosphate 2-kinase and changes in kidney structure in early diabetic kidney disease in type 1 diabetes. A higher prevalence of detectable urinary inositol 1,3,4,5,6-pentakisphosphate 2-kinase (IPP2K) in type 1 diabetes correlates with early renal function decline. Proximal tubule cells from people with type 1 diabetes and diabetic kidney disease (DKD) express more IPP2K compared with controls. Demographics and clinical characteristics by tertile of baseline urine inositol 1,3,4,5,6-pentakisphosphate 2-kinase/creatinine (IPP2K/Cr), overview |
760326 |