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|Status||Page||User||Date/Time||GO Term (Aspect)||Reference||Evidence||Notes||Links|
|ECOLI:OMPF||Gilbe205, MichSt14A 34||2014-04-06 15:45:02 CDT||GO:0015288 porin activity (F)||PMID:8702816||ECO:0000315 mutant phenotype evidence used in manual assertion|
Figure 3 shows the differing growth rate of wild-type and OmpF mutants when grown on maltotriose and maltooligosaccharides. The N-terminal mutations allow for growth on carbon sources larger than the normal exclusion limit.
|HUMAN:INO1||Gilbe205, MichSt14A 34||2014-04-06 14:23:22 CDT||GO:0004512 inositol-3-phosphate synthase activity (F)||PMID:23902760||ECO:0000315 mutant phenotype evidence used in manual assertion|
Figure 8C shows the effect of point mutations on the activity of the inositol-3-phosphate synthase. The assay measured the inorganic phosphate liberated from glucose 6-phosphate which is dependent on the activity of the synthase enzyme.
|ECOLI:GLGB||Gilbe205, MichSt14A 34||2014-04-06 12:57:04 CDT||GO:0004373 glycogen (starch) synthase activity (F)||PMID:19244233||ECO:0000266 sequence orthology evidence used in manual assertion|
Table 2 presents the partial alignment of conserved residues between Escherichia coli glycogen synthase and other bacterial glycogen syntheses and plant starch syntheses.
|ECOLI:GLGB||Gilbe205, MichSt14A 34||2014-04-06 12:32:45 CDT||GO:0003844 1,4-alpha-glucan branching enzyme activity (F)||PMID:12196524||ECO:0000315 mutant phenotype evidence used in manual assertion|
Table 5 shows sequence point mutations, deletions or truncations that result in glycogen storage disease type IV, caused by lethal or retarded function of glycogen branching enzyme.
|BOMMO:H9JTG9||Gilbe205, MichSt14A 34||2014-04-06 12:13:51 CDT||GO:0004033 aldo-keto reductase (NADP) activity (F)||PMID:24012638||ECO:0000266 sequence orthology evidence used in manual assertion|
Figure 2 shows sequence and structural homology to other defined aldo-keto reductases, notably human aldo-keto reductase AKR1C2.
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