GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.
|Status||Page||Date/Time||GO Term (Aspect)||Reference||Evidence||Notes||Links|
|RHOCA:RNFA||2013-09-13 20:36:33 CDT||GO:0016021 integral to membrane (C)||PMID:9154934||ECO:0000314 direct assay evidence used in manual assertion|
Figure 1B illustrates the PhoA activity of diazotrophically grown cells split into chromatophore and soluble fractions. The high PhoA activity in chromatophore fragments and low PhoA activity in soluble fragments suggests that RnfA has alternating hydrophobic and hydrophilic regions; thus, RnfA is a transmembrane protein.
|VIBFM:B5FFH2||2013-09-28 09:12:38 CDT||GO:0045892 negative regulation of transcription, DNA-dependent (P)||PMID:9353217||ECO:0000315 mutant phenotype evidence used in manual assertion|
Figure 2 shows that hns- and hns-rpoS-mutants of MC4110/pW21A and MC4110/pHK555 strains rapidly developed high luminescence levels. In addition, Figure 4 illustrates that both novobiocin and nalidixic-acid, DNA gyrase inhibitors, increase the luminescence of MC4110 rpoS/ptv1073 cells more than 100-fold. Together, these data suggest that the H-NS protein inhibits transcription in E. Coli of the lux systems of all or most luminous bacteria.
|RHOCA:RNFA||2013-09-28 09:34:22 CDT||GO:0070111 organellar chromatophore (C)||PMID:9154934||ECO:0000314 direct assay evidence used in manual assertion|
Figure 1B illustrates a high amount of alkaline phosphatase activity in the chromatophore fraction of R. capsulatus cells; therefore, a high amount of RnfA activity.
|HUMAN:TRAP1||2013-10-13 12:53:02 CDT||GO:0009386 translational attenuation (P)||PMID:24113185||ECO:0000315 mutant phenotype evidence used in manual assertion|
Figure 1a: Control cells incorporate less radioactively labeled amino acids compared with TRAP1 KD cells (total lysates brief exposure), suggesting a role for TRAP1 in the global attenuation of translation.
|MYCTU:GLND||2013-11-06 16:50:24 CST||GO:0070566 adenylyltransferase activity (F)||PMID:23352854||ECO:0000315 mutant phenotype evidence used in manual assertion|
glnD deletion mutant was unable to adenylylate GlnK, while it was adenylylated in the wild type strain (Suppl. Figure S2).
|ACEWO:C4N8U0||2013-11-10 16:10:56 CST||GO:0005886 plasma membrane (C)||PMID:19222539||ECO:0000314 direct assay evidence used in manual assertion|
Figure 3. Western blot with antisera against RnfC; samples from cell extract and membranes match
|ACEWO:C4N8U2||2013-11-10 16:17:54 CST||GO:0005886 plasma membrane (C)||PMID:19222539||ECO:0000314 direct assay evidence used in manual assertion|
Figure 3. Western blot with antisera against RnfG yielded identical band patterns for cellular extract and membrane
|SHEON:Q8EG33||2013-11-10 16:39:56 CST||GO:0022904 respiratory electron transport chain (P)||PMID:22360295||ECO:0000315 mutant phenotype evidence used in manual assertion|
Figure 1C: the surface density of cells of the (-)omcA mutant attributable to hematite-specific cell accumulation (A) decreased to 45% of Amax
Annotations challenged by Semanchik
|Status||Author,Group||Page||GO Term (Aspect)||Reference||Evidence||Links||Page history|
Team People that mess up
|ALIFS:B9UP04||GO:0009927 - histidine phosphotransfer kinase activity (F)||PMID:18441062||ECO:0000315 mutant phenotype evidence used in manual assertion||challenge||C: 2|
fixed by Atruchon
|?||PMID:7592489||IDA: Inferred from Direct Assay||challenge||C: 2|
0 annotations fixed by Semanchik