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Search results 1 to 42 out of 42 for reactive oxygen species

Category restricted to UniProtFeature (x)

0.032s

Categories

Category: UniProtFeature
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Type Details Score
UniProt Feature
UniProt Feature
Begin: 351
Description: Reactive bond
Type: site
End: 352
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UniProt Feature
UniProt Feature
Begin: 36
Description: Reactive site
Type: site
End: 36
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UniProt Feature
UniProt Feature
Begin: 48
Description: Reactive bond
Type: site
End: 49
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UniProt Feature
UniProt Feature
Begin: 394
Description: Reactive bond
Type: site
End: 395
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UniProt Feature
UniProt Feature
Begin: 48
Description: Reactive bond
Type: site
End: 49
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UniProt Feature
UniProt Feature
Begin: 47
Description: Reactive bond
Type: site
End: 48
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UniProt Feature
UniProt Feature
Begin: 49
Description: Reactive bond
Type: site
End: 50
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UniProt Feature
UniProt Feature
Begin: 29
Description: Reactive site
Type: site
End: 29
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UniProt Feature
UniProt Feature
Begin: 30
Description: Reactive site
Type: site
End: 30
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UniProt Feature
UniProt Feature
Begin: 37
Description: Reactive site
Type: site
End: 37
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UniProt Feature
UniProt Feature
Begin: 46
Description: Reactive site
Type: site
End: 46
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UniProt Feature
UniProt Feature
Begin: 49
Description: Reactive bond
Type: site
End: 50
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UniProt Feature
UniProt Feature
Begin: 331
Description: Reactive bond
Type: site
End: 332
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UniProt Feature
UniProt Feature
Begin: 358
Description: Reactive bond
Type: site
End: 359
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UniProt Feature
UniProt Feature
Begin: 351
Description: Reactive bond
Type: site
End: 352
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UniProt Feature
UniProt Feature
Begin: 48
Description: Reactive bond
Type: site
End: 49
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UniProt Feature
UniProt Feature
Begin: 356
Description: Reactive bond
Type: site
End: 357
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UniProt Feature
UniProt Feature
Begin: 347
Description: Reactive bond
Type: site
End: 348
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UniProt Feature
UniProt Feature
Begin: 579
Description: Reactive bond
Type: site
End: 580
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UniProt Feature
UniProt Feature
Begin: 38
Description: Reactive site
Type: site
End: 38
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UniProt Feature
UniProt Feature
Begin: 11
Description: Reactive site
Type: site
End: 11
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UniProt Feature
UniProt Feature
Begin: 227
Description: Abolishes cyanide-resistant oxygen consumption.
Type: mutagenesis site
End: 227
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UniProt Feature
UniProt Feature
Begin: 296
Description: Abolishes cyanide-resistant oxygen consumption.
Type: mutagenesis site
End: 296
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UniProt Feature
UniProt Feature
Begin: 299
Description: Abolishes cyanide-resistant oxygen consumption.
Type: mutagenesis site
End: 299
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UniProt Feature
UniProt Feature
Begin: 136
Description: Abolishes cyanide-resistant oxygen consumption.
Type: mutagenesis site
End: 136
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UniProt Feature
UniProt Feature
Begin: 178
Description: Abolishes cyanide-resistant oxygen consumption.
Type: mutagenesis site
End: 178
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UniProt Feature
UniProt Feature
Begin: 175
Description: Abolishes cyanide-resistant oxygen consumption.
Type: mutagenesis site
End: 175
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UniProt Feature
UniProt Feature
Begin: 56
Description: Impaired seedling growth inhibition and altered induction of reactive oxygen species (ROS) burst. Loss of MIK2 binding and subsequent association with BAK1/SERK3, and impaired MIK2-dependent seedling and root growth inhibition and altered induction of reactive oxygen species (ROS) burst; when associated with A-58.
Type: mutagenesis site
End: 56
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UniProt Feature
UniProt Feature
Begin: 59
Description: Reactive Intermediate Deaminase A, chloroplastic
Type: chain
End: 187
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UniProt Feature
UniProt Feature
Begin: 58
Description: Impaired seedling growth inhibition. Loss of MIK2 binding and subsequent association with BAK1/SERK3, and impaired MIK2-dependent seedling and root growth inhibition and altered induction of reactive oxygen species (ROS) burst; when associated with A-56.
Type: mutagenesis site
End: 58
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UniProt Feature
UniProt Feature
Begin: 228
Description: In ise1-1; increased PD-mediated transport, with higher frequency of branched and twinned PD, and impaired mitochondrial metabolism accompanied by a disrupted mitochondrial proton gradient and an increased production of reactive oxygen species.
Type: mutagenesis site
End: 228
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UniProt Feature
UniProt Feature
Begin: 170
Description: Impaired flg22-induced ubiquination, internalization of BIK1 and FLS2 from the plasma membrane and reactive oxygen species (ROS) production, as well as enhanced susceptibilitye to the bacterial pathogen Pseudomonas syringae pv. tomato (Pst) DC3000 and to the fungal pathogen Botrytis cinerea, but normal phosphorylation; when associated with R-31, R-41, R-95, R-186, R-286, R-337, R-358 and R-366.
Type: mutagenesis site
End: 170
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UniProt Feature
UniProt Feature
Begin: 31
Description: Impaired flg22-induced ubiquination, internalization of BIK1 and FLS2 from the plasma membrane and reactive oxygen species (ROS) production, as well as enhanced susceptibilitye to the bacterial pathogen Pseudomonas syringae pv. tomato (Pst) DC3000 and to the fungal pathogen Botrytis cinerea, but normal phosphorylation; when associated with R-41, R-95, R-170, R-186, R-286, R-337, R-358 and R-366.
Type: mutagenesis site
End: 31
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UniProt Feature
UniProt Feature
Begin: 366
Description: Impaired flg22-induced ubiquination, internalization of BIK1 and FLS2 from the plasma membrane and reactive oxygen species (ROS) production, as well as enhanced susceptibilitye to the bacterial pathogen Pseudomonas syringae pv. tomato (Pst) DC3000 and to the fungal pathogen Botrytis cinerea, but normal phosphorylation; when associated with R-31, R-41, R-95, R-170, R-186, R-286, R-337 and R-358.
Type: mutagenesis site
End: 366
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UniProt Feature
UniProt Feature
Begin: 286
Description: Impaired flg22-induced ubiquination, internalization of BIK1 and FLS2 from the plasma membrane and reactive oxygen species (ROS) production, as well as enhanced susceptibilitye to the bacterial pathogen Pseudomonas syringae pv. tomato (Pst) DC3000 and to the fungal pathogen Botrytis cinerea, but normal phosphorylation; when associated with R-31, R-41, R-95, R-170, R-186, R-337, R-358 and R-366.
Type: mutagenesis site
End: 286
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UniProt Feature
UniProt Feature
Begin: 95
Description: Impaired flg22-induced ubiquination, internalization of BIK1 and FLS2 from the plasma membrane and reactive oxygen species (ROS) production, as well as enhanced susceptibilitye to the bacterial pathogen Pseudomonas syringae pv. tomato (Pst) DC3000 and to the fungal pathogen Botrytis cinerea, but normal phosphorylation; when associated with R-31, R-41, R-170, R-186, R-286, R-337, R-358 and R-366.
Type: mutagenesis site
End: 95
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UniProt Feature
UniProt Feature
Begin: 358
Description: Impaired flg22-induced ubiquination, internalization of BIK1 and FLS2 from the plasma membrane and reactive oxygen species (ROS) production, as well as enhanced susceptibilitye to the bacterial pathogen Pseudomonas syringae pv. tomato (Pst) DC3000 and to the fungal pathogen Botrytis cinerea, but normal phosphorylation; when associated with R-31, R-41, R-95, R-170, R-186, R-286, R-337 and R-366.
Type: mutagenesis site
End: 358
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UniProt Feature
UniProt Feature
Begin: 41
Description: Impaired flg22-induced ubiquination, internalization of BIK1 and FLS2 from the plasma membrane and reactive oxygen species (ROS) production, as well as enhanced susceptibilitye to the bacterial pathogen Pseudomonas syringae pv. tomato (Pst) DC3000 and to the fungal pathogen Botrytis cinerea, but normal phosphorylation; when associated with R-31, R-95, R-170, R-186, R-286, R-337, R-358 and R-366.
Type: mutagenesis site
End: 41
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UniProt Feature
UniProt Feature
Begin: 337
Description: Impaired flg22-induced ubiquination, internalization of BIK1 and FLS2 from the plasma membrane and reactive oxygen species (ROS) production, as well as enhanced susceptibilitye to the bacterial pathogen Pseudomonas syringae pv. tomato (Pst) DC3000 and to the fungal pathogen Botrytis cinerea, but normal phosphorylation; when associated with R-31, R-41, R-95, R-170, R-186, R-286, R-358 and R-366.
Type: mutagenesis site
End: 337
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UniProt Feature
UniProt Feature
Begin: 186
Description: Impaired flg22-induced ubiquination, internalization of BIK1 and FLS2 from the plasma membrane and reactive oxygen species (ROS) production, as well as enhanced susceptibilitye to the bacterial pathogen Pseudomonas syringae pv. tomato (Pst) DC3000 and to the fungal pathogen Botrytis cinerea, but normal phosphorylation; when associated with R-31, R-41, R-95, R-170, R-286, R-337, R-358 and R-366.
Type: mutagenesis site
End: 186
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UniProt Feature
UniProt Feature
Begin: 183
Description: Susceptibility to the nonhost powdery mildew species B.graminis and E.pisi. Loss of myrosinase activity but intact glucosidase activity.
Type: mutagenesis site
End: 183
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UniProt Feature
UniProt Feature
Begin: 173
Description: In zed1-D; normal growth of plants grown below 22 degrees Celsius, but high temperature (above 22 degrees Celsius)-dependent RPP13L4/ZAR1-influenced autoimmunity and growth retardation. Plants cultivated above 23 degrees Celsius are dwarf with crinkled lamina, shortened petiole, reduced pedicel length and silique numbers, increased branches, severely shortened inflorescence stem and clustered siliques. These phenotypes are associated with inhibited cell elongation and/or expansion and disturbed differentiation of trichomes and stomata, disorganized interfascicular fibers and fewer pith tissues in inflorescence stems as well as increased lignin deposition in the vasculatures. Elevated reactive oxygen species (ROS) content and extensive cell death as well as reduced expression of pathogenesis related genes (e.g. PR1 and PR2) but accumulation of SNC1 when grown at 25 degrees Celsius. The high temperature-induced autoimmune phenotype is blocked in the double mutant zed1-D zar1-3. Stronger binding activity with RPP13L4/ZAR1. Confined to the cytosol. Fully rescued by the over-expression of RKS1/ZRK1 and ZRK12, and partially by the over-expression of ZRK4, ZRK10, ZRK13 and ZRK14. The double mutants zed1-D snc1-11 and zed1-D nahG have restored normal growth phenotypes and rescued autoimmunity defects. These pleiotropic phenotypes are suppressed in plants lacking SZE1 and SZE2.
Type: mutagenesis site
End: 173
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