DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structural biochemistry of a fungal LOV domain photoreceptor reveals an evolutionarily conserved pathway integrating light and oxidative stress. Structural biochemistry of a fungal LOV domain photoreceptor reveals an evolutionarily conserved pathway integrating light and oxidative stress. Structure (London, England : 1993) 2015 imex curation Lokhandwala J., Hopkins HC., Rodriguez-Iglesias A., Dattenböck C., Schmoll M., Zoltowski BD. Only protein-protein interactions in vitro In vitro comigration in sds comigration in sds page comigration in sds weight by staining molecular weight estimation by staining weight by staining Lokhandwala J., Hopkins HC., Rodriguez-Iglesias A., Dattenböck C., Schmoll M., Zoltowski BD. DIP original experiment: DIP-264710X Structure (London, England : 1993) 2015 IMEx Structural biochemistry of a fungal LOV domain photoreceptor reveals an evolutionarily conserved pathway integrating light and oxidative stress. Structural biochemistry of a fungal LOV domain photoreceptor reveals an evolutionarily conserved pathway integrating light and oxidative stress. Structural biochemistry of a fungal LOV domain photoreceptor reveals an evolutionarily conserved pathway integrating light and oxidative stress. Structure (London, England : 1993) 2015 imex curation Lokhandwala J., Hopkins HC., Rodriguez-Iglesias A., Dattenböck C., Schmoll M., Zoltowski BD. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Lokhandwala J., Hopkins HC., Rodriguez-Iglesias A., Dattenböck C., Schmoll M., Zoltowski BD. DIP original experiment: DIP-264711X Structure (London, England : 1993) 2015 IMEx Structural biochemistry of a fungal LOV domain photoreceptor reveals an evolutionarily conserved pathway integrating light and oxidative stress. Structural biochemistry of a fungal LOV domain photoreceptor reveals an evolutionarily conserved pathway integrating light and oxidative stress. Structural biochemistry of a fungal LOV domain photoreceptor reveals an evolutionarily conserved pathway integrating light and oxidative stress. Structure (London, England : 1993) 2015 imex curation Lokhandwala J., Hopkins HC., Rodriguez-Iglesias A., Dattenböck C., Schmoll M., Zoltowski BD. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Lokhandwala J., Hopkins HC., Rodriguez-Iglesias A., Dattenböck C., Schmoll M., Zoltowski BD. DIP original experiment: DIP-264708X Structure (London, England : 1993) 2015 IMEx Structural biochemistry of a fungal LOV domain photoreceptor reveals an evolutionarily conserved pathway integrating light and oxidative stress. Structural biochemistry of a fungal LOV domain photoreceptor reveals an evolutionarily conserved pathway integrating light and oxidative stress. Structural biochemistry of a fungal LOV domain photoreceptor reveals an evolutionarily conserved pathway integrating light and oxidative stress. Structure (London, England : 1993) 2015 imex curation Lokhandwala J., Hopkins HC., Rodriguez-Iglesias A., Dattenböck C., Schmoll M., Zoltowski BD. Only protein-protein interactions in vitro In vitro light scattering light scattering predetermined predetermined participant predetermined Lokhandwala J., Hopkins HC., Rodriguez-Iglesias A., Dattenböck C., Schmoll M., Zoltowski BD. DIP original experiment: DIP-264709X Structure (London, England : 1993) 2015 IMEx Structural biochemistry of a fungal LOV domain photoreceptor reveals an evolutionarily conserved pathway integrating light and oxidative stress. g0ruc2_hypjq env1 TRIREDRAFT_81609 protein protein hypjq Hypocrea jecorina (strain QM6a) Trichoderma reesei MLEAPIMVSSGSSDLPLQLNPWEAQALNYGFPQEPSTNGHAGSNSNNNNNTPAWIQLPDPIIYPGIYSASGIDVMGILLRIASRPNPTIDLGPLDCSVSLTLCDISLPDAPIVYASPGFYQLTGYSAPEIMGRNCRFLQNSPHMPPPGRVSDAVQEMRRAIRAHQEVQVRIVNYKKNGTPFTNVVTILPLWADPSGHHFAVGLQAEL DIP protein G0RUC2 original sequence version: 15 env1-1 2 5 unspecified role unspecified role unspecified role unspecified role Region 65-207 Region 65-207 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction env1-2 3 5 unspecified role unspecified role unspecified role unspecified role Region65-207 Region65-207 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain G0RUC2:p.Cys96Thr C96T mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain C T This feature has been corrected as a result of our quality control procedures. The original label was 'C96T'. Wed May 02 14:47:59 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys96thr' Tue Jun 30 20:25:00 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys96Thr' ecolx Escherichia coli direct interaction direct interaction env1-3 4 5 unspecified role unspecified role unspecified role unspecified role Region 65-207 Region 65-207 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain G0RUC2:p.Cys96Thr C96T mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain C T This feature has been corrected as a result of our quality control procedures. The original label was 'C96T'. Wed May 02 17:26:14 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys96thr' Tue Jun 30 16:08:36 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys96Thr' ecolx Escherichia coli direct interaction direct interaction env1-4 1 5 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction