MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it Conformational modulation and hydrodynamic radii of CP12 protein and its complexes probed by Fluorescence Correlation Spectroscopy. Conformational modulation and hydrodynamic radii of CP12 protein and its complexes probed by Fluorescence Correlation Spectroscopy. FEBS J. (1742-464X) 2014 imex curation Moparthi S.B., Thieulin-Pardo G., Mansuelle P., Rigneault H., Gontero B., Wenger J. satish.moparthi@fresnel.fr 11-Jun-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro fcs fluorescence correlation spectroscopy FCS FCS fcs tag fluorescence tag visualisation by fluorescence tag fluorescence satish.moparthi@fresnel.fr Accepted 2014-MAY-21 by LUANA 2014 imex curation kppr_chlre Phosphoribulokinase, chloroplastic PRKA Phosphopentokinase protein protein chlre Chlamydomonas reinhardtii Chlamydomonas smithii MAFTMRAPAPRATAQSRVTANRARRSLVVRADKDKTVVIGLAADSGCGKSTFMRRMTSIFGGVPKPPAGGNPDSNTLISDMTTVICLDDYHCLDRNGRKVKGVTALAPEAQNFDLMYNQVKALKEGKSVDKPIYNHVSGLIDAPEKIESPPILVIEGLHPFYDKRVAELLDFKIYLDISDDIKFAWKIQRDMAERGHSLESIKSSIAARKPDFDAYIDPQKKDADMIIQVLPTQLVPDDKGQYLRVRLIMKEGSKMFDPVYLFDEGSTISWIPCGRKLTCSFPGIKMFYGPDTWYGQEVSVLEMDGQFDKLEELIYVESHLSNTSAKFYGEITQQMLKNSGFPGSNNGTGLFQTIVGLKVREVYERIVKKDVVPV g3pa_chlre Glyceraldehyde-3-phosphate dehydrogenase A, chloroplastic GAPA NADP-dependent glyceraldehydephosphate dehydrogenase subunit A protein protein chlre Chlamydomonas reinhardtii Chlamydomonas smithii MAAMMQKSAFTGSAVSSKSGVRAKAARAVVDVRAEKKIRVAINGFGRIGRNFLRCWHGRQNTLLDVVAINDSGGVKQASHLLKYDSTLGTFAADVKIVDDSHISVDGKQIKIVSSRDPLQLPWKEMNIDLVIEGTGVFIDKVGAGKHIQAGASKVLITAPAKDKDIPTFVVGVNEGDYKHEYPIISNASCTTNCLAPFVKVLEQKFGIVKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTTTGAAKAVSLVLPSLKGKLNGIALRVPTPTVSVVDLVVQVEKKTFAEEVNAAFREAANGPMKGVLHVEDAPLVSIDFKCTDQSTSIDASLTMVMGDDMVKVVAWYDNEWGYSQRVVDLAEVTAKKWVA cp12_chlre Calvin cycle protein CP12, chloroplastic CP12 CP12 domain-containing protein Chloroplast protein 12 CHLREDRAFT_148487 protein protein chlre Chlamydomonas reinhardtii Chlamydomonas smithii MMLTKSVVISRPAVRPVSTRRAVVVRASGQPAVDLNKKVQDAVKEAEDACAKGTSADCAVAWDTVEELSAAVSHKKDAVKADVTLTDPLEAFCKDAPDADECRVYED cp12-prka 1 PRK 2 predetermined predetermined participant predetermined tag fluorescence tag visualisation by fluorescence tag fluorescence unspecified role unspecified role neutral component neutral component purified purified CP12 4 tag fluorescence tag visualisation by fluorescence tag fluorescence tag fluorescence tag visualisation by fluorescence tag fluorescence unspecified role unspecified role neutral component neutral component purified purified tag fluorophore fluorophore undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined A6Q0K5:p.Pro31Ser mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain P S Wed May 02 16:08:48 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'pro31ser' Tue Jun 30 19:41:15 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Pro31Ser' direct interaction direct interaction T1 T2 F2 F3 F4 Our results showed that the disruption of the N-terminal disulfide bridge on CP12 affects the formation of the CP12C31S-PRK complex, while it has no effect on the CP12C31S-GAPDH complex. On the other hand, we observed the opposite effect with the mutant CP12C75S affected at the C-terminal disulfide bridge that forms a complex with PRK but not with GAPDH. cp12-prka-1 1 CP12 4 tag fluorescence tag visualisation by fluorescence tag fluorescence tag fluorescence tag visualisation by fluorescence tag fluorescence unspecified role unspecified role neutral component neutral component purified purified A6Q0K5:p.Lys75Ser mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain K S Wed May 02 19:08:19 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys75ser' Tue Jun 30 16:10:50 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys75Ser' tag fluorophore fluorophore undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined GAPDH 3 predetermined predetermined participant predetermined tag fluorescence tag visualisation by fluorescence tag fluorescence unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction T1 T2 F2 F3 F4 Our results showed that the disruption of the N-terminal disulfide bridge on CP12 affects the formation of the CP12C31S-PRK complex, while it has no effect on the CP12C31S-GAPDH complex. On the other hand, we observed the opposite effect with the mutant CP12C75S affected at the C-terminal disulfide bridge that forms a complex with PRK but not with GAPDH. cp12-gapa-1 1 PRK 2 predetermined predetermined participant predetermined tag fluorescence tag visualisation by fluorescence tag fluorescence unspecified role unspecified role neutral component neutral component purified purified CP12 4 tag fluorescence tag visualisation by fluorescence tag fluorescence tag fluorescence tag visualisation by fluorescence tag fluorescence unspecified role unspecified role neutral component neutral component purified purified tag fluorophore fluorophore undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined A6Q0K5:p.Lys75Ser mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain K S Wed May 02 14:54:16 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys75ser' Tue Jun 30 16:55:18 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys75Ser' GAPDH 3 predetermined predetermined participant predetermined tag fluorescence tag visualisation by fluorescence tag fluorescence unspecified role unspecified role neutral component neutral component purified purified physical association physical association T1 T2 F2 F3 F4 Our results showed that the disruption of the N-terminal disulfide bridge on CP12 affects the formation of the CP12C31S-PRK complex, while it has no effect on the CP12C31S-GAPDH complex. On the other hand, we observed the opposite effect with the mutant CP12C75S affected at the C-terminal disulfide bridge that forms a complex with PRK but not with GAPDH.