IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ Structural basis of LSD1-CoREST selectivity in histone H3 recognition. Structural basis of LSD1-CoREST selectivity in histone H3 recognition. J. Biol. Chem. (0021-9258) 2007 Forneris F., Binda C., Adamo A., Battaglioli E., Mattevi A. Chromatin - Epigenetic interactions resulting in chromatin modulation mattevi@ipvgen.unipv.it 07-Aug-2007: Contacted by JYOTI. davet in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Forneris F., Binda C., Adamo A., Battaglioli E., Mattevi A. Chromatin - Epigenetic interactions resulting in chromatin modulation mattevi@ipvgen.unipv.it Accepted 2007-AUG-5 by DAVET. J. Biol. Chem. (0021-9258) 2007 davet Structural basis of LSD1-CoREST selectivity in histone H3 recognition. Structural basis of LSD1-CoREST selectivity in histone H3 recognition. J. Biol. Chem. (0021-9258) 2007 Forneris F., Binda C., Adamo A., Battaglioli E., Mattevi A. Chromatin - Epigenetic interactions resulting in chromatin modulation mattevi@ipvgen.unipv.it 07-Aug-2007: Contacted by JYOTI. davet in vitro In vitro enzymatic study enzymatic study ms participant Identification by mass spectrometry ms participant Forneris F., Binda C., Adamo A., Battaglioli E., Mattevi A. Chromatin - Epigenetic interactions resulting in chromatin modulation Enzymatic activities were measured under aerobic conditions by using a peroxidase coupled assay monomethylated Lys 4 peptide and Lys4Met peptides were used as substrates. mattevi@ipvgen.unipv.it Accepted 2007-AUG-5 by DAVET. 07-Aug-2007: Contacted by JYOTI. J. Biol. Chem. (0021-9258) 2007 davet kdm1a_human Lysine-specific histone demethylase 1A Flavin-containing amine oxidase domain-containing protein 2 BRAF35-HDAC complex protein BHC110 KDM1A KIAA0601 LSD1 AOF2 KDM1 [histone H3]-dimethyl-L-lysine(4) FAD-dependent demethylase 1A protein protein human Homo sapiens Human MLSGKKAAAAAAAAAAAATGTEAGPGTAGGSENGSEVAAQPAGLSGPAEVGPGAVGERTPRKKEPPRASPPGGLAEPPGSAGPQAGPTVVPGSATPMETGIAETPEGRRTSRRKRAKVEYREMDESLANLSEDEYYSEEERNAKAEKEKKLPPPPPQAPPEEENESEPEEPSGVEGAAFQSRLPHDRMTSQEAACFPDIISGPQQTQKVFLFIRNRTLQLWLDNPKIQLTFEATLQQLEAPYNSDTVLVHRVHSYLERHGLINFGIYKRIKPLPTKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPMAVVSKQVNMELAKIKQKCPLYEANGQAVPKEKDEMVEQEFNRLLEATSYLSHQLDFNVLNNKPVSLGQALEVVIQLQEKHVKDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVKPPRDITAEFLVKSKHRDLTALCKEYDELAETQGKLEEKLQELEANPPSDVYLSSRDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHLTVRNGYSCVPVALAEGLDIKLNTAVRQVRYTASGCEVIAVNTRSTSQTFIYKCDAVLCTLPLGVLKQQPPAVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFWNLYKAPILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSSAVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITPGPSIPGAPQPIPRLFFAGEHTIRNYPATVHGALLSGLREAGRIADQFLGAMYTLPRQATPGVPAQQSPSM A61CEDE51E4E0C1D h31t_human Histone H3.1t H3-4 H3/g H3FT HIST3H3 Histone H3.4 protein protein human Homo sapiens Human MARTKQTARKSTGGKAPRKQLATKVARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLMREIAQDFKTDLRFQSSAVMALQEACESYLVGLFEDTNLCVIHAKRVTIMPKDIQLARRIRGERA DIP protein Q16695 original sequence version: 117 37375A2C3A377B2B fad FAD - Flavin adenine dinucleotide Adenosine 5'-(trihydrogen pyrophosphate), 5'-5'-ester with riboflavine adenosine 5'-[3-(riboflavin-5'-yl) dihydrogen diphosphate] FAD Flavin adenine dinucleotide FLAVIN-ADENINE DINUCLEOTIDE Riboflavin 5'-(trihydrogen diphosphate), 5'-5'-ester with adenosine Riboflavin 5'-adenosine diphosphate adenosine 5'-(3-{D-ribo-5-[7,8-dimethyl-2,4-dioxo-3,4-dihydrobenzo[g]pteridin-10(2H)-yl]-2,3,4-trihydroxypentyl} dihydrogen diphosphate) small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) Flavin adenine dinucleotide Flavin adenine dinucleotide rcor1_human REST corepressor 1 RCOR1 KIAA0071 RCOR Protein CoREST protein protein human Homo sapiens Human MPAMVEKGPEVSGKRRGRNNAAASASAAAASAAASAACASPAATAASGAAASSASAAAASAAAAPNNGQNKSLAAAAPNGNSSSNSWEEGSSGSSSDEEHGGGGMRVGPQYQAVVPDFDPAKLARRSQERDNLGMLVWSPNQNLSEAKLDEYIAIAKEKHGYNMEQALGMLFWHKHNIEKSLADLPNFTPFPDEWTVEDKVLFEQAFSFHGKTFHRIQQMLPDKSIASLVKFYYSWKKTRTKTSVMDRHARKQKREREESEDELEEANGNNPIDIEVDQNKESKKEVPPTETVPQVKKEKHSTQAKNRAKRKPPKGMFLSQEDVEAVSANATAATTVLRQLDMELVSVKRQIQNIKQTNSALKEKLDGGIEPYRLPEVIQKCNARWTTEEQLLAVQAIRKYGRDFQAISDVIGNKSVVQVKNFFVNYRRRFNIDEVLQEWEAEHGKEETNGPSNQKPVKSPDNSIKMPEEEDEAPVLDVRYASAS DIP protein Q9UKL0 original sequence version: 132 DIP protein Q9UKL0 original sequence version: 126 DIP protein Q9UKL0 original sequence version: 115 DIP protein Q9UKL0 original sequence version: 91 DIP protein Q9UKL0 original sequence version: 144 DIP protein Q9UKL0 original sequence version: 80 77E90FB0EFD514B2 lsd1-rcor1-1 1 5 unspecified role unspecified role neutral component neutral component 4 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain lys4met 4hypro 4-hydroxy-L-proline (2S,4R)-4-hydroxypyrrolidine-2-carboxylic acid 4-hydroxy-L-proline 4-hydroxylated L-proline 4-hydroxyproline 4-trans-hydroxy-L-proline L-threo-4-hydroxyproline MOD_RES 4-hydroxyproline gamma-hydroxypyrrolidine-alpha-carboxylic acid 4HyPro certain certain sequence position certain certain certain sequence position certain 6 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 3 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) physical association physical association 3.10 A working 22.3%, free 23.9% Figure 1, Table 2 Crystal structure of LSD1-CoREST in complex with pLys4Met H3 peptide. lsd1-rcor1-2 2 6 unspecified role unspecified role ancillary ancillary region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 3 enzyme enzyme unspecified role unspecified role region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 4 enzyme target enzyme target substrate substrate unspecified role unspecified role Q16695:p.Lys5Met mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain K M Wed May 02 16:23:37 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys5met' Tue Jun 30 16:46:06 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys5Met' region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain lys4 melys methylated lysine MeLys certain certain sequence position certain certain certain sequence position certain physical association physical association Table 1 Ki in the presence of the mutant peptide is 0.05 micromoles. lsd1-rcor1-3 2 4 enzyme target enzyme target substrate substrate unspecified role unspecified role lys4 melys methylated lysine MeLys certain certain sequence position certain certain certain sequence position certain Q16695:p.Lys5Met mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain K M Thu Jul 07 12:18:37 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was lys5met Wed May 02 16:51:05 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys5met' Tue Jun 30 17:15:51 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys5Met' region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 3 enzyme enzyme unspecified role unspecified role region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) physical association physical association Table 1 Ki in the presence of the mutant peptide is 0.04 micromoles