DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Molecular mimicry and ligand recognition in binding and catalysis by the histone demethylase LSD1-CoREST complex. Molecular mimicry and ligand recognition in binding and catalysis by the histone demethylase LSD1-CoREST complex. Structure (London, England : 1993) 2011 imex curation Baron R., Binda C., Tortorici M., McCammon JA., Mattevi A. 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 Baron R., Binda C., Tortorici M., McCammon JA., Mattevi A. DIP original experiment: DIP-218763X Structure (London, England : 1993) 2011 IMEx Molecular mimicry and ligand recognition in binding and catalysis by the histone demethylase LSD1-CoREST complex. Molecular mimicry and ligand recognition in binding and catalysis by the histone demethylase LSD1-CoREST complex. Molecular mimicry and ligand recognition in binding and catalysis by the histone demethylase LSD1-CoREST complex. Structure (London, England : 1993) 2011 imex curation Baron R., Binda C., Tortorici M., McCammon JA., Mattevi A. Only protein-protein interactions in vitro In vitro pull down pull down predetermined predetermined participant predetermined Baron R., Binda C., Tortorici M., McCammon JA., Mattevi A. DIP original experiment: DIP-218764X Structure (London, England : 1993) 2011 IMEx Molecular mimicry and ligand recognition in binding and catalysis by the histone demethylase LSD1-CoREST complex. Molecular mimicry and ligand recognition in binding and catalysis by the histone demethylase LSD1-CoREST complex. Molecular mimicry and ligand recognition in binding and catalysis by the histone demethylase LSD1-CoREST complex. Structure (London, England : 1993) 2011 imex curation Baron R., Binda C., Tortorici M., McCammon JA., Mattevi A. Only protein-protein interactions in vitro In vitro demethylase assay demethylase assay predetermined predetermined participant predetermined Baron R., Binda C., Tortorici M., McCammon JA., Mattevi A. DIP original experiment: DIP-218767X Structure (London, England : 1993) 2011 IMEx Molecular mimicry and ligand recognition in binding and catalysis by the histone demethylase LSD1-CoREST complex. Molecular mimicry and ligand recognition in binding and catalysis by the histone demethylase LSD1-CoREST complex. Molecular mimicry and ligand recognition in binding and catalysis by the histone demethylase LSD1-CoREST complex. Structure (London, England : 1993) 2011 imex curation Baron R., Binda C., Tortorici M., McCammon JA., Mattevi A. Only protein-protein interactions in vitro In vitro pull down pull down predetermined predetermined participant predetermined Baron R., Binda C., Tortorici M., McCammon JA., Mattevi A. DIP original experiment: DIP-218765X Structure (London, England : 1993) 2011 IMEx Molecular mimicry and ligand recognition in binding and catalysis by the histone demethylase LSD1-CoREST complex. Molecular mimicry and ligand recognition in binding and catalysis by the histone demethylase LSD1-CoREST complex. Molecular mimicry and ligand recognition in binding and catalysis by the histone demethylase LSD1-CoREST complex. Structure (London, England : 1993) 2011 imex curation Baron R., Binda C., Tortorici M., McCammon JA., Mattevi A. 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 Baron R., Binda C., Tortorici M., McCammon JA., Mattevi A. DIP original experiment: DIP-218766X Structure (London, England : 1993) 2011 IMEx Molecular mimicry and ligand recognition in binding and catalysis by the histone demethylase LSD1-CoREST complex. q8cig3-1 Lysine-specific histone demethylase 1B Kdm1b Aof1 Lsd2 Flavin-containing amine oxidase domain-containing protein 1 Lysine-specific histone demethylase 2 protein protein mouse Mus musculus Mouse MAASRGRSKKRSNLELSPDNLPLRSSGRQAKKKAVEIPDEDEDGSSEKKYRKCEKAGCTAAYPVCFASASERCAKNGYTSRWYHLSCGEHFCNECFDHYYRSHKDGYDKYSAWKRVWTSNGKTEPSPKAFMADQQLPYWVQCTKPECGKWRQLTKEIQLTPHMARTYRCGMKPNTITKPDTPDHCSFPEDLRVLEVSNHWWYPMLIQPPLLKDSVAAPLLSAYYPDCVGMSPSCTSTHRATVTAATTTTGSASPGEMEPSKAAPSSLVLGMNRYFQPFYQPNECGKALCVRPDVMELDELYEFPEYSRDPTMYLALRNLILALWYTNCKEALTPQKCIPHIIVRGLVRIRCVQEVERILYFMTRKGLINTGVLTVAAGQHLLPKHYHNKSVLVVGAGPAGLAAARQLHNFGMKVTVLEAKDRIGGRVWDDKSFKGVVVGRGPQIVNGCINNPVALMCEQLGISMRKLGERCDLIQEGGRITDPTVDKRMDFHFNALLDVVSEWRKDKTLLQDVPLGEKIEEIYRAFVKESGIQFSELEGQVLQFHLSNLEYACGSSLHQVSARSWDHNEFFAQFAGDHTLLTPGYSTIIEKLAEGLDIRLKSPVQSIDYTGDEVQVTTTDGMGHSAQKVLVTVPLAILQRGAIQFNPPLSEKKMKAINSLGAGIIEKIALQFPYRFWDSKVQGADFFGHVPPSASQRGLFAVFYDMDSQQSVLMSVITGEAVASLRTMDDKQVLQQCMGILRELFKEQEIPEPTKYFVTRWSTEPWIQMAYSFVKTFGSGEAYDIIAEEIQGTVFFAGEATNRHFPQTVTGAYLSGVREASKIAAF DIP protein Q8CIG3-1 original sequence version: 63 snai1_human Zinc finger protein SNAI1 Protein snail homolog 1 SNAI1 SNAH protein protein human Homo sapiens Human MPRSFLVRKPSDPNRKPNYSELQDSNPEFTFQQPYDQAHLLAAIPPPEILNPTASLPMLIWDSVLAPQAQPIAWASLRLQESPRVAELTSLSDEDSGKGSQPPSPPSPAPSSFSSTSVSSLEAEAYAAFPGLGQVPKQLAQLSEAKDLQARKAFNCKYCNKEYLSLGALKMHIRSHTLPCVCGTCGKAFSRPWLLQGHVRTHTGEKPFSCPHCSRAFADRSNLRAHLQTHSDVKKYQCQACARTFSRMSLLHKHQESGCSGCPR DIP protein O95863 original sequence version: 109 DIP protein O95863 original sequence version: 141 70E298C9BB154115 o60341-1 Lysine-specific histone demethylase 1A KDM1A AOF2 KDM1 KIAA0601 LSD1 BRAF35-HDAC complex protein BHC110 Flavin-containing amine oxidase domain-containing protein 2 [histone H3]-dimethyl-L-lysine(4) FAD-dependent demethylase 1A protein protein human Homo sapiens Human MLSGKKAAAAAAAAAAAATGTEAGPGTAGGSENGSEVAAQPAGLSGPAEVGPGAVGERTPRKKEPPRASPPGGLAEPPGSAGPQAGPTVVPGSATPMETGIAETPEGRRTSRRKRAKVEYREMDESLANLSEDEYYSEEERNAKAEKEKKLPPPPPQAPPEEENESEPEEPSGVEGAAFQSRLPHDRMTSQEAACFPDIISGPQQTQKVFLFIRNRTLQLWLDNPKIQLTFEATLQQLEAPYNSDTVLVHRVHSYLERHGLINFGIYKRIKPLPTKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPMAVVSKQVNMELAKIKQKCPLYEANGQAVPKEKDEMVEQEFNRLLEATSYLSHQLDFNVLNNKPVSLGQALEVVIQLQEKHVKDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVKPPRDITAEFLVKSKHRDLTALCKEYDELAETQGKLEEKLQELEANPPSDVYLSSRDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHLTVRNGYSCVPVALAEGLDIKLNTAVRQVRYTASGCEVIAVNTRSTSQTFIYKCDAVLCTLPLGVLKQQPPAVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFWNLYKAPILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSSAVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITPGPSIPGAPQPIPRLFFAGEHTIRNYPATVHGALLSGLREAGRIADQFLGAMYTLPRQATPGVPAQQSPSM DIP protein O60341-1 original sequence version: 151 DIP protein O60341 original sequence version: 99 DIP protein O60341 original sequence version: 123 DIP protein O60341 original sequence version: 134 DIP protein O60341 original sequence version: 137 DIP protein O60341-1 original sequence version: 137 DIP protein O60341-1 original sequence version: 109 DIP protein O60341 original sequence version: 163 DIP protein O60341 original sequence version: 97 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 h3k9-2 Histone H3 N-terminal Peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) ARTKQTARKSTGGKAPRKQLA kdm1a-rcor1-5 1 7 unspecified role unspecified role unspecified role unspecified role Region 2-21 Region 2-21 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain in vitro In vitro 9 unspecified role unspecified role unspecified role unspecified role Region 308-440 Region 308-440 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 8 unspecified role unspecified role unspecified role unspecified role Region 171-836 Region 171-836 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association kdm1a-rcor1-6 5 9 unspecified role unspecified role unspecified role unspecified role Region 308-440 Region 308-440 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 8 unspecified role unspecified role unspecified role unspecified role Region 171-836 Region 171-836 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction rcor1-kdm1a-2 4 9 unspecified role unspecified role bait bait Region 308-440 Region 308-440 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain GST-tag GST-tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli 8 unspecified role unspecified role prey prey Region 171-836 Region 171-836 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain His-tag His-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli direct interaction direct interaction h3-kdm1b-1 3 6 enzyme enzyme unspecified role unspecified role ecolx Escherichia coli 10 enzyme target enzyme target substrate substrate unspecified role unspecified role K4me1 K4me1 n6me1lys N6-methyl-L-lysine (2S)-2-amino-6-methylaminohexanoic acid MOD_RES N6-methyllysine N(zeta)-methyllysine N6-methyl-L-lysine N6-methylated L-lysine epsilon-methyllysine Methyl Methylation N-methyl Lysyl N6Me1Lys certain certain sequence position certain certain certain sequence position certain K4me2 K4me2 n6me2lys N6,N6-dimethyl-L-lysine (2S)-2-amino-6-(dimethylamino)hexanoic acid MOD_RES N6,N6-dimethyllysine N(zeta)-dimethyllysine N6,N6-dimethyl-L-lysine N6,N6-dimethylated L-lysine epsilon-dimethyllysine lysine derivative Lys(y) Dimethyl N6Me2Lys di-Methylation dimethylk certain certain sequence position certain certain certain sequence position certain in vitro In vitro demethylation demethylation reaction demethylation kdm1a-rcor1-7 2 9 unspecified role unspecified role prey prey Region 308-440 Region 308-440 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain GST-tag GST-tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli 8 unspecified role unspecified role bait bait Region 171-836 Region 171-836 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain His-tag His-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli direct interaction direct interaction