DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structure and function of the CSL-KyoT2 corepressor complex: a negative regulator of Notch signaling. Structure and function of the CSL-KyoT2 corepressor complex: a negative regulator of Notch signaling. Structure (London, England : 1993) 2014 imex curation Collins KJ., Yuan Z., Kovall RA. 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 Collins KJ., Yuan Z., Kovall RA. DIP original experiment: DIP-259605X Structure (London, England : 1993) 2014 IMEx Structure and function of the CSL-KyoT2 corepressor complex: a negative regulator of Notch signaling. Structure and function of the CSL-KyoT2 corepressor complex: a negative regulator of Notch signaling. Structure and function of the CSL-KyoT2 corepressor complex: a negative regulator of Notch signaling. Structure (London, England : 1993) 2014 imex curation Collins KJ., Yuan Z., Kovall RA. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Collins KJ., Yuan Z., Kovall RA. DIP original experiment: DIP-259607X Structure (London, England : 1993) 2014 IMEx Structure and function of the CSL-KyoT2 corepressor complex: a negative regulator of Notch signaling. Structure and function of the CSL-KyoT2 corepressor complex: a negative regulator of Notch signaling. Structure and function of the CSL-KyoT2 corepressor complex: a negative regulator of Notch signaling. Structure (London, England : 1993) 2014 imex curation Collins KJ., Yuan Z., Kovall RA. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Collins KJ., Yuan Z., Kovall RA. DIP original experiment: DIP-259606X Structure (London, England : 1993) 2014 IMEx Structure and function of the CSL-KyoT2 corepressor complex: a negative regulator of Notch signaling. Structure and function of the CSL-KyoT2 corepressor complex: a negative regulator of Notch signaling. Structure and function of the CSL-KyoT2 corepressor complex: a negative regulator of Notch signaling. Structure (London, England : 1993) 2014 imex curation Collins KJ., Yuan Z., Kovall RA. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Collins KJ., Yuan Z., Kovall RA. DIP original experiment: DIP-259608X Structure (London, England : 1993) 2014 IMEx Structure and function of the CSL-KyoT2 corepressor complex: a negative regulator of Notch signaling. suh_mouse Recombining binding protein suppressor of hairless Rbpj Igkjrb1 Igkrsbp Rbpsuh J kappa-recombination signal-binding protein RBP-J kappa protein protein mouse Mus musculus Mouse MPSGFPQSPRTSPRARPKTRITGALPMDYSEGLSAEERPAHAPSAGKFGERPPPKRLTREAMRNYLKERGDQTVLILHAKVAQKSYGNEKRFFCPPPCVYLMGSGWKKKKEQMERDGCSEQESQPCAFIGIGNSDQEMQQLNLEGKNYCTAKTLYISDSDKRKHFMLSVKMFYGNSDDIGVFLSKRIKVISKPSKKKQSLKNADLCIASGTKVALFNRLRSQTVSTRYLHVEGGNFHASSQQWGAFYIHLLDDDESEGEEFTVRDGYIHYGQTVKLVCSVTGMALPRLIIRKVDKQTALLDADDPVSQLHKCAFYLKDTERMYLCLSQERIIQFQATPCPKEQNKEMINDGASWTIISTDKAEYTFYEGMGPVLAPVTPVPVVESLQLNGGGDVAMLELTGQNFTPNLRVWFGDVEAETMYRCGESMLCVVPDISAFREGWRWVRQPVQVPVTLVRNDGVIYSTSLTFTYTPEPGPRPHCSAAGAILRANSSQVPSNESNTNSEGNYTNASTNSTSVTSSTATVVS DIP protein P31266 original sequence version: 143 DIP protein P31266 original sequence version: 89 DIP protein P31266-1 original sequence version: 141 8BF517CC24099E03 p97447-2 Four and a half LIM domains protein 1 Fhl1 RBP-associated molecule 14-1 Skeletal muscle LIM-protein 1 KyoT2 KyoT protein protein mouse Mus musculus Mouse MSEKFDCHYCRDPLQGKKYVQKDGRHCCLKCFDKFCANTCVDCRKPISADAKEVHYKNRYWHDNCFRCAKCLHPLASETFVSKDGKILCNKCATREDSPRCKGCFKAIVAGDQNVEYKGTVWHKDCFTCSNCKQVIGTGSFFPKGEDFYCVTCHETKFAKHCVKCNKGLVKAPVWWPMKDNPGTTTASTAKNAP DIP protein P97447-2 original sequence version: 114 fhl1-rbpj-3 1 6 unspecified role unspecified role unspecified role unspecified role Region 168-194 Region 168-194 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 5 unspecified role unspecified role unspecified role unspecified role Region 53-474 Region 53-474 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 fhl1-rbpj-4 2 6 unspecified role unspecified role unspecified role unspecified role Region 168-184 Region 168-184 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain P97447-2:p.[Trp175Ala;Trp176Ala] W175A/W176A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain W A certain certain sequence position certain certain certain sequence position certain W A This feature has been corrected as a result of our quality control procedures. The original label was 'W175A/W176A'. Wed May 02 19:35:00 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'trp175ala,trp176ala' Tue Jun 30 18:25:25 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Trp175Ala;Trp176Ala]' ecolx Escherichia coli 5 unspecified role unspecified role unspecified role unspecified role Region 53-474 Region 53-474 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 fhl1-rbpj-5 3 6 unspecified role unspecified role unspecified role unspecified role Region 168-194 Region 168-194 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 5 unspecified role unspecified role unspecified role unspecified role Region 203-393 Region 203-393 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain P31266:p.Phe261Arg F261R mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain F R This feature has been corrected as a result of our quality control procedures. The original label was 'F261R'. Wed May 02 16:00:48 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe261arg' Tue Jun 30 18:22:16 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe261Arg' P31266:p.Ala284Arg A284R mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain A R This feature has been corrected as a result of our quality control procedures. The original label was 'A284R'. Wed May 02 17:21:30 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ala284arg' Tue Jun 30 16:37:27 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ala284Arg' ecolx Escherichia coli direct interaction direct interaction fhl1-rbpj-6 4 6 unspecified role unspecified role unspecified role unspecified role Region 171-180 Region 171-180 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain in vitro In vitro 5 unspecified role unspecified role unspecified role unspecified role Region 53-474 Region 53-474 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