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 basis for recognition of H3K56-acetylated histone H3-H4 by the chaperone Rtt106. Structural basis for recognition of H3K56-acetylated histone H3-H4 by the chaperone Rtt106. Nature 2012 imex curation Su D., Hu Q., Li Q., Thompson JR., Cui G., Fazly A., Davies BA., Botuyan MV., Zhang Z., Mer G. Only protein-protein interactions ecolx Escherichia coli nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Su D., Hu Q., Li Q., Thompson JR., Cui G., Fazly A., Davies BA., Botuyan MV., Zhang Z., Mer G. DIP original experiment: DIP-249433X Nature 2012 IMEx Structural basis for recognition of H3K56-acetylated histone H3-H4 by the chaperone Rtt106. Structural basis for recognition of H3K56-acetylated histone H3-H4 by the chaperone Rtt106. Structural basis for recognition of H3K56-acetylated histone H3-H4 by the chaperone Rtt106. Nature 2012 imex curation Su D., Hu Q., Li Q., Thompson JR., Cui G., Fazly A., Davies BA., Botuyan MV., Zhang Z., Mer G. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Su D., Hu Q., Li Q., Thompson JR., Cui G., Fazly A., Davies BA., Botuyan MV., Zhang Z., Mer G. DIP original experiment: DIP-249431X Nature 2012 IMEx Structural basis for recognition of H3K56-acetylated histone H3-H4 by the chaperone Rtt106. Structural basis for recognition of H3K56-acetylated histone H3-H4 by the chaperone Rtt106. Structural basis for recognition of H3K56-acetylated histone H3-H4 by the chaperone Rtt106. Nature 2012 imex curation Su D., Hu Q., Li Q., Thompson JR., Cui G., Fazly A., Davies BA., Botuyan MV., Zhang Z., Mer G. Only protein-protein interactions yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast tap tandem affinity purification TAP TAP tap western blot western blot Immuno blot Immuno blot Su D., Hu Q., Li Q., Thompson JR., Cui G., Fazly A., Davies BA., Botuyan MV., Zhang Z., Mer G. DIP original experiment: DIP-249434X Nature 2012 IMEx Structural basis for recognition of H3K56-acetylated histone H3-H4 by the chaperone Rtt106. Structural basis for recognition of H3K56-acetylated histone H3-H4 by the chaperone Rtt106. Structural basis for recognition of H3K56-acetylated histone H3-H4 by the chaperone Rtt106. Nature 2012 imex curation Su D., Hu Q., Li Q., Thompson JR., Cui G., Fazly A., Davies BA., Botuyan MV., Zhang Z., Mer G. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Su D., Hu Q., Li Q., Thompson JR., Cui G., Fazly A., Davies BA., Botuyan MV., Zhang Z., Mer G. DIP original experiment: DIP-249435X Nature 2012 IMEx Structural basis for recognition of H3K56-acetylated histone H3-H4 by the chaperone Rtt106. Structural basis for recognition of H3K56-acetylated histone H3-H4 by the chaperone Rtt106. Structural basis for recognition of H3K56-acetylated histone H3-H4 by the chaperone Rtt106. Nature 2012 imex curation Su D., Hu Q., Li Q., Thompson JR., Cui G., Fazly A., Davies BA., Botuyan MV., Zhang Z., Mer G. Only protein-protein interactions ecolx Escherichia coli ms of complexes mass spectrometry studies of complexes ms of complexes predetermined predetermined participant predetermined Su D., Hu Q., Li Q., Thompson JR., Cui G., Fazly A., Davies BA., Botuyan MV., Zhang Z., Mer G. DIP original experiment: DIP-249432X Nature 2012 IMEx Structural basis for recognition of H3K56-acetylated histone H3-H4 by the chaperone Rtt106. h3_yeast Histone H3 SIN2 YNL031C N2749 HHT1 YBR010W YBR0201 HHT2 protein protein yeast Saccharomyces cerevisiae Baker's yeast MARTKQTARKSTGGKAPRKQLASKAARKSAPSTGGVKKPHRYKPGTVALREIRRFQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAIGALQESVEAYLVSLFEDTNLAAIHAKRVTIQKKDIKLARRLRGERS A6115FEB480AC67A A6115FEB480AC67A rt106_yeast Histone chaperone RTT106 Regulator of Ty1 transposition protein 106 YNL206C N1346 RTT106 protein protein yeast Saccharomyces cerevisiae Baker's yeast MSKLFLDELPESLSRKIGTVVRVLPSSLEIFEELYKYALNENSNDRSGRHKKPRIDVSSDLLKTDEISETNTIFKLEGVSVLSPLRKKLDLVFYLSNVDGSPVITLLKGNDRELSIYQLNKNIKMASFLPVPEKPNLIYLFMTYTSCEDNKFSEPVVMTLNKENTLNQFKNLGLLDSNVTDFEKCVEYIRKQAILTGFKISNPFVNSTLVDTDAEKINSFHLQCHRGTKEGTLYFLPDHIIFGFKKPILLFDASDIESITYSSITRLTFNASLVTKDGEKYEFSMIDQTEYAKIDDYVKRKQMKDKSMSEELKAKSKSKGQATDGTADQPSILQEATRQMQDEKKAGVFSDDDEENDQNFEAESDLSDGSGQESSDGAEDGEEAEEDDEEDDEEEDKKGQSALNRDNSFASINGQPEQELQYKEFKEPLELEDIPIEIDNDDDEDDEDGSGVEYD 79CACA659A7F4F4D 79CACA659A7F4F4D rtt106-h3-1 3 6 unspecified role unspecified role prey prey yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 7 unspecified role unspecified role bait bait TAP-tag TAP-tag tandem tag tandem tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range P40161:p.Ile259Ala I259A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain I A This feature has been corrected as a result of our quality control procedures. The original label was 'I259A'. Wed May 02 17:02:29 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile259ala' Tue Jun 30 16:29:42 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile259Ala' P40161:p.Gln288Ala Q288A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain Q A This feature has been corrected as a result of our quality control procedures. The original label was 'Q288A'. Wed May 02 15:56:23 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gln288ala' Tue Jun 30 19:10:23 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gln288Ala' P40161:p.Tyr261Ala Y261A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain Y A This feature has been corrected as a result of our quality control procedures. The original label was 'Y261A'. Wed May 02 18:36:32 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr261ala' Tue Jun 30 16:01:41 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr261Ala' P40161:p.Phe269Ala F269A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain F A This feature has been corrected as a result of our quality control procedures. The original label was 'F269A'. Wed May 02 19:02:05 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe269ala' Tue Jun 30 20:19:37 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe269Ala' P40161:p.Tyr291Ala Y291A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain Y A This feature has been corrected as a result of our quality control procedures. The original label was 'Y291A'. Wed May 02 19:06:54 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr291ala' Tue Jun 30 18:20:04 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr291Ala' P40161:p.Ile294Ala I294A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain I A This feature has been corrected as a result of our quality control procedures. The original label was 'I294A'. Wed May 02 17:00:37 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile294ala' Tue Jun 30 16:35:40 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile294Ala' yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast physical association physical association rtt106-1 2 7 unspecified role unspecified role unspecified role unspecified role Region 1-67 Region 1-67 required to bind necessary binding region required to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain Region 1-301 Region 1-301 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 rtt106-2 5 7 unspecified role unspecified role unspecified role unspecified role Region 1-301 Region 1-301 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 rtt106-3 1 7 unspecified role unspecified role unspecified role unspecified role Region 1-67 Region 1-67 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 h3-rtt106-1 4 6 unspecified role unspecified role unspecified role unspecified role Region 52-62 Region 52-62 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain K57ace K57ace naclys N-acetylated L-lysine NAcLys certain certain sequence position certain certain certain sequence position certain in vitro In vitro 7 unspecified role unspecified role unspecified role unspecified role Region 68-301 Region 68-301 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P40161:p.Ile259Ala I259A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain I A This feature has been corrected as a result of our quality control procedures. The original label was 'I259A'. Wed May 02 15:40:57 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile259ala' Tue Jun 30 16:11:58 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile259Ala' P40161:p.Tyr291Ala Y291A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain Y A This feature has been corrected as a result of our quality control procedures. The original label was 'Y291A'. Wed May 02 20:13:42 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr291ala' Tue Jun 30 18:27:17 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr291Ala' P40161:p.Ile294Ala I294A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain I A This feature has been corrected as a result of our quality control procedures. The original label was 'I294A'. Wed May 02 15:02:03 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile294ala' Tue Jun 30 20:11:08 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile294Ala' P40161:p.Tyr297Ala Y297A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain Y A This feature has been corrected as a result of our quality control procedures. The original label was 'Y297A'. Wed May 02 15:09:55 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr297ala' Tue Jun 30 17:55:21 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr297Ala' P40161:p.Asp295Ala D295A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain D A This feature has been corrected as a result of our quality control procedures. The original label was 'D295A'. Wed May 02 17:10:02 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp295ala' Tue Jun 30 18:26:42 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp295Ala' ecolx Escherichia coli direct interaction direct interaction