DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Crystal structure of a conserved N-terminal domain of histone deacetylase 4 reveals functional insights into glutamine-rich domains. Crystal structure of a conserved N-terminal domain of histone deacetylase 4 reveals functional insights into glutamine-rich domains. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Guo L., Han A., Bates DL., Cao J., Chen L. Only protein-protein interactions ecolx Escherichia coli light scattering light scattering predetermined predetermined participant predetermined Guo L., Han A., Bates DL., Cao J., Chen L. DIP original experiment: DIP-261168X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx Crystal structure of a conserved N-terminal domain of histone deacetylase 4 reveals functional insights into glutamine-rich domains. Crystal structure of a conserved N-terminal domain of histone deacetylase 4 reveals functional insights into glutamine-rich domains. Crystal structure of a conserved N-terminal domain of histone deacetylase 4 reveals functional insights into glutamine-rich domains. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Guo L., Han A., Bates DL., Cao J., Chen L. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Guo L., Han A., Bates DL., Cao J., Chen L. DIP original experiment: DIP-261167X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx Crystal structure of a conserved N-terminal domain of histone deacetylase 4 reveals functional insights into glutamine-rich domains. Crystal structure of a conserved N-terminal domain of histone deacetylase 4 reveals functional insights into glutamine-rich domains. Crystal structure of a conserved N-terminal domain of histone deacetylase 4 reveals functional insights into glutamine-rich domains. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Guo L., Han A., Bates DL., Cao J., Chen L. Only protein-protein interactions ecolx Escherichia coli crosslink cross-linking study crosslink predetermined predetermined participant predetermined Guo L., Han A., Bates DL., Cao J., Chen L. DIP original experiment: DIP-261170X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx Crystal structure of a conserved N-terminal domain of histone deacetylase 4 reveals functional insights into glutamine-rich domains. Crystal structure of a conserved N-terminal domain of histone deacetylase 4 reveals functional insights into glutamine-rich domains. Crystal structure of a conserved N-terminal domain of histone deacetylase 4 reveals functional insights into glutamine-rich domains. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Guo L., Han A., Bates DL., Cao J., Chen L. 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 Guo L., Han A., Bates DL., Cao J., Chen L. DIP original experiment: DIP-261169X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx Crystal structure of a conserved N-terminal domain of histone deacetylase 4 reveals functional insights into glutamine-rich domains. hdac4_human Histone deacetylase 4 HDAC4 KIAA0288 protein protein human Homo sapiens Human MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL DIP protein P56524 original sequence version: 158 DIP protein P56524 original sequence version: 149 DIP protein P56524 original sequence version: 151 BB7FD37652D12398 hdac4-1 2 5 unspecified role unspecified role unspecified role unspecified role Region 62-153 Region 62-153 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 hdac4-4 3 5 unspecified role unspecified role unspecified role unspecified role Region 62-153 Region 62-153 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 hdac4-5 1 5 unspecified role unspecified role unspecified role unspecified role Region 62-153 Region 62-153 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P56524:p.His97Phe H97F mutation increasing strength mutation increasing interaction strength mutation increasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain H F This feature has been corrected as a result of our quality control procedures. The original label was 'H97F'. Wed May 02 17:10:01 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'his97phe' Tue Jun 30 18:10:49 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.His97Phe' P56524:p.Phe93Asp F93D mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain F D This feature has been corrected as a result of our quality control procedures. The original label was 'F93D'. Wed May 02 19:57:53 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe93asp' Tue Jun 30 19:08:23 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe93Asp' ecolx Escherichia coli direct interaction direct interaction hdac4-6 4 5 unspecified role unspecified role unspecified role unspecified role Region 62-153 Region 62-153 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P56524:p.His97Phe H97F mutation increasing strength mutation increasing interaction strength mutation increasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain H F This feature has been corrected as a result of our quality control procedures. The original label was 'H97F'. Wed May 02 16:35:36 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'his97phe' Tue Jun 30 15:57:57 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.His97Phe' P56524:p.Phe93Asp F93D mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain F D This feature has been corrected as a result of our quality control procedures. The original label was 'F93D'. Wed May 02 16:02:52 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe93asp' Tue Jun 30 19:49:43 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe93Asp' ecolx Escherichia coli direct interaction direct interaction