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 insights into Rhino-mediated germline piRNA cluster formation. Structural insights into Rhino-mediated germline piRNA cluster formation. Cell research 2015 imex curation Yu B., Cassani M., Wang M., Liu M., Ma J., Li G., Zhang Z., Huang Y. huangy@sibcb.ac.cn, zhang@ciwemb.edu 21-Nov-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Yu B., Cassani M., Wang M., Liu M., Ma J., Li G., Zhang Z., Huang Y. huangy@sibcb.ac.cn, zhang@ciwemb.edu Accepted 2019-OCT-10 AT 11:33 BST AT 11:33 BST by PPORRAS Cell research 2015 Only protein-protein interactions imex curation imex curation Structural insights into Rhino-mediated germline piRNA cluster formation. Structural insights into Rhino-mediated germline piRNA cluster formation. Cell research 2015 imex curation Yu B., Cassani M., Wang M., Liu M., Ma J., Li G., Zhang Z., Huang Y. huangy@sibcb.ac.cn, zhang@ciwemb.edu 21-Nov-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Yu B., Cassani M., Wang M., Liu M., Ma J., Li G., Zhang Z., Huang Y. huangy@sibcb.ac.cn, zhang@ciwemb.edu Accepted 2019-OCT-10 AT 11:33 BST AT 11:33 BST by PPORRAS Cell research 2015 Only protein-protein interactions imex curation imex curation cbx5_mouse Chromobox protein homolog 5 Cbx5 Hp1a Heterochromatin protein 1 homolog alpha protein protein mouse Mus musculus Mouse MGKKTKRTADSSSSEDEEEYVVEKVLDRRMVKGQVEYLLKWKGFSEEHNTWEPEKNLDCPELISEFMKKYKKMKEGENNKPREKSEGNKRKSSFSNSADDIKSKKKREQSNDIARGFERGLEPEKIIGATDSCGDLMFLMKWKDTDEADLVLAKEANVKCPQIVIAFYEERLTWHAYPEDAENKEKESAKS DIP protein Q61686 original sequence version: 105 DIP protein Q61686 original sequence version: 91 DIP protein Q61686 original sequence version: 107 8AB87E2F00DB8C40 h31_human Histone H3.1 H3FA H3FL H3FD H3FI H3FH H3FK H3FF H3FJ H3FB Histone H3/a Histone H3/b Histone H3/c Histone H3/d Histone H3/f Histone H3/h Histone H3/i Histone H3/j Histone H3/k Histone H3/l H3C1 HIST1H3A H3C2 HIST1H3B H3C3 H3FC HIST1H3C H3C4 HIST1H3D H3C6 HIST1H3E H3C7 HIST1H3F H3C8 HIST1H3G H3C10 HIST1H3H H3C11 HIST1H3I H3C12 HIST1H3J protein protein human Homo sapiens Human MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA DIP protein P68431 original sequence version: 78 DIP protein P68431 original sequence version: 79 DIP protein P68431 original sequence version: 76 DIP protein P68431 original sequence version: 92 DIP protein P68431 original sequence version: 87 DIP protein P68431 original sequence version: 101 DIP protein P68431 original sequence version: 130 DIP protein P68431 original sequence version: 115 9B89008EA50A0EF6 q7jxa8_drome rhi rhino hp1d Dmel\CG10683 HP1 HP1D HP1d RHI Rhi Rhino rno CG10683 Dmel_CG10683 protein protein drome Drosophila melanogaster (Fruit fly) Fruit fly MSRNHQRPNLGLVDAPPNDHVEEYVVEKILGKRFVNGRPQVLVKWSGFPNENNTWEPLENVGNCMKLVSDFESEVFRLHRKAAAKSVGKSKSSPSSSGPLITENGPSSSKKTQQHSKSVQAKNTAGMSKMNQKKGKNIKKTAGKIKDIENYPKTQMPSTSQVSTDSTEVFDGNPSATTTNMIKSPRIQSLFSDLNLIEPTKDKDVGDTSLKTPPKSRRLIEFPQREDAPLSSKHVSPMLIRKESQPLQSSCTDDSDLGESSSSMSLPTVSSTSSEKSIKVTKSEPKTLGQIKFSSRSSDGGHAASSLGAPKEGDIGLDLSGSDSMDSEVESMRRCPRRKRKKTYPDWKFPEMTKPFGVNRGLDLDKILHCYQMNDDLFMFVTWKGCSSIDAVHINDIKEAYPLQIIKYFESLRIIVPK 8996711F329D4B45 hist1h3a-rhi-1 1 4 unspecified role unspecified role neutral component neutral component purified purified possible N6Me3+Lys-10 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain observed-ptm observed-ptm observed ptm observed-ptm N-terminal tail sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain unknown Unknown 5 unspecified role unspecified role neutral component neutral component purified purified Chromodomain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecobd Escherichia coli (strain B / BL21-DE3) 5 unspecified role unspecified role neutral component neutral component purified purified Chromodomain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecobd Escherichia coli (strain B / BL21-DE3) 4 unspecified role unspecified role neutral component neutral component purified purified N-terminal tail sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain possible N6Me3+Lys-10 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain observed-ptm observed-ptm observed ptm observed-ptm unknown Unknown 11 9 11 13 13 15 direct interaction direct interaction Fig.1A,B,G and H 1.8A Rwork=18.4% Rfree=20.6% hist1h3a-q7jxa8_drome-1 2 4 unspecified role unspecified role neutral component neutral component purified purified possible N6Me3+Lys-10 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain observed-ptm observed-ptm observed ptm observed-ptm N-terminal tail sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain unknown Unknown 5 unspecified role unspecified role neutral component neutral component purified purified Chromodomain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q7JXA8:p.Trp45Ala mutation disrupting mutation disrupting interaction mutation disrupting certain certain sequence position certain certain certain sequence position certain W A Tue Jun 30 17:18:39 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Trp45Ala' Q7JXA8:p.[Phe34Ala;Phe76Ala] mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain F A certain certain sequence position certain certain certain sequence position certain F A The double mutation disrupts a pi-pi interaction between two chromodomains. While the monomeric domains are stable and still bind the histone H2 N-terminal tail, the Kd of the interaction is weakened. Tue Jun 30 16:51:33 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Phe34Ala;Phe76Ala]' Q7JXA8:p.Phe48Ala mutation disrupting mutation disrupting interaction mutation disrupting certain certain sequence position certain certain certain sequence position certain F A Tue Jun 30 19:47:50 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe48Ala' ecobd Escherichia coli (strain B / BL21-DE3) 22 20 direct interaction direct interaction Fig.1C hist1h3a-rhi-2 2 4 unspecified role unspecified role neutral component neutral component purified purified possible N6Me3+Lys-10 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain observed-ptm observed-ptm observed ptm observed-ptm N-terminal tail sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain unknown Unknown 3 unspecified role unspecified role neutral component neutral component purified purified chromodomain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecobd Escherichia coli (strain B / BL21-DE3) 29 31 direct interaction direct interaction Fig.1C, fig.S1A