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/ Methylation-independent binding to histone H3 and cell cycle-dependent incorporation of HP1beta into heterochromatin. Methylation-independent binding to histone H3 and cell cycle-dependent incorporation of HP1beta into heterochromatin. J. Biol. Chem. (0021-9258) 2006 imex curation Dialynas GK., Makatsori D., Kourmouli N., Theodoropoulos PA., McLean K., Terjung S., Singh PB., Georgatos SD. Chromatin - Epigenetic interactions resulting in chromatin modulation BioCreative - Critical Assessment of Information Extraction systems in Biology sgeorgat@cc.uoi.gr 24-JAN-2007: Contacted by JYOTI. Only protein-protein interactions in vitro In vitro pull down pull down ms participant Identification by mass spectrometry ms participant Dialynas GK., Makatsori D., Kourmouli N., Theodoropoulos PA., McLean K., Terjung S., Singh PB., Georgatos SD. Chromatin - Epigenetic interactions resulting in chromatin modulation sgeorgat@cc.uoi.gr Accepted 2006-SEP-18 by ORCHARD. 24-JAN-2007: Contacted by JYOTI. J. Biol. Chem. (0021-9258) 2006 Only protein-protein interactions imex curation Methylation-independent binding to histone H3 and cell cycle-dependent incorporation of HP1beta into heterochromatin. Methylation-independent binding to histone H3 and cell cycle-dependent incorporation of HP1beta into heterochromatin. J. Biol. Chem. (0021-9258) 2006 imex curation Dialynas GK., Makatsori D., Kourmouli N., Theodoropoulos PA., McLean K., Terjung S., Singh PB., Georgatos SD. Chromatin - Epigenetic interactions resulting in chromatin modulation BioCreative - Critical Assessment of Information Extraction systems in Biology sgeorgat@cc.uoi.gr 24-JAN-2007: Contacted by JYOTI. Only protein-protein interactions in vitro In vitro pull down pull down western blot western blot Immuno blot Immuno blot Dialynas GK., Makatsori D., Kourmouli N., Theodoropoulos PA., McLean K., Terjung S., Singh PB., Georgatos SD. Chromatin - Epigenetic interactions resulting in chromatin modulation sgeorgat@cc.uoi.gr Accepted 2006-SEP-18 by ORCHARD. J. Biol. Chem. (0021-9258) 2006 Only protein-protein interactions imex curation cbx1_mouse Chromobox protein homolog 1 Cbx1 Cbx Heterochromatin protein 1 homolog beta Modifier 1 protein M31 Heterochromatin protein p25 protein protein mouse Mus musculus Mouse MGKKQNKKKVEEVLEEEEEEYVVEKVLDRRVVKGKVEYLLKWKGFSDEDNTWEPEENLDCPDLIAEFLQSQKTAHETDKSEGGKRKADSDSEDKGEESKPKKKKEESEKPRGFARGLEPERIIGATDSSGELMFLMKWKNSDEADLVPAKEANVKCPQVVISFYEERLTWHSYPSEDDDKKDDKN DIP protein P83917 original sequence version: 93 BE687AF9C66E48E3 h31_mouse Histone H3.1 H3c1 H3c10 H3c11 H3c8 H3.1-221 H3.1-291 H3.1-I H3a H3g H3h H3i Hist1h3a Hist1h3g Hist1h3h Hist1h3i protein protein mouse Mus musculus Mouse MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA 9B89008EA50A0EF6 h3_peptide_31-41 consensus H3 peptide AA 31- 41 peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) STGGVKKPHRY An amino acid sequence which is not represented in UniProt Region of the peptide corresponding to the AA 31-41. Similar to P84244 Similar to P84243 379F4328633322C8 cbx1-h3-2 2 5 unspecified role unspecified role prey prey chemical synthesis Chemical synthesis (Chemical synthesis) 3 unspecified role unspecified role bait bait region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) direct interaction direct interaction 1D tail" peptides that represented either the non-modified or the me3K9-modified NH2-terminal region of H3 exhibited marginal binding to HP1beta at 0.3 M salt and did not compete with the full-length protein, even at a 200 molar excess. Marginal binding observed. Cbx1_mouse was chosen as the interacting protein as indicated from authors previous studies. The CBX1 proteins share 100% identity between mouse and human. cbx1-h3-3 2 4 unspecified role unspecified role prey prey ecoli Escherichia coli (strain K12) 3 unspecified role unspecified role bait bait region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) direct interaction direct interaction 1A, B, C, D tail" peptides that represented either the non-modified or the me3K9-modified NH2-terminal region of H3 exhibited marginal binding to HP1beta at 0.3 M salt and did not compete with the full-length protein, even at a 200 molar excess. Strong binding observed even at a high ionic strength of 0.75 M NaCl. Interaction is independent of RNA or DNA. Cbx1_mouse was chosen as the interacting protein as indicated from authors previous studies. The CBX1 proteins share 100% identity between mouse and human. The source of recombinant H3 is not mentioned in the paper however 100% identity between the sequence in Fig1F and the following was observed: H3_ONCMY, H31_MOUSE, H32_MOUSE, H3_CHITH, H3_CAIMO , H32_BOVIN, H3_PORAF, H3_DROHY, H3_MORAP, H3_PLADU, H31_HUMAN, H3_TIGCA, H3_DROME, H3_URECA, H31_CHICK, H3_ICTBU, H31_BOVIN, Tail H3 peptide did not compete out this binding. cbx1-h3-4 1 4 unspecified role unspecified role prey prey histone fold sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 3 unspecified role unspecified role bait bait region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) direct interaction direct interaction 1E, F this fragment can be assigned to the stretch extending between amino acids 40-129, i.e. the so-called "histone fold" domain. Thus, at least under in vitro conditions, HP1beta has the capacity to bind histone H3 independently of post-translational modifications, associating primarily with the central, helical part of the molecule. Cbx1_mouse was chosen as the interacting protein as indicated from authors previous studies. The CBX1 proteins share 100% identity between mouse and human. The source of recombinant H3 is not mentioned in the paper however 100% identity between the sequence in Fig 1F andthe following was observed: H3_ONCMY, H31_MOUSE, H32_MOUSE, H3_CHITH, H3_CAIMO , H32_BOVIN, H3_PORAF, H3_DROHY, H3_MORAP, H3_PLADU, H31_HUMAN, H3_TIGCA, H3_DROME, H3_URECA, H31_CHICK, H3_ICTBU, H31_BOVIN