DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu The FACT Spt16 "peptidase" domain is a histone H3-H4 binding module. The FACT Spt16 "peptidase" domain is a histone H3-H4 binding module. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Stuwe T., Hothorn M., Lejeune E., Rybin V., Bortfeld M., Scheffzek K., Ladurner AG. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Stuwe T., Hothorn M., Lejeune E., Rybin V., Bortfeld M., Scheffzek K., Ladurner AG. DIP original experiment: DIP-111173X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx The FACT Spt16 "peptidase" domain is a histone H3-H4 binding module. The FACT Spt16 "peptidase" domain is a histone H3-H4 binding module. The FACT Spt16 "peptidase" domain is a histone H3-H4 binding module. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Stuwe T., Hothorn M., Lejeune E., Rybin V., Bortfeld M., Scheffzek K., Ladurner AG. Only protein-protein interactions in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati weight identificat confirmation by molecular weight weight identificat Stuwe T., Hothorn M., Lejeune E., Rybin V., Bortfeld M., Scheffzek K., Ladurner AG. DIP original experiment: DIP-111171X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx The FACT Spt16 "peptidase" domain is a histone H3-H4 binding module. The FACT Spt16 "peptidase" domain is a histone H3-H4 binding module. The FACT Spt16 "peptidase" domain is a histone H3-H4 binding module. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Stuwe T., Hothorn M., Lejeune E., Rybin V., Bortfeld M., Scheffzek K., Ladurner AG. Only protein-protein interactions in vitro In vitro pull down pull down weight by staining molecular weight estimation by staining weight by staining Stuwe T., Hothorn M., Lejeune E., Rybin V., Bortfeld M., Scheffzek K., Ladurner AG. DIP original experiment: DIP-111169X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx The FACT Spt16 "peptidase" domain is a histone H3-H4 binding module. The FACT Spt16 "peptidase" domain is a histone H3-H4 binding module. The FACT Spt16 "peptidase" domain is a histone H3-H4 binding module. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Stuwe T., Hothorn M., Lejeune E., Rybin V., Bortfeld M., Scheffzek K., Ladurner AG. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column weight identificat confirmation by molecular weight weight identificat Stuwe T., Hothorn M., Lejeune E., Rybin V., Bortfeld M., Scheffzek K., Ladurner AG. DIP original experiment: DIP-111170X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx The FACT Spt16 "peptidase" domain is a histone H3-H4 binding module. The FACT Spt16 "peptidase" domain is a histone H3-H4 binding module. The FACT Spt16 "peptidase" domain is a histone H3-H4 binding module. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Stuwe T., Hothorn M., Lejeune E., Rybin V., Bortfeld M., Scheffzek K., Ladurner AG. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Stuwe T., Hothorn M., Lejeune E., Rybin V., Bortfeld M., Scheffzek K., Ladurner AG. DIP original experiment: DIP-111172X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx The FACT Spt16 "peptidase" domain is a histone H3-H4 binding module. spt16_schpo FACT complex subunit spt16 spt16 SPBP8B7.19 Facilitates chromatin transcription complex subunit spt16 protein protein schpo Schizosaccharomyces pombe (strain ATCC 38366 / 972) Fission yeast MAEYEIDEITFHKRLGILLTSWKNEEDGKTLFQDCDSILVTVGAHDDTNPYQKSTALHTWLLGYEFPSTLILLEKHRITILTSVNKANMLTKLAETKGAAADVNILKRTKDAEENKKLFEKIIEYIRATNKKVGVFPKDKTQGKFINEWDSIFEPVKSEFNLVDASLGLAKCLAIKDEQELANIKGASRVSVAVMSKYFVDELSTYIDQGKKITHSKFSDQMESLIDNEAFFQTKSLKLGDIDLDQLEWCYTPIIQSGGSYDLKPSAITDDRNLHGDVVLCSLGFRYKSYCSNVGRTYLFDPDSEQQKNYSFLVALQKKLFEYCRDGAVIGDIYTKILGLIRAKRPDLEPNFVRNLGAGIGIEFRESSLLVNAKNPRVLQAGMTLNLSIGFGNLINPHPKNSQSKEYALLLIDTIQITRSDPIVFTDSPKAQGDISYFFGEDDSSLEDGVKPRKPPTRGTATISSHKGKTRSETRDLDDSAEKRRVEHQKQLASRKQAEGLQRFAQGSVPSSGIEKPTVKRFESYKRDSQLPQAIGELRILVDYRAQSIILPIFGRPVPFHISTLKNASKNDEGNFVYLRLNFVSPGQIGGKKDELPFEDPNAQFIRSFTFRSSNNSRMSQVFKDIQDMKKAATKRETERKEFADVIEQDKLIEIKNKRPAHINDVYVRPAIDGKRLPGFIEIHQNGIRYQSPLRSDSHIDLLFSNMKHLFFQPCEGELIVLIHVHLKAPIMVGKRKTQDVQFYREVSDIQFDETGNKKRKYMYGDEDELEQEQEERRRRAQLDREFKSFAEKIAEASEGRIELDIPFRELAFNGVPFRSNVLLQPTTDCLVQLTDTPFTVITLNEIEIAHLERVQFGLKNFDLVFIFQDFRRPPIHINTIPMEQLDNVKEWLDSCDICFYEGPLNLNWTTIMKTVNEDPIAFFEEGGWGFLGAPSDDEGDDSVEEVSEYEASDADPSDEEEEESEEYSEDASEEDGYSESEVEDEESGEDWDELERKARQEDAKHDAFEERPSKKRHR 50AD706DD6C03313 mint Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishement of the nucleosome following the passage of RNA polymerase II 50AD706DD6C03313 h4_drome Histone H4 H4 His4r H4r CG3379 His4:CG31611 CG31611 His4 His4:CG33869 His4:CG33871 His4:CG33873 His4:CG33875 His4:CG33877 His4:CG33879 His4:CG33881 His4:CG33883 His4:CG33885 His4:CG33887 His4:CG33889 His4:CG33891 His4:CG33893 His4:CG33895 His4:CG33897 His4:CG33899 His4:CG33901 His4:CG33903 His4:CG33905 His4:CG33907 His4:CG33909 CG33869 CG33871 CG33873 CG33875 CG33877 CG33879 CG33881 CG33883 CG33885 CG33887 CG33889 CG33891 CG33893 CG33895 CG33897 CG33899 CG33901 CG33903 CG33905 CG33907 CG33909 protein protein drome Drosophila melanogaster (Fruit fly) Fruit fly MTGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG DIP protein P84040 original sequence version: 97 DIP protein P84040 original sequence version: 36 DIP protein P84040 original sequence version: 50 DF3EB26393BD208C h3_drome Histone H3 His3 His3:CG31613 His3:CG33857 His3:CG33860 His3:CG33863 His3:CG33866 CG31613 CG33803 CG33806 CG33809 CG33812 CG33815 CG33818 CG33821 CG33824 CG33827 CG33830 CG33833 CG33836 CG33839 CG33842 CG33845 CG33848 CG33851 CG33854 CG33857 CG33860 CG33863 CG33866 His3:CG33803 His3:CG33806 His3:CG33809 His3:CG33812 His3:CG33815 His3:CG33818 His3:CG33821 His3:CG33824 His3:CG33827 His3:CG33830 His3:CG33833 His3:CG33836 His3:CG33839 His3:CG33842 His3:CG33845 His3:CG33848 His3:CG33851 His3:CG33854 protein protein drome Drosophila melanogaster (Fruit fly) Fruit fly MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA DIP protein P02299 original sequence version: 100 6FD8508EA50A0EEC spt16-his3-1 3 6 unspecified role unspecified role bait bait GST tag GST tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag predetermined featur predetermined feature predetermined featur n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli 7 unspecified role unspecified role prey prey drome Drosophila melanogaster (Fruit fly) Fruit fly 8 unspecified role unspecified role prey prey drome Drosophila melanogaster (Fruit fly) Fruit fly association association his3-his4-1 2 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 7 unspecified role unspecified role unspecified role unspecified role drome Drosophila melanogaster (Fruit fly) Fruit fly 8 unspecified role unspecified role unspecified role unspecified role drome Drosophila melanogaster (Fruit fly) Fruit fly physical association physical association his3-spt16-1 1 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 8 unspecified role unspecified role unspecified role unspecified role binding site 1-38 binding site 1-38 sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain drome Drosophila melanogaster (Fruit fly) Fruit fly physical association physical association his3-his4-2 4 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 7 unspecified role unspecified role unspecified role unspecified role drome Drosophila melanogaster (Fruit fly) Fruit fly 8 unspecified role unspecified role unspecified role unspecified role drome Drosophila melanogaster (Fruit fly) Fruit fly physical association physical association his4-spt16-1 5 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 7 unspecified role unspecified role unspecified role unspecified role binding site 1-35 binding site 1-35 sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain drome Drosophila melanogaster (Fruit fly) Fruit fly physical association physical association