DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ agez-2007-1 in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Agez M., Chen J., Guerois R., van Heijenoort C., Thuret JY., Mann C., Ochsenbein F. DIP original experiment: DIP-66724X Structure (London, England : 1993) 2007 IMEx Structure of the histone chaperone ASF1 bound to the histone H3 C-terminal helix and functional insights. Agez M., Chen J., Guerois R., van Heijenoort C., Thuret JY., Mann C., Ochsenbein F. Only protein-protein interactions imex curation h3-1 Histone 3 [fragment] GAMGKDIQLARRIRGERA peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) GAMGKDIQLARRIRGERA asf1a_human Histone chaperone ASF1A Anti-silencing function protein 1 homolog A CCG1-interacting factor A ASF1A CGI-98 HSPC146 protein protein human Homo sapiens Human MAKVQVNNVVVLDNPSPFYNPFQFEITFECIEDLSEDLEWKIIYVGSAESEEYDQVLDSVLVGPVPAGRHMFVFQADAPNPGLIPDADAVGVTVVLITCTYRGQEFIRVGYYVNNEYTETELRENPPVKPDFSKLQRNILASNPRVTRFHINWEDNTEKLEDAESSNPNLQSLLSTDALPSASKGWSTSENSLNVMLESHMDCM This sequence has been withdrawn from Uniprot. asf1a-h3-1 3152929 N/A 3152930 unspecified role unspecified role unspecified role unspecified role in vitro In vitro N/A 3152931 unspecified role unspecified role unspecified role unspecified role Region 1-156 Region 1-156 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false