DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Cooperative interaction of transcription termination factors with the RNA polymerase II C-terminal domain. Cooperative interaction of transcription termination factors with the RNA polymerase II C-terminal domain. Nature structural & molecular biology 2010 imex curation Lunde BM., Reichow SL., Kim M., Suh H., Leeper TC., Yang F., Mutschler H., Buratowski S., Meinhart A., Varani G. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Lunde BM., Reichow SL., Kim M., Suh H., Leeper TC., Yang F., Mutschler H., Buratowski S., Meinhart A., Varani G. DIP original experiment: DIP-218346X Nature structural & molecular biology 2010 IMEx Cooperative interaction of transcription termination factors with the RNA polymerase II C-terminal domain. Cooperative interaction of transcription termination factors with the RNA polymerase II C-terminal domain. Cooperative interaction of transcription termination factors with the RNA polymerase II C-terminal domain. Nature structural & molecular biology 2010 imex curation Lunde BM., Reichow SL., Kim M., Suh H., Leeper TC., Yang F., Mutschler H., Buratowski S., Meinhart A., Varani G. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Lunde BM., Reichow SL., Kim M., Suh H., Leeper TC., Yang F., Mutschler H., Buratowski S., Meinhart A., Varani G. DIP original experiment: DIP-218347X Nature structural & molecular biology 2010 IMEx Cooperative interaction of transcription termination factors with the RNA polymerase II C-terminal domain. Cooperative interaction of transcription termination factors with the RNA polymerase II C-terminal domain. Cooperative interaction of transcription termination factors with the RNA polymerase II C-terminal domain. Nature structural & molecular biology 2010 imex curation Lunde BM., Reichow SL., Kim M., Suh H., Leeper TC., Yang F., Mutschler H., Buratowski S., Meinhart A., Varani G. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Lunde BM., Reichow SL., Kim M., Suh H., Leeper TC., Yang F., Mutschler H., Buratowski S., Meinhart A., Varani G. DIP original experiment: DIP-218345X Nature structural & molecular biology 2010 IMEx Cooperative interaction of transcription termination factors with the RNA polymerase II C-terminal domain. Cooperative interaction of transcription termination factors with the RNA polymerase II C-terminal domain. Cooperative interaction of transcription termination factors with the RNA polymerase II C-terminal domain. Nature structural & molecular biology 2010 imex curation Lunde BM., Reichow SL., Kim M., Suh H., Leeper TC., Yang F., Mutschler H., Buratowski S., Meinhart A., Varani G. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Lunde BM., Reichow SL., Kim M., Suh H., Leeper TC., Yang F., Mutschler H., Buratowski S., Meinhart A., Varani G. DIP original experiment: DIP-218348X Nature structural & molecular biology 2010 IMEx Cooperative interaction of transcription termination factors with the RNA polymerase II C-terminal domain. pcf11_yeast Protein PCF11 PCF11 YDR228C YD9934.13C protein 1 of CF I protein protein yeast Saccharomyces cerevisiae Baker's yeast MDHDTEVIVKDFNSILEELTFNSRPIITTLTKLAEENISCAQYFVDAIESRIEKCMPKQKLYAFYALDSICKNVGSPYTIYFSRNLFNLYKRTYLLVDNTTRTKLINMFKLWLNPNDTGLPLFEGSALEKIEQFLIKASALHQKNLQAMLPTPTVPLLLRDIDKLTCLTSERLKNQPNDEKLKMKLLVLSQLKQELKREKLTLNALKQVQMQLRQVFSQDQQVLQERMRYHELQQQQQQQQQQQQQQQQQQQQYHETKDMVGSYTQNSNSAIPLFGNNSDTTNQQNSLSSSLFGNISGVESFQEIEKKKSLNKINNLYASLKAEGLIYTPPKESIVTLYKKLNGHSNYSLDSHEKQLMKNLPKIPLLNDILSDCKAYFATVNIDVLNNPSLQLSEQTLLQENPIVQNNLIHLLYRSKPNKCSVCGKRFGNSESEKLLQNEHLDWHFRINTRIKGSQNTANTGISNSNLNTTTTRKNIQSRNWYLSDSQWAAFKDDEITSTKHKNDYTDPHANKNIDKSALNIHADENDEGSVDNTLGSDRSNELEIRGKYVVVPETSQDMAFKCPICKETVTGVYDEESGEWVWKNTIEVNGKYFHSTCYHETSQNSSKSNSGKVGLDDLKKLVTK 66F91BA9577E82F1 66F91BA9577E82F1 rt103_yeast Regulator of Ty1 transposition protein 103 RTT103 YDR289C protein protein yeast Saccharomyces cerevisiae Baker's yeast MPFSSEQFTTKLNTLEDSQESISSASKWLLLQYRDAPKVAEMWKEYMLRPSVNTRRKLLGLYLMNHVVQQAKGQKIIQFQDSFGKVAAEVLGRINQEFPRDLKKKLSRVVNILKERNIFSKQVVNDIERSLKTESSPVEALVLPQKLKDFAKDYEKLVKMHHNVCAMKMRFDKSSDELDPSSSVYEENFKTISKIGNMAKDIINESILKRESGIHKLQSTLDDEKRHLDEEQNMLSEIEFVLSAKDPSRLNKNVDEDNIIPTYEVGDGDDDDDDGDNDDDDDDDDDDKNYDDRSNDSNYGVTNISTTDKKNEVVEKTDSEHKNSTHNPSDNQFGMKRTHDMIGHDDANDIPEKKVHLDSKTSEDGTFNSEDGHYELDIEGHVGAQTDEGVENSGGVSSSIQDLLSKLAN 08D37739466E3010 08D37739466E3010 ctd-1 C-terminal domain peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) YSPTSPSYSPTSPS ctd-pcf11-1 2 5 unspecified role unspecified role unspecified role unspecified role CTD-interacting domain Region 1-140 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 7 unspecified role unspecified role unspecified role unspecified role in vitro In vitro direct interaction direct interaction ctd-rtt103-2 3 7 unspecified role unspecified role unspecified role unspecified role in vitro In vitro 6 unspecified role unspecified role unspecified role unspecified role CTD-interacting domain Region 1-131 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction ctd-rtt103-3 1 7 unspecified role unspecified role unspecified role unspecified role Fluorescein-label Fluorescein-label fluorescein fluorescein label fluorescein n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal in vitro In vitro 6 unspecified role unspecified role unspecified role unspecified role CTD-interacting domain Region 1-131 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Q05543:p.Arg108Asn R108N mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain R N This feature has been corrected as a result of our quality control procedures. The original label was 'R108N'. Wed May 02 15:02:42 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg108asn' Tue Jun 30 19:06:54 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg108Asn' ecolx Escherichia coli direct interaction direct interaction ctd-pcf11-2 4 5 unspecified role unspecified role unspecified role unspecified role CTD-interacting domain Region 1-140 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 7 unspecified role unspecified role unspecified role unspecified role Fluorescein-label Fluorescein-label fluorescein fluorescein label fluorescein n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal in vitro In vitro direct interaction direct interaction