MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it Biophysical characterization of the interaction between FAAP20-UBZ4 domain and Rev1-BRCT domain. Biophysical characterization of the interaction between FAAP20-UBZ4 domain and Rev1-BRCT domain. FEBS letters 2015 imex curation Lim K., Lee MK., Duong PT., Liu D., Sung S., Choi BS. byongseok.choi@kaist.ac.kr 03-Dec-2015: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Lim K., Lee MK., Duong PT., Liu D., Sung S., Choi BS. byongseok.choi@kaist.ac.kr Accepted 2015-NOV-09 AT 14:24 GMT AT 14:24 GMT by LUANA FEBS letters 2015 Only protein-protein interactions imex curation imex curation fap20_human Fanconi anemia core complex-associated protein 20 FANCA-associated protein of 20 kDa Fanconi anemia-associated protein of 20 kDa FP7162 FAAP20 C1orf86 protein protein human Homo sapiens Human MEAARRPRLGLSRRRPRPAGGPSGGRPWFLLGGDERERLWAELLRTVSPELILDHEVPSLPAFPGQEPRCGPEPTEVFTVGPKTFSWTPFPPDLWGPGRSYRLLHGAGGHLESPARSLPQRPAPDPCRAPRVEQQPSVEGAAALRSCPMCQKEFAPRLTQLDVDSHLAQCLAESTEDVTW D8FC889A20AF732F rev1_human DNA repair protein REV1 REV1 REV1L Rev1-like terminal deoxycytidyl transferase Alpha integrin-binding protein 80 protein protein human Homo sapiens Human MRRGGWRKRAENDGWETWGGYMAAKVQKLEEQFRSDAAMQKDGTSSTIFSGVAIYVNGYTDPSAEELRKLMMLHGGQYHVYYSRSKTTHIIATNLPNAKIKELKGEKVIRPEWIVESIKAGRLLSYIPYQLYTKQSSVQKGLSFNPVCRPEDPLPGPSNIAKQLNNRVNHIVKKIETENEVKVNGMNSWNEEDENNDFSFVDLEQTSPGRKQNGIPHPRGSTAIFNGHTPSSNGALKTQDCLVPMVNSVASRLSPAFSQEEDKAEKSSTDFRDCTLQQLQQSTRNTDALRNPHRTNSFSLSPLHSNTKINGAHHSTVQGPSSTKSTSSVSTFSKAAPSVPSKPSDCNFISNFYSHSRLHHISMWKCELTEFVNTLQRQSNGIFPGREKLKKMKTGRSALVVTDTGDMSVLNSPRHQSCIMHVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGTGRAPLRPGANPQLEWQYYQNKILKGKAADIPDSSLWENPDSAQANGIDSVLSRAEIASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILAETKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKIMVRKPGAPVETAKFGGHGICDNIARTVTLDQATDNAKIIGKAMLNMFHTMKLNISDMRGVGIHVNQLVPTNLNPSTCPSRPSVQSSHFPSGSYSVRDVFQVQKAKKSTEEEHKEVFRAAVDLEISSASRTCTFLPPFPAHLPTSPDTNKAESSGKWNGLHTPVSVQSRLNLSIEVPSPSQLDQSVLEALPPDLREQVEQVCAVQQAESHGDKKKEPVNGCNTGILPQPVGTVLLQIPEPQESNSDAGINLIALPAFSQVDPEVFAALPAELQRELKAAYDQRQRQGENSTHQQSASASVPKNPLLHLKAAVKEKKRNKKKKTIGSPKRIQSPLNNKLLNSPAKTLPGACGSPQKLIDGFLKHEGPPAEKPLEELSASTSGVPGLSSLQSDPAGCVRPPAPNLAGAVEFNDVKTLLREWITTISDPMEEDILQVVKYCTDLIEEKDLEKLDLVIKYMKRLMQQSVESVWNMAFDFILDNVQVVLQQTYGSTLKVT mint homomint Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents 010E261D537DBA80 faap20-rev1-1 1 3 unspecified role unspecified role neutral component neutral component purified purified binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain undefined mutation mutation disrupting mutation disrupting interaction mutation disrupting certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain Wed Jul 06 16:31:26 BST 2016 Sequence change details about this feature cannot be ascertained or do not fit with the current version of the referenced protein, so they have been deleted as a result of our quality control procedures. The original label was 'lys104ala_glu106ala' 2 unspecified role unspecified role neutral component neutral component purified purified binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f3 sf3 sf4 sf5 faap20-rev1-2 1 3 unspecified role unspecified role neutral component neutral component purified purified binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 2 unspecified role unspecified role neutral component neutral component purified purified binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain physical association physical association f4 f5 sf5 sf9 We decided to examine the effect of the interaction between UBZ4 and ubiquitin on the BRCT binding to UBZ4. We performed an NMR titration experiment, questioning whether ubiquitin and BRCT compete for the interaction with UBZ4 or if the binding surface of BRCT is separate from the ubiquitin binding site on UBZ4. Unlabeled BRCT was titrated into a 1:2 mixture of 15N-UBZ4 and unlabeled ubiquitin. As shown in Fig. 4A and B, addition of BRCT resulted in peak broadening and CSP in some amide resonances, indicating that BRCT can bind to the UBZ4–ubiquitin complex and that the binding is in the intermediate to fast exchange on the NMR time scale. Moreover, this result did not show the peaks returning to the position of 15N-UBZ4 bound to BRCT, implying that BRCT does not compete with ubiquitin or displace it from a single binding site