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 RNF4 interacts with both SUMO and nucleosomes to promote the DNA damage response. RNF4 interacts with both SUMO and nucleosomes to promote the DNA damage response. EMBO Rep. (1469-221X) 2014 imex curation Groocock L.M., Nie M., Prudden J., Moiani D., Wang T., Cheltsov A., Rambo R.P., Arvai A.S., Hitomi C., Tainer J.A., Luger K., Perry J.J., Lazzerini-Denchi E., Boddy M.N. nboddy@scripps.edu; edenchi@scripps.edu; jjperry@scripps.edu 05-Jan-2015: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro saxs x ray scattering saxs predetermined predetermined participant predetermined Groocock L.M., Nie M., Prudden J., Moiani D., Wang T., Cheltsov A., Rambo R.P., Arvai A.S., Hitomi C., Tainer J.A., Luger K., Perry J.J., Lazzerini-Denchi E., Boddy M.N. nboddy@scripps.edu; edenchi@scripps.edu; jjperry@scripps.edu Accepted 2014-DEC-01 by MARTA EMBO Rep. (1469-221X) 2014 Only protein-protein interactions imex curation RNF4 interacts with both SUMO and nucleosomes to promote the DNA damage response. RNF4 interacts with both SUMO and nucleosomes to promote the DNA damage response. EMBO Rep. (1469-221X) 2014 imex curation Groocock L.M., Nie M., Prudden J., Moiani D., Wang T., Cheltsov A., Rambo R.P., Arvai A.S., Hitomi C., Tainer J.A., Luger K., Perry J.J., Lazzerini-Denchi E., Boddy M.N. nboddy@scripps.edu; edenchi@scripps.edu; jjperry@scripps.edu 05-Jan-2015: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Groocock L.M., Nie M., Prudden J., Moiani D., Wang T., Cheltsov A., Rambo R.P., Arvai A.S., Hitomi C., Tainer J.A., Luger K., Perry J.J., Lazzerini-Denchi E., Boddy M.N. nboddy@scripps.edu; edenchi@scripps.edu; jjperry@scripps.edu Accepted 2014-DEC-01 by MARTA EMBO Rep. (1469-221X) 2014 Only protein-protein interactions imex curation rnf4_human E3 ubiquitin-protein ligase RNF4 SNURF RING finger protein 4 Small nuclear ring finger protein RNF4 RES4-26 RING-type E3 ubiquitin transferase RNF4 protein protein human Homo sapiens Human MSTRKRRGGAINSRQAQKRTREATSTPEISLEAEPIELVETAGDEIVDLTCESLEPVVVDLTHNDSVVIVDERRRPRRNARRLPQDHADSCVVSSDDEELSRDRDVYVTTHTPRNARDEGATGLRPSGTVSCPICMDGYSEIVQNGRLIVSTECGHVFCSQCLRDSLKNANTCPTCRKKINHKRYHPIYI E5E3AE4A9B28CF9D rnf4-2 2 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role unspecified role unspecified role purified purified bindin range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction ST1 rnf4-2 1 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role unspecified role unspecified role purified purified bindin range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction SF2 SF4