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 Structure and function of a HECT domain ubiquitin-binding site. Structure and function of a HECT domain ubiquitin-binding site. EMBO Rep. (1469-221X) 2011 imex curation Kim HC., Steffen AM., Oldham ML., Chen J., Huibregtse JM. 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 Kim HC., Steffen AM., Oldham ML., Chen J., Huibregtse JM. EMBO Rep. (1469-221X) 2011 Only protein-protein interactions imex curation rsp5_yeast E3 ubiquitin-protein ligase RSP5 RSP5 MDP1 NPI1 YER125W SYGP-ORF41 Reverses SPT-phenotype protein 5 HECT-type E3 ubiquitin transferase RSP5 protein protein yeast Saccharomyces cerevisiae Baker's yeast MPSSISVKLVAAESLYKRDVFRSPDPFAVLTIDGYQTKSTSAAKKTLNPYWNETFKFDDINENSILTIQVFDQKKFKKKDQGFLGVVNVRVGDVLGHLDEDTATSSGRPREETITRDLKKSNDGMAVSGRLIVVLSKLPSSSPHSQAPSGHTASSSTNTSSTTRTNGHSTSSTRNHSTSHPSRGTAQAVESTLQSGTTAATNTATTSHRSTNSTSSATRQYSSFEDQYGRLPPGWERRTDNFGRTYYVDHNTRTTTWKRPTLDQTEAERGNQLNANTELERRQHRGRTLPGGSSDNSSVTVQVGGGSNIPPVNGAAAAAFAATGGTTSGLGELPSGWEQRFTPEGRAYFVDHNTRTTTWVDPRRQQYIRTYGPTNTTIQQQPVSQLGPLPSGWEMRLTNTARVYFVDHNTKTTTWDDPRLPSSLDQNVPQYKRDFRRKVIYFRSQPALRILPGQCHIKVRRKNIFEDAYQEIMRQTPEDLKKRLMIKFDGEEGLDYGGVSREFFFLLSHEMFNPFYCLFEYSAYDNYTIQINPNSGINPEHLNYFKFIGRVVGLGVFHRRFLDAFFVGALYKMMLRKKVVLQDMEGVDAEVYNSLNWMLENSIDGVLDLTFSADDERFGEVVTVDLKPDGRNIEVTDGNKKEYVELYTQWRIVDRVQEQFKAFMDGFNELIPEDLVTVFDERELELLIGGIAEIDIEDWKKHTDYRGYQESDEVIQWFWKCVSEWDNEQRARLLQFTTGTSRIPVNGFKDLQGSDGPRRFTIEKAGEVQQLPKSHTCFNRVDLPQYVDYDSMKQKLTLAVEETIGFGQE 6F1836384479E70F 6F1836384479E70F ubi4p_yeast Polyubiquitin UBI4 SCD2 YLL039C protein protein yeast Saccharomyces cerevisiae Baker's yeast MQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGN Protein modifier which can be covalently attached to target lysines either as a monomer or as a lysine-linked polymer. Attachment to proteins as a Lys-48-linked polymer usually leads to their degradation by proteasome. Attachment to proteins as a monomer or as an alternatively linked polymer does not lead to proteasomal degradation and may be required for numerous functions, including maintenance of chromatin structure, regulation of gene expression, stress response, ribosome biogenesis and DNA repair mint 68C6235F9909A2AE rsp5-ubi4 1 ubiquitin 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain RSP5 2 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction homomint domino mint The Protein Data Bank code for this structure is 3OLM. t1 f1 sf1