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 Solution structure of a CUE-ubiquitin complex reveals a conserved mode of ubiquitin binding. Solution structure of a CUE-ubiquitin complex reveals a conserved mode of ubiquitin binding. Cell (0092-8674) 2003 Kang RS., Daniels CM., Francis SA., Shih SC., Salerno WJ., Hicke L., Radhakrishnan I. Virus - Publications including interactions involving viral proteins no in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence Kang RS., Daniels CM., Francis SA., Shih SC., Salerno WJ., Hicke L., Radhakrishnan I. Virus - Publications including interactions involving viral proteins no Cell (0092-8674) 2003 cue2_yeast Ubiquitin-binding protein CUE2 CUE2 YKL090W Coupling of ubiquitin conjugation to ER degradation protein 2 protein protein yeast Saccharomyces cerevisiae Baker's yeast MSMDNNDDHESKLSILMDMFPAISKSKLQVHLLENNNDLDLTIGLLLKENDDKSTVDNELHQLYDMFPQLDCSVIKDQFVINEKSVESTISDLLNYETLQKLKDNQANSPDSVKRNEKKNNWESTNDHIESIIKFTDAPKNIAQEYLAENGFDTVKAIIKIILDYYDKRDFKKDVDTFKVKRSPNTTVRGGRVQSSTGLAHVLKKGKESANVAQESLKRPRSYKHSLDSPQMVELNELVADNRDLKAINHEFLQKCLQFYDGDVVKVLNISSLLIEDDKNITKTWNFDEGFTLTSRDNCKQHLPKFSTPQISRRNEVGNTYKLPLHDKETPEGAVPVINNLFQTYRLDFHGFLPSEAVSTLKLALNKWWSKEVAERELNSHNINSYGSKVQFVSPLIVVTGRGIHSIGGISKVRLQVKSFLEKNHYIFWEESSYFRIEGKKKK 8B7BB872C2BDC734 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 cue2-ubi4 1 3 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 1.0 2 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 1.0 direct interaction direct interaction mint In the xray complex 1otr, P36075 is chain A and P04838 is chain B Resolution