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 Subcellular localization of Daxx determines its opposing functions in ischemic cell death. Subcellular localization of Daxx determines its opposing functions in ischemic cell death. FEBS Lett. (0014-5793) 2007 imex curation Jung YS., Kim HY., Lee YJ., Kim E. 2009-01-08 Only protein-protein interactions rat-h9c2 h9c2 rat myoblasts h9c2 h9c2 rat myoblasts imaging technique imaging technique microscopy experimental particp experimental participant identification experimental particp Jung YS., Kim HY., Lee YJ., Kim E. FEBS Lett. (0014-5793) 2007 2009-01-08 Only protein-protein interactions imex curation p53_rat Cellular tumor antigen p53 Tp53 P53 Tumor suppressor p53 protein protein rat Rattus norvegicus (Rat) Rat MEDSQSDMSIELPLSQETFSCLWKLLPPDDILPTTATGSPNSMEDLFLPQDVAELLEGPEEALQVSAPAAQEPGTEAPAPVAPASATPWPLSSSVPSQKTYQGNYGFHLGFLQSGTAKSVMCTYSISLNKLFCQLAKTCPVQLWVTSTPPPGTRVRAMAIYKKSQHMTEVVRRCPHHERCSDGDGLAPPQHLIRVEGNPYAEYLDDRQTFRHSVVVPYEPPEVGSDYTTIHYKYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRDSFEVRVCACPGRDRRTEEENFRKKEEHCPELPPGSAKRALPTSTSSSPQQKKKPLDGEYFTLKIRGRERFEMFRELNEALELKDARAAEESGDSRAHSSYPKTKKGQSTSRHKKPMIKKVGPDSD DIP protein P10361 original sequence version: 135 E62522313A5C872F sumo1_rat Small ubiquitin-related modifier 1 Sumo1 protein protein rat Rattus norvegicus (Rat) Rat MSDQEAKPSTEDLGDKKEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRIADNHTPKELGMEEEDVIEVYQEQTGGHSTV DIP protein Q5I0H3 original sequence version: 67 DIP protein Q5I0H3 original sequence version: 28 DIP protein Q5I0H3 original sequence version: 65 mint Ubiquitin-like protein which can be covalently attached to target lysines as a monomer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process. Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalent attachment to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4 89BE97D2D054FB33 daxx_rat Death domain-associated protein 6 Daxx Daxx protein protein rat Rattus norvegicus (Rat) Rat MATDDSIIVLDDDDEDEAAAQPGPSNPASNPVSPGPEASGPSESHGDGGSSNSGSRKCYKLENEKLFEEFLELCKMQTSDHPEVVPFLHKLQQRAQSAFLASAEFRNILSRVLSRSRNRPAKLYVYINELCTVLKAHSIKKKLNLAPAASAESSGDNPPTDPPSDLTNTETTASEASRTRGSRRQIQRLEQLLALYVAEIQRLQEKELDLSELDDPDSSYLQEARLKRKLIRLFGRLCDLKDCSSLTGKVIEQRIPYRGTRYPEVNRRIERLINKPGPDTFPDYGDVLRAVEKAATRHSLGLPRQQLQLLAQDAFRDVGVRLQERRHLDLIYNFGCHLTDDYRPGVDPALTDPTLARRLRENRTLAMSRLDEVISKYAMMQDKSEEGERQKRRARLLATSQSSDLPKASSDSGEGPSGVASQEDPTTPKAETEDEEDDEESDDEEEEEEEEEEEATEDEDEDLEQLQEDQDDEEEEEGDNEDDKSPASPSPIFRRKEFSNPQKGSGPQEEQQERGLTGTPASPLEASPGLPSTDAESSGEQLQERLLAGESPVSQLSELDMEALPEETIPSPEERGISSSRRKSDSSLPTILENGAAMVTSTSFNGRVSSHPCRDASPPSKRFRKEKKQLGPGPLGNSYVKKQTMAQQDSGWKISVLSTPSSPLASVGPVADSSTRVDSPSHELVTSSLCNPSPSLILQTPQSQSPRPCIYKTSVATQCDPEEIIVLSDSD Proposed to mediate activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Down-regulates basal and activated transcription. Seems to act as a transcriptional co-repressor and inhibits PAX3 and ETS1 through direct protein-protein interaction. Modulates PAX5 activity. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively mint homomint 17EEBAAB5AA73157 daxx-tp53-6 1 P53 2 experimental particp experimental participant identification experimental particp predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell Daxx 4 experimental particp experimental participant identification experimental particp predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell colocalization colocalization F2B FEBS-Letters homomint mint daxx-sumo1 1 Daxx 4 experimental particp experimental participant identification experimental particp predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell Sumo1 3 experimental particp experimental participant identification experimental particp predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell colocalization colocalization F2C FEBS-Letters homomint mint