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 http://mint.bio.uniroma2.it/mint jeanclos-2001-2 The chaperone protein 14-3-3eta interacts with the nicotinic acetylcholine receptor alpha 4 subunit. Evidence for a dynamic role in subunit stabilization. in vivo in vivo coip coimmunoprecipitation co-immunoprecipitation CoIp immunoprecipitation Co-IP co-immunoprecipitation CoIp immunoprecipitation Co-IP coip predetermined predetermined participant predetermined Jeanclos EM., Lin L., Treuil MW., Rao J., DeCoster MA., Anand R. J. Biol. Chem. (0021-9258) 2001 partial coverage rapid curation rapid curation jeanclos-2001-1 The chaperone protein 14-3-3eta interacts with the nicotinic acetylcholine receptor alpha 4 subunit. Evidence for a dynamic role in subunit stabilization. in vivo in vivo 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid predetermined predetermined participant predetermined Jeanclos EM., Lin L., Treuil MW., Rao J., DeCoster MA., Anand R. J. Biol. Chem. (0021-9258) 2001 partial coverage rapid curation rapid curation jeanclos-2001-3 The chaperone protein 14-3-3eta interacts with the nicotinic acetylcholine receptor alpha 4 subunit. Evidence for a dynamic role in subunit stabilization. in vivo in vivo imaging technique imaging technique microscopy predetermined predetermined participant predetermined Jeanclos EM., Lin L., Treuil MW., Rao J., DeCoster MA., Anand R. J. Biol. Chem. (0021-9258) 2001 partial coverage rapid curation rapid curation jeanclos-2001-4 The chaperone protein 14-3-3eta interacts with the nicotinic acetylcholine receptor alpha 4 subunit. Evidence for a dynamic role in subunit stabilization. unknown Unknown pull down pull down predetermined predetermined participant predetermined Jeanclos EM., Lin L., Treuil MW., Rao J., DeCoster MA., Anand R. J. Biol. Chem. (0021-9258) 2001 partial coverage rapid curation rapid curation acha4_rat Neuronal acetylcholine receptor subunit alpha-4 Chrna4 Acra4 protein protein rat Rattus norvegicus (Rat) Rat MANSGTGAPPPLLLLPLLLLLGTGLLPASSHIETRAHAEERLLKRLFSGYNKWSRPVANISDVVLVRFGLSIAQLIDVDEKNQMMTTNVWVKQEWHDYKLRWDPGDYENVTSIRIPSELIWRPDIVLYNNADGDFAVTHLTKAHLFYDGRVQWTPPAIYKSSCSIDVTFFPFDQQNCTMKFGSWTYDKAKIDLVSMHSRVDQLDFWESGEWVIVDAVGTYNTRKYECCAEIYPDITYAFIIRRLPLFYTINLIIPCLLISCLTVLVFYLPSECGEKVTLCISVLLSLTVFLLLITEIIPSPTSLVIPLIGEYLLFTMIFVTLSIVITVFVLNVHHRSPRTHTMPAWVRRVFLDIVPRLLFMKRPSVVKDNCRRLIESMHKMANAPRFWPEPVGEPGILSDICNQGLSPAPTFCNPTDTAVETQPTCRSPPLEVPDLKTSEVEKASPCPSPGSCPPPKSSSGAPMLIKARSLSVQHVPSSQEAAEDGIRCRSRSIQYCVSQDGAASLADSKPTSSPTSLKARPSQLPVSDQASPCKCTCKEPSPVSPVTVLKAGGTKAPPQHLPLSPALTRAVEGVQYIADHLKAEDTDFSVKEDWKYVAMVIDRIFLWMFIIVCLLGTVGLFLPPWLAAC mint After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane 1433f_mouse 14-3-3 protein eta Ywhah protein protein mouse Mus musculus Mouse MGDREQLLQRARLAEQAERYDDMASAMKAVTELNEPLSNEDRNLLSVAYKNVVGARRSSWRVISSIEQKTMADGNEKKLEKVKAYREKIEKELETVCNDVLALLDKFLIKNCNDFQYESKVFYLKMKGDYYRYLAEVASGEKKNSVVEASEAAYKEAFEISKEHMQPTHPIRLGLALNFSVFYYEIQNAPEQACLLAKQAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQDEEAGEGN 1433f_human 14-3-3 protein eta YWHAH YWHA1 Protein AS1 protein protein human Homo sapiens Human MGDREQLLQRARLAEQAERYDDMASAMKAVTELNEPLSNEDRNLLSVAYKNVVGARRSSWRVISSIEQKTMADGNEKKLEKVKAYREKIEKELETVCNDVLSLLDKFLIKNCNDFQYESKVFYLKMKGDYYRYLAEVASGEKKNSVVEASEAAYKEAFEISKEQMQPTHPIRLGLALNFSVFYYEIQNAPEQACLLAKQAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQDEEAGEGN chrna4-ywhah-1 5478 acha4_rat 5482 unspecified role unspecified role bait bait over-expressed over expressed level over-expressed phosphoserine o-phospho-serine opser O-phospho-L-serine (2S)-2-amino-3-(phosphonooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)propanoic acid ACT_SITE Phosphoserine intermediate MOD_RES Phosphoserine O-phospho-L-serine O-phosphonoserine O-phosphorylated L-serine O3-phosphoserine serine phosphate ester OPSer Phospho Phospho Seryl Phosphorylation phosphorylations certain certain sequence position certain certain certain sequence position certain false binding site binding region binding-associated region binding region mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false CYTOPLASMIC REGION Stoichiometry: 1.0 1433f_mouse 5483 unspecified role unspecified role prey prey over-expressed over expressed level over-expressed Stoichiometry: 1.0 physical association physical association false false false 14-3-3s eta interact with AChR alpha 4 in a phosphorylation dependent manner and significantly increase the steady state levels of the alpha 4 subunits alone and alpha4beta2 AChRs mint ywhah-chrna4 5478 acha4_rat 5482 unspecified role unspecified role prey prey physiological level physiological level endogenous level endogenous endogenous endogenous level phosphoserine o-phospho-serine opser O-phospho-L-serine (2S)-2-amino-3-(phosphonooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)propanoic acid ACT_SITE Phosphoserine intermediate MOD_RES Phosphoserine O-phospho-L-serine O-phosphonoserine O-phosphorylated L-serine O3-phosphoserine serine phosphate ester OPSer Phospho Phospho Seryl Phosphorylation phosphorylations certain certain sequence position certain certain certain sequence position certain false binding site binding region binding-associated region binding region mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false CYTOPLASMIC REGION Stoichiometry: 1.0 1433f_mouse 5483 unspecified role unspecified role bait bait physiological level physiological level endogenous level endogenous endogenous endogenous level Stoichiometry: 1.0 physical association physical association false false false 14-3-3s eta interact with AChR alpha 4 in a phosphorylation dependent manner and significantly increase the steady state levels of the alpha 4 subunits alone and alpha4beta2 AChRs mint chrna4-ywhah 5479 acha4_rat 5482 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence unspecified role unspecified role bait bait over-expressed over expressed level over-expressed binding site binding region binding-associated region binding region mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false CYTOPLASMIC REGION tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false phosphoserine o-phospho-serine opser O-phospho-L-serine (2S)-2-amino-3-(phosphonooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)propanoic acid ACT_SITE Phosphoserine intermediate MOD_RES Phosphoserine O-phospho-L-serine O-phosphonoserine O-phosphorylated L-serine O3-phosphoserine serine phosphate ester OPSer Phospho Phospho Seryl Phosphorylation phosphorylations certain certain sequence position certain certain certain sequence position certain false Stoichiometry: 1.0 1433f_mouse 5483 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence unspecified role unspecified role prey prey over-expressed over expressed level over-expressed tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 physical association physical association false false false 14-3-3s eta interact with AChR alpha 4 in a phosphorylation dependent manner and significantly increase the steady state levels of the alpha 4 subunits alone and alpha4beta2 AChRs mint chrna4-ywhah-2 5480 acha4_rat 5482 predetermined predetermined participant predetermined unspecified role unspecified role unspecified role unspecified role over-expressed over expressed level over-expressed phosphoserine o-phospho-serine opser O-phospho-L-serine (2S)-2-amino-3-(phosphonooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)propanoic acid ACT_SITE Phosphoserine intermediate MOD_RES Phosphoserine O-phospho-L-serine O-phosphonoserine O-phosphorylated L-serine O3-phosphoserine serine phosphate ester OPSer Phospho Phospho Seryl Phosphorylation phosphorylations certain certain sequence position certain certain certain sequence position certain false binding site binding region binding-associated region binding region mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false CYTOPLASMIC REGION Stoichiometry: 1.0 1433f_mouse 5483 predetermined predetermined participant predetermined unspecified role unspecified role unspecified role unspecified role over-expressed over expressed level over-expressed tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 colocalization colocalization false false false 14-3-3s eta interact with AChR alpha 4 in a phosphorylation dependent manner and significantly increase the steady state levels of the alpha 4 subunits alone and alpha4beta2 AChRs mint chrna4-ywhah-3 5481 acha4_rat ACHA4_RAT 5482 unspecified role unspecified role unspecified role unspecified role 1433f_human 1433F_HUMAN 5484 unspecified role unspecified role unspecified role unspecified role association association false false false homomint domino mint