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 Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex. a role for scaffolding in enzyme regulation. Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex. a role for scaffolding in enzyme regulation. Cell (0092-8674) 2001 Obsil T., Ghirlando R., Klein DC., Ganguly S., Dyda F. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Obsil T., Ghirlando R., Klein DC., Ganguly S., Dyda F. Accepted 2010-JAN-10 by SKERRIEN (applied to all records created before 2005-Sep-01). Cell (0092-8674) 2001 Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex. a role for scaffolding in enzyme regulation. Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex. a role for scaffolding in enzyme regulation. Cell (0092-8674) 2001 Obsil T., Ghirlando R., Klein DC., Ganguly S., Dyda F. in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Obsil T., Ghirlando R., Klein DC., Ganguly S., Dyda F. Accepted 2010-JAN-10 by SKERRIEN (applied to all records created before 2005-Sep-01). Cell (0092-8674) 2001 Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex. a role for scaffolding in enzyme regulation. Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex. a role for scaffolding in enzyme regulation. Cell (0092-8674) 2001 Obsil T., Ghirlando R., Klein DC., Ganguly S., Dyda F. in vitro In vitro cosedimentation cosedimentation predetermined predetermined participant predetermined Obsil T., Ghirlando R., Klein DC., Ganguly S., Dyda F. Accepted 2010-JAN-10 by SKERRIEN (applied to all records created before 2005-Sep-01). Cell (0092-8674) 2001 1433z_human 14-3-3 protein zeta/delta YWHAZ Protein kinase C inhibitor protein 1 protein protein human Homo sapiens Human MDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEERNLLSVAYKNVVGARRSSWRVVSSIEQKTEGAEKKQQMAREYREKIETELRDICNDVLSLLEKFLIPNASQAESKVFYLKMKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDTQGDEAEAGEGGEN DIP protein P63104 original sequence version: 144 D464DF2286BBFE60 snat_sheep Serotonin N-acetyltransferase Aralkylamine N-acetyltransferase AANAT SNAT protein protein sheep Ovis aries (Sheep) Sheep MSTPSVHCLKPSPLHLPSGIPGSPGRQRRHTLPANEFRCLTPEDAAGVFEIEREAFISVSGNCPLNLDEVQHFLTLCPELSLGWFVEGRLVAFIIGSLWDEERLTQESLALHRPRGHSAHLHALAVHRSFRQQGKGSVLLWRYLHHVGAQPAVRRAVLMCEDALVPFYQRFGFHPAGPCAIVVGSLTFTEMHCSLRGHAALRRNSDR F6752A872F436DF9 ywhaz-aanat-1 2 4 unspecified role unspecified role neutral component neutral component ecobb Escherichia coli (strain B / BL21) 5 unspecified role unspecified role neutral component neutral component phosphrylted thr required phosres phosphorylated residue PhosRes Phospho Phosphorylation Phosphorylation (O of Serine, Threonine, Tyrosine and Aspartate, N epsilon of Lysine) certain certain sequence position certain certain certain sequence position certain phosphorylated ser possible phosres phosphorylated residue PhosRes Phospho Phosphorylation Phosphorylation (O of Serine, Threonine, Tyrosine and Aspartate, N epsilon of Lysine) certain certain sequence position certain certain certain sequence position certain ecobb Escherichia coli (strain B / BL21) physical association physical association ywhaz-aanat-2 3 5 unspecified role unspecified role neutral component neutral component phosphorylated thr required phosres phosphorylated residue PhosRes Phospho Phosphorylation Phosphorylation (O of Serine, Threonine, Tyrosine and Aspartate, N epsilon of Lysine) certain certain sequence position certain certain certain sequence position certain ecobb Escherichia coli (strain B / BL21) 4 unspecified role unspecified role neutral component neutral component region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecobb Escherichia coli (strain B / BL21) physical association physical association ywhaz-aanat-3 1 5 unspecified role unspecified role neutral component neutral component gcn5acetyl_trans binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecobb Escherichia coli (strain B / BL21) 4 unspecified role unspecified role neutral component neutral component phosphorylated thr phosres phosphorylated residue PhosRes Phospho Phosphorylation Phosphorylation (O of Serine, Threonine, Tyrosine and Aspartate, N epsilon of Lysine) certain certain sequence position certain certain certain sequence position certain full length binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecobb Escherichia coli (strain B / BL21) 18 21 direct interaction direct interaction presence of COA-S-ACETYL TRYPTAMINE (COT) in the crystal 2.70 working 20.4%, free 22.8%