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 structures of the XLP protein SAP reveal a class of SH2 domains with extended, phosphotyrosine-independent sequence recognition. Crystal structures of the XLP protein SAP reveal a class of SH2 domains with extended, phosphotyrosine-independent sequence recognition. Mol. Cell (1097-2765) 1999 Poy F., Yaffe MB., Sayos J., Saxena K., Morra M., Sumegi J., Cantley LC., Terhorst C., Eck MJ. SH2 PMID_in_GD partial coverage rapid curation unknown Unknown pull down pull down predetermined predetermined participant predetermined Poy F., Yaffe MB., Sayos J., Saxena K., Morra M., Sumegi J., Cantley LC., Terhorst C., Eck MJ. SH2 PMID_in_GD PMID_in_GD Mol. Cell (1097-2765) 1999 partial coverage rapid curation slaf1_human Signaling lymphocytic activation molecule SLAMF1 SLAM family member 1 SLAM CDw150 IPO-3 protein protein human Homo sapiens Human MDPKGLLSLTFVLFLSLAFGASYGTGGRMMNCPKILRQLGSKVLLPLTYERINKSMNKSIHIVVTMAKSLENSVENKIVSLDPSEAGPPRYLGDRYKFYLENLTLGIRESRKEDEGWYLMTLEKNVSVQRFCLQLRLYEQVSTPEIKVLNKTQENGTCTLILGCTVEKGDHVAYSWSEKAGTHPLNPANSSHLLSLTLGPQHADNIYICTVSNPISNNSQTFSPWPGCRTDPSETKPWAVYAGLLGGVIMILIMVVILQLRRRGKTNHYQTTVEKKSLTIYAQVQKPGPLQKKLDSFPAQDPCTTIYVAATEPVPESVQETNSITVYASVTLPES DIP protein Q13291 original sequence version: 151 DIP protein Q13291 original sequence version: 110 DIP protein Q13291 original sequence version: 106 DIP protein Q13291 original sequence version: 112 BFB0F27EA31D8C04 sh21b_human SH2 domain-containing protein 1B SH2D1B EAT2 EWS/FLI1-activated transcript 2 protein protein human Homo sapiens Human MDLPYYHGRLTKQDCETLLLKEGVDGNFLLRDSESIPGVLCLCVSFKNIVYTYRIFREKHGYYRIQTAEGSPKQVFPSLKELISKFEKPNQGMVVHLLKPIKRTSPSLRWRGLKLELETFVNSNSDYVDVLP BC9FEA398B6B27DE sh21a_human SH2 domain-containing protein 1A SH2D1A DSHP SAP Signaling lymphocytic activation molecule-associated protein T-cell signal transduction molecule SAP Duncan disease SH2-protein protein protein human Homo sapiens Human MDAVAVYHGKISRETGEKLLLATGLDGSYLLRDSESVPGVYCLCVLYHGYIYTYRVSQTETGSWSAETAPGVHKRYFRKIKNLISAFQKPDQGIVIPLQYPVEKKSSARSTQGTTGIREDPDVCLKAP mint Inhibitor of the SLAM self-association. Acts by blocking recruitment of the SH2-domain-containing signal-transduction molecule SHP-2 to a docking site in the slam cytoplasmic region Defects in SH2D1A are a cause of lymphoproliferative syndrome X-linked type 1 (XLP1) [MIM:308240]; also known as X-linked lymphoproliferative disease (XLPD) or Duncan disease. XLP is a rare immunodeficiency characterized by extreme susceptibility to infection with Epstein-Barr virus (EBV). Symptoms include severe or fatal mononucleosis, acquired hypogammaglobulinemia, pancytopenia and malignant lymphoma 90234E7A6614EE3D sh2d1b-slamf1 1 SH21B_HUMAN 3 unspecified role unspecified role unspecified role unspecified role SLAF1_HUMAN 2 unspecified role unspecified role unspecified role unspecified role phosphorylated phosphorylated residue 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 binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain association association homomint mint sh2d1a-slamf1-1 1 SH21A_HUMAN 4 unspecified role unspecified role unspecified role unspecified role SLAF1_HUMAN 2 unspecified role unspecified role unspecified role unspecified role binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain phosphorylated phosphorylated residue 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 association association homomint mint