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 Fyn-induced phosphorylation of beta-adducin at tyrosine 489 and its role in their subcellular localization. Fyn-induced phosphorylation of beta-adducin at tyrosine 489 and its role in their subcellular localization. Biochem. Biophys. Res. Commun. (0006-291X) 2006 Gotoh H., Okumura N., Yagi T., Okumura A., Shima T., Nagai K. SH2 PMID_in_GD partial coverage rapid curation unknown Unknown pull down pull down predetermined predetermined participant predetermined Gotoh H., Okumura N., Yagi T., Okumura A., Shima T., Nagai K. SH2 PMID_in_GD PMID_in_GD Biochem. Biophys. Res. Commun. (0006-291X) 2006 partial coverage rapid curation addb_mouse Beta-adducin Erythrocyte adducin subunit beta Add97 Add2 protein protein mouse Mus musculus Mouse MSEDTVPEAASPPPSQGQHYFDRFSEDDPEYLRLRNRAADLRQDFNLMEQKKRVTMILQSPSFREELEGLIQEQMKKGNNSSNIWALRQIADFMASTSHAVFPASSMNFSMMTPINDLHTADSLNLAKGERLMRCKISSVYRLLDLYGWAQLSDTYVTLRVSKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEKGSSCFPVDTTGFSLHSAIYAARPDVRCAIHLHTPATAAVSAMKCGLLPVSHNALLVGDMAYYDFNGEMEQEADRINLQKCLGPTCKILVLRNHGMVALGDTVEEAFYKVFHLQAACEVQVSALSSAGGTENLILLEQEKHRPHEVGSVQWAGSTFGPMQKSRLGEHEFEALMRMLDNLGYRTGYTYRHPFVQEKTKHKSEVEIPATVTAFVFEEDGVPVPALRQHAQKQQKEKTRWLNTPNTYLRVNVADEVQRNMGSPRPKTTWMKADEVEKSSSGMPIRIENPNQFVPLYTDPQEVLDMRNKIREQNRQDIKSAGPQSQLLASVIAEKSRSPSTESQLMSKGDADTKDESEETVPNPFSQLTDQELEEYKKEVERKKLEQEQEGEKDIATEKPGSPVKSTPASPVQSPSKAGTKSPAVSPSKTSEDTKKTEVSEANTEPEPVKPEGLVVNGKEEEPSVEEALSKGLGQMTTNADTDGDSYKDKTESVTSGPLSPEGSPSKSPSKKKKKFRTPSFLKKSKKKEKVES 479153AB1BD6C0DA fyn_mouse Tyrosine-protein kinase Fyn p59-Fyn Fyn Proto-oncogene c-Fyn protein protein mouse Mus musculus Mouse MGCVQCKDKEAAKLTEERDGSLNQSSGYRYGTDPTPQHYPSFGVTSIPNYNNFHAAGGQGLTVFGGVNSSSHTGTLRTRGGTGVTLFVALYDYEARTEDDLSFHKGEKFQILNSSEGDWWEARSLTTGETGYIPSNYVAPVDSIQAEEWYFGKLGRKDAERQLLSFGNPRGTFLIRESETTKGAYSLSIRDWDDMKGDHVKHYKIRKLDNGGYYITTRAQFETLQQLVQHYSERAAGLCCRLVVPCHKGMPRLTDLSVKTKDVWEIPRESLQLIKRLGNGQFGEVWMGTWNGNTKVAIKTLKPGTMSPESFLEEAQIMKKLKHDKLVQLYAVVSEEPIYIVTEYMSKGSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPQDCPISLHELMIHCWKKDPEERPTFEYLQGFLEDYFTATEPQYQPGENL 99558702596DAEE0 add2-fyn 1 FYN_MOUSE 3 unspecified role unspecified role unspecified role unspecified role ADDB_MOUSE 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