IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ The SH2 domain from the tyrosine kinase Fyn in complex with a phosphotyrosyl peptide reveals insights into domain stability and binding specificity. The SH2 domain from the tyrosine kinase Fyn in complex with a phosphotyrosyl peptide reveals insights into domain stability and binding specificity. Structure (London, England : 1993) 1997 imex curation Mulhern TD., Shaw GL., Morton CJ., Day AJ., Campbell ID. idc@bioch.ox.ac 30-Aug-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Mulhern TD., Shaw GL., Morton CJ., Day AJ., Campbell ID. idc@bioch.ox.ac Accepted 2019-JUL-30 AT 09:43 BST AT 09:43 BST by PPORRAS Structure (London, England : 1993) 1997 Only protein-protein interactions imex curation imex curation fyn_human Tyrosine-protein kinase Fyn p59-Fyn Proto-oncogene c-Fyn Src-like kinase FYN Proto-oncogene Syn protein protein human Homo sapiens Human MGCVQCKDKEATKLTEERDGSLNQSSGYRYGTDPTPQHYPSFGVTSIPNYNNFHAAGGQGLTVFGGVNSSSHTGTLRTRGGTGVTLFVALYDYEARTEDDLSFHKGEKFQILNSSEGDWWEARSLTTGETGYIPSNYVAPVDSIQAEEWYFGKLGRKDAERQLLSFGNPRGTFLIRESETTKGAYSLSIRDWDDMKGDHVKHYKIRKLDNGGYYITTRAQFETLQQLVQHYSERAAGLCCRLVVPCHKGMPRLTDLSVKTKDVWEIPRESLQLIKRLGNGQFGEVWMGTWNGNTKVAIKTLKPGTMSPESFLEEAQIMKKLKHDKLVQLYAVVSEEPIYIVTEYMNKGSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPQDCPISLHELMIHCWKKDPEERPTFEYLQSFLEDYFTATEPQYQPGENL DIP protein P06241 original sequence version: 195 DIP protein P06241 original sequence version: 147 DIP protein P06241 original sequence version: 164 4A1E443A4B5A0977 mt_povha Middle T antigen protein protein povha povha HaPyV MDRILTKEEKQALISLLDLEPQYWGDYGRMQKCYKKKCLQLHPDKGGNEELMQQLNTLWTKLKDGLYRVRLLLGPSQVRRLGKDQWNLSLQQTFSGTYFRRLCRLPITCLRNKGISTCNCILCLLRKQHFLLKKSWRVPCLVLGECYCIDCFALWFGLPVTNMLVPLYAQFLAPIPVDWLDLNVHEVYNPASGMTLMLPPPPADPESSTILTQEDTGPTLMGQQDTLTSRRNTGKSFSLSGMLMRTSPAKKSYHHQKMNSPPGIPIPPPPLFLFPVTAPVPPVTRNTQETQAERENEYMPMAPQIHLYSQIREPTHQEEEEPQYEEIPIYLELLPENPNQHLALTSTARRSLRRKYHKHNSHIITQRQRNRLRRLVLMIFLLSLGGFFLTLFFLIKRKMHL mint 91B6172F4293F448 fyn-mt_povha-1 1 3 unspecified role unspecified role neutral component neutral component purified purified Binding region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain possible phosphotyr-324 optyr O4'-phospho-L-tyrosine (2S)-2-amino-3-(4-phosphonooxyphenyl)propanoic acid 2-azanyl-3-(4-phosphonooxyphenyl)propanoic acid MOD_RES Phosphotyrosine O4-phosphotyrosine tyrosine phosphate 2-amino-3-(4-hydroxyphenyl)propanoic acid 4'-phosphate O4'-phospho-L-tyrosine O4'-phosphorylated L-tyrosine OPTyr Phospho Phospho Tyrosinyl Phosphorylation phosphorylationy certain certain sequence position certain certain certain sequence position certain observed-ptm observed-ptm observed ptm observed-ptm chemical synthesis Chemical synthesis (Chemical synthesis) 2 unspecified role unspecified role neutral component neutral component purified purified SH2 domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 13C radiolabelled 13c label 13c label C13 13C C13 13C undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 15N radiolabelled 15n label 15n label 15N N15 15N N15 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) 6 9 direct interaction direct interaction Fig.2 and 3