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 Novel autophosphorylation sites of Src family kinases regulate kinase activity and SH2 domain-binding capacity. Novel autophosphorylation sites of Src family kinases regulate kinase activity and SH2 domain-binding capacity. FEBS letters 2016 imex curation Weir ME., Mann JE., Corwin T., Fulton ZW., Hao JM., Maniscalco JF., Kenney MC., Roman Roque KM., Chapdelaine EF., Stelzl U., Deming PB., Ballif BA., Hinkle KL. khinkle@norwich.edu; bballif@uvm.edu 17-Oct-2016: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro protein kinase assay protein kinase assay western blot western blot Immuno blot Immuno blot Weir ME., Mann JE., Corwin T., Fulton ZW., Hao JM., Maniscalco JF., Kenney MC., Roman Roque KM., Chapdelaine EF., Stelzl U., Deming PB., Ballif BA., Hinkle KL. khinkle@norwich.edu; bballif@uvm.edu Accepted 2016-SEP-13 AT 09:06 BST AT 09:06 BST by MARTA FEBS letters 2016 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 fyn-1 1 2 enzyme enzyme neutral component neutral component purified purified 2 enzyme target enzyme target substrate substrate neutral component neutral component purified purified gst tag gst tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain P06241:p.[Tyr185Phe;Tyr213Phe;Tyr214Phe] mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain Y F certain certain sequence position certain certain certain sequence position certain Y F certain certain sequence position certain certain certain sequence position certain Y F Fri Jul 22 10:58:37 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'Tyr185_213_214_phe' Wed May 02 16:52:37 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr185phe,tyr213phe,tyr214phe' Tue Jun 30 19:30:51 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Tyr185Phe;Tyr213Phe;Tyr214Phe]' 185_phosres 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 214_phosres 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 213_phosres 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 phosphorylation phosphorylation reaction phosphorylation f3