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 Dok-R plays a pivotal role in angiopoietin-1-dependent cell migration through recruitment and activation of Pak. Dok-R plays a pivotal role in angiopoietin-1-dependent cell migration through recruitment and activation of Pak. EMBO J. (0261-4189) 2001 Master Z., Jones N., Tran J., Jones J., Kerbel RS., Dumont DJ. SH2 PMID_in_GD partial coverage rapid curation unknown Unknown coip coimmunoprecipitation co-immunoprecipitation CoIp immunoprecipitation Co-IP co-immunoprecipitation CoIp immunoprecipitation Co-IP coip predetermined predetermined participant predetermined Master Z., Jones N., Tran J., Jones J., Kerbel RS., Dumont DJ. SH2 PMID_in_GD PMID_in_GD EMBO J. (0261-4189) 2001 partial coverage rapid curation nck1_human Cytoplasmic protein NCK1 NCK1 NCK NCK adaptor protein 1 SH2/SH3 adaptor protein NCK-alpha protein protein human Homo sapiens Human MAEEVVVVAKFDYVAQQEQELDIKKNERLWLLDDSKSWWRVRNSMNKTGFVPSNYVERKNSARKASIVKNLKDTLGIGKVKRKPSVPDSASPADDSFVDPGERLYDLNMPAYVKFNYMAEREDELSLIKGTKVIVMEKCSDGWWRGSYNGQVGWFPSNYVTEEGDSPLGDHVGSLSEKLAAVVNNLNTGQVLHVVQALYPFSSSNDEELNFEKGDVMDVIEKPENDPEWWKCRKINGMVGLVPKNYVTVMQNNPLTSGLEPSPPQCDYIRPSLTGKFAGNPWYYGKVTRHQAEMALNERGHEGDFLIRDSESSPNDFSVSLKAQGKNKHFKVQLKETVYCIGQRKFSTMEELVEHYKKAPIFTSEQGEKLYLVKHLS 554E9B1A936AEF30 dok2_mouse Docking protein 2 Frip Dok-related protein Downstream of tyrosine kinase 2 IL-four receptor-interacting protein p56(dok-2) Dok2 protein protein mouse Mus musculus Mouse MVRMEEPAVKQGFLHLQQQQTFGKKWRRFAAVLYGESGCALARLELQDVPEKTRRGEATRKVVRLSDCLRVAEVGSEASSPRDTSAFILETKERLYLLAAPSAERSDWIQAICLLAFPGQRKGSPGLEEKSGSPCMEENELYSSSTTGLCKEYMVTIRPTEASERCRLRGSYTLRTGVSALELWGGPEPGTQLYDWPYRFLRRFGRDKATFSFEAGRRCLSGEGNFEFETRHGNEIFQALEKVIAVQKNATPSGPPSLPATGPMMPTVLPRPESPYSRPHDSLPSPSPGTLVPGMRPGAPEGEYAVPFDTVAHSLRKSFRGLLTGPPPHLPDPLYDSIQEDPGAPLPDHIYDEPEGVAALSLYDRTQRPSGETWREQATADGGPSSLQQDSSVPDWPQATEYDNVILKKGPK 02AC02530DBED053 dok2-nck1-1 1 NCK1_HUMAN 2 unspecified role unspecified role unspecified role unspecified role DOK2_MOUSE 3 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 mint