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 The Ras-Byr2RBD complex: structural basis for Ras effector recognition in yeast. The Ras-Byr2RBD complex: structural basis for Ras effector recognition in yeast. Structure (0969-2126) 2001 Scheffzek K., Grunewald P., Wohlgemuth S., Kabsch W., Tu H., Wigler M., Wittinghofer A., Herrmann C. PDBe - Data obtained from the Protein Data Bank Europe in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Scheffzek K., Grunewald P., Wohlgemuth S., Kabsch W., Tu H., Wigler M., Wittinghofer A., Herrmann C. PDBe - Data obtained from the Protein Data Bank Europe Structure (0969-2126) 2001 byr2_schpo Protein kinase byr2 byr2 ste8 SPBC1D7.05 SPBC2F12.01 Protein kinase ste8 MAPK kinase kinase protein protein schpo Schizosaccharomyces pombe (strain ATCC 38366 / 972) Fission yeast MEYYTSKEVAEWLKSIGLEKYIEQFSQNNIEGRHLNHLTLPLLKDLGIENTAKGKQFLKQRDYLREFPRPCILRFIACNGQTRAVQSRGDYQKTLAIALKKFSLEDASKFIVCVSQSSRIKLITEEEFKQICFNSSSPERDRLIIVPKEKPCPSFEDLRRSWEIELAQPAALSSQSSLSPKLSSVLPTSTQKRSVRSNNAKPFESYQRPPSELINSRISDFFPDHQPKLLEKTISNSLRRNLSIRTSQGHNLGNFGQEILPRSSRRARPSELVCPLSSLRISVAEDVNRLPRIDRGFDPPLTVSSTQRISRPPSLQKSITMVGVEPLYQSNGNEKSSKYNVFSESAHGNHQVLSFSPGSSPSFIEQPSPISPTSTTSEDTNTLEEDTDDQSIKWIRGALIGSGSFGQVYLGMNASSGELMAVKQVILDSVSESKDRHAKLLDALAGEIALLQELSHEHIVQYLGSNLNSDHLNIFLEYVPGGSVAGLLTMYGSFEETLVKNFIKQTLKGLEYLHSRGIVHRDIKGANILVDNKGKIKISDFGISKKLELNSTSTKTGGARPSFQGSSFWMAPEVVKQTMHTEKTDIWSLGCLVIEMLTSKHPYPNCDQMQAIFRIGENILPEFPSNISSSAIDFLEKTFAIDCNLRPTASELLSHPFVS 18CD78F1D1FABBCD 18CD78F1D1FABBCD rash_human GTPase HRas HRAS HRAS1 Transforming protein p21 p21ras H-Ras-1 c-H-ras Ha-Ras protein protein human Homo sapiens Human MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDLAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHKLRKLNPPDESGPGCMSCKCVLS DIP protein P01112 original sequence version: 91 DIP protein P01112 original sequence version: 106 DIP protein P01112 original sequence version: 144 DIP protein P01112 original sequence version: 118 DIP protein P01112 original sequence version: 143 DIP protein P01112 original sequence version: 152 DIP protein P01112-1 original sequence version: 159 DIP protein P01112 original sequence version: 170 DIP protein P01112-1 original sequence version: 185 DIP protein P01112 original sequence version: 192 DIP protein P01112-1 original sequence version: 196 DIP protein P01112-1 original sequence version: 202 EE6DC2D933E2856A byr2-hras-1 1 2 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 3 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) direct interaction direct interaction tetrameric, multimeric working 76.500%, free 69.500% 3A