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 A Ras activation pathway dependent on Syk phosphorylation of protein kinase C. A Ras activation pathway dependent on Syk phosphorylation of protein kinase C. Proc. Natl. Acad. Sci. U.S.A. (0027-8424) 2003 Kawakami Y., Kitaura J., Yao L., McHenry RW., Kawakami Y., Newton AC., Kang S., Kato RM., Leitges M., Rawlings DJ., Kawakami T. SH2 PMID_in_GD yuko@liai.org 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 Kawakami Y., Kitaura J., Yao L., McHenry RW., Kawakami Y., Newton AC., Kang S., Kato RM., Leitges M., Rawlings DJ., Kawakami T. SH2 PMID_in_GD PMID_in_GD yuko@liai.org Proc. Natl. Acad. Sci. U.S.A. (0027-8424) 2003 partial coverage rapid curation grb2_mouse Growth factor receptor-bound protein 2 Grb2 Adapter protein GRB2 SH2/SH3 adapter GRB2 protein protein mouse Mus musculus Mouse MEAIAKYDFKATADDELSFKRGDILKVLNEECDQNWYKAELNGKDGFIPKNYIEMKPHPWFFGKIPRAKAEEMLSKQRHDGAFLIRESESAPGDFSLSVKFGNDVQHFKVLRDGAGKYFLWVVKFNSLNELVDYHRSTSVSRNQQIFLRDIEQMPQQPTYVQALFDFDPQEDGELGFRRGDFIHVMDNSDPNWWKGACHGQTGMFPRNYVTPVNRNV 97F4A4FE4B248DDF kpca_mouse Protein kinase C alpha type Prkca Pkca protein protein mouse Mus musculus Mouse MADVYPANDSTASQDVANRFARKGALRQKNVHEVKDHKFIARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPDTDDPRSKHKFKIHTYGSPTFCDHCGSLLYGLIHQGMKCDTCDMNVHKQCVINDPSLCGMDHTEKRGRIYLKAEVTDEKLHVTVRDAKNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSNLNPQWNESFTFKLKPSDKDRRLSVEIWDWDRTTRNDFMGSLSFGVSELMKMPASGWYKAHNQEEGEYYNVPIPEGDEEGNMELRQKFEKAKLGPVGNKVISPSEDRKQPSNNLDRVKLTDFNFLMVLGKGSFGKVMLADRKGTEELYAIKILKKDVVIQDDDVECTMVEKRVLALLDKPPFLTQLHSCFQTVDRLYFVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISIGLFFLHKRGIIYRDLKLNNVMLNSEGHIKIADFGMCKEHMMDGVTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLMTKQPAKRLGCGPEGERDVREHAFFRRIDWEKLENREIQPPFKPKVCGKGAENFDKFFTRGQPVLTPPDQLVIANIDQSDFEGFSYVNPQFVHPILQSAV mint This is a calcium-activated, phospholipid-dependent, serine- and threonine-specific enzyme. May play a role in cell motility by phosphorylating CSPG4 PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters Expression of the mutant form UV25 causes malignant transformation of cells 394B48C952BB6D50 grb2-prkca 1 KPCA_MOUSE 3 unspecified role unspecified role unspecified role unspecified role binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 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 GRB2_MOUSE 2 unspecified role unspecified role unspecified role unspecified role association association mint