DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu The repeat domain of the melanosome fibril protein Pmel17 forms the amyloid core promoting melanin synthesis. The repeat domain of the melanosome fibril protein Pmel17 forms the amyloid core promoting melanin synthesis. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation McGlinchey RP., Shewmaker F., McPhie P., Monterroso B., Thurber K., Wickner RB. Only protein-protein interactions in vitro In vitro tem transmission electron microscopy tem predetermined predetermined participant predetermined McGlinchey RP., Shewmaker F., McPhie P., Monterroso B., Thurber K., Wickner RB. DIP original experiment: DIP-134427X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx The repeat domain of the melanosome fibril protein Pmel17 forms the amyloid core promoting melanin synthesis. The repeat domain of the melanosome fibril protein Pmel17 forms the amyloid core promoting melanin synthesis. The repeat domain of the melanosome fibril protein Pmel17 forms the amyloid core promoting melanin synthesis. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation McGlinchey RP., Shewmaker F., McPhie P., Monterroso B., Thurber K., Wickner RB. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined McGlinchey RP., Shewmaker F., McPhie P., Monterroso B., Thurber K., Wickner RB. DIP original experiment: DIP-134429X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx The repeat domain of the melanosome fibril protein Pmel17 forms the amyloid core promoting melanin synthesis. The repeat domain of the melanosome fibril protein Pmel17 forms the amyloid core promoting melanin synthesis. The repeat domain of the melanosome fibril protein Pmel17 forms the amyloid core promoting melanin synthesis. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation McGlinchey RP., Shewmaker F., McPhie P., Monterroso B., Thurber K., Wickner RB. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined McGlinchey RP., Shewmaker F., McPhie P., Monterroso B., Thurber K., Wickner RB. DIP original experiment: DIP-134428X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx The repeat domain of the melanosome fibril protein Pmel17 forms the amyloid core promoting melanin synthesis. The repeat domain of the melanosome fibril protein Pmel17 forms the amyloid core promoting melanin synthesis. The repeat domain of the melanosome fibril protein Pmel17 forms the amyloid core promoting melanin synthesis. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation McGlinchey RP., Shewmaker F., McPhie P., Monterroso B., Thurber K., Wickner RB. Only protein-protein interactions in vitro In vitro electron diffraction electron diffraction predetermined predetermined participant predetermined McGlinchey RP., Shewmaker F., McPhie P., Monterroso B., Thurber K., Wickner RB. DIP original experiment: DIP-134430X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx The repeat domain of the melanosome fibril protein Pmel17 forms the amyloid core promoting melanin synthesis. pmel_human Melanocyte protein PMEL PMEL D12S53E PMEL17 SILV ME20-M Melanocyte protein Pmel 17 Melanocytes lineage-specific antigen GP100 Melanoma-associated ME20 antigen P1 P100 Premelanosome protein Silver locus protein homolog protein protein human Homo sapiens Human MDLVLKRCLLHLAVIGALLAVGATKVPRNQDWLGVSRQLRTKAWNRQLYPEWTEAQRLDCWRGGQVSLKVSNDGPTLIGANASFSIALNFPGSQKVLPDGQVIWVNNTIINGSQVWGGQPVYPQETDDACIFPDGGPCPSGSWSQKRSFVYVWKTWGQYWQVLGGPVSGLSIGTGRAMLGTHTMEVTVYHRRGSRSYVPLAHSSSAFTITDQVPFSVSVSQLRALDGGNKHFLRNQPLTFALQLHDPSGYLAEADLSYTWDFGDSSGTLISRALVVTHTYLEPGPVTAQVVLQAAIPLTSCGSSPVPGTTDGHRPTAEAPNTTAGQVPTTEVVGTTPGQAPTAEPSGTTSVQVPTTEVISTAPVQMPTAESTGMTPEKVPVSEVMGTTLAEMSTPEATGMTPAEVSIVVLSGTTAAQVTTTEWVETTARELPIPEPEGPDASSIMSTESITGSLGPLLDGTATLRLVKRQVPLDCVLYRYGSFSVTLDIVQGIESAEILQAVPSGEGDAFELTVSCQGGLPKEACMEISSPGCQPPAQRLCQPVLPSPACQLVLHQILKGGSGTYCLNVSLADTNSLAVVSTQLIMPGQEAGLGQVPLIVGILLVLMAVVLASLIYRRRLMKQDFSVPQLPHSSSHWLRLPRIFCSCPIGENSPLLSGQQV DIP protein P40967 original sequence version: 100 8A904FAB16715653 pmel-1 4 5 unspecified role unspecified role unspecified role unspecified role Region 315-444 Region 315-444 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction pmel-2 1 5 unspecified role unspecified role unspecified role unspecified role Region 315-444 Region 315-444 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction pmel-3 3 5 unspecified role unspecified role unspecified role unspecified role Region 315-444 Region 315-444 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction pmel-4 2 5 unspecified role unspecified role unspecified role unspecified role Region 315-444 Region 315-444 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction