DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu A common mechanism of PLP/DM20 misfolding causes cysteine-mediated endoplasmic reticulum retention in oligodendrocytes and Pelizaeus-Merzbacher disease. A common mechanism of PLP/DM20 misfolding causes cysteine-mediated endoplasmic reticulum retention in oligodendrocytes and Pelizaeus-Merzbacher disease. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Dhaunchak AS., Nave KA. Only protein-protein interactions mouse Mus musculus Mouse comigration in sds comigration in sds page comigration in sds western blot western blot Immuno blot Immuno blot Dhaunchak AS., Nave KA. DIP original experiment: DIP-111353X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx f.2e,f A common mechanism of PLP/DM20 misfolding causes cysteine-mediated endoplasmic reticulum retention in oligodendrocytes and Pelizaeus-Merzbacher disease. A common mechanism of PLP/DM20 misfolding causes cysteine-mediated endoplasmic reticulum retention in oligodendrocytes and Pelizaeus-Merzbacher disease. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Dhaunchak AS., Nave KA. Only protein-protein interactions mouse Mus musculus Mouse comig non denat gel comigration in non denaturing gel electrophoresis comig non denat gel western blot western blot Immuno blot Immuno blot Dhaunchak AS., Nave KA. DIP original experiment: DIP-111354X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx A common mechanism of PLP/DM20 misfolding causes cysteine-mediated endoplasmic reticulum retention in oligodendrocytes and Pelizaeus-Merzbacher disease. A common mechanism of PLP/DM20 misfolding causes cysteine-mediated endoplasmic reticulum retention in oligodendrocytes and Pelizaeus-Merzbacher disease. A common mechanism of PLP/DM20 misfolding causes cysteine-mediated endoplasmic reticulum retention in oligodendrocytes and Pelizaeus-Merzbacher disease. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Dhaunchak AS., Nave KA. Only protein-protein interactions mouse Mus musculus Mouse comig non denat gel comigration in non denaturing gel electrophoresis comig non denat gel western blot western blot Immuno blot Immuno blot Dhaunchak AS., Nave KA. DIP original experiment: DIP-111356X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx A common mechanism of PLP/DM20 misfolding causes cysteine-mediated endoplasmic reticulum retention in oligodendrocytes and Pelizaeus-Merzbacher disease. A common mechanism of PLP/DM20 misfolding causes cysteine-mediated endoplasmic reticulum retention in oligodendrocytes and Pelizaeus-Merzbacher disease. A common mechanism of PLP/DM20 misfolding causes cysteine-mediated endoplasmic reticulum retention in oligodendrocytes and Pelizaeus-Merzbacher disease. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Dhaunchak AS., Nave KA. Only protein-protein interactions mouse Mus musculus Mouse comig non denat gel comigration in non denaturing gel electrophoresis comig non denat gel western blot western blot Immuno blot Immuno blot Dhaunchak AS., Nave KA. DIP original experiment: DIP-111355X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx A common mechanism of PLP/DM20 misfolding causes cysteine-mediated endoplasmic reticulum retention in oligodendrocytes and Pelizaeus-Merzbacher disease. p60202-1 Myelin proteolipid protein Plp1 Plp Lipophilin protein protein mouse Mus musculus Mouse MGLLECCARCLVGAPFASLVATGLCFFGVALFCGCGHEALTGTEKLIETYFSKNYQDYEYLINVIHAFQYVIYGTASFFFLYGALLLAEGFYTTGAVRQIFGDYKTTICGKGLSATVTGGQKGRGSRGQHQAHSLERVCHCLGKWLGHPDKFVGITYALTVVWLLVFACSAVPVYIYFNTWTTCQSIAFPSKTSASIGSLCADARMYGVLPWNAFPGKVCGSNLLSICKTAEFQMTFHLFIAAFVGAAATLVSLLTFMIAATYNFAVLKLMGRGTKF DIP protein P60202-1 original sequence version: 53 p60202-2 Myelin proteolipid protein Plp1 Plp Lipophilin protein protein mouse Mus musculus Mouse MGLLECCARCLVGAPFASLVATGLCFFGVALFCGCGHEALTGTEKLIETYFSKNYQDYEYLINVIHAFQYVIYGTASFFFLYGALLLAEGFYTTGAVRQIFGDYKTTICGKGLSATFVGITYALTVVWLLVFACSAVPVYIYFNTWTTCQSIAFPSKTSASIGSLCADARMYGVLPWNAFPGKVCGSNLLSICKTAEFQMTFHLFIAAFVGAAATLVSLLTFMIAATYNFAVLKLMGRGTKF DIP protein P60202-2 original sequence version: 53 p60201-1 Myelin proteolipid protein PLP1 PLP Lipophilin protein protein human Homo sapiens Human MGLLECCARCLVGAPFASLVATGLCFFGVALFCGCGHEALTGTEKLIETYFSKNYQDYEYLINVIHAFQYVIYGTASFFFLYGALLLAEGFYTTGAVRQIFGDYKTTICGKGLSATVTGGQKGRGSRGQHQAHSLERVCHCLGKWLGHPDKFVGITYALTVVWLLVFACSAVPVYIYFNTWTTCQSIAFPSKTSASIGSLCADARMYGVLPWNAFPGKVCGSNLLSICKTAEFQMTFHLFIAAFVGAAATLVSLLTFMIAATYNFAVLKLMGRGTKF DIP protein P60201-1 original sequence version: 59 plp1-plp1-1 3 7 unspecified role unspecified role unspecified role unspecified role mouse Mus musculus Mouse 6 unspecified role unspecified role unspecified role unspecified role mouse Mus musculus Mouse physical association physical association plp1-1 1 7 unspecified role unspecified role unspecified role unspecified role mouse Mus musculus Mouse physical association physical association plp1-2 2 7 unspecified role unspecified role unspecified role unspecified role P60201-1:p.Cys220Tyr C219Y mutation increasing mutation increasing interaction mutation increasing certain certain sequence position certain certain certain sequence position certain C Y Wed May 02 15:56:36 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys220tyr' Tue Jun 30 17:01:05 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys220Tyr' mouse Mus musculus Mouse physical association physical association plp1-plp1-2 4 6 unspecified role unspecified role unspecified role unspecified role mouse Mus musculus Mouse 5 unspecified role unspecified role unspecified role unspecified role mouse Mus musculus Mouse physical association physical association