{"context":{"query":">>uniprot>>ufeature","source_dataset":"uniprot","target_dataset":"ufeature"},"stats":{"queried":1,"total":67,"mapped":1},"pagination":{"has_next":false},"schema":"id|type|description|location_begin|location_end","mappings":[{"input":"P10415","source":"P10415|Apoptosis regulator Bcl-2","targets":["O02718_F10|modified residue|phosphothreonine; by mapk8|62|62","O02718_F11|modified residue|phosphoserine; by mapk8 and pkc|63|63","O02718_F12|modified residue|phosphoserine; by mapk8|77|77","P10417_F7|modified residue|phosphothreonine; by mapk8|69|69","P10417_F9|modified residue|phosphoserine; by mapk8|84|84","P49950_F7|modified residue|phosphothreonine; by mapk8|69|69","P49950_F8|modified residue|phosphoserine; by mapk8 and pkc|70|70","P49950_F9|modified residue|phosphoserine; by mapk8|84|84","Q6R755_F7|modified residue|phosphothreonine; by mapk8|69|69","Q6R755_F8|modified residue|phosphoserine; by mapk8 and pkc|70|70","Q6R755_F9|modified residue|phosphoserine; by mapk8|84|84","Q9JJV8_F7|modified residue|phosphothreonine; by mapk8|69|69","Q9JJV8_F8|modified residue|phosphoserine; by mapk8 and pkc|70|70","Q9JJV8_F9|modified residue|phosphoserine; by mapk8|84|84","P10415_F0|chain|apoptosis regulator bcl-2|1|239","P10415_F1|transmembrane region|helical|212|233","P10415_F10|modified residue|phosphothreonine; by mapk8|69|69","P10415_F11|modified residue|phosphoserine; by mapk8 and pkc|70|70","P10415_F12|modified residue|phosphoserine; by mapk8|87|87","P10415_F13|splice variant|in isoform beta.|196|239","P10415_F14|sequence variant||7|7","P10415_F15|sequence variant|in dbsnp:rs1800477.|43|43","P10415_F16|sequence variant|in non-hodgkin lymphoma; somatic mutation.|59|59","P10415_F17|sequence variant|in non-hodgkin lymphoma; somatic mutation.|93|93","P10415_F18|mutagenesis site|abolishes cleavage by caspase-3.|34|34","P10415_F19|mutagenesis site|no effect on cleavage by caspase-3.|64|64","P10415_F2|region of interest|disordered|39|85","P10415_F20|mutagenesis site|loss of bax-binding and of anti-apoptotic activity.|138|141","P10415_F21|mutagenesis site|loss of bax-binding and of anti-apoptotic activity; when associated with a-145 and a146.|144|144","P10415_F22|mutagenesis site|loss of bax-binding and of anti-apoptotic activity. no effect on nlrp1-induced il1b release, nor on homodimerization. loss of bax-binding and of anti-apoptotic activity; when associated with a-145 and a146.|145|145","P10415_F23|mutagenesis site|loss of bax-binding and of anti-apoptotic activity. no effect on homodimerization.|145|145","P10415_F24|mutagenesis site|loss of bax-binding and of anti-apoptotic activity; when associated with a-144 and a145.|146|146","P10415_F25|mutagenesis site|loss of bax-binding and of anti-apoptotic activity. no effect on homodimerization.|188|188","P10415_F26|mutagenesis site|partial loss of bax-binding and 50% decrease in anti-apoptotic activity; when associated with a-191 and a-192. no effect on homodimerization; when associated with l-190 and a-191.|190|190","P10415_F27|mutagenesis site|no effect on bax-binding, nor on anti-apoptotic activity. partial loss of bax-binding and 50% decrease in anti-apoptotic activity; when associated with l-190 and a-192. no effect on homodimerization; when associated with l-190 and a-191.|191|191","P10415_F28|mutagenesis site|partial loss of bax-binding and 50% decrease in anti-apoptotic activity; when associated with l-190 and a-191. no effect on homodimerization; when associated with l-190 and a-191.|192|192","P10415_F29|mutagenesis site|loss of bax-binding and of anti-apoptotic activity. may also affect protein stability.|194|197","P10415_F3|region of interest|required for interaction with septin4 isoform arts. required xiap-mediated ubiquitination and apoptosis|92|107","P10415_F30|mutagenesis site|partial loss of bax-binding and 50% decrease in anti-apoptotic activity.|200|200","P10415_F31|sequence conflict|in ref. 4; caa29778.|48|48","P10415_F32|sequence conflict|in ref. 3; aaa35591.|59|59","P10415_F33|sequence conflict|in ref. 10; aad14111.|96|96","P10415_F34|sequence conflict|in ref. 10; aad14111.|110|110","P10415_F35|sequence conflict|in ref. 3; aaa35591.|117|117","P10415_F36|sequence conflict|in ref. 4; caa29778.|129|129","P10415_F37|helix||11|24","P10415_F38|turn||25|27","P10415_F39|helix||31|34","P10415_F4|short sequence motif|bh4|10|30","P10415_F40|helix||50|52","P10415_F41|helix||63|66","P10415_F42|helix||93|107","P10415_F43|helix||109|118","P10415_F44|turn||123|125","P10415_F45|helix||126|137","P10415_F46|turn||138|140","P10415_F47|helix||144|163","P10415_F48|helix||169|184","P10415_F49|helix||186|191","P10415_F5|short sequence motif|bh3|93|107","P10415_F50|helix||194|202","P10415_F51|strand||203|205","P10415_F52|sequence conflict|in ref. 1; aaa51814.|199|199","P10415_F6|short sequence motif|bh1|136|155","P10415_F7|short sequence motif|bh2|187|202","P10415_F8|compositionally biased region|low complexity|75|85","P10415_F9|site|cleavage; by caspase-3|34|35"]}]}