##gff-version 3 P10415 UniProtKB Chain 1 239 . . . ID=PRO_0000143048;Note=Apoptosis regulator Bcl-2 P10415 UniProtKB Transmembrane 212 233 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P10415 UniProtKB Region 39 85 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P10415 UniProtKB Region 92 107 . . . Note=Required for interaction with SEPTIN4 isoform ARTS. Required XIAP-mediated ubiquitination and apoptosis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29020630;Dbxref=PMID:29020630 P10415 UniProtKB Motif 10 30 . . . Note=BH4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00025 P10415 UniProtKB Motif 93 107 . . . Note=BH3;Ontology_term=ECO:0000255;evidence=ECO:0000255 P10415 UniProtKB Motif 136 155 . . . Note=BH1;Ontology_term=ECO:0000255;evidence=ECO:0000255 P10415 UniProtKB Motif 187 202 . . . Note=BH2;Ontology_term=ECO:0000255;evidence=ECO:0000255 P10415 UniProtKB Site 34 35 . . . Note=Cleavage%3B by caspase-3 P10415 UniProtKB Modified residue 69 69 . . . Note=Phosphothreonine%3B by MAPK8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18570871;Dbxref=PMID:18570871 P10415 UniProtKB Modified residue 70 70 . . . Note=Phosphoserine%3B by MAPK8 and PKC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18570871;Dbxref=PMID:18570871 P10415 UniProtKB Modified residue 87 87 . . . Note=Phosphoserine%3B by MAPK8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18570871;Dbxref=PMID:18570871 P10415 UniProtKB Alternative sequence 196 239 . . . ID=VSP_000512;Note=In isoform Beta. DAFVELYGPSMRPLFDFSWLSLKTLLSLALVGACITLGAYLGHK->VGALGDVSLG;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:3523487;Dbxref=PMID:3523487 P10415 UniProtKB Natural variant 7 7 . . . ID=VAR_000827;Note=T->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:2834197,ECO:0000269|PubMed:3285301;Dbxref=PMID:2834197,PMID:3285301 P10415 UniProtKB Natural variant 43 43 . . . ID=VAR_014716;Note=A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.6;Dbxref=dbSNP:rs1800477 P10415 UniProtKB Natural variant 59 59 . . . ID=VAR_000828;Note=In non-Hodgkin lymphoma%3B somatic mutation. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1339299;Dbxref=PMID:1339299 P10415 UniProtKB Natural variant 93 93 . . . ID=VAR_000829;Note=In non-Hodgkin lymphoma%3B somatic mutation. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1339299;Dbxref=PMID:1339299 P10415 UniProtKB Mutagenesis 34 34 . . . Note=Abolishes cleavage by caspase-3. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9395403;Dbxref=PMID:9395403 P10415 UniProtKB Mutagenesis 64 64 . . . Note=No effect on cleavage by caspase-3. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9395403;Dbxref=PMID:9395403 P10415 UniProtKB Mutagenesis 138 141 . . . Note=Loss of BAX-binding and of anti-apoptotic activity. FRDG->AAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8183370;Dbxref=PMID:8183370 P10415 UniProtKB Mutagenesis 144 144 . . . Note=Loss of BAX-binding and of anti-apoptotic activity%3B when associated with A-145 and A146. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8183370;Dbxref=PMID:8183370 P10415 UniProtKB Mutagenesis 145 145 . . . Note=Loss of BAX-binding and of anti-apoptotic activity. No effect on NLRP1-induced IL1B release%2C nor on homodimerization. Loss of BAX-binding and of anti-apoptotic activity%3B when associated with A-145 and A146. G->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17418785,ECO:0000269|PubMed:8183370;Dbxref=PMID:17418785,PMID:8183370 P10415 UniProtKB Mutagenesis 145 145 . . . Note=Loss of BAX-binding and of anti-apoptotic activity. No effect on homodimerization. G->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17418785,ECO:0000269|PubMed:8183370;Dbxref=PMID:17418785,PMID:8183370 P10415 UniProtKB Mutagenesis 146 146 . . . Note=Loss of BAX-binding and of anti-apoptotic activity%3B when associated with A-144 and A145. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8183370;Dbxref=PMID:8183370 P10415 UniProtKB Mutagenesis 188 188 . . . Note=Loss of BAX-binding and of anti-apoptotic activity. No effect on homodimerization. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8183370;Dbxref=PMID:8183370 P10415 UniProtKB Mutagenesis 190 190 . . . Note=Partial loss of BAX-binding and 50%25 decrease in anti-apoptotic activity%3B when associated with A-191 and A-192. No effect on homodimerization%3B when associated with L-190 and A-191. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8183370;Dbxref=PMID:8183370 P10415 UniProtKB Mutagenesis 191 191 . . . Note=No effect on BAX-binding%2C nor on anti-apoptotic activity. Partial loss of BAX-binding and 50%25 decrease in anti-apoptotic activity%3B when associated with L-190 and A-192. No effect on homodimerization%3B when associated with L-190 and A-191. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8183370;Dbxref=PMID:8183370 P10415 UniProtKB Mutagenesis 192 192 . . . Note=Partial loss of BAX-binding and 50%25 decrease in anti-apoptotic activity%3B when associated with L-190 and A-191. No effect on homodimerization%3B when associated with L-190 and A-191. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8183370;Dbxref=PMID:8183370 P10415 UniProtKB Mutagenesis 194 197 . . . Note=Loss of BAX-binding and of anti-apoptotic activity. May also affect protein stability. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8183370;Dbxref=PMID:8183370 P10415 UniProtKB Mutagenesis 200 200 . . . Note=Partial loss of BAX-binding and 50%25 decrease in anti-apoptotic activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8183370;Dbxref=PMID:8183370 P10415 UniProtKB Sequence conflict 48 48 . . . Note=I->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 P10415 UniProtKB Sequence conflict 59 59 . . . Note=P->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 P10415 UniProtKB Sequence conflict 96 96 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 P10415 UniProtKB Sequence conflict 110 110 . . . Note=R->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 P10415 UniProtKB Sequence conflict 117 117 . . . Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 P10415 UniProtKB Sequence conflict 129 129 . . . Note=R->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 P10415 UniProtKB Helix 11 25 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6GL8 P10415 UniProtKB Helix 31 33 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6GL8 P10415 UniProtKB Helix 63 66 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5VAX P10415 UniProtKB Helix 93 98 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6GL8 P10415 UniProtKB Helix 103 107 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6GL8 P10415 UniProtKB Helix 109 119 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6GL8 P10415 UniProtKB Turn 123 125 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6GL8 P10415 UniProtKB Helix 126 138 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6GL8 P10415 UniProtKB Helix 144 163 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6GL8 P10415 UniProtKB Helix 169 184 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6GL8 P10415 UniProtKB Helix 186 191 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6GL8 P10415 UniProtKB Helix 194 202 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6GL8 P10415 UniProtKB Helix 203 205 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5VAX P10415 UniProtKB Sequence conflict 199 199 . . . Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305