##gff-version 3 Q8N6T7 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19413330;Dbxref=PMID:19413330 Q8N6T7 UniProtKB Chain 2 355 . . . ID=PRO_0000110269;Note=NAD-dependent protein deacylase sirtuin-6 Q8N6T7 UniProtKB Domain 27 272 . . . Note=Deacetylase sirtuin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236 Q8N6T7 UniProtKB Region 284 355 . . . Note=Disordered;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33067423;Dbxref=PMID:33067423 Q8N6T7 UniProtKB Active site 133 133 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000305,ECO:0000305,ECO:0000305,ECO:0000305;evidence=ECO:0000255|PROSITE-ProRule:PRU00236,ECO:0000269|PubMed:18337721,ECO:0000305|PubMed:23552949,ECO:0000305|PubMed:23892288,ECO:0000305|PubMed:27322069,ECO:0000305|PubMed:28406396;Dbxref=PMID:18337721,PMID:23552949,PMID:23892288,PMID:27322069,PMID:28406396 Q8N6T7 UniProtKB Binding site 53 53 . . . Ontology_term=ECO:0000305,ECO:0007744,ECO:0007744;evidence=ECO:0000305|PubMed:21362626,ECO:0007744|PDB:3K35,ECO:0007744|PDB:3ZG6;Dbxref=PMID:21362626 Q8N6T7 UniProtKB Binding site 57 57 . . . Ontology_term=ECO:0000269,ECO:0000305,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:23552949,ECO:0000305|PubMed:21362626,ECO:0007744|PDB:3K35,ECO:0007744|PDB:3ZG6;Dbxref=PMID:21362626,PMID:23552949 Q8N6T7 UniProtKB Binding site 64 64 . . . Ontology_term=ECO:0000269,ECO:0000305,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:23552949,ECO:0000305|PubMed:21362626,ECO:0007744|PDB:3K35,ECO:0007744|PDB:3ZG6;Dbxref=PMID:21362626,PMID:23552949 Q8N6T7 UniProtKB Binding site 65 65 . . . Ontology_term=ECO:0000269,ECO:0000305,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:23552949,ECO:0000305|PubMed:21362626,ECO:0007744|PDB:3K35,ECO:0007744|PDB:3ZG6;Dbxref=PMID:21362626,PMID:23552949 Q8N6T7 UniProtKB Binding site 71 71 . . . Ontology_term=ECO:0000269,ECO:0000305,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:23552949,ECO:0000305|PubMed:21362626,ECO:0007744|PDB:3K35,ECO:0007744|PDB:3ZG6;Dbxref=PMID:21362626,PMID:23552949 Q8N6T7 UniProtKB Binding site 113 113 . . . Ontology_term=ECO:0000269,ECO:0000305,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:23552949,ECO:0000305|PubMed:21362626,ECO:0007744|PDB:3K35,ECO:0007744|PDB:3ZG6;Dbxref=PMID:21362626,PMID:23552949 Q8N6T7 UniProtKB Binding site 133 133 . . . Ontology_term=ECO:0000269,ECO:0000305,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:23552949,ECO:0000305|PubMed:21362626,ECO:0007744|PDB:3K35,ECO:0007744|PDB:3ZG6;Dbxref=PMID:21362626,PMID:23552949 Q8N6T7 UniProtKB Binding site 141 141 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU00236,ECO:0000269|PubMed:21362626,ECO:0000269|PubMed:23552949,ECO:0000269|PubMed:27990725,ECO:0007744|PDB:3K35,ECO:0007744|PDB:3PKI,ECO:0007744|PDB:3PKJ,ECO:0007744|PDB:3ZG6,ECO:0007744|PDB:5MF6,ECO:0007744|PDB:5MFP,ECO:0007744|PDB:5MFZ,ECO:0007744|PDB:5MGN;Dbxref=PMID:21362626,PMID:23552949,PMID:27990725 Q8N6T7 UniProtKB Binding site 144 144 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU00236,ECO:0000269|PubMed:21362626,ECO:0000269|PubMed:23552949,ECO:0000269|PubMed:27990725,ECO:0007744|PDB:3K35,ECO:0007744|PDB:3PKI,ECO:0007744|PDB:3PKJ,ECO:0007744|PDB:3ZG6,ECO:0007744|PDB:5MF6,ECO:0007744|PDB:5MFP,ECO:0007744|PDB:5MFZ,ECO:0007744|PDB:5MGN;Dbxref=PMID:21362626,PMID:23552949,PMID:27990725 Q8N6T7 UniProtKB Binding site 166 166 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU00236,ECO:0000269|PubMed:21362626,ECO:0000269|PubMed:23552949,ECO:0000269|PubMed:27990725,ECO:0007744|PDB:3K35,ECO:0007744|PDB:3PKI,ECO:0007744|PDB:3PKJ,ECO:0007744|PDB:3ZG6,ECO:0007744|PDB:5MF6,ECO:0007744|PDB:5MFP,ECO:0007744|PDB:5MFZ,ECO:0007744|PDB:5MGN;Dbxref=PMID:21362626,PMID:23552949,PMID:27990725 Q8N6T7 UniProtKB Binding site 177 177 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU00236,ECO:0000269|PubMed:21362626,ECO:0000269|PubMed:23552949,ECO:0000269|PubMed:27990725,ECO:0007744|PDB:3K35,ECO:0007744|PDB:3PKI,ECO:0007744|PDB:3PKJ,ECO:0007744|PDB:3ZG6,ECO:0007744|PDB:5MF6,ECO:0007744|PDB:5MFP,ECO:0007744|PDB:5MFZ,ECO:0007744|PDB:5MGN;Dbxref=PMID:21362626,PMID:23552949,PMID:27990725 Q8N6T7 UniProtKB Binding site 214 214 . . . Ontology_term=ECO:0000269,ECO:0000305,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:23552949,ECO:0000305|PubMed:21362626,ECO:0007744|PDB:3K35,ECO:0007744|PDB:3ZG6;Dbxref=PMID:21362626,PMID:23552949 Q8N6T7 UniProtKB Binding site 216 216 . . . Ontology_term=ECO:0000269,ECO:0000305,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:23552949,ECO:0000305|PubMed:21362626,ECO:0007744|PDB:3K35,ECO:0007744|PDB:3ZG6;Dbxref=PMID:21362626,PMID:23552949 Q8N6T7 UniProtKB Binding site 240 240 . . . Ontology_term=ECO:0000269,ECO:0000305,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:23552949,ECO:0000305|PubMed:21362626,ECO:0007744|PDB:3K35,ECO:0007744|PDB:3ZG6;Dbxref=PMID:21362626,PMID:23552949 Q8N6T7 UniProtKB Binding site 242 242 . . . Ontology_term=ECO:0000269,ECO:0000305,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:23552949,ECO:0000305|PubMed:21362626,ECO:0007744|PDB:3K35,ECO:0007744|PDB:3ZG6;Dbxref=PMID:21362626,PMID:23552949 Q8N6T7 UniProtKB Binding site 258 258 . . . Ontology_term=ECO:0000269,ECO:0000305,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:23552949,ECO:0000305|PubMed:21362626,ECO:0007744|PDB:3K35,ECO:0007744|PDB:3ZG6;Dbxref=PMID:21362626,PMID:23552949 Q8N6T7 UniProtKB Site 18 18 . . . Note=Formation of an covalent adduct with nitro-fatty acid activators;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33122195;Dbxref=PMID:33122195 Q8N6T7 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19413330;Dbxref=PMID:19413330 Q8N6T7 UniProtKB Modified residue 10 10 . . . Note=Phosphoserine%3B by MAPK8;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:27568560,ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163,PMID:27568560 Q8N6T7 UniProtKB Modified residue 33 33 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32538779;Dbxref=PMID:32538779 Q8N6T7 UniProtKB Modified residue 294 294 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 Q8N6T7 UniProtKB Modified residue 303 303 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:23186163 Q8N6T7 UniProtKB Modified residue 330 330 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q8N6T7 UniProtKB Cross-link 170 170 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24043303;Dbxref=PMID:24043303 Q8N6T7 UniProtKB Alternative sequence 179 205 . . . ID=VSP_008733;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 Q8N6T7 UniProtKB Natural variant 25 25 . . . ID=VAR_086083;Note=Found in non-small cell lung cancer%3B somatic mutation%3B reduced localization to chromatin%3B reduced histone deacetylase activity%3B does not affect the protein-lysine demyristoylase activity. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26456828;Dbxref=dbSNP:rs752121167,PMID:26456828 Q8N6T7 UniProtKB Natural variant 36 36 . . . ID=VAR_086084;Note=Found in kidney cancer%3B somatic mutation%3B reduced histone deacetylase activity%3B does not affect the protein-lysine demyristoylase activity. E->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26456828;Dbxref=PMID:26456828 Q8N6T7 UniProtKB Natural variant 46 46 . . . ID=VAR_017154;Note=Does not affect histone deacetylase activity. S->N;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14702039,ECO:0000269|PubMed:15489334,ECO:0000269|PubMed:26456828,ECO:0000269|Ref.5;Dbxref=dbSNP:rs352493,PMID:14702039,PMID:15489334,PMID:26456828 Q8N6T7 UniProtKB Natural variant 63 63 . . . ID=VAR_086085;Note=Found in a family presenting with four cases of perinatal lethality caused by severe neurodevelopmental and cardiac anomalies%3B abolished histone deacetylase activity%3B abolished protein demyristoylase activity%3B decreased ability to recognize and bind double-strand breaks (DSBs) sites%3B does not affect nuclear localization. D->H;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:29555651,ECO:0000269|PubMed:31995034;Dbxref=dbSNP:rs779174928,PMID:29555651,PMID:31995034 Q8N6T7 UniProtKB Natural variant 63 63 . . . ID=VAR_086086;Note=Found in non-small cell lung cancer%3B somatic mutation%3B does not affect ability to recognize and bind double-strand breaks (DSBs) sites%3B strongly reduced histone deacetylase activity%3B strongly reduced the protein-lysine demyristoylase activity. D->Y;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:26456828,ECO:0000269|PubMed:31995034;Dbxref=PMID:26456828,PMID:31995034 Q8N6T7 UniProtKB Natural variant 89 89 . . . ID=VAR_086087;Note=Found in non-small cell lung cancer%3B somatic mutation%3B reduced histone deacetylase activity%3B does not affect the protein-lysine demyristoylase activity. A->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26456828;Dbxref=PMID:26456828 Q8N6T7 UniProtKB Natural variant 116 116 . . . ID=VAR_086088;Note=Found in non-small cell lung cancer%3B somatic mutation%3B reduced localization to chromatin%3B strongly reduced histone deacetylase activity%3B strongly reduced the protein-lysine demyristoylase activity. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26456828;Dbxref=dbSNP:rs964309225,PMID:26456828 Q8N6T7 UniProtKB Natural variant 260 355 . . . ID=VAR_086089;Note=Found in non-small cell lung cancer%3B somatic mutation%3B reduced localization to chromatin. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26456828;Dbxref=PMID:26456828 Q8N6T7 UniProtKB Natural variant 263 263 . . . ID=VAR_086090;Note=Found in cervical cancer%3B somatic mutation%3B reduced histone deacetylase activity%3B slightly reduced the protein-lysine demyristoylase activity. T->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26456828;Dbxref=dbSNP:rs1259485520,PMID:26456828 Q8N6T7 UniProtKB Natural variant 274 274 . . . ID=VAR_086091;Note=Found in melanoma%3B somatic mutation%3B reduced histone deacetylase activity%3B does not affect the protein-lysine demyristoylase activity. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26456828;Dbxref=PMID:26456828 Q8N6T7 UniProtKB Mutagenesis 10 10 . . . Note=Abolishes ability to promote DNA repair and recruit PARP1 to double-strand breaks (DSBs). S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27568560;Dbxref=PMID:27568560 Q8N6T7 UniProtKB Mutagenesis 10 10 . . . Note=Mimics phosphorylation%3B increased ability to promote DNA repair and recruit PARP1 to double-strand breaks (DSBs). S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27568560;Dbxref=PMID:27568560 Q8N6T7 UniProtKB Mutagenesis 13 13 . . . Note=Increased protein-lysine demyristoylase activity. A->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31995034;Dbxref=PMID:31995034 Q8N6T7 UniProtKB Mutagenesis 15 15 . . . Note=Does not affect acetylation level. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32538779;Dbxref=PMID:32538779 Q8N6T7 UniProtKB Mutagenesis 17 17 . . . Note=Does not affect acetylation level. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32538779;Dbxref=PMID:32538779 Q8N6T7 UniProtKB Mutagenesis 33 33 . . . Note=Mimics acetylation%2C leading to impaired ability to recognize and bind double-strand breaks (DSBs) sites. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32538779;Dbxref=PMID:32538779 Q8N6T7 UniProtKB Mutagenesis 33 33 . . . Note=Decreased acetylation level. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32538779;Dbxref=PMID:32538779 Q8N6T7 UniProtKB Mutagenesis 45 45 . . . Note=In AAA mutant%3B strongly decreased nucleosome-binding%3B when associated with 206-A--A-208. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33067423;Dbxref=PMID:33067423 Q8N6T7 UniProtKB Mutagenesis 56 56 . . . Note=Abolished NAD-dependent protein deacetylase%2C defatty-acylase and mono-ADP-ribosyltransferase activities. S->Y;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:21680843,ECO:0000269|PubMed:22753495,ECO:0000269|PubMed:27322069,ECO:0000269|PubMed:32789493;Dbxref=PMID:21680843,PMID:22753495,PMID:27322069,PMID:32789493 Q8N6T7 UniProtKB Mutagenesis 60 60 . . . Note=Does not affect the NAD-dependent protein defatty-acylase activity. Abolished NAD-dependent protein deacetylase and mono-ADP-ribosyltransferase activities. G->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:21680843,ECO:0000269|PubMed:22753495,ECO:0000269|PubMed:27322069,ECO:0000269|PubMed:28406396;Dbxref=PMID:21680843,PMID:22753495,PMID:27322069,PMID:28406396 Q8N6T7 UniProtKB Mutagenesis 65 65 . . . Note=Does not affect the mono-ADP-ribosyltransferase activity. Abolished NAD-dependent protein deacetylase and defatty-acylase activities. R->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:21680843,ECO:0000269|PubMed:22753495,ECO:0000269|PubMed:27322069;Dbxref=PMID:21680843,PMID:22753495,PMID:27322069 Q8N6T7 UniProtKB Mutagenesis 82 82 . . . Note=Reduced MDL-800 and MDL-801 compounds-binding. F->A%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30374165;Dbxref=PMID:30374165 Q8N6T7 UniProtKB Mutagenesis 86 86 . . . Note=Strongly reduced MDL-800 and MDL-801 compounds-binding. F->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30374165;Dbxref=PMID:30374165 Q8N6T7 UniProtKB Mutagenesis 86 86 . . . Note=Slightly reduced MDL-800 and MDL-801 compounds-binding. F->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30374165;Dbxref=PMID:30374165 Q8N6T7 UniProtKB Mutagenesis 133 133 . . . Note=Abolished NAD-dependent protein deacetylase%2C deacylase and mono-ADP-ribosyltransferase activities. Impaired ability to recognize and bind double-strand breaks (DSBs) sites. H->Y;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18337721,ECO:0000269|PubMed:23142079,ECO:0000269|PubMed:23552949,ECO:0000269|PubMed:23892288,ECO:0000269|PubMed:23911928,ECO:0000269|PubMed:26787900,ECO:0000269|PubMed:27043296,ECO:0000269|PubMed:27322069,ECO:0000269|PubMed:28406396,ECO:0000269|PubMed:29474172,ECO:0000269|PubMed:31995034,ECO:0000269|PubMed:32538779,ECO:0000269|PubMed:32789493;Dbxref=PMID:18337721,PMID:23142079,PMID:23552949,PMID:23892288,PMID:23911928,PMID:26787900,PMID:27043296,PMID:27322069,PMID:28406396,PMID:29474172,PMID:31995034,PMID:32538779,PMID:32789493 Q8N6T7 UniProtKB Mutagenesis 170 170 . . . Note=Decreased ubiquitination. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24043303;Dbxref=PMID:24043303 Q8N6T7 UniProtKB Mutagenesis 206 208 . . . Note=In AAA mutant%3B strongly decreased nucleosome-binding%3B when associated with A-45. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33067423;Dbxref=PMID:33067423 Q8N6T7 UniProtKB Mutagenesis 294 294 . . . Note=Does not affect ability to promote DNA repair. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27568560;Dbxref=PMID:27568560 Q8N6T7 UniProtKB Mutagenesis 296 300 . . . Note=In 4KR mutant%3B abolished sumoylation%2C leading to increased H3K56ac%3B when associated with R-316 and R-332. KLEPK->RLEPR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26898756;Dbxref=PMID:26898756 Q8N6T7 UniProtKB Mutagenesis 303 303 . . . Note=Does not affect ability to promote DNA repair. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27568560;Dbxref=PMID:27568560 Q8N6T7 UniProtKB Mutagenesis 316 316 . . . Note=In 4KR mutant%3B abolished sumoylation%2C leading to increased H3K56ac%3B when associated with 296-R--R-300 and R-332. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26898756;Dbxref=PMID:26898756 Q8N6T7 UniProtKB Mutagenesis 330 330 . . . Note=Does not affect ability to promote DNA repair. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27568560;Dbxref=PMID:27568560 Q8N6T7 UniProtKB Mutagenesis 332 332 . . . Note=In 4KR mutant%3B abolished sumoylation%2C leading to increased H3K56ac%3B when associated with 296-R--R-300 and R-316. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26898756;Dbxref=PMID:26898756 Q8N6T7 UniProtKB Mutagenesis 338 338 . . . Note=Does not affect ability to promote DNA repair. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27568560;Dbxref=PMID:27568560 Q8N6T7 UniProtKB Sequence conflict 42 42 . . . Note=W->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q8N6T7 UniProtKB Sequence conflict 249 249 . . . Note=H->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q8N6T7 UniProtKB Sequence conflict 267 267 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q8N6T7 UniProtKB Helix 5 9 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6XV6 Q8N6T7 UniProtKB Turn 10 12 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6XV6 Q8N6T7 UniProtKB Helix 27 43 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6HOY Q8N6T7 UniProtKB Beta strand 45 51 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6HOY Q8N6T7 UniProtKB Helix 53 55 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6HOY Q8N6T7 UniProtKB Helix 57 59 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6HOY Q8N6T7 UniProtKB Beta strand 64 66 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6HOY Q8N6T7 UniProtKB Helix 70 75 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6HOY Q8N6T7 UniProtKB Turn 86 88 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6HOY Q8N6T7 UniProtKB Helix 93 103 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6HOY Q8N6T7 UniProtKB Beta strand 108 112 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6HOY Q8N6T7 UniProtKB Helix 118 121 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6HOY Q8N6T7 UniProtKB Beta strand 122 125 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3PKI Q8N6T7 UniProtKB Helix 126 128 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6HOY Q8N6T7 UniProtKB Beta strand 129 131 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6HOY Q8N6T7 UniProtKB Beta strand 138 141 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6HOY Q8N6T7 UniProtKB Turn 142 144 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6HOY Q8N6T7 UniProtKB Beta strand 147 149 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6HOY Q8N6T7 UniProtKB Beta strand 161 165 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6HOY Q8N6T7 UniProtKB Turn 171 174 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5X16 Q8N6T7 UniProtKB Beta strand 180 183 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6HOY Q8N6T7 UniProtKB Beta strand 188 190 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3PKJ Q8N6T7 UniProtKB Helix 194 206 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6HOY Q8N6T7 UniProtKB Beta strand 208 214 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6HOY Q8N6T7 UniProtKB Helix 222 224 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6HOY Q8N6T7 UniProtKB Helix 225 228 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6HOY Q8N6T7 UniProtKB Helix 229 233 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6HOY Q8N6T7 UniProtKB Beta strand 235 239 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6HOY Q8N6T7 UniProtKB Helix 247 249 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6HOY Q8N6T7 UniProtKB Beta strand 251 254 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6HOY Q8N6T7 UniProtKB Helix 258 269 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6HOY Q8N6T7 UniProtKB Beta strand 278 280 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6HOY Q8N6T7 UniProtKB Beta strand 282 284 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6XV1