##gff-version 3 Q8IXJ6 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19413330;Dbxref=PMID:19413330 Q8IXJ6 UniProtKB Chain 2 389 . . . ID=PRO_0000110258;Note=NAD-dependent protein deacetylase sirtuin-2 Q8IXJ6 UniProtKB Domain 57 338 . . . Note=Deacetylase sirtuin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236 Q8IXJ6 UniProtKB Region 1 34 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8IXJ6 UniProtKB Region 351 389 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8IXJ6 UniProtKB Motif 41 51 . . . Note=Nuclear export signal Q8IXJ6 UniProtKB Compositional bias 374 389 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8IXJ6 UniProtKB Active site 187 187 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236 Q8IXJ6 UniProtKB Binding site 85 89 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:25672491,ECO:0007744|PDB:4RMG;Dbxref=PMID:25672491 Q8IXJ6 UniProtKB Binding site 95 97 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:25672491,ECO:0007744|PDB:4RMG;Dbxref=PMID:25672491 Q8IXJ6 UniProtKB Binding site 167 170 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:25672491,ECO:0007744|PDB:4RMG;Dbxref=PMID:25672491 Q8IXJ6 UniProtKB Binding site 195 195 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU00236,ECO:0000269|PubMed:11427894,ECO:0000269|PubMed:23454361,ECO:0000269|PubMed:24389023,ECO:0000269|PubMed:25672491,ECO:0000269|PubMed:25704306,ECO:0007744|PDB:4R8M;Dbxref=PMID:11427894,PMID:23454361,PMID:24389023,PMID:25672491,PMID:25704306 Q8IXJ6 UniProtKB Binding site 200 200 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU00236,ECO:0000269|PubMed:11427894,ECO:0000269|PubMed:23454361,ECO:0000269|PubMed:24389023,ECO:0000269|PubMed:25672491,ECO:0000269|PubMed:25704306,ECO:0007744|PDB:4R8M;Dbxref=PMID:11427894,PMID:23454361,PMID:24389023,PMID:25672491,PMID:25704306 Q8IXJ6 UniProtKB Binding site 221 221 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU00236,ECO:0000269|PubMed:11427894,ECO:0000269|PubMed:23454361,ECO:0000269|PubMed:24389023,ECO:0000269|PubMed:25672491,ECO:0000269|PubMed:25704306,ECO:0007744|PDB:4R8M;Dbxref=PMID:11427894,PMID:23454361,PMID:24389023,PMID:25672491,PMID:25704306 Q8IXJ6 UniProtKB Binding site 224 224 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU00236,ECO:0000269|PubMed:11427894,ECO:0000269|PubMed:23454361,ECO:0000269|PubMed:24389023,ECO:0000269|PubMed:25672491,ECO:0000269|PubMed:25704306,ECO:0007744|PDB:4R8M;Dbxref=PMID:11427894,PMID:23454361,PMID:24389023,PMID:25672491,PMID:25704306 Q8IXJ6 UniProtKB Binding site 262 263 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:25672491,ECO:0007744|PDB:4RMG;Dbxref=PMID:25672491 Q8IXJ6 UniProtKB Binding site 286 288 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:25672491,ECO:0007744|PDB:4RMG;Dbxref=PMID:25672491 Q8IXJ6 UniProtKB Binding site 324 324 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:25672491,ECO:0007744|PDB:4RMG;Dbxref=PMID:25672491 Q8IXJ6 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19413330;Dbxref=PMID:19413330 Q8IXJ6 UniProtKB Modified residue 23 23 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 Q8IXJ6 UniProtKB Modified residue 25 25 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 Q8IXJ6 UniProtKB Modified residue 27 27 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 Q8IXJ6 UniProtKB Modified residue 53 53 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5RJQ4 Q8IXJ6 UniProtKB Modified residue 100 100 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5RJQ4 Q8IXJ6 UniProtKB Modified residue 207 207 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5RJQ4 Q8IXJ6 UniProtKB Modified residue 368 368 . . . Note=Phosphoserine%3B by CDK2 and CDK5;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:17488717,ECO:0000269|PubMed:17516032,ECO:0000269|PubMed:18332217,ECO:0007744|PubMed:23186163;Dbxref=PMID:17488717,PMID:17516032,PMID:18332217,PMID:23186163 Q8IXJ6 UniProtKB Modified residue 372 372 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17516032;Dbxref=PMID:17516032 Q8IXJ6 UniProtKB Alternative sequence 1 38 . . . ID=VSP_008726;Note=In isoform 3. MAEPDPSHPLETQAGKVQEAQDSDSDSEGGAAGGEADM->MPLAECPSCRCLSSFRSV;Ontology_term=ECO:0000303;evidence=ECO:0000303|Ref.5 Q8IXJ6 UniProtKB Alternative sequence 1 37 . . . ID=VSP_008724;Note=In isoform 2. Missing;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:10393250,ECO:0000303|PubMed:10931946,ECO:0000303|PubMed:12065666,ECO:0000303|PubMed:14702039,ECO:0000303|PubMed:15489334;Dbxref=PMID:10393250,PMID:10931946,PMID:12065666,PMID:14702039,PMID:15489334 Q8IXJ6 UniProtKB Alternative sequence 6 76 . . . ID=VSP_055328;Note=In isoform 5. PSHPLETQAGKVQEAQDSDSDSEGGAAGGEADMDFLRNLFSQTLSLGSQKERLLDELTLEGVARYMQSERC->R;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:24177535;Dbxref=PMID:24177535 Q8IXJ6 UniProtKB Alternative sequence 266 271 . . . ID=VSP_008727;Note=In isoform 4. VQPFAS->GRGLAG;Ontology_term=ECO:0000303;evidence=ECO:0000303|Ref.10 Q8IXJ6 UniProtKB Alternative sequence 272 389 . . . ID=VSP_008728;Note=In isoform 4. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|Ref.10 Q8IXJ6 UniProtKB Mutagenesis 53 53 . . . Note=Reduces deacetylase activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17516032;Dbxref=PMID:17516032 Q8IXJ6 UniProtKB Mutagenesis 97 97 . . . Note=No effect on deacetylase activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11427894;Dbxref=PMID:11427894 Q8IXJ6 UniProtKB Mutagenesis 98 98 . . . Note=Inhibits deacetylase activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17516032;Dbxref=PMID:17516032 Q8IXJ6 UniProtKB Mutagenesis 100 100 . . . Note=Reduces deacetylase activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17516032;Dbxref=PMID:17516032 Q8IXJ6 UniProtKB Mutagenesis 116 116 . . . Note=Reduces binding for the peptide inhibitor S2iL5. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24389023;Dbxref=PMID:24389023 Q8IXJ6 UniProtKB Mutagenesis 120 120 . . . Note=Reduces binding for the peptide inhibitor S2iL5. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24389023;Dbxref=PMID:24389023 Q8IXJ6 UniProtKB Mutagenesis 167 167 . . . Note=Reduces deacetylase activity. Inhibits the block of entry to chromosome condensation and subsequent hyperploidy cell formation in response to mitotic stress%3B when associated with A-168 and A-187. Q->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11427894,ECO:0000269|PubMed:16909107;Dbxref=PMID:11427894,PMID:16909107 Q8IXJ6 UniProtKB Mutagenesis 168 168 . . . Note=Abolishes deacetylation of alpha-tubulin. Inhibits deacetylation of histone H3 at 'Lys-18'. Inhibits the block of entry to chromosome condensation and subsequent hyperploidy cell formation in response to mitotic stress%3B when associated with A-167 and A-187. N->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11427894,ECO:0000269|PubMed:12620231,ECO:0000269|PubMed:16909107,ECO:0000269|PubMed:23908241,ECO:0000269|PubMed:24769394;Dbxref=PMID:11427894,PMID:12620231,PMID:16909107,PMID:23908241,PMID:24769394 Q8IXJ6 UniProtKB Mutagenesis 170 170 . . . Note=Reduces deacetylase activity. D->A%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11427894;Dbxref=PMID:11427894 Q8IXJ6 UniProtKB Mutagenesis 187 187 . . . Note=Inhibits deacetylase activity toward histone%2C alpha-tubulin%2C FZR1 and CDC20. No effect on CDK2-dependent phosphorylation. Does not inhibit interaction with alpha-tubulin%2C HDAC6%2C HIF1A and the cyclin E-CDK2 complex. Inhibits interaction with BEX4 and KMT5A. Abolishes deacetylation%2C dimeric formation and enzymatic activity increase of G6PD. Prevents histone H4 methylation at 'Lys-20'(H4K20me1) in metaphase chromosomes. Inhibits the block of entry to chromosome condensation and subsequent hyperploidy cell formation in response to mitotic stress%3B when associated with A-167 and A-168. Strongly reduced activity toward long-chain fatty acyl groups. H->Y%2CA;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:10381378,ECO:0000269|PubMed:11427894,ECO:0000269|PubMed:11812793,ECO:0000269|PubMed:12620231,ECO:0000269|PubMed:12697818,ECO:0000269|PubMed:16909107,ECO:0000269|PubMed:17488717,ECO:0000269|PubMed:17516032,ECO:0000269|PubMed:17726514,ECO:0000269|PubMed:22014574,ECO:0000269|PubMed:24681946,ECO:0000269|PubMed:27512957,ECO:0000269|PubMed:29239724;Dbxref=PMID:10381378,PMID:11427894,PMID:11812793,PMID:12620231,PMID:12697818,PMID:16909107,PMID:17488717,PMID:17516032,PMID:17726514,PMID:22014574,PMID:24681946,PMID:27512957,PMID:29239724 Q8IXJ6 UniProtKB Mutagenesis 244 244 . . . Note=Strongly reduces binding for the peptide inhibitor S2iL5. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24389023;Dbxref=PMID:24389023 Q8IXJ6 UniProtKB Mutagenesis 265 265 . . . Note=Reduces binding for the peptide inhibitor S2iL5. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24389023;Dbxref=PMID:24389023 Q8IXJ6 UniProtKB Mutagenesis 271 271 . . . Note=Reduces binding for the peptide inhibitor S2iL5. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24389023;Dbxref=PMID:24389023 Q8IXJ6 UniProtKB Mutagenesis 279 279 . . . Note=Reduces deacetylase activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17516032;Dbxref=PMID:17516032 Q8IXJ6 UniProtKB Mutagenesis 280 280 . . . Note=Reduces deacetylase activity. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17516032;Dbxref=PMID:17516032 Q8IXJ6 UniProtKB Mutagenesis 294 294 . . . Note=Reduces binding for the peptide inhibitor S2iL5. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24389023;Dbxref=PMID:24389023 Q8IXJ6 UniProtKB Mutagenesis 311 311 . . . Note=Reduces deacetylase activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17516032;Dbxref=PMID:17516032 Q8IXJ6 UniProtKB Mutagenesis 315 315 . . . Note=Reduces deacetylase activity. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17516032;Dbxref=PMID:17516032 Q8IXJ6 UniProtKB Mutagenesis 364 364 . . . Note=Abolishes CDK2-dependent phosphorylation. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17516032;Dbxref=PMID:17516032 Q8IXJ6 UniProtKB Mutagenesis 368 368 . . . Note=Does not affect deacetylase activity. Abolishes CDK2-dependent phosphorylation. Inhibits cellular proliferation delay in the early metaphase to prevent chromosomal instability. Does not inhibit interaction with a cyclin E-CDK2 complex. Does not inhibit interaction with HDAC6 and ubiquitination. Inhibits cell adhesion and migration and neurite outgrowth. Inhibits deacetylase activity%3B when associated with A-372. S->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17488717,ECO:0000269|PubMed:17516032,ECO:0000269|PubMed:18332217;Dbxref=PMID:17488717,PMID:17516032,PMID:18332217 Q8IXJ6 UniProtKB Mutagenesis 368 368 . . . Note=Abolishes CDK2-dependent phosphorylation. Inhibits interaction with a cyclin E-CDK2 complex. Reduces strongly histone deacetylation activity. S->D;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17488717,ECO:0000269|PubMed:17516032,ECO:0000269|PubMed:18332217;Dbxref=PMID:17488717,PMID:17516032,PMID:18332217 Q8IXJ6 UniProtKB Mutagenesis 368 368 . . . Note=Abolishes CDK2-dependent phosphorylation. S->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17488717,ECO:0000269|PubMed:17516032,ECO:0000269|PubMed:18332217;Dbxref=PMID:17488717,PMID:17516032,PMID:18332217 Q8IXJ6 UniProtKB Mutagenesis 372 372 . . . Note=Reduces phosphorylation. Does not inhibit interaction with HDAC6%2C ubiquitination and deacetylase activity. Inhibits deacetylase activity%3B when associated with A-368. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17516032;Dbxref=PMID:17516032 Q8IXJ6 UniProtKB Sequence conflict 199 199 . . . Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q8IXJ6 UniProtKB Sequence conflict 219 219 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q8IXJ6 UniProtKB Helix 35 45 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZGO Q8IXJ6 UniProtKB Beta strand 60 63 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RMH Q8IXJ6 UniProtKB Helix 64 71 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RMH Q8IXJ6 UniProtKB Beta strand 73 75 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L66 Q8IXJ6 UniProtKB Beta strand 79 83 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RMH Q8IXJ6 UniProtKB Helix 85 87 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RMH Q8IXJ6 UniProtKB Helix 89 91 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RMH Q8IXJ6 UniProtKB Beta strand 96 98 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RMI Q8IXJ6 UniProtKB Helix 99 101 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RMH Q8IXJ6 UniProtKB Helix 103 105 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4X3O Q8IXJ6 UniProtKB Helix 108 110 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4X3O Q8IXJ6 UniProtKB Helix 115 119 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RMH Q8IXJ6 UniProtKB Helix 121 126 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RMH Q8IXJ6 UniProtKB Helix 129 138 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RMH Q8IXJ6 UniProtKB Beta strand 139 142 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZGO Q8IXJ6 UniProtKB Helix 147 157 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RMH Q8IXJ6 UniProtKB Beta strand 161 166 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RMH Q8IXJ6 UniProtKB Helix 172 175 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RMH Q8IXJ6 UniProtKB Helix 180 182 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RMH Q8IXJ6 UniProtKB Beta strand 183 185 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RMH Q8IXJ6 UniProtKB Beta strand 188 196 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RMH Q8IXJ6 UniProtKB Turn 198 200 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RMH Q8IXJ6 UniProtKB Beta strand 203 205 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RMH Q8IXJ6 UniProtKB Helix 206 215 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RMH Q8IXJ6 UniProtKB Turn 222 224 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RMH Q8IXJ6 UniProtKB Beta strand 227 232 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RMH Q8IXJ6 UniProtKB Helix 241 250 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RMH Q8IXJ6 UniProtKB Turn 251 253 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RMI Q8IXJ6 UniProtKB Beta strand 255 261 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RMH Q8IXJ6 UniProtKB Beta strand 264 266 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5Y0Z Q8IXJ6 UniProtKB Helix 269 275 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RMH Q8IXJ6 UniProtKB Beta strand 282 288 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RMH Q8IXJ6 UniProtKB Turn 295 297 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4X3O Q8IXJ6 UniProtKB Helix 301 303 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5DY4 Q8IXJ6 UniProtKB Beta strand 309 311 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RMH Q8IXJ6 UniProtKB Beta strand 316 322 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RMH Q8IXJ6 UniProtKB Helix 324 334 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RMH Q8IXJ6 UniProtKB Helix 338 353 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4RMH