##gff-version 3 Q923E4 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96EB6 Q923E4 UniProtKB Chain 2 737 . . . ID=PRO_0000110257;Note=NAD-dependent protein deacetylase sirtuin-1 Q923E4 UniProtKB Chain 2 525 . . . ID=PRO_0000415290;Note=SirtT1 75 kDa fragment;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96EB6 Q923E4 UniProtKB Domain 228 488 . . . Note=Deacetylase sirtuin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236 Q923E4 UniProtKB Region 1 56 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q923E4 UniProtKB Region 2 268 . . . Note=Interaction with H1-4;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96EB6 Q923E4 UniProtKB Region 2 131 . . . Note=Interaction with CLOCK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18662547;Dbxref=PMID:18662547 Q923E4 UniProtKB Region 75 125 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q923E4 UniProtKB Region 135 533 . . . Note=Interaction with CCAR2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96EB6 Q923E4 UniProtKB Region 152 171 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q923E4 UniProtKB Region 248 251 . . . Note=Required for interaction with the sumoylated form of CCAR2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96EB6 Q923E4 UniProtKB Region 514 539 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q923E4 UniProtKB Region 653 713 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q923E4 UniProtKB Motif 32 39 . . . Note=Nuclear localization signal Q923E4 UniProtKB Motif 138 145 . . . Note=Nuclear export signal Q923E4 UniProtKB Motif 223 230 . . . Note=Nuclear localization signal Q923E4 UniProtKB Motif 425 431 . . . Note=Nuclear export signal Q923E4 UniProtKB Compositional bias 28 42 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q923E4 UniProtKB Compositional bias 524 539 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q923E4 UniProtKB Compositional bias 653 676 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q923E4 UniProtKB Compositional bias 677 691 . . . Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q923E4 UniProtKB Active site 355 355 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00236,ECO:0000269|PubMed:11672522,ECO:0000269|PubMed:12887892,ECO:0000269|PubMed:15220471,ECO:0000269|PubMed:16892051;Dbxref=PMID:11672522,PMID:12887892,PMID:15220471,PMID:16892051 Q923E4 UniProtKB Binding site 253 272 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8IXJ6 Q923E4 UniProtKB Binding site 337 340 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8IXJ6 Q923E4 UniProtKB Binding site 363 363 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236 Q923E4 UniProtKB Binding site 366 366 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236 Q923E4 UniProtKB Binding site 387 387 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236 Q923E4 UniProtKB Binding site 390 390 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236 Q923E4 UniProtKB Binding site 432 434 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8IXJ6 Q923E4 UniProtKB Binding site 457 459 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8IXJ6 Q923E4 UniProtKB Binding site 474 474 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q923E4 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96EB6 Q923E4 UniProtKB Modified residue 14 14 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96EB6 Q923E4 UniProtKB Modified residue 25 25 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96EB6 Q923E4 UniProtKB Modified residue 46 46 . . . Note=Phosphoserine%3B by MAPK8;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96EB6 Q923E4 UniProtKB Modified residue 151 151 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q923E4 UniProtKB Modified residue 154 154 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q923E4 UniProtKB Modified residue 164 164 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96EB6 Q923E4 UniProtKB Modified residue 165 165 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96EB6 Q923E4 UniProtKB Modified residue 230 230 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28923965;Dbxref=PMID:28923965 Q923E4 UniProtKB Modified residue 369 369 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28923965;Dbxref=PMID:28923965 Q923E4 UniProtKB Modified residue 387 387 . . . Note=S-nitrosocysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20972425;Dbxref=PMID:20972425 Q923E4 UniProtKB Modified residue 390 390 . . . Note=S-nitrosocysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20972425;Dbxref=PMID:20972425 Q923E4 UniProtKB Modified residue 422 422 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:28923965;Dbxref=PMID:28923965 Q923E4 UniProtKB Modified residue 505 505 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:28923965;Dbxref=PMID:28923965 Q923E4 UniProtKB Modified residue 522 522 . . . Note=Phosphothreonine%3B by DYRK1A%2C DYRK3 and MAPK8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20167603;Dbxref=PMID:20167603 Q923E4 UniProtKB Modified residue 527 527 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96EB6 Q923E4 UniProtKB Modified residue 536 536 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96EB6 Q923E4 UniProtKB Modified residue 600 600 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:28923965;Dbxref=PMID:28923965 Q923E4 UniProtKB Modified residue 649 649 . . . Note=Phosphoserine%3B by CaMK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19680552;Dbxref=PMID:19680552 Q923E4 UniProtKB Modified residue 651 651 . . . Note=Phosphoserine%3B by CaMK2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96EB6 Q923E4 UniProtKB Modified residue 737 737 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96EB6 Q923E4 UniProtKB Alternative sequence 446 629 . . . ID=VSP_042190;Note=In isoform 2. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q923E4 UniProtKB Mutagenesis 37 38 . . . Note=Abolishes nuclear localization%3B when associated with A-227%3B A-228%3B A-229 and A-230. RR->AA Q923E4 UniProtKB Mutagenesis 138 145 . . . Note=Abolishes nuclear export%3B when associated with A-425%3B A-427%3B A-428%3B A-429%3B A-430 and A-431. LLLTDGLL->AAATGAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17197703;Dbxref=PMID:17197703 Q923E4 UniProtKB Mutagenesis 154 154 . . . Note=Abolishes in vitro phosphorylation by CaMK2%3B when associated with A-649%3B A-651 and A-683. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19680552;Dbxref=PMID:19680552 Q923E4 UniProtKB Mutagenesis 227 230 . . . Note=Abolishes nuclear localization%3B when associated with A-37 and A-38. KKRK->AAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17197703;Dbxref=PMID:17197703 Q923E4 UniProtKB Mutagenesis 230 230 . . . Note=Decreased acetylation%2C leading to increased protein deacetylase activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28923965;Dbxref=PMID:28923965 Q923E4 UniProtKB Mutagenesis 261 261 . . . Note=Abolished ADP-ribosyltransferase activity in vitro without affecting the NAD-dependent protein deacetylase activity. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15716268;Dbxref=PMID:15716268 Q923E4 UniProtKB Mutagenesis 355 355 . . . Note=Loss of deacetylation activity. Loss of inhibition of E2F1 and loss of coactivation of FOXO1-mediated transcription. H->Y;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11672522,ECO:0000269|PubMed:12887892,ECO:0000269|PubMed:15220471,ECO:0000269|PubMed:16892051;Dbxref=PMID:11672522,PMID:12887892,PMID:15220471,PMID:16892051 Q923E4 UniProtKB Mutagenesis 363 363 . . . Note=Does not affect S-nitrosylation. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20972425;Dbxref=PMID:20972425 Q923E4 UniProtKB Mutagenesis 366 366 . . . Note=Does not affect S-nitrosylation. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20972425;Dbxref=PMID:20972425 Q923E4 UniProtKB Mutagenesis 369 369 . . . Note=Does not affect protein deacetylase activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28923965;Dbxref=PMID:28923965 Q923E4 UniProtKB Mutagenesis 387 387 . . . Note=Impairs S-nitrosylation. Abolishes S-nitrosylation%3B when associated with S-390. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20972425;Dbxref=PMID:20972425 Q923E4 UniProtKB Mutagenesis 390 390 . . . Note=Impairs S-nitrosylation. Abolishes S-nitrosylation%3B when associated with S-387. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20972425;Dbxref=PMID:20972425 Q923E4 UniProtKB Mutagenesis 425 431 . . . Note=Abolishes nuclear export%3B when associated with A-138%3B A-139%3B A-140%3B A-144 and A-145. VDLLIVI->ADAAAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17197703;Dbxref=PMID:17197703 Q923E4 UniProtKB Mutagenesis 505 505 . . . Note=Does not affect protein deacetylase activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28923965;Dbxref=PMID:28923965 Q923E4 UniProtKB Mutagenesis 522 522 . . . Note=Increased deacetylase activity toward p53/TP53 and increases resistance to genotoxic stress (mimicks residue phosphorylation). T->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20167603;Dbxref=PMID:20167603 Q923E4 UniProtKB Mutagenesis 522 522 . . . Note=Reduces phosphorylation. Impairs deacetylase activity toward p53/TP53 and decreases resistance to genotoxic stress. Does not change nuclear localization. T->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20167603;Dbxref=PMID:20167603 Q923E4 UniProtKB Mutagenesis 600 600 . . . Note=Does not affect protein deacetylase activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28923965;Dbxref=PMID:28923965 Q923E4 UniProtKB Mutagenesis 649 649 . . . Note=Abolishes in vitro phosphorylation by CaMK2%3B when associated with A-154%3B A-651 and A-683. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19680552;Dbxref=PMID:19680552 Q923E4 UniProtKB Mutagenesis 651 651 . . . Note=Abolishes in vitro phosphorylation by CaMK2%3B when associated with A-154%3B A-649 and A-683. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19680552;Dbxref=PMID:19680552 Q923E4 UniProtKB Mutagenesis 683 683 . . . Note=Abolishes in vitro phosphorylation by CaMK2%3B when associated with A-154%3B A-649 and A-651. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19680552;Dbxref=PMID:19680552