394:
371:
1449:. As mentioned above, orthologs of acetyl-CoA synthetase exist in the cytoplasm (AceCS1) and in mitochondria (AceCS2) in mammals. The presence of the sirtuin deacetylase SIRT3 in the mitochondrial matrix suggests the existence of lysine acetylated mitochondrial proteins. Indeed, SIRT3 deacetylates and activates the mammalian mitochondrial acetyl-coA synthetase (AceCS2). Furthermore, SIRT3 and AceCS2 are found complexed with one another, suggesting a critical role for control of AceCS2 activity by SIRT3.
268:
293:
645:
652:
659:
400:
299:
29:
1540:
protein. Although some evidence attributes SIRT3 activity in bypassing growth arrest in bladder carcinoma cells via regulation of p53 in the mitochondria. Damaged and aberrant mitochondrial function, similar to gene mutations, may be an early event that ultimately leads to the development of cancers.
1423:
BAT. BAT is different from WAT because it harbors large numbers of mitochondria and is important for thermogenesis in rodents. Thermogenesis in BAT is mediated by the uncoupling protein 1 (UCP1), which induces proton leakage and thereby generates heat instead of ATP. Mechanistic insights into how
1299:
Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes, and the protein encoded by this gene is included in class I of the sirtuin family. The human sirtuins have a range of molecular functions and have emerged as important proteins in aging, stress
2240:
Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P,
2060:
Bellizzi D, Rose G, Cavalcante P, Covello G, Dato S, De Rango F, Greco V, Maggiolini M, Feraco E, Mari V, Franceschi C, Passarino G, De
Benedictis G (February 2005). "A novel VNTR enhancer within the SIRT3 gene, a human homologue of SIR2, is associated with survival at oldest ages".
55:
2155:
Kim HS, Patel K, Muldoon-Jacobs K, Bisht KS, Aykin-Burns N, Pennington JD, van der Meer R, Nguyen P, Savage J, Owens KM, Vassilopoulos A, Ozden O, Park SH, Singh KK, Abdulkadir SA, Spitz DR, Deng CX, Gius D (January 2010).
1468:
In addition to its reported mitochondrial function, some researchers have proposed a very small pool of active nuclear SIRT3 exists. This pool is reported to consist of the long form of SIRT3 and has been suggested to have
2210:
Bellizzi D, Dato S, Cavalcante P, Covello G, Di Cianni F, Passarino G, Rose G, De
Benedictis G (2007). "Characterization of a bidirectional promoter shared between two human genes related to aging: SIRT3 and PSMD13".
2241:
Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network".
2344:
Frye RA (1999). "Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity".
1549:
receptor (ER/PR) positive breast mammary tumors. In tumor samples from women with breast cancer, SIRT3 expression was decreased, as compared to normal breast tissues. Thus, the Sirt3
407:
306:
2286:
Yang YH, Chen YH, Zhang CY, Nimmakayalu MA, Ward DC, Weissman S (2001). "Cloning and characterization of two mouse genes with homology to the yeast Sir2 gene".
1387:
and have been implicated in regulating metabolic processes. Endogenous SIRT3 is a soluble protein located in the mitochondrial matrix. Overexpression of
1311:. In addition to protein deacetylation, studies have shown that the human sirtuins may also function as intracellular regulatory proteins with mono ADP
927:
908:
229:
1350:, a reaction intermediate structure trapped by a thioacetyl peptide, and a structure with the dethioacetylated peptide bond. These structures show the
2418:
1630:
1612:
1667:"The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase"
2010:"SIRT3 is a stress responsive deacetylase in cardiomyocytes that protects cells from stress-mediated cell death by deacetylation of Ku-70"
1435:
In addition to controlling metabolism at the transcriptional level, sirtuins also directly control the activity of metabolic enzymes. In
393:
1214:
2158:"SIRT3 is a mitochondria-localized tumor suppressor required for maintenance of mitochondrial integrity and metabolism during stress"
1791:
Jin L, Wei W, Jiang Y, Peng H, Cai J, Mao C, Dai H, Choy W, Bemis JE, Jirousek MR, Milne JC, Westphal CH, Perni RB (September 2009).
1457:
1355:
370:
1651:
1207:
1359:
1599:
1578:
292:
267:
1595:
52:
1312:
1574:
209:
406:
305:
1391:
in cultured cells increases respiration and decreases the production of reactive oxygen species. Fasting increases
1961:"SirT3 is a nuclear NAD+-dependent histone deacetylase that translocates to the mitochondria upon cellular stress"
399:
298:
1530:
1351:
972:
217:
953:
1914:
1446:
1546:
1537:
1332:
281:
1354:
changes induced by the two substrates required for the reaction, the acetylated substrate peptide and
2250:
2109:
1855:
1502:
1460:(NAD+) biosynthetic pathway by SIRT3 may be a means of inhibiting axon degeneration and dysfunction.
1400:
1396:
1324:
196:
1652:"Entrez Gene: SIRT3 sirtuin (silent mating type information regulation 2 homolog) 3 (S. cerevisiae)"
1477:
from stress mediated cell death and that this effect was due to deacetylation of a nuclear factor,
1470:
1437:
1293:
1186:
1182:
1161:
1157:
1153:
1149:
1145:
1141:
1137:
1133:
1129:
1125:
1121:
1111:
1107:
1103:
1095:
1071:
1067:
1042:
1473:
activity. The observation that SIRT3 has nuclear activity came from a report that SIRT3 protected
2274:
1521:
There is a significant body of published literature suggesting a strong mechanistic link between
1289:
241:
2315:
Frye RA (2000). "Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins".
1190:
1099:
1075:
1046:
2396:
2361:
2332:
2303:
2266:
2228:
2187:
2137:
2078:
2039:
1990:
1941:
1883:
1824:
1763:
1745:
1696:
1542:
1510:
644:
189:
45:
2386:
2353:
2324:
2295:
2258:
2220:
2177:
2169:
2127:
2117:
2070:
2029:
2021:
1980:
1972:
1931:
1923:
1873:
1863:
1814:
1804:
1735:
1727:
1686:
1678:
1362:
suggests that the acetylated peptide is the first substrate to bind to SIRT3, prior to NAD.
1336:
486:
417:
361:
316:
651:
237:
1844:"SIRT3, a human SIR2 homologue, is an NAD-dependent deacetylase localized to mitochondria"
658:
461:
2254:
2113:
1859:
2182:
2157:
2132:
2097:
2034:
2009:
1985:
1960:
1936:
1909:
1819:
1793:"Crystal structures of human SIRT3 displaying substrate-induced conformational changes"
1792:
1740:
1715:
1691:
1666:
1304:
28:
1878:
1843:
1716:"The Nuts and Bolts of Transcriptionally Silent Chromatin in Saccharomyces cerevisiae"
842:
837:
832:
827:
822:
817:
812:
807:
802:
797:
781:
776:
771:
766:
761:
745:
740:
735:
730:
725:
720:
715:
710:
705:
700:
2412:
1522:
1474:
1441:, the bacterial sirtuin CobB regulates the activity of the enzyme acetyl-coenzyme A (
1420:
1308:
687:
221:
2278:
1478:
1384:
1300:
resistance, and metabolic regulation. Yeast sirtuin proteins are known to regulate
479:
258:
1910:"Mitochondrial Sirtuin 3: New emerging biological function and therapeutic target"
2122:
245:
2224:
2074:
1731:
1635:
National Center for
Biotechnology Information, U.S. National Library of Medicine
1617:
National Center for
Biotechnology Information, U.S. National Library of Medicine
1412:
1301:
2098:"p53-Induced growth arrest Is regulated by the mitochondrial SirT3 deacetylase"
1848:
Proceedings of the
National Academy of Sciences of the United States of America
562:
2173:
1526:
1442:
1328:
378:
275:
225:
1525:
function, aging, and carcinogenesis. SIRT3 inhibits cancers that depend upon
2375:"Normalization and subtraction: two approaches to facilitate gene discovery"
1809:
1506:
1498:
1494:
There is a strong association between SIRT3 alleles and longevity in males.
872:
622:
500:
445:
432:
344:
331:
233:
2365:
2357:
2336:
2328:
2307:
2299:
2270:
2232:
2191:
2141:
2082:
2043:
2008:
Sundaresan NR, Samant SA, Pillai VB, Rajamohan SB, Gupta MP (August 2008).
1994:
1945:
1887:
1868:
1828:
1749:
1700:
2400:
1682:
1553:
model may be used to investigate ER/PR positive breast tumor development.
1254:
1249:
2025:
1550:
1408:
1238:
1017:
998:
2262:
1976:
1842:
Onyango P, Celic I, McCaffery JM, Boeke JD, Feinberg AP (October 2002).
2391:
2374:
1927:
1285:
1274:
984:
939:
1785:
1779:
1773:
1767:
166:
162:
158:
154:
150:
146:
142:
138:
134:
130:
126:
122:
118:
114:
110:
106:
102:
98:
94:
90:
86:
82:
78:
74:
1453:
1343:
1340:
1222:
894:
1335:
of human SIRT3 have been solved, including an apo-structure with no
1380:
1376:
1347:
857:
853:
1281:
833:
negative regulation of reactive oxygen species metabolic process
667:
213:
2096:
Li S, Banck M, Mujtaba S, Zhou MM, Sugrue MM, Walsh MJ (2010).
1665:
Schwer B, North BJ, Frye RA, Ott M, Verdin E (August 2002).
1292:
to the yeast Sir2 protein. SIRT3 exhibits NAD+-dependent
1509:, inhibiting cell death, and thus could be used to treat
1327:, and contains a mitochondrial processing peptide at the
469:
1407:
in HIB1B brown adipocytes increases the expression of
634:
1428:
affects thermogenesis in BAT is lacking and whether
1175:
1094:
1060:
1035:
1591:
1589:
1587:
1570:
1568:
1566:
1403:(WAT and BAT, respectively) and overexpression of
1267:NAD-dependent deacetylase sirtuin-3, mitochondrial
1541:Mice genetically altered to delete Sirt3 develop
416:
315:
1908:Zhang J, Xiang H, Rong-Rong He R, Liu B (2020).
1456:enzyme, which catalyze an essential step in the
2055:
2053:
1903:
1901:
1899:
1897:
16:Protein-coding gene in the species Homo sapiens
1959:Scher MB, Vaquero A, Reinberg D (April 2007).
1596:GRCm38: Ensembl release 89: ENSMUSG00000025486
1432:affects UCP1 activity directly is not known.
8:
823:negative regulation of ERK1 and ERK2 cascade
1575:GRCh38: Ensembl release 89: ENSG00000142082
1323:SIRT3 is a soluble protein located in the
1091:
868:
736:NAD-dependent protein deacetylase activity
731:NAD-dependent histone deacetylase activity
683:
457:
356:
253:
63:
2390:
2181:
2131:
2121:
2033:
1984:
1935:
1877:
1867:
1818:
1808:
1739:
1690:
2373:Bonaldo MF, Lennon G, Soares MB (1997).
1646:
1644:
1529:, but promotes cancers that depend upon
1339:, a structure with a peptide containing
828:positive regulation of insulin secretion
1714:Gartenberg MR, Smith JS (August 2016).
1562:
18:
421:
382:
377:
320:
279:
274:
7:
701:NAD+ ADP-ribosyltransferase activity
1536:Sirt3 functions as a mitochondrial
1284:. SIRT3 is member of the mammalian
1358:. In addition, a binding study by
1172:
1057:
1032:
1008:
989:
963:
944:
918:
899:
639:
557:
495:
474:
14:
1497:Activation of SIRT3 inhibits the
1458:nicotinamide adenine dinucleotide
1277:that in humans is encoded by the
1360:isothermal titration calorimetry
657:
650:
643:
405:
398:
392:
369:
304:
297:
291:
266:
27:
1307:and suppress recombination of
1288:family of proteins, which are
668:More reference expression data
623:More reference expression data
1:
2346:Biochem. Biophys. Res. Commun
2317:Biochem. Biophys. Res. Commun
813:peptidyl-lysine deacetylation
741:sequence-specific DNA binding
390:
289:
2419:Genes on human chromosome 11
2123:10.1371/journal.pone.0010486
2225:10.1016/j.ygeno.2006.09.004
2075:10.1016/j.ygeno.2004.11.003
1732:10.1534/genetics.112.145243
2435:
1511:neurodegenerative diseases
808:mitochondrion organization
772:protein-containing complex
605:lateral geniculate nucleus
2174:10.1016/j.ccr.2009.11.023
1631:"Mouse PubMed Reference:"
1613:"Human PubMed Reference:"
1531:oxidative phosphorylation
1346:of its natural substrate
1253:
1248:
1244:
1237:
1221:
1215:Chr 7: 140.44 – 140.46 Mb
1202:
1179:
1118:
1087:
1064:
1039:
1028:
1015:
1011:
996:
992:
983:
970:
966:
951:
947:
938:
925:
921:
906:
902:
893:
878:
871:
867:
851:
686:
682:
665:
642:
633:
620:
601:medial geniculate nucleus
589:medial vestibular nucleus
569:
560:
507:
498:
468:
460:
456:
439:
426:
389:
368:
359:
355:
338:
325:
288:
265:
256:
252:
207:
204:
194:
187:
182:
71:
66:
49:
44:
39:
35:
26:
21:
1415:, suggesting a role for
818:protein ADP-ribosylation
593:dorsal tegmental nucleus
1810:10.1074/jbc.M109.014928
1671:Journal of Cell Biology
1501:leading to age-related
1375:Three sirtuins, SIRT3,
1348:acetyl-CoA synthetase 2
2358:10.1006/bbrc.1999.0897
2329:10.1006/bbrc.2000.3000
2300:10.1006/geno.2000.6360
1869:10.1073/pnas.222538099
1208:Chr 11: 0.22 – 0.24 Mb
1683:10.1083/jcb.200205057
1485:Clinical significance
843:histone deacetylation
798:protein deacetylation
282:Chromosome 11 (human)
2026:10.1128/MCB.00426-08
1503:macular degeneration
1401:brown adipose tissue
1325:mitochondrial matrix
767:mitochondrial matrix
585:facial motor nucleus
384:Chromosome 7 (mouse)
67:List of PDB id codes
40:Available structures
2263:10.1038/nature04209
2255:2005Natur.437.1173R
2114:2010PLoSO...510486L
1977:10.1101/gad.1527307
1860:2002PNAS...9913653O
1471:histone deacetylase
1438:Salmonella enterica
803:aerobic respiration
531:right lobe of liver
200:, SIR2L3, sirtuin 3
2392:10.1101/gr.6.9.791
1928:10.7150/thno.45922
1452:Activation of the
1333:crystal structures
1313:ribosyltransferase
973:ENSMUSG00000025486
791:Biological process
755:Cellular component
711:hydrolase activity
694:Molecular function
581:left lobe of liver
543:anterior pituitary
527:right uterine tube
511:right frontal lobe
2249:(7062): 1173–78.
1922:(18): 8315–8342.
1803:(36): 24394–405.
1383:, are located in
1264:
1263:
1260:
1259:
1233:
1232:
1198:
1197:
1169:
1168:
1083:
1082:
1054:
1053:
1024:
1023:
1005:
1004:
979:
978:
960:
959:
934:
933:
915:
914:
863:
862:
721:metal ion binding
678:
677:
674:
673:
629:
628:
616:
615:
554:
553:
535:nucleus accumbens
452:
451:
351:
350:
246:SIRT3 - orthologs
178:
177:
174:
173:
50:Ortholog search:
2426:
2404:
2394:
2369:
2340:
2311:
2282:
2236:
2196:
2195:
2185:
2152:
2146:
2145:
2135:
2125:
2093:
2087:
2086:
2057:
2048:
2047:
2037:
2020:(20): 6384–401.
2005:
1999:
1998:
1988:
1956:
1950:
1949:
1939:
1905:
1892:
1891:
1881:
1871:
1854:(21): 13653–58.
1839:
1833:
1832:
1822:
1812:
1788:
1782:
1776:
1770:
1760:
1754:
1753:
1743:
1726:(4): 1563–1599.
1711:
1705:
1704:
1694:
1662:
1656:
1655:
1648:
1639:
1638:
1627:
1621:
1620:
1609:
1603:
1593:
1582:
1572:
1538:tumor suppressor
1505:. SIRT3 induced
1246:
1245:
1217:
1210:
1193:
1173:
1164:
1092:
1088:RefSeq (protein)
1078:
1058:
1049:
1033:
1009:
990:
964:
945:
919:
900:
869:
726:zinc ion binding
684:
670:
661:
654:
647:
640:
625:
597:substantia nigra
565:
563:Top expressed in
558:
503:
501:Top expressed in
496:
475:
458:
448:
435:
424:
409:
402:
396:
385:
373:
357:
347:
334:
323:
308:
301:
295:
284:
270:
254:
248:
199:
192:
169:
64:
58:
37:
36:
31:
19:
2434:
2433:
2429:
2428:
2427:
2425:
2424:
2423:
2409:
2408:
2407:
2372:
2343:
2314:
2285:
2239:
2209:
2205:
2203:Further reading
2200:
2199:
2154:
2153:
2149:
2095:
2094:
2090:
2059:
2058:
2051:
2014:Mol. Cell. Biol
2007:
2006:
2002:
1958:
1957:
1953:
1907:
1906:
1895:
1841:
1840:
1836:
1790:
1784:
1778:
1772:
1762:
1761:
1757:
1713:
1712:
1708:
1664:
1663:
1659:
1650:
1649:
1642:
1629:
1628:
1624:
1611:
1610:
1606:
1594:
1585:
1573:
1564:
1559:
1519:
1492:
1487:
1466:
1373:
1368:
1321:
1255:View/Edit Mouse
1250:View/Edit Human
1213:
1206:
1203:Location (UCSC)
1189:
1185:
1181:
1160:
1156:
1152:
1148:
1144:
1140:
1136:
1132:
1128:
1124:
1120:
1114:
1110:
1106:
1102:
1098:
1074:
1070:
1066:
1045:
1041:
954:ENSG00000142082
847:
786:
750:
706:protein binding
666:
656:
655:
649:
648:
621:
612:
607:
603:
599:
595:
591:
587:
583:
579:
575:
573:proximal tubule
561:
550:
547:Brodmann area 9
545:
541:
539:caudate nucleus
537:
533:
529:
525:
521:
517:
513:
499:
443:
430:
423:7|7 F4- F5
422:
412:
411:
410:
403:
383:
360:Gene location (
342:
329:
321:
311:
310:
309:
302:
280:
257:Gene location (
208:
195:
188:
73:
51:
17:
12:
11:
5:
2432:
2430:
2422:
2421:
2411:
2410:
2406:
2405:
2385:(9): 791–806.
2370:
2341:
2312:
2283:
2237:
2206:
2204:
2201:
2198:
2197:
2147:
2088:
2049:
2000:
1951:
1893:
1834:
1755:
1706:
1657:
1640:
1622:
1604:
1583:
1561:
1560:
1558:
1555:
1518:
1517:Carcinogenesis
1515:
1491:
1488:
1486:
1483:
1475:cardiomyocytes
1465:
1462:
1395:expression in
1372:
1369:
1367:
1364:
1352:conformational
1320:
1317:
1305:gene silencing
1269:also known as
1262:
1261:
1258:
1257:
1252:
1242:
1241:
1235:
1234:
1231:
1230:
1228:
1226:
1219:
1218:
1211:
1204:
1200:
1199:
1196:
1195:
1177:
1176:
1170:
1167:
1166:
1116:
1115:
1089:
1085:
1084:
1081:
1080:
1062:
1061:
1055:
1052:
1051:
1037:
1036:
1030:
1026:
1025:
1022:
1021:
1013:
1012:
1006:
1003:
1002:
994:
993:
987:
981:
980:
977:
976:
968:
967:
961:
958:
957:
949:
948:
942:
936:
935:
932:
931:
923:
922:
916:
913:
912:
904:
903:
897:
891:
890:
885:
880:
876:
875:
865:
864:
861:
860:
849:
848:
846:
845:
840:
835:
830:
825:
820:
815:
810:
805:
800:
794:
792:
788:
787:
785:
784:
779:
774:
769:
764:
758:
756:
752:
751:
749:
748:
746:enzyme binding
743:
738:
733:
728:
723:
718:
713:
708:
703:
697:
695:
691:
690:
680:
679:
676:
675:
672:
671:
663:
662:
637:
631:
630:
627:
626:
618:
617:
614:
613:
611:
610:
606:
602:
598:
594:
590:
586:
582:
578:
574:
570:
567:
566:
555:
552:
551:
549:
548:
544:
540:
536:
532:
528:
524:
520:
516:
512:
508:
505:
504:
492:
491:
483:
472:
466:
465:
462:RNA expression
454:
453:
450:
449:
441:
437:
436:
428:
425:
420:
414:
413:
404:
397:
391:
387:
386:
381:
375:
374:
366:
365:
353:
352:
349:
348:
340:
336:
335:
327:
324:
319:
313:
312:
303:
296:
290:
286:
285:
278:
272:
271:
263:
262:
250:
249:
206:
202:
201:
193:
185:
184:
180:
179:
176:
175:
172:
171:
69:
68:
60:
59:
48:
42:
41:
33:
32:
24:
23:
15:
13:
10:
9:
6:
4:
3:
2:
2431:
2420:
2417:
2416:
2414:
2402:
2398:
2393:
2388:
2384:
2380:
2376:
2371:
2367:
2363:
2359:
2355:
2352:(1): 273–79.
2351:
2347:
2342:
2338:
2334:
2330:
2326:
2323:(2): 793–98.
2322:
2318:
2313:
2309:
2305:
2301:
2297:
2294:(3): 355–69.
2293:
2289:
2284:
2280:
2276:
2272:
2268:
2264:
2260:
2256:
2252:
2248:
2244:
2238:
2234:
2230:
2226:
2222:
2219:(1): 143–50.
2218:
2214:
2208:
2207:
2202:
2193:
2189:
2184:
2179:
2175:
2171:
2167:
2163:
2159:
2151:
2148:
2143:
2139:
2134:
2129:
2124:
2119:
2115:
2111:
2108:(5): e10486.
2107:
2103:
2099:
2092:
2089:
2084:
2080:
2076:
2072:
2069:(2): 258–63.
2068:
2064:
2056:
2054:
2050:
2045:
2041:
2036:
2031:
2027:
2023:
2019:
2015:
2011:
2004:
2001:
1996:
1992:
1987:
1982:
1978:
1974:
1971:(8): 920–28.
1970:
1966:
1962:
1955:
1952:
1947:
1943:
1938:
1933:
1929:
1925:
1921:
1917:
1916:
1911:
1904:
1902:
1900:
1898:
1894:
1889:
1885:
1880:
1875:
1870:
1865:
1861:
1857:
1853:
1849:
1845:
1838:
1835:
1830:
1826:
1821:
1816:
1811:
1806:
1802:
1798:
1797:J. Biol. Chem
1794:
1787:
1781:
1775:
1769:
1765:
1759:
1756:
1751:
1747:
1742:
1737:
1733:
1729:
1725:
1721:
1717:
1710:
1707:
1702:
1698:
1693:
1688:
1684:
1680:
1677:(4): 647–57.
1676:
1672:
1668:
1661:
1658:
1653:
1647:
1645:
1641:
1636:
1632:
1626:
1623:
1618:
1614:
1608:
1605:
1601:
1597:
1592:
1590:
1588:
1584:
1580:
1576:
1571:
1569:
1567:
1563:
1556:
1554:
1552:
1548:
1544:
1539:
1534:
1532:
1528:
1524:
1523:mitochondrial
1516:
1514:
1512:
1508:
1504:
1500:
1495:
1489:
1484:
1482:
1480:
1476:
1472:
1463:
1461:
1459:
1455:
1450:
1448:
1444:
1440:
1439:
1433:
1431:
1427:
1422:
1421:thermogenesis
1418:
1414:
1410:
1406:
1402:
1398:
1394:
1390:
1386:
1382:
1378:
1371:Mitochondrial
1370:
1365:
1363:
1361:
1357:
1353:
1349:
1345:
1342:
1338:
1334:
1330:
1326:
1318:
1316:
1314:
1310:
1306:
1303:
1297:
1295:
1291:
1287:
1283:
1280:
1276:
1272:
1268:
1256:
1251:
1247:
1243:
1240:
1236:
1229:
1227:
1224:
1220:
1216:
1212:
1209:
1205:
1201:
1194:
1192:
1188:
1184:
1178:
1174:
1171:
1165:
1163:
1159:
1155:
1151:
1147:
1143:
1139:
1135:
1131:
1127:
1123:
1117:
1113:
1109:
1105:
1101:
1097:
1093:
1090:
1086:
1079:
1077:
1073:
1069:
1063:
1059:
1056:
1050:
1048:
1044:
1038:
1034:
1031:
1029:RefSeq (mRNA)
1027:
1020:
1019:
1014:
1010:
1007:
1001:
1000:
995:
991:
988:
986:
982:
975:
974:
969:
965:
962:
956:
955:
950:
946:
943:
941:
937:
930:
929:
924:
920:
917:
911:
910:
905:
901:
898:
896:
892:
889:
886:
884:
881:
877:
874:
870:
866:
859:
855:
850:
844:
841:
839:
836:
834:
831:
829:
826:
824:
821:
819:
816:
814:
811:
809:
806:
804:
801:
799:
796:
795:
793:
790:
789:
783:
780:
778:
775:
773:
770:
768:
765:
763:
762:mitochondrion
760:
759:
757:
754:
753:
747:
744:
742:
739:
737:
734:
732:
729:
727:
724:
722:
719:
717:
714:
712:
709:
707:
704:
702:
699:
698:
696:
693:
692:
689:
688:Gene ontology
685:
681:
669:
664:
660:
653:
646:
641:
638:
636:
632:
624:
619:
608:
604:
600:
596:
592:
588:
584:
580:
576:
572:
571:
568:
564:
559:
556:
546:
542:
538:
534:
530:
526:
522:
518:
515:apex of heart
514:
510:
509:
506:
502:
497:
494:
493:
490:
488:
484:
482:
481:
477:
476:
473:
471:
467:
463:
459:
455:
447:
442:
438:
434:
429:
419:
415:
408:
401:
395:
388:
380:
376:
372:
367:
363:
358:
354:
346:
341:
337:
333:
328:
318:
314:
307:
300:
294:
287:
283:
277:
273:
269:
264:
260:
255:
251:
247:
243:
239:
235:
231:
227:
223:
219:
215:
211:
203:
198:
191:
186:
181:
170:
168:
164:
160:
156:
152:
148:
144:
140:
136:
132:
128:
124:
120:
116:
112:
108:
104:
100:
96:
92:
88:
84:
80:
76:
70:
65:
62:
61:
57:
54:
47:
43:
38:
34:
30:
25:
20:
2382:
2378:
2349:
2345:
2320:
2316:
2291:
2287:
2246:
2242:
2216:
2212:
2168:(1): 41–52.
2165:
2161:
2150:
2105:
2101:
2091:
2066:
2062:
2017:
2013:
2003:
1968:
1964:
1954:
1919:
1915:Theranostics
1913:
1851:
1847:
1837:
1800:
1796:
1758:
1723:
1719:
1709:
1674:
1670:
1660:
1634:
1625:
1616:
1607:
1547:progesterone
1535:
1520:
1496:
1493:
1467:
1451:
1436:
1434:
1429:
1425:
1419:in adaptive
1416:
1404:
1392:
1388:
1385:mitochondria
1374:
1322:
1298:
1278:
1270:
1266:
1265:
1187:NP_001171275
1183:NP_001120823
1180:
1162:NP_001357254
1158:NP_001357253
1154:NP_001357252
1150:NP_001357251
1146:NP_001357250
1142:NP_001357249
1138:NP_001357248
1134:NP_001357247
1130:NP_001357246
1126:NP_001357245
1122:NP_001357244
1119:
1112:NP_001357243
1108:NP_001357241
1104:NP_001357239
1096:NP_001017524
1072:NM_001177804
1068:NM_001127351
1065:
1043:NM_001017524
1040:
1016:
997:
971:
952:
926:
907:
887:
882:
838:human ageing
716:NAD+ binding
609:human kidney
577:right kidney
523:right testis
485:
478:
444:140,462,222
431:140,443,579
205:External IDs
72:
2162:Cancer Cell
1331:. A set of
1294:deacetylase
782:nucleoplasm
519:left testis
183:Identifiers
2379:Genome Res
1602:, May 2017
1581:, May 2017
1557:References
1527:glycolysis
1447:synthetase
1443:acetyl-CoA
1329:N-terminus
1315:activity.
1302:epigenetic
1296:activity.
489:(ortholog)
226:HomoloGene
1965:Genes Dev
1789:;
1783:,
1777:,
1771:,
1507:mitophagy
1499:apoptosis
1337:substrate
1319:Structure
1191:NP_071878
1100:NP_036371
1076:NM_022433
1047:NM_012239
873:Orthologs
777:cytoplasm
234:GeneCards
2413:Category
2366:10381378
2337:10873683
2308:11056054
2288:Genomics
2271:16189514
2233:17059877
2213:Genomics
2192:20129246
2142:20463968
2102:PLOS ONE
2083:15676284
2063:Genomics
2044:18710944
1995:17437997
1946:32724473
1888:12374852
1829:19535340
1750:27516616
1720:Genetics
1701:12186850
1598:–
1577:–
1551:knockout
1543:estrogen
1366:Function
1290:homologs
1239:Wikidata
852:Sources:
343:236,931
330:215,030
2401:8889548
2279:4427026
2251:Bibcode
2183:3711519
2133:2864751
2110:Bibcode
2035:2577434
1986:1847710
1937:7381741
1856:Bibcode
1820:2782032
1741:4981263
1692:2174009
1600:Ensembl
1579:Ensembl
1464:Nuclear
1286:sirtuin
1275:protein
985:UniProt
940:Ensembl
879:Species
858:QuickGO
464:pattern
322:11p15.5
222:1927665
190:Aliases
2399:
2364:
2335:
2306:
2277:
2269:
2243:Nature
2231:
2190:
2180:
2140:
2130:
2081:
2042:
2032:
1993:
1983:
1944:
1934:
1886:
1879:129731
1876:
1827:
1817:
1748:
1738:
1699:
1689:
1454:NMNAT2
1409:PGC-1α
1344:lysine
1341:acetyl
1225:search
1223:PubMed
1018:Q8R104
999:Q9NTG7
895:Entrez
635:BioGPS
214:604481
2275:S2CID
1490:Aging
1479:Ku-70
1430:SIRT3
1426:SIRT3
1417:SIRT3
1405:SIRT3
1397:white
1393:SIRT3
1389:SIRT3
1381:SIRT5
1377:SIRT4
1279:SIRT3
1273:is a
1271:SIRT3
928:64384
909:23410
888:Mouse
883:Human
854:Amigo
487:Mouse
480:Human
427:Start
362:Mouse
326:Start
259:Human
238:SIRT3
230:81827
197:SIRT3
22:SIRT3
2397:PMID
2362:PMID
2333:PMID
2304:PMID
2267:PMID
2229:PMID
2188:PMID
2138:PMID
2079:PMID
2040:PMID
1991:PMID
1942:PMID
1884:PMID
1825:PMID
1786:3GLU
1780:3GLT
1774:3GLS
1768:3GLR
1746:PMID
1697:PMID
1545:and
1413:UCP1
1411:and
1399:and
1379:and
1309:rDNA
1282:gene
470:Bgee
418:Band
379:Chr.
317:Band
276:Chr.
210:OMIM
167:5BWO
163:5BWN
159:5D7N
155:4V1C
151:4O8Z
147:4JT9
143:4JT8
139:4JSR
135:4HD8
131:4FZ3
127:4FVT
123:4C7B
119:4C78
115:4BVH
111:4BVG
107:4BVF
103:4BVE
99:4BVB
95:4BV3
91:4BN5
87:4BN4
83:3GLU
79:3GLS
75:3GLR
56:RCSB
53:PDBe
2387:doi
2354:doi
2350:260
2325:doi
2321:273
2296:doi
2259:doi
2247:437
2221:doi
2178:PMC
2170:doi
2128:PMC
2118:doi
2071:doi
2030:PMC
2022:doi
1981:PMC
1973:doi
1932:PMC
1924:doi
1874:PMC
1864:doi
1815:PMC
1805:doi
1801:284
1764:PDB
1736:PMC
1728:doi
1724:203
1687:PMC
1679:doi
1675:158
1356:NAD
440:End
339:End
242:OMA
218:MGI
46:PDB
2415::
2395:.
2381:.
2377:.
2360:.
2348:.
2331:.
2319:.
2302:.
2292:69
2290:.
2273:.
2265:.
2257:.
2245:.
2227:.
2217:89
2215:.
2186:.
2176:.
2166:17
2164:.
2160:.
2136:.
2126:.
2116:.
2104:.
2100:.
2077:.
2067:85
2065:.
2052:^
2038:.
2028:.
2018:28
2016:.
2012:.
1989:.
1979:.
1969:21
1967:.
1963:.
1940:.
1930:.
1920:10
1918:.
1912:.
1896:^
1882:.
1872:.
1862:.
1852:99
1850:.
1846:.
1823:.
1813:.
1799:.
1795:.
1766::
1744:.
1734:.
1722:.
1718:.
1695:.
1685:.
1673:.
1669:.
1643:^
1633:.
1615:.
1586:^
1565:^
1533:.
1513:.
1481:.
1445:)
856:/
446:bp
433:bp
345:bp
332:bp
240:;
236::
232:;
228::
224:;
220::
216:;
212::
165:,
161:,
157:,
153:,
149:,
145:,
141:,
137:,
133:,
129:,
125:,
121:,
117:,
113:,
109:,
105:,
101:,
97:,
93:,
89:,
85:,
81:,
77:,
2403:.
2389::
2383:6
2368:.
2356::
2339:.
2327::
2310:.
2298::
2281:.
2261::
2253::
2235:.
2223::
2194:.
2172::
2144:.
2120::
2112::
2106:5
2085:.
2073::
2046:.
2024::
1997:.
1975::
1948:.
1926::
1890:.
1866::
1858::
1831:.
1807::
1752:.
1730::
1703:.
1681::
1654:.
1637:.
1619:.
364:)
261:)
244::
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