500:
484:
clusters, tightly binding the zinc atoms and stabilizing the structure. The SET domain itself contains a catalytic core rich in β-strands that, in turn, make up several regions of β-sheets. Often, the β-strands found in the pre-SET domain will form β-sheets with the β-strands of the SET domain, leading to slight variations to the SET domain structure. These small changes alter the target residue site specificity for methylation and allow the SET domain methyltransferases to target many different residues. This interplay between the pre-SET domain and the catalytic core is critical for enzyme function.
288:
296:
598:. Methylated histones can either repress or activate transcription as different experimental findings suggest, depending on the site of methylation. For example, it is likely that the methylation of lysine 9 on histone H3 (H3K9me3) in the promoter region of genes prevents excessive expression of these genes and, therefore, delays cell cycle transition and/or proliferation. In contrast, methylation of histone residues H3K4, H3K36, and H3K79 is associated with transcriptionally active euchromatin.
496:(SAM) and the lysine residue of the substrate histone tail must first be bound and properly oriented in the catalytic pocket of the SET domain. Next, a nearby tyrosine residue deprotonates the ε-amino group of the lysine residue. The lysine chain then makes a nucleophilic attack on the methyl group on the sulfur atom of the SAM molecule, transferring the methyl group to the lysine side chain.
2894:
284:. The level of chromatin compaction depends heavily on histone methylation and other post-translational modifications of histones. Histone methylation is a principal epigenetic modification of chromatin that determines gene expression, genomic stability, stem cell maturation, cell lineage development, genetic imprinting, DNA methylation, and cell mitosis.
580:
PRMTs determine the next methylation step: either catalyzing the dimethylation of one nitrogen or allowing the symmetric methylation of both groups. However, in both cases the proton stripped from the nitrogen is dispersed through a histidine–aspartate proton relay system and released into the surrounding matrix.
512:
Instead of SET, non-SET domain-containing histone methyltransferase utilizes the enzyme Dot1. Unlike the SET domain, which targets the lysine tail region of the histone, Dot1 methylates a lysine residue in the globular core of the histone, and is the only enzyme known to do so. A possible homolog of
667:
Histone methyltransferase may be able to be used as biomarkers for the diagnosis and prognosis of cancers. Additionally, many questions still remain about the function and regulation of histone methyltransferases in malignant transformation of cells, carcinogenesis of the tissue, and tumorigenesis.
626:
or its signaling pathways, however they may be a contributing factor. For example, down-regulation of methylation of lysine 9 on histone 3 (H3K9me3) has been observed in several types of human cancer (such as colorectal cancer, ovarian cancer, and lung cancer), which arise from either the deficiency
601:
Depending on the site and symmetry of methylation, methylated arginines are considered activating (histone H4R3me2a, H3R2me2s, H3R17me2a, H3R26me2a) or repressive (H3R2me2a, H3R8me2a, H3R8me2s, H4R3me2s) histone marks. Generally, the effect of a histone methyltransferase on gene expression strongly
570:
The catalytic domain of PRMTs consists of a SAM binding domain and substrate binding domain (about 310 amino acids in total). Each PRMT has a unique N-terminal region and a catalytic core. The arginine residue and SAM must be correctly oriented within the binding pocket. SAM is secured inside the
483:
The structures involved in methyltransferase activity are the SET domain (composed of approximately 130 amino acids), the pre-SET, and the post-SET domains. The pre-SET and post-SET domains flank the SET domain on either side. The pre-SET region contains cysteine residues that form triangular zinc
579:
A glutamate on a nearby loop interacts with nitrogens on the target arginine residue. This interaction redistributes the positive charge and leads to the deprotonation of one nitrogen group, which can then make a nucleophilic attack on the methyl group of SAM. Differences between the two types of
521:
The N terminal of Dot1 contains the active site. A loop serving as the binding site for SAM links the N-terminal and the C-terminal domains of the Dot1 catalytic domain. The C-terminal is important for the substrate specificity and binding of Dot1 because the region carries a positive charge,
618:
and malignant transformation of cells or formation of tumors. In recent years, epigenetic modification of the histone proteins, especially the methylation of the histone H3, in cancer development has been an area of emerging research. It is now generally accepted that in addition to genetic
308:
The class of lysine-specific histone methyltransferases is subdivided into SET domain-containing and non-SET domain-containing. As indicated by their monikers, these differ in the presence of a SET domain, which is a type of protein domain.
619:
aberrations, cancer can be initiated by epigenetic changes in which gene expression is altered without genomic abnormalities. These epigenetic changes include loss or gain of methylations in both DNA and histone proteins.
254:. The attachment of methyl groups occurs predominantly at specific lysine or arginine residues on histones H3 and H4. Two major types of histone methyltranferases exist, lysine-specific (which can be SET (
819:
1674:"The Dot1 histone methyltransferase and the Rad9 checkpoint adaptor contribute to cohesin-dependent double-strand break repair by sister chromatid recombination in Saccharomyces cerevisiae"
562:(Rme2s). The third type (PRMT7) produces only monomethylated arginine. The differences in methylation patterns of PRMTs arise from restrictions in the arginine binding pocket.
2224:
2425:
184:
2379:
692:
203:
2280:
522:
allowing for a favorable interaction with the negatively charged backbone of DNA. Due to structural constraints, Dot1 is only able to methylate histone H3.
2443:
2349:
2544:
343:
1215:
Chen D, Ma H, Hong H, Koh SS, Huang SM, Schurter BT, Aswad DW, Stallcup MR (June 1999). "Regulation of transcription by a protein methyltransferase".
2323:
1769:
614:
Abnormal expression or activity of methylation-regulating enzymes has been noted in some types of human cancers, suggesting associations between
2554:
2270:
2217:
1915:
1486:
794:
2508:
503:
Active site of
Histone Lysine N-Methyltransferase. Lysine residue (in yellow) and S-Adenosyl methionine (SAM) (in blue) clearly visible.
2580:
2300:
2296:
867:"Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association"
2613:
1293:"Analysis of the yeast arginine methyltransferase Hmt1p/Rmt1p and its in vivo function. Cofactor binding and substrate interactions"
744:
2464:
2210:
196:
2539:
2420:
2119:
2529:
2524:
2448:
2328:
147:
123:
2769:
499:
2305:
2265:
2884:
2534:
2374:
534:(PRMTs) and three types of methylation that can occur at arginine residues on histone tails. The first type of PRMTs (
2549:
1762:
551:
299:
Back view of the human enzyme
Histone Lysine N-Methyltransferase, H3 lysine-4 specific. Active sites clearly visible.
1795:
925:"PRMT5 (Janus kinase-binding protein 1) catalyzes the formation of symmetric dimethylarginine residues in proteins"
656:
2754:
2870:
2857:
2844:
2831:
2818:
2805:
2792:
2568:
2483:
2393:
2275:
2246:
1992:
1928:
1876:
682:
677:
2764:
1737:
559:
513:
Dot1 was found in archaea which shows the ability to methylate archaeal histone-like protein in recent studies.
141:
2718:
2661:
2412:
2237:
2172:
2147:
2114:
1786:
1778:
1741:
1731:
648:
34:
1727:
1722:
270:
containing or non-SET domain containing) and arginine-specific. In both types of histone methyltransferases,
774:
128:
2666:
2167:
2135:
2109:
2093:
1782:
287:
275:
1672:
Conde F, Refolio E, Cordón-Preciado V, Cortés-Ledesma F, Aragón L, Aguilera A, San-Segundo PA (June 2009).
295:
2469:
2002:
1755:
1176:"Structure of the catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase"
724:
1466:
1418:
208:
2687:
2606:
2369:
2186:
2181:
2049:
1951:
493:
271:
116:
2759:
2924:
2919:
2364:
2083:
1997:
1963:
1857:
731:. Advances in Protein Chemistry. Vol. 67. Amsterdam: Elsevier Academic Press. pp. 201–222.
51:
2723:
2333:
2066:
2034:
1920:
1894:
697:
687:
623:
615:
588:
531:
144:
46:
571:
pocket by a hydrophobic interaction between an adenine ring and a phenyl ring of a phenylalanine.
68:
2656:
1835:
1572:
996:
847:
547:
2202:
1592:"Histone methylation in DNA repair and clinical practice: new findings during the past 5-years"
1543:
Hamamoto R, Furukawa Y, Morita M, Iimura Y, Silva FP, Li M, Yagyu R, Nakamura Y (August 2004).
2914:
2435:
2250:
2154:
1703:
1660:
1656:
1621:
1564:
1525:
1482:
1438:
1399:
1358:
1314:
1273:
1232:
1197:
1156:
1115:
1050:
988:
946:
896:
839:
800:
790:
750:
740:
622:
There is not yet compelling evidence that suggests cancers develop purely by abnormalities in
467:
135:
1467:"Methylation of Lysine 9 of Histone H3: Role of Heterochromatin Modulation and Tumorigenesis"
2702:
2697:
2671:
2599:
2076:
2059:
1693:
1685:
1652:
1611:
1603:
1556:
1515:
1474:
1430:
1389:
1348:
1304:
1263:
1224:
1187:
1146:
1105:
1040:
1032:
980:
936:
886:
878:
831:
782:
732:
426:
386:
231:(e.g., histone-lysine N-methyltransferases and histone-arginine N-methyltransferases), that
451:
439:
435:
398:
104:
2749:
2733:
2646:
2487:
1940:
595:
1545:"SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells"
820:"Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain"
80:
1747:
291:
Front view of the human enzyme
Histone Lysine N-Methyltransferase, H3 lysine-4 specific.
39:
2898:
2787:
2728:
2150:
2138:
2088:
1698:
1673:
1616:
1591:
1478:
786:
267:
179:
1394:
1377:
1192:
1175:
1151:
1134:
1045:
1020:
891:
866:
835:
736:
159:
2908:
2692:
2651:
2397:
1852:
1434:
1021:"Crystal structure of the conserved core of protein arginine methyltransferase PRMT3"
923:
Branscombe TL, Frankel A, Lee JH, Cook JR, Yang Z, Pestka S, Clarke S (August 2001).
865:
Ng HH, Feng Q, Wang H, Erdjument-Bromage H, Tempst P, Zhang Y, Struhl K (June 2002).
818:
Feng Q, Wang H, Ng HH, Erdjument-Bromage H, Tempst P, Struhl K, Zhang Y (June 2002).
154:
1576:
1000:
851:
627:
of H3K9 methyltransferases or elevated activity or expression of H3K9 demethylases.
2641:
2315:
1252:"The predominant protein-arginine methyltransferase from Saccharomyces cerevisiae"
1228:
967:
Weiss VH, McBride AE, Soriano MA, Filman DJ, Silver PA, Hogle JM (December 2000).
1353:
1336:
969:"The structure and oligomerization of the yeast arginine methyltransferase, Hmt1"
2865:
2800:
2636:
2233:
2039:
2007:
1910:
1689:
163:
2893:
1110:
1093:
1036:
312:
Human genes encoding proteins with histone methyltransferase activity include:
2191:
1885:
1840:
1830:
1825:
1820:
1815:
781:. Advances in Genetics. Vol. 70. Boston: Academic Press. pp. 57–85.
640:
592:
374:
1268:
1251:
1135:"Structure and catalytic mechanism of a SET domain protein methyltransferase"
2839:
2813:
2493:
1847:
1544:
968:
281:
1707:
1664:
1643:
Trievel RC (2004). "Structure and function of histone methyltransferases".
1625:
1568:
1529:
1403:
1362:
1318:
1309:
1292:
1236:
1201:
1160:
1119:
1054:
992:
950:
941:
924:
900:
843:
804:
754:
1442:
1277:
2054:
2044:
244:
232:
882:
92:
2572:
2014:
1881:
652:
644:
603:
459:
455:
251:
248:
111:
1607:
1520:
1503:
2852:
2622:
2402:
2354:
1810:
636:
431:
422:
382:
378:
240:
236:
228:
191:
87:
75:
63:
1560:
1291:
McBride AE, Weiss VH, Kim HK, Hogle JM, Silver PA (February 2000).
1133:
Trievel RC, Beach BM, Dirk LM, Houtz RL, Hurley JH (October 2002).
2826:
2071:
1923:
984:
555:
543:
539:
535:
498:
463:
447:
443:
418:
414:
410:
406:
402:
394:
390:
369:
330:
326:
321:
316:
294:
286:
2142:
1972:
1903:
1378:"State of the arg: protein methylation at arginine comes of age"
364:
359:
355:
351:
347:
338:
334:
99:
2595:
2206:
1751:
1471:
Handbook of
Epigenetics: The New Molecular and Medical Genetics
280:
The genomic DNA of eukaryotes associates with histones to form
1419:"The charge relay system in chymotrypsin and chymotrypsinogen"
1250:
Gary JD, Lin WJ, Yang MC, Herschman HR, Clarke S (May 1996).
1068:
725:"Posttranslational Modifications of Histones by Methylation"
2591:
1590:
Wei S, Li C, Yin Z, Wen J, Meng H, Xue L, Wang J (2018).
1504:"Histone modifications as a platform for cancer therapy"
2882:
1502:
Espino PS, Drobic B, Dunn KL, Davie JR (April 2005).
602:
depends on which histone residue it methylates. See
2778:
2742:
2711:
2680:
2629:
2567:
2517:
2501:
2482:
2457:
2434:
2411:
2392:
2342:
2314:
2289:
2258:
2245:
2163:
2128:
2102:
2027:
1985:
1962:
1939:
1875:
1868:
1803:
1794:
1723:
GeneReviews/NCBI/NIH/UW entry on
Kleefstra Syndrome
718:
716:
714:
712:
202:
190:
178:
173:
153:
134:
122:
110:
98:
86:
74:
62:
57:
45:
33:
28:
21:
1174:Min J, Feng Q, Li Z, Zhang Y, Xu RM (March 2003).
639:has an important role in choosing the pathway for
651:repair, while dimethylated H4K20 can recruit the
2426:3-methyl-2-oxobutanoate hydroxymethyltransferase
1460:
1458:
1456:
1454:
1452:
2607:
2380:Cyclopropane-fatty-acyl-phospholipid synthase
2218:
1763:
1330:
1328:
693:RNA polymerase control by chromatin structure
8:
2281:Phosphatidylethanolamine N-methyltransferase
1473:. Boston: Academic Press. pp. 149–157.
1094:"Chromatin modifications and their function"
1087:
1085:
918:
916:
914:
912:
910:
2444:Phosphoribosylglycinamide formyltransferase
2350:Phosphatidyl ethanolamine methyltransferase
1335:Blanc, Roméo S.; Richard, Stéphane (2017).
2614:
2600:
2592:
2545:3-hydroxymethylcephem carbamoyltransferase
2498:
2408:
2255:
2225:
2211:
2203:
1872:
1800:
1770:
1756:
1748:
170:
1740:at the U.S. National Library of Medicine
1730:at the U.S. National Library of Medicine
1697:
1657:10.1615/CritRevEukaryotGeneExpr.v14.i3.10
1615:
1519:
1393:
1352:
1337:"Arginine Methylation: The Coming of Age"
1308:
1267:
1191:
1150:
1109:
1044:
940:
890:
779:Epigenetics and Cancer, Part A, Volume 70
768:
766:
764:
508:Non-SET domain-containing lysine-specific
2889:
1417:Fersht AR, Sperling J (February 1973).
1014:
1012:
1010:
962:
960:
708:
2555:N-acetylornithine carbamoyltransferase
2324:Betaine-homocysteine methyltransferase
2271:Phenylethanolamine N-methyltransferase
1019:Zhang X, Zhou L, Cheng X (July 2000).
492:In order for the reaction to proceed,
18:
1916:Histone acetylation and deacetylation
655:protein for repair by the pathway of
474:SET domain-containing lysine-specific
7:
2509:methylmalonyl-CoA carboxytransferase
1738:Protein-Arginine+N-Methyltransferase
1465:Chen F, Kan H, Castranova V (2010).
729:Proteins in eukaryotic transcription
727:. In Conaway JW, Conaway RC (eds.).
2581:Arginine:glycine amidinotransferase
2301:Acetylserotonin O-methyltransferase
2297:5-hydroxyindole-O-methyltransferase
1376:McBride AE, Silver PA (July 2001).
532:protein arginine methyltransferases
530:There are three different types of
235:the transfer of one, two, or three
1728:Histone-Lysine+N-Methyltransferase
1479:10.1016/B978-0-12-375709-8.00010-1
787:10.1016/B978-0-12-380866-0.60003-4
777:. In Ushijima T, Herceg Z (eds.).
775:"Histone Modifications and Cancer"
641:repairing DNA double-strand breaks
14:
2892:
2465:Glutamate formimidoyltransferase
554:(Rme2a). The second type (JBP1⧸
2540:Putrescine carbamoyltransferase
2421:Serine hydroxymethyltransferase
2120:Archaeal transcription factor B
683:Histone acetyltransferase (HAT)
546:⧸PRMT4, and Rmt1⧸Hmt1) produce
2530:Ornithine carbamoyltransferase
2525:Aspartate carbamoyltransferase
2449:Inosine monophosphate synthase
2329:Homocysteine methyltransferase
1645:Crit. Rev. Eukaryot. Gene Expr
1092:Kouzarides T (February 2007).
723:Wood A, Shilatifard A (2004).
1:
2306:Catechol-O-methyl transferase
2266:Histamine N-methyltransferase
1395:10.1016/S0092-8674(01)00423-8
1229:10.1126/science.284.5423.2174
1193:10.1016/S0092-8674(03)00114-4
1152:10.1016/S0092-8674(02)01000-0
836:10.1016/S0960-9822(02)00901-6
737:10.1016/S0065-3233(04)67008-2
2535:Oxamate carbamoyltransferase
2375:Thiopurine methyltransferase
1435:10.1016/0022-2836(73)90103-4
1354:10.1016/j.molcel.2016.11.003
604:Histone#Chromatin regulation
2550:Lysine carbamoyltransferase
2236:: one carbon transferases (
1690:10.1534/genetics.109.101899
635:The methylation of histone
591:plays an important role in
552:asymmetric dimethylarginine
2941:
1796:Transcriptional regulation
1469:. In Tollefsbol TO (ed.).
1111:10.1016/j.cell.2007.02.005
773:Sawan C, Herceg Z (2010).
688:Histone deacetylase (HDAC)
657:non-homologous end joining
649:homologous recombinational
560:symmetric dimethylarginine
221:Histone methyltransferases
2770:Michaelis–Menten kinetics
2360:Histone methyltransferase
2276:Amine N-methyltransferase
1993:Transcription coregulator
1929:Histone acetyltransferase
1899:Histone methyltransferase
1877:Histone-modifying enzymes
678:Histone-Modifying Enzymes
558:) produces monomethyl or
169:
16:Histone-modifying enzymes
2662:Diffusion-limited enzyme
2413:Hydroxymethyltransferase
1742:Medical Subject Headings
1732:Medical Subject Headings
1269:10.1074/jbc.271.21.12585
1037:10.1093/emboj/19.14.3509
278:and methyl donor group.
227:) are histone-modifying
2094:Internal control region
584:Role in gene regulation
2470:Aminomethyltransferase
1310:10.1074/jbc.275.5.3128
942:10.1074/jbc.M105412200
504:
300:
292:
2755:Eadie–Hofstee diagram
2688:Allosteric regulation
2370:DNA methyltransferase
2187:Intrinsic termination
1952:DNA methyltransferase
502:
494:S-Adenosyl methionine
298:
290:
272:S-Adenosyl methionine
2765:Lineweaver–Burk plot
2365:Thymidylate synthase
1964:Chromatin remodeling
645:tri-methylated H3K36
2334:Methionine synthase
1921:Histone deacetylase
1911:Histone demethylase
1895:Histone methylation
1069:"Chromatin Network"
883:10.1101/gad.1001502
698:Histone methylation
624:histone methylation
616:histone methylation
589:Histone methylation
575:Catalytic mechanism
488:Catalytic mechanism
24:N-methyltransferase
2724:Enzyme superfamily
2657:Enzyme promiscuity
643:. As an example,
548:monomethylarginine
505:
301:
293:
274:(SAM) serves as a
262:nhancer of Zeste,
2880:
2879:
2589:
2588:
2563:
2562:
2478:
2477:
2436:Formyltransferase
2388:
2387:
2200:
2199:
2155:RNA polymerase II
2023:
2022:
1981:
1980:
1608:10.7150/jca.23427
1602:(12): 2072–2081.
1521:10.1002/jcb.20387
1488:978-0-12-375709-8
973:Nat. Struct. Biol
796:978-0-12-380866-0
610:Disease relevance
526:Arginine-specific
218:
217:
214:
213:
117:metabolic pathway
2932:
2897:
2896:
2888:
2760:Hanes–Woolf plot
2703:Enzyme activator
2698:Enzyme inhibitor
2672:Enzyme catalysis
2616:
2609:
2602:
2593:
2499:
2409:
2256:
2227:
2220:
2213:
2204:
2077:Response element
2060:Response element
1873:
1801:
1772:
1765:
1758:
1749:
1711:
1701:
1668:
1630:
1629:
1619:
1587:
1581:
1580:
1540:
1534:
1533:
1523:
1508:J. Cell. Biochem
1499:
1493:
1492:
1462:
1447:
1446:
1414:
1408:
1407:
1397:
1373:
1367:
1366:
1356:
1332:
1323:
1322:
1312:
1288:
1282:
1281:
1271:
1262:(21): 12585–94.
1247:
1241:
1240:
1223:(5423): 2174–7.
1212:
1206:
1205:
1195:
1171:
1165:
1164:
1154:
1130:
1124:
1123:
1113:
1089:
1080:
1079:
1077:
1075:
1065:
1059:
1058:
1048:
1016:
1005:
1004:
964:
955:
954:
944:
920:
905:
904:
894:
862:
856:
855:
815:
809:
808:
770:
759:
758:
720:
663:Further research
647:is required for
171:
19:
2940:
2939:
2935:
2934:
2933:
2931:
2930:
2929:
2905:
2904:
2903:
2891:
2883:
2881:
2876:
2788:Oxidoreductases
2774:
2750:Enzyme kinetics
2738:
2734:List of enzymes
2707:
2676:
2647:Catalytic triad
2625:
2620:
2590:
2585:
2559:
2513:
2491:
2474:
2453:
2430:
2401:
2384:
2338:
2310:
2285:
2241:
2231:
2201:
2196:
2171:
2165:
2159:
2124:
2098:
2019:
1977:
1958:
1941:DNA methylation
1935:
1879:
1864:
1790:
1776:
1719:
1714:
1671:
1642:
1638:
1636:Further reading
1633:
1589:
1588:
1584:
1561:10.1038/ncb1151
1542:
1541:
1537:
1514:(6): 1088–102.
1501:
1500:
1496:
1489:
1464:
1463:
1450:
1416:
1415:
1411:
1375:
1374:
1370:
1334:
1333:
1326:
1290:
1289:
1285:
1249:
1248:
1244:
1214:
1213:
1209:
1173:
1172:
1168:
1132:
1131:
1127:
1091:
1090:
1083:
1073:
1071:
1067:
1066:
1062:
1031:(14): 3509–19.
1018:
1017:
1008:
979:(12): 1165–71.
966:
965:
958:
935:(35): 32971–6.
922:
921:
908:
877:(12): 1518–27.
864:
863:
859:
817:
816:
812:
797:
772:
771:
762:
747:
722:
721:
710:
706:
674:
665:
633:
612:
596:gene regulation
586:
577:
568:
528:
519:
510:
490:
481:
476:
306:
279:
23:
17:
12:
11:
5:
2938:
2936:
2928:
2927:
2922:
2917:
2907:
2906:
2902:
2901:
2878:
2877:
2875:
2874:
2861:
2848:
2835:
2822:
2809:
2796:
2782:
2780:
2776:
2775:
2773:
2772:
2767:
2762:
2757:
2752:
2746:
2744:
2740:
2739:
2737:
2736:
2731:
2726:
2721:
2715:
2713:
2712:Classification
2709:
2708:
2706:
2705:
2700:
2695:
2690:
2684:
2682:
2678:
2677:
2675:
2674:
2669:
2664:
2659:
2654:
2649:
2644:
2639:
2633:
2631:
2627:
2626:
2621:
2619:
2618:
2611:
2604:
2596:
2587:
2586:
2584:
2583:
2577:
2575:
2565:
2564:
2561:
2560:
2558:
2557:
2552:
2547:
2542:
2537:
2532:
2527:
2521:
2519:
2515:
2514:
2512:
2511:
2505:
2503:
2496:
2480:
2479:
2476:
2475:
2473:
2472:
2467:
2461:
2459:
2455:
2454:
2452:
2451:
2446:
2440:
2438:
2432:
2431:
2429:
2428:
2423:
2417:
2415:
2406:
2390:
2389:
2386:
2385:
2383:
2382:
2377:
2372:
2367:
2362:
2357:
2352:
2346:
2344:
2340:
2339:
2337:
2336:
2331:
2326:
2320:
2318:
2312:
2311:
2309:
2308:
2303:
2293:
2291:
2287:
2286:
2284:
2283:
2278:
2273:
2268:
2262:
2260:
2253:
2243:
2242:
2232:
2230:
2229:
2222:
2215:
2207:
2198:
2197:
2195:
2194:
2189:
2184:
2178:
2176:
2161:
2160:
2158:
2157:
2151:RNA polymerase
2145:
2139:RNA polymerase
2132:
2130:
2126:
2125:
2123:
2122:
2117:
2112:
2106:
2104:
2100:
2099:
2097:
2096:
2091:
2086:
2081:
2080:
2079:
2074:
2064:
2063:
2062:
2057:
2052:
2047:
2042:
2031:
2029:
2025:
2024:
2021:
2020:
2018:
2017:
2012:
2011:
2010:
2005:
2000:
1989:
1987:
1983:
1982:
1979:
1978:
1976:
1975:
1969:
1967:
1960:
1959:
1957:
1956:
1955:
1954:
1946:
1944:
1937:
1936:
1934:
1933:
1932:
1931:
1926:
1913:
1908:
1907:
1906:
1891:
1889:
1870:
1866:
1865:
1863:
1862:
1861:
1860:
1855:
1845:
1844:
1843:
1838:
1833:
1828:
1823:
1818:
1807:
1805:
1798:
1792:
1791:
1777:
1775:
1774:
1767:
1760:
1752:
1746:
1745:
1735:
1725:
1718:
1717:External links
1715:
1713:
1712:
1669:
1639:
1637:
1634:
1632:
1631:
1582:
1549:Nat. Cell Biol
1535:
1494:
1487:
1448:
1409:
1368:
1341:Molecular Cell
1324:
1303:(5): 3128–36.
1283:
1242:
1207:
1166:
1125:
1104:(4): 693–705.
1081:
1060:
1006:
956:
906:
857:
830:(12): 1052–8.
810:
795:
760:
745:
707:
705:
702:
701:
700:
695:
690:
685:
680:
673:
670:
664:
661:
632:
629:
611:
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573:
567:
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527:
524:
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429:
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362:
341:
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216:
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96:
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90:
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72:
71:
66:
60:
59:
55:
54:
49:
43:
42:
37:
31:
30:
26:
25:
22:Histone-lysine
15:
13:
10:
9:
6:
4:
3:
2:
2937:
2926:
2923:
2921:
2918:
2916:
2913:
2912:
2910:
2900:
2895:
2890:
2886:
2872:
2868:
2867:
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2859:
2855:
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2833:
2829:
2828:
2823:
2820:
2816:
2815:
2810:
2807:
2803:
2802:
2797:
2794:
2790:
2789:
2784:
2783:
2781:
2777:
2771:
2768:
2766:
2763:
2761:
2758:
2756:
2753:
2751:
2748:
2747:
2745:
2741:
2735:
2732:
2730:
2729:Enzyme family
2727:
2725:
2722:
2720:
2717:
2716:
2714:
2710:
2704:
2701:
2699:
2696:
2694:
2693:Cooperativity
2691:
2689:
2686:
2685:
2683:
2679:
2673:
2670:
2668:
2665:
2663:
2660:
2658:
2655:
2653:
2652:Oxyanion hole
2650:
2648:
2645:
2643:
2640:
2638:
2635:
2634:
2632:
2628:
2624:
2617:
2612:
2610:
2605:
2603:
2598:
2597:
2594:
2582:
2579:
2578:
2576:
2574:
2570:
2566:
2556:
2553:
2551:
2548:
2546:
2543:
2541:
2538:
2536:
2533:
2531:
2528:
2526:
2523:
2522:
2520:
2516:
2510:
2507:
2506:
2504:
2500:
2497:
2495:
2489:
2485:
2481:
2471:
2468:
2466:
2463:
2462:
2460:
2456:
2450:
2447:
2445:
2442:
2441:
2439:
2437:
2433:
2427:
2424:
2422:
2419:
2418:
2416:
2414:
2410:
2407:
2405:- and Related
2404:
2399:
2398:Hydroxymethyl
2395:
2391:
2381:
2378:
2376:
2373:
2371:
2368:
2366:
2363:
2361:
2358:
2356:
2353:
2351:
2348:
2347:
2345:
2341:
2335:
2332:
2330:
2327:
2325:
2322:
2321:
2319:
2317:
2313:
2307:
2304:
2302:
2298:
2295:
2294:
2292:
2288:
2282:
2279:
2277:
2274:
2272:
2269:
2267:
2264:
2263:
2261:
2257:
2254:
2252:
2248:
2244:
2239:
2235:
2228:
2223:
2221:
2216:
2214:
2209:
2208:
2205:
2193:
2190:
2188:
2185:
2183:
2180:
2179:
2177:
2174:
2169:
2162:
2156:
2152:
2149:
2146:
2144:
2140:
2137:
2134:
2133:
2131:
2127:
2121:
2118:
2116:
2113:
2111:
2108:
2107:
2105:
2101:
2095:
2092:
2090:
2087:
2085:
2082:
2078:
2075:
2073:
2070:
2069:
2068:
2065:
2061:
2058:
2056:
2053:
2051:
2048:
2046:
2043:
2041:
2038:
2037:
2036:
2033:
2032:
2030:
2026:
2016:
2013:
2009:
2006:
2004:
2001:
1999:
1996:
1995:
1994:
1991:
1990:
1988:
1984:
1974:
1971:
1970:
1968:
1965:
1961:
1953:
1950:
1949:
1948:
1947:
1945:
1942:
1938:
1930:
1927:
1925:
1922:
1919:
1918:
1917:
1914:
1912:
1909:
1905:
1902:
1901:
1900:
1896:
1893:
1892:
1890:
1887:
1883:
1878:
1874:
1871:
1867:
1859:
1858:trp repressor
1856:
1854:
1853:lac repressor
1851:
1850:
1849:
1846:
1842:
1839:
1837:
1834:
1832:
1829:
1827:
1824:
1822:
1819:
1817:
1814:
1813:
1812:
1809:
1808:
1806:
1802:
1799:
1797:
1793:
1788:
1784:
1780:
1779:Transcription
1773:
1768:
1766:
1761:
1759:
1754:
1753:
1750:
1743:
1739:
1736:
1733:
1729:
1726:
1724:
1721:
1720:
1716:
1709:
1705:
1700:
1695:
1691:
1687:
1684:(2): 437–46.
1683:
1679:
1675:
1670:
1666:
1662:
1658:
1654:
1651:(3): 147–69.
1650:
1646:
1641:
1640:
1635:
1627:
1623:
1618:
1613:
1609:
1605:
1601:
1597:
1593:
1586:
1583:
1578:
1574:
1570:
1566:
1562:
1558:
1555:(8): 731–40.
1554:
1550:
1546:
1539:
1536:
1531:
1527:
1522:
1517:
1513:
1509:
1505:
1498:
1495:
1490:
1484:
1480:
1476:
1472:
1468:
1461:
1459:
1457:
1455:
1453:
1449:
1444:
1440:
1436:
1432:
1429:(2): 137–49.
1428:
1424:
1420:
1413:
1410:
1405:
1401:
1396:
1391:
1387:
1383:
1379:
1372:
1369:
1364:
1360:
1355:
1350:
1346:
1342:
1338:
1331:
1329:
1325:
1320:
1316:
1311:
1306:
1302:
1298:
1297:J. Biol. Chem
1294:
1287:
1284:
1279:
1275:
1270:
1265:
1261:
1257:
1256:J. Biol. Chem
1253:
1246:
1243:
1238:
1234:
1230:
1226:
1222:
1218:
1211:
1208:
1203:
1199:
1194:
1189:
1186:(5): 711–23.
1185:
1181:
1177:
1170:
1167:
1162:
1158:
1153:
1148:
1145:(1): 91–103.
1144:
1140:
1136:
1129:
1126:
1121:
1117:
1112:
1107:
1103:
1099:
1095:
1088:
1086:
1082:
1070:
1064:
1061:
1056:
1052:
1047:
1042:
1038:
1034:
1030:
1026:
1022:
1015:
1013:
1011:
1007:
1002:
998:
994:
990:
986:
985:10.1038/82028
982:
978:
974:
970:
963:
961:
957:
952:
948:
943:
938:
934:
930:
929:J. Biol. Chem
926:
919:
917:
915:
913:
911:
907:
902:
898:
893:
888:
884:
880:
876:
872:
868:
861:
858:
853:
849:
845:
841:
837:
833:
829:
825:
821:
814:
811:
806:
802:
798:
792:
788:
784:
780:
776:
769:
767:
765:
761:
756:
752:
748:
746:0-12-034267-7
742:
738:
734:
730:
726:
719:
717:
715:
713:
709:
703:
699:
696:
694:
691:
689:
686:
684:
681:
679:
676:
675:
671:
669:
662:
660:
658:
654:
650:
646:
642:
638:
630:
628:
625:
620:
617:
609:
607:
605:
599:
597:
594:
590:
583:
581:
574:
572:
565:
563:
561:
557:
553:
549:
545:
541:
537:
533:
525:
523:
516:
514:
507:
501:
497:
495:
487:
485:
478:
473:
469:
465:
461:
457:
453:
449:
445:
441:
437:
433:
430:
428:
424:
420:
416:
412:
408:
404:
400:
396:
392:
388:
384:
380:
376:
373:
371:
368:
366:
363:
361:
357:
353:
349:
345:
342:
340:
336:
332:
328:
325:
323:
320:
318:
315:
314:
313:
310:
303:
297:
289:
285:
283:
277:
273:
269:
265:
261:
257:
253:
250:
246:
242:
238:
234:
230:
226:
222:
210:
207:
205:
201:
198:
195:
193:
189:
186:
183:
181:
177:
172:
168:
165:
161:
158:
156:
155:Gene Ontology
152:
149:
146:
143:
140:
137:
133:
130:
127:
125:
121:
118:
115:
113:
109:
106:
103:
101:
97:
94:
93:NiceZyme view
91:
89:
85:
82:
79:
77:
73:
70:
67:
65:
61:
56:
53:
50:
48:
44:
41:
38:
36:
32:
27:
20:
2866:Translocases
2863:
2850:
2837:
2824:
2811:
2801:Transferases
2798:
2785:
2642:Binding site
2359:
2316:Homocysteine
1898:
1681:
1677:
1648:
1644:
1599:
1595:
1585:
1552:
1548:
1538:
1511:
1507:
1497:
1470:
1426:
1423:J. Mol. Biol
1422:
1412:
1385:
1381:
1371:
1344:
1340:
1300:
1296:
1286:
1259:
1255:
1245:
1220:
1216:
1210:
1183:
1179:
1169:
1142:
1138:
1128:
1101:
1097:
1072:. Retrieved
1063:
1028:
1024:
976:
972:
932:
928:
874:
870:
860:
827:
823:
813:
778:
728:
666:
634:
621:
613:
600:
587:
578:
569:
529:
520:
511:
491:
482:
311:
307:
263:
259:
255:
247:residues of
224:
220:
219:
81:BRENDA entry
2925:Methylation
2920:Epigenetics
2637:Active site
2234:Transferase
2164:Termination
2040:Pribnow box
2008:Corepressor
2003:Coactivator
1804:prokaryotic
1347:(1): 8–24.
258:u(var)3-9,
69:IntEnz view
29:Identifiers
2909:Categories
2840:Isomerases
2814:Hydrolases
2681:Regulation
2192:Rho factor
2182:Terminator
2173:eukaryotic
2148:eukaryotic
2129:Elongation
2115:Eukaryotic
2103:Initiation
1886:nucleosome
1869:eukaryotic
1841:gal operon
1836:ara operon
1831:Gua Operon
1826:gab operon
1821:trp operon
1816:lac operon
1787:Eukaryotic
1388:(1): 5–8.
824:Curr. Biol
704:References
631:DNA repair
593:epigenetic
266:rithorax)
239:groups to
138:structures
105:KEGG entry
52:9055-08-7
2719:EC number
2518:Carbamoyl
2494:Carbamoyl
2168:bacterial
2136:bacterial
2110:Bacterial
2084:Insulator
2028:Promotion
1998:Activator
1848:Repressor
1783:Bacterial
871:Genes Dev
566:Structure
517:Structure
479:Structure
282:chromatin
58:Databases
2915:EC 2.1.1
2743:Kinetics
2667:Cofactor
2630:Activity
2089:Silencer
2067:Enhancer
2055:CAAT box
2045:TATA box
2035:Promoter
1708:19332880
1678:Genetics
1665:15248813
1626:29937925
1596:J Cancer
1577:13456531
1569:15235609
1530:15723344
1404:11461695
1363:28061334
1319:10652296
1237:10381882
1202:12628190
1161:12372303
1120:17320507
1055:10899106
1001:11575783
993:11101900
951:11413150
901:12080090
852:17263035
844:12123582
805:20920745
755:14969729
672:See also
468:SUV420H2
276:cofactor
252:proteins
245:arginine
233:catalyze
209:proteins
197:articles
185:articles
142:RCSB PDB
40:2.1.1.43
2899:Biology
2853:Ligases
2623:Enzymes
2573:Amidine
2502:Carboxy
2488:Carboxy
2251:Methyl-
2015:Inducer
1882:histone
1699:2691753
1617:6010677
1443:4689953
1278:8647869
1217:Science
1074:1 March
460:SUV39H2
456:SUV39H1
249:histone
229:enzymes
164:QuickGO
129:profile
112:MetaCyc
47:CAS no.
2885:Portal
2827:Lyases
2403:Formyl
2355:DNMT3B
1811:Operon
1744:(MeSH)
1734:(MeSH)
1706:
1696:
1663:
1624:
1614:
1575:
1567:
1528:
1485:
1441:
1402:
1361:
1317:
1276:
1235:
1200:
1159:
1118:
1053:
1046:313989
1043:
1025:EMBO J
999:
991:
949:
899:
892:186335
889:
850:
842:
803:
793:
753:
743:
637:lysine
432:SETMAR
427:SETDB2
423:SETDB1
387:SETD1B
383:SETD1A
379:SETBP1
268:domain
241:lysine
237:methyl
192:PubMed
174:Search
160:AmiGO
148:PDBsum
88:ExPASy
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