Knowledge (XXG)

Succinylation

Source 📝

1097: 1350: 259: 1090: 1938: 1083: 252: 1695: 227: 63:. The potential role of succinylation is under investigation, but as addition of succinyl group changes lysine's charge from +1 to −1 (at 1913: 245: 1106: 1306: 272: 28: 1519: 922: 1464: 962: 373: 268: 237: 1404: 1729: 1016: 99: 1901: 900: 1770: 1151: 291: 306: 1114: 378: 727: 1760: 1128: 717: 621: 471: 68: 1430: 575: 461: 420: 223:
Succinylation, Yet A Novel PTM Pathway for Biological Regulation, But Ready to Be Investigated
201: 152: 84: 1690: 1649: 1644: 1619: 1609: 1604: 1594: 1394: 878: 856: 755: 674: 565: 542: 466: 438: 191: 183: 142: 132: 64: 1665: 1599: 1896: 1119: 989: 689: 580: 456: 415: 232: 1443: 1438: 851: 745: 722: 664: 514: 496: 383: 349: 196: 171: 147: 120: 119:
Xie, Z.; Dai, J.; Dai, L.; Tan, M.; Cheng, Z.; Wu, Y.; Boeke, J. D.; Zhao, Y. (2012).
1932: 870: 815: 797: 773: 707: 659: 654: 603: 560: 481: 425: 329: 72: 32: 1799: 1781: 669: 486: 301: 286: 95: 20: 1075: 172:"Identification of lysine succinylation as a new post-translational modification" 1875: 1743: 791: 750: 679: 644: 639: 598: 570: 537: 519: 491: 344: 334: 324: 296: 91: 80: 76: 1705: 1133: 1031: 937: 914: 910: 866: 830: 807: 590: 394: 360: 316: 1453: 1399: 1060: 973: 783: 702: 649: 613: 552: 529: 476: 407: 339: 137: 205: 156: 1733: 1366: 1358: 1048: 1044: 1040: 977: 950: 892: 843: 839: 737: 684: 506: 448: 430: 222: 187: 60: 1484: 1371: 1331: 1262: 1257: 1252: 1247: 1242: 1197: 1008: 1000: 981: 954: 765: 56: 1700: 1675: 1670: 1660: 1624: 1614: 1589: 1574: 1569: 1564: 1559: 1554: 1549: 1544: 1539: 1504: 1489: 1336: 1301: 1286: 1281: 1276: 1237: 1232: 1227: 1222: 1217: 1212: 1207: 1202: 1192: 1187: 1182: 1177: 1172: 1052: 1004: 946: 888: 631: 403: 52: 1891: 1881: 1871: 1856: 1838: 1833: 1828: 1823: 1755: 1715: 1680: 1654: 1639: 1634: 1629: 1584: 1579: 1534: 1529: 1524: 1494: 1479: 1376: 1345: 1326: 1321: 1316: 1311: 1296: 1291: 1271: 1167: 1160: 1156: 1146: 1141: 697: 368: 170:
Zhang, Z.; Tan, M.; Xie, Z.; Dai, L.; Chen, Y.; Zhao, Y. (2010).
59:
molecule. This modification is found in many proteins, including
1906: 1886: 1866: 1861: 1811: 1794: 1750: 1738: 1720: 1710: 1509: 1499: 1474: 1469: 1414: 1409: 1079: 241: 83:(14 Da), it is expected to lead to more significant changes in 233:
The dawn of succinylation: a posttranslational modification.
16:
Addition of a succinyl group to a lysine group of a protein
121:"Lysine succinylation and lysine malonylation in histones" 990:
4-(p-hydroxybenzylidene)-5-imidazolinone (HBI) formation
1849: 1780: 1769: 1452: 1429: 1387: 1127: 1113: 1039: 1029: 999: 972: 945: 935: 909: 887: 865: 838: 828: 806: 782: 764: 736: 630: 612: 589: 551: 528: 505: 447: 402: 392: 359: 315: 279: 963:p-Hydroxybenzylidene-imidazolinone (HBI) formation 67:) and introduces a relatively large structural 1091: 253: 8: 923:Tryptophan tryptophylquinone (TTQ) formation 1777: 1124: 1098: 1084: 1076: 1036: 942: 835: 399: 260: 246: 238: 195: 146: 136: 102:of enzyme-mediated lysine succinylation. 46: 42: 38: 1017:Methylidene-imidazolone (MIO) formation 111: 901:Lysine tyrosylquinone (LTQ) formation 7: 374:Glycosyl phosphatidylinositol (GPI) 125:Molecular & Cellular Proteomics 1914:Prokaryotic ubiquitin-like protein 14: 685:Oxidative deamination to aldehyde 1939:Post-translational modification 273:posttranslational modifications 1444:Mitochondrial targeting signal 1107:Posttranslational modification 29:posttranslational modification 1: 94:, it has been suggested that 1520:Ubiquitin-conjugating enzyme 1808:E2 SUMO-conjugating enzyme 1465:Ubiquitin-activating enzyme 492:Topaquinone (TPQ) formation 1955: 1791:E1 SUMO-activating enzyme 936:Crosslinks between three 269:Protein primary structure 1405:Survival of motor neuron 1030:Crosslinks between four 1771:Ubiquitin-like proteins 1730:Deubiquitinating enzyme 829:Crosslinks between two 228:Succinyl group at ChEBI 176:Nature Chemical Biology 138:10.1074/mcp.M111.015875 477:Porphyrin ring linkage 538:Succinimide formation 292:Protein biosynthesis 188:10.1038/nchembio.495 1129:Heat shock proteins 622:Transglutamination 1926: 1925: 1922: 1921: 1431:Protein targeting 1425: 1424: 1073: 1072: 1069: 1068: 1025: 1024: 931: 930: 824: 823: 576:Polyglutamylation 462:Dephosphorylation 421:Dephosphorylation 85:protein structure 1946: 1778: 1691:Ubiquitin ligase 1457:(ubiquitylation) 1395:Alpha crystallin 1125: 1100: 1093: 1086: 1077: 1037: 943: 879:Sulfilimine bond 857:ADP-ribosylation 836: 756:ADP-ribosylation 675:ADP-ribosylation 566:ADP-ribosylation 543:ADP-ribosylation 467:ADP-ribosylation 439:ADP-ribosylation 400: 393:Single specific 262: 255: 248: 239: 210: 209: 199: 167: 161: 160: 150: 140: 116: 65:physiological pH 51:) is added to a 50: 1954: 1953: 1949: 1948: 1947: 1945: 1944: 1943: 1929: 1928: 1927: 1918: 1845: 1820:E3 SUMO ligase 1784: 1773: 1765: 1456: 1448: 1421: 1383: 1362: 1354: 1132: 1120:protein folding 1118: 1109: 1104: 1074: 1065: 1021: 995: 968: 927: 905: 883: 861: 820: 816:C-mannosylation 802: 778: 760: 732: 698:Imine formation 626: 608: 585: 581:Polyglycylation 547: 524: 501: 457:Phosphorylation 443: 416:Phosphorylation 388: 355: 311: 275: 266: 219: 214: 213: 169: 168: 164: 118: 117: 113: 108: 75:), bigger than 48: 44: 40: 36: 17: 12: 11: 5: 1952: 1950: 1942: 1941: 1931: 1930: 1924: 1923: 1920: 1919: 1917: 1916: 1910: 1909: 1904: 1899: 1894: 1889: 1884: 1879: 1869: 1864: 1859: 1853: 1851: 1847: 1846: 1844: 1843: 1842: 1841: 1836: 1831: 1826: 1817: 1816: 1815: 1814: 1805: 1804: 1803: 1802: 1797: 1788: 1786: 1775: 1767: 1766: 1764: 1763: 1758: 1753: 1747: 1746: 1741: 1736: 1726: 1725: 1724: 1723: 1718: 1713: 1708: 1703: 1698: 1686: 1685: 1684: 1683: 1678: 1673: 1668: 1663: 1658: 1652: 1647: 1642: 1637: 1632: 1627: 1622: 1617: 1612: 1607: 1602: 1597: 1592: 1587: 1582: 1577: 1572: 1567: 1562: 1557: 1552: 1547: 1542: 1537: 1532: 1527: 1515: 1514: 1513: 1512: 1507: 1502: 1497: 1492: 1487: 1482: 1477: 1472: 1460: 1458: 1450: 1449: 1447: 1446: 1441: 1439:Signal peptide 1435: 1433: 1427: 1426: 1423: 1422: 1420: 1419: 1418: 1417: 1412: 1402: 1397: 1391: 1389: 1385: 1384: 1382: 1381: 1380: 1379: 1374: 1369: 1364: 1360: 1356: 1352: 1342: 1341: 1340: 1339: 1334: 1329: 1324: 1319: 1314: 1309: 1304: 1299: 1294: 1289: 1284: 1279: 1268: 1267: 1266: 1265: 1260: 1255: 1250: 1245: 1240: 1235: 1230: 1225: 1220: 1215: 1210: 1205: 1200: 1195: 1190: 1185: 1180: 1175: 1164: 1163: 1154: 1149: 1144: 1138: 1136: 1122: 1111: 1110: 1105: 1103: 1102: 1095: 1088: 1080: 1071: 1070: 1067: 1066: 1064: 1063: 1057: 1055: 1034: 1027: 1026: 1023: 1022: 1020: 1019: 1013: 1011: 997: 996: 994: 993: 986: 984: 970: 969: 967: 966: 959: 957: 940: 933: 932: 929: 928: 926: 925: 919: 917: 907: 906: 904: 903: 897: 895: 885: 884: 882: 881: 875: 873: 863: 862: 860: 859: 854: 852:Disulfide bond 848: 846: 833: 826: 825: 822: 821: 819: 818: 812: 810: 804: 803: 801: 800: 795: 788: 786: 780: 779: 777: 776: 770: 768: 762: 761: 759: 758: 753: 748: 746:Citrullination 742: 740: 734: 733: 731: 730: 725: 723:Propionylation 720: 715: 710: 705: 700: 695: 693:-glycosylation 687: 682: 677: 672: 667: 665:Ubiquitination 662: 657: 652: 647: 642: 636: 634: 628: 627: 625: 624: 618: 616: 610: 609: 607: 606: 601: 595: 593: 587: 586: 584: 583: 578: 573: 568: 563: 557: 555: 549: 548: 546: 545: 540: 534: 532: 526: 525: 523: 522: 517: 515:Palmitoylation 511: 509: 503: 502: 500: 499: 497:Detyrosination 494: 489: 487:Flavin linkage 484: 479: 474: 469: 464: 459: 453: 451: 445: 444: 442: 441: 436: 428: 423: 418: 412: 410: 397: 390: 389: 387: 386: 384:Detyrosination 381: 376: 371: 365: 363: 357: 356: 354: 353: 350:Myristoylation 347: 342: 337: 332: 327: 321: 319: 313: 312: 310: 309: 307:N–O acyl shift 304: 299: 294: 289: 283: 281: 277: 276: 267: 265: 264: 257: 250: 242: 236: 235: 230: 225: 218: 217:External links 215: 212: 211: 162: 110: 109: 107: 104: 90:By analogy to 87:and function. 15: 13: 10: 9: 6: 4: 3: 2: 1951: 1940: 1937: 1936: 1934: 1915: 1912: 1911: 1908: 1905: 1903: 1900: 1898: 1895: 1893: 1890: 1888: 1885: 1883: 1880: 1877: 1873: 1870: 1868: 1865: 1863: 1860: 1858: 1855: 1854: 1852: 1848: 1840: 1837: 1835: 1832: 1830: 1827: 1825: 1822: 1821: 1819: 1818: 1813: 1810: 1809: 1807: 1806: 1801: 1798: 1796: 1793: 1792: 1790: 1789: 1787: 1785:(SUMOylation) 1783: 1779: 1776: 1772: 1768: 1762: 1759: 1757: 1754: 1752: 1749: 1748: 1745: 1742: 1740: 1737: 1735: 1731: 1728: 1727: 1722: 1719: 1717: 1714: 1712: 1709: 1707: 1704: 1702: 1699: 1697: 1694: 1693: 1692: 1688: 1687: 1682: 1679: 1677: 1674: 1672: 1669: 1667: 1664: 1662: 1659: 1656: 1653: 1651: 1648: 1646: 1643: 1641: 1638: 1636: 1633: 1631: 1628: 1626: 1623: 1621: 1618: 1616: 1613: 1611: 1608: 1606: 1603: 1601: 1598: 1596: 1593: 1591: 1588: 1586: 1583: 1581: 1578: 1576: 1573: 1571: 1568: 1566: 1563: 1561: 1558: 1556: 1553: 1551: 1548: 1546: 1543: 1541: 1538: 1536: 1533: 1531: 1528: 1526: 1523: 1522: 1521: 1517: 1516: 1511: 1508: 1506: 1503: 1501: 1498: 1496: 1493: 1491: 1488: 1486: 1483: 1481: 1478: 1476: 1473: 1471: 1468: 1467: 1466: 1462: 1461: 1459: 1455: 1451: 1445: 1442: 1440: 1437: 1436: 1434: 1432: 1428: 1416: 1413: 1411: 1408: 1407: 1406: 1403: 1401: 1398: 1396: 1393: 1392: 1390: 1386: 1378: 1375: 1373: 1370: 1368: 1365: 1363: 1357: 1355: 1349: 1348: 1347: 1344: 1343: 1338: 1335: 1333: 1330: 1328: 1325: 1323: 1320: 1318: 1315: 1313: 1310: 1308: 1305: 1303: 1300: 1298: 1295: 1293: 1290: 1288: 1285: 1283: 1280: 1278: 1275: 1274: 1273: 1270: 1269: 1264: 1261: 1259: 1256: 1254: 1251: 1249: 1246: 1244: 1241: 1239: 1236: 1234: 1231: 1229: 1226: 1224: 1221: 1219: 1216: 1214: 1211: 1209: 1206: 1204: 1201: 1199: 1196: 1194: 1191: 1189: 1186: 1184: 1181: 1179: 1176: 1174: 1171: 1170: 1169: 1166: 1165: 1162: 1158: 1155: 1153: 1150: 1148: 1145: 1143: 1140: 1139: 1137: 1135: 1130: 1126: 1123: 1121: 1116: 1112: 1108: 1101: 1096: 1094: 1089: 1087: 1082: 1081: 1078: 1062: 1059: 1058: 1056: 1054: 1050: 1046: 1042: 1038: 1035: 1033: 1028: 1018: 1015: 1014: 1012: 1010: 1006: 1002: 998: 992:(chromophore) 991: 988: 987: 985: 983: 979: 975: 971: 965:(chromophore) 964: 961: 960: 958: 956: 952: 948: 944: 941: 939: 934: 924: 921: 920: 918: 916: 912: 908: 902: 899: 898: 896: 894: 890: 886: 880: 877: 876: 874: 872: 871:Hydroxylysine 868: 864: 858: 855: 853: 850: 849: 847: 845: 841: 837: 834: 832: 827: 817: 814: 813: 811: 809: 805: 799: 798:Adenylylation 796: 793: 790: 789: 787: 785: 781: 775: 774:Hydroxylation 772: 771: 769: 767: 763: 757: 754: 752: 749: 747: 744: 743: 741: 739: 735: 729: 726: 724: 721: 719: 716: 714: 713:Succinylation 711: 709: 708:Carbamylation 706: 704: 701: 699: 696: 694: 692: 688: 686: 683: 681: 678: 676: 673: 671: 668: 666: 663: 661: 660:Hydroxylation 658: 656: 655:Adenylylation 653: 651: 648: 646: 643: 641: 638: 637: 635: 633: 629: 623: 620: 619: 617: 615: 611: 605: 604:Glycosylation 602: 600: 597: 596: 594: 592: 588: 582: 579: 577: 574: 572: 569: 567: 564: 562: 561:Carboxylation 559: 558: 556: 554: 550: 544: 541: 539: 536: 535: 533: 531: 527: 521: 518: 516: 513: 512: 510: 508: 504: 498: 495: 493: 490: 488: 485: 483: 482:Adenylylation 480: 478: 475: 473: 470: 468: 465: 463: 460: 458: 455: 454: 452: 450: 446: 440: 437: 435: 433: 429: 427: 426:Glycosylation 424: 422: 419: 417: 414: 413: 411: 409: 405: 401: 398: 396: 391: 385: 382: 380: 379:O-methylation 377: 375: 372: 370: 367: 366: 364: 362: 358: 351: 348: 346: 343: 341: 338: 336: 333: 331: 330:Carbamylation 328: 326: 323: 322: 320: 318: 314: 308: 305: 303: 300: 298: 295: 293: 290: 288: 285: 284: 282: 278: 274: 270: 263: 258: 256: 251: 249: 244: 243: 240: 234: 231: 229: 226: 224: 221: 220: 216: 207: 203: 198: 193: 189: 185: 181: 177: 173: 166: 163: 158: 154: 149: 144: 139: 134: 130: 126: 122: 115: 112: 105: 103: 101: 97: 93: 88: 86: 82: 78: 74: 70: 66: 62: 58: 55:residue of a 54: 34: 30: 26: 25:succinylation 22: 1782:SUMO protein 728:Butyrylation 712: 690: 431: 302:Racemization 287:Peptide bond 182:(1): 58–63. 179: 175: 165: 131:(5): 100–7. 128: 124: 114: 96:succinyl-CoA 89: 24: 21:biochemistry 18: 1876:neddylation 1142:Hsp10/GroES 1134:Chaperonins 792:Diphthamide 751:Methylation 718:Lactylation 680:Deamination 670:Sumoylation 645:Acetylation 640:Methylation 599:Deamidation 571:Methylation 520:Prenylation 345:Methylation 335:Formylation 325:Acetylation 297:Proteolysis 92:acetylation 81:methylation 79:(42 Da) or 77:acetylation 1168:Hsp40/DnaJ 1115:Chaperones 915:Tryptophan 911:Tryptophan 867:Methionine 808:Tryptophan 591:Asparagine 361:C terminus 317:N terminus 106:References 1454:Ubiquitin 1400:Clusterin 1061:Desmosine 974:Histidine 794:formation 784:Histidine 703:Glycation 650:Acylation 614:Glutamine 553:Glutamate 530:Aspartate 472:Sulfation 408:Threonine 369:Amidation 340:Glycation 1933:Category 1734:Ataxin 3 1049:Allysine 1045:Allysine 1041:Allysine 978:Tyrosine 951:Tyrosine 893:Tyrosine 844:Cysteine 840:Cysteine 738:Arginine 507:Cysteine 449:Tyrosine 206:21151122 157:22389435 100:cofactor 61:histones 33:succinyl 31:where a 1657:(CDC34) 1009:Glycine 1001:Alanine 982:Glycine 955:Glycine 766:Proline 434:-GlcNAc 280:General 197:3065206 148:3418837 98:is the 57:protein 35:group ( 1701:Cullin 1053:Lysine 1005:Serine 947:Serine 889:Lysine 632:Lysine 404:Serine 204:  194:  155:  145:  69:moiety 53:lysine 37:−CO−CH 1892:ATG12 1882:FAT10 1872:NEDD8 1857:ISG15 1850:Other 1839:PIAS4 1834:PIAS3 1829:PIAS2 1824:PIAS1 1774:(UBL) 1756:BIRC6 1716:FANCL 1388:Other 1377:TRAP1 1346:Hsp90 1272:Hsp70 1161:GroEL 1157:HSP60 1152:Hsp47 1147:Hsp27 352:(Gly) 71:(100 27:is a 1907:UBL5 1897:FUB1 1887:ATG8 1867:UFM1 1862:URM1 1812:UBC9 1800:SAE2 1795:SAE1 1761:UFC1 1751:ATG3 1744:CYLD 1739:USP6 1721:UBR1 1711:MDM2 1510:SAE1 1505:NAE1 1500:ATG7 1495:UBA7 1490:UBA6 1485:UBA5 1480:UBA3 1475:UBA2 1470:UBA1 1415:SMN2 1410:SMN1 271:and 202:PMID 153:PMID 1902:MUB 1706:CBL 1696:VHL 1689:E3 1518:E2 1463:E1 1332:12A 1263:C19 1258:C14 1253:C13 1248:C11 1243:C10 1198:B11 1032:AAs 938:AAs 831:AAs 395:AAs 192:PMC 184:doi 143:PMC 133:doi 45:−CO 41:−CH 19:In 1935:: 1732:: 1676:V2 1671:V1 1661:R2 1655:R1 1650:Q2 1645:Q1 1625:L6 1620:L4 1615:L3 1610:L2 1605:L1 1595:J2 1590:J1 1575:G2 1570:G1 1565:E3 1560:E2 1555:E1 1550:D3 1545:D2 1540:D1 1372:ER 1337:14 1302:4L 1287:1L 1282:1B 1277:1A 1238:C7 1233:C6 1228:C5 1223:C3 1218:C1 1213:B9 1208:B6 1203:B4 1193:B2 1188:B1 1183:A3 1178:A2 1173:A1 200:. 190:. 178:. 174:. 151:. 141:. 129:11 127:. 123:. 73:Da 23:, 1878:) 1874:( 1681:Z 1666:S 1640:O 1635:N 1630:M 1600:K 1585:I 1580:H 1535:C 1530:B 1525:A 1367:β 1361:2 1359:α 1353:1 1351:α 1327:9 1322:8 1317:7 1312:6 1307:5 1297:4 1292:2 1159:/ 1131:/ 1117:/ 1099:e 1092:t 1085:v 1051:– 1047:– 1043:– 1007:– 1003:– 980:– 976:– 953:– 949:– 913:– 891:– 869:– 842:– 691:O 432:O 406:/ 261:e 254:t 247:v 208:. 186:: 180:7 159:. 135:: 49:H 47:2 43:2 39:2

Index

biochemistry
posttranslational modification
succinyl
lysine
protein
histones
physiological pH
moiety
Da
acetylation
methylation
protein structure
acetylation
succinyl-CoA
cofactor
"Lysine succinylation and lysine malonylation in histones"
doi
10.1074/mcp.M111.015875
PMC
3418837
PMID
22389435
"Identification of lysine succinylation as a new post-translational modification"
doi
10.1038/nchembio.495
PMC
3065206
PMID
21151122
Succinylation, Yet A Novel PTM Pathway for Biological Regulation, But Ready to Be Investigated

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