1167:
with transcriptional upregulation observed in liver, uterine cervix, ovarian, pancreatic, gastric and small intestine adenocarcinomas, but not in thyroid, prostate or kidney cancers. In hepatic cancer cells, increased expression of UBD was associated with
Proliferating Cell Nuclear Antigen, a cell proliferation marker, and reported to provide a growth advantage over cells without UBD expression. High UBD expression also promoted hepatocellular carcinoma development in a mouse model and formation of Mallory–Denk bodies, which are preneoplastic changes in chronic liver disease. Overexpression of UBD in gastric cancer has been correlated with metastasis and tumor staging, and both UBD mRNA and protein levels were identified as independent prognostic factors for this disease. Increased UBD has also been positively correlated with mutant p53 expression, which may activate UBD expression and indirectly facilitate gastric cancer progression. Interferon-γ and tumor necrosis factor-α act synergistically to induce the UBD promoter through an interferon sequence resposive element. Collectively, these data indicate that UBD may be a marker for precancerous lesions and may promote cancer progression.
1135:
means that the degradation rate of a protein, that is, the half-life of a protein, varies depending on what the amino-terminal amino acid residue is. In the amino-terminal rule of yeast, it is known that the half-life of proteins varies depending on the presence of 12 unstable amino acid residues (arginine, lysine, histidine, tyrosine, tryptophan, isoleucine, aspartic acid, glutamic acid, asparagine, glutamine) out of 20 amino acids. When methionine, glycine, serine, valine, or proline is located at the amino-terminus, it has a half-life of more than 20 hours, whereas when residues such as tyrosine, glutamine, leucine, phenylalanine, aspartate, lysine, or arginine are located, the half-life is reduced to less than 10 minutes.
310:
287:
184:
209:
316:
215:
1102:
1139:
degradation signal in the substrate protein, and then the E2 enzyme helps to form a multi-ubiquitin chain at the lysine residue of the substrate protein. In order to form a multi-ubiquitin chain, the C-terminal region of the next ubiquitin molecule is linked to the lysine residue of the preceding ubiquitin.
1166:
UBD also has important roles in cell mitosis, chromosome instability, apoptosis and immune response. UBD deregulation may induce abnormal alterations in apoptosis, cell division or chromosome instability, which are associated with neoplastic change. Tumor UBD expression shows some tissue specificity,
1134:
In particular, E3 enzymes can be divided into four types such as HECT, RING-finger, U-box, and PHD-finger according to the method of determining the specificity of the substrate protein. Among them, the RING-finger E3 enzyme is known to follow the amino terminal rule the best. The amino-terminal rule
1117:
Proteolysis in cells is an essential process to prevent the production of unwanted or abnormal proteins. During protein degradation, the process in which proteolytic enzymes act in an ATP-dependent manner mainly occurs in the degradation of substrate proteins with short half-lives. In particular, in
1108:
Ubiquitin is a protein composed of 76 amino acids. In order for ubiquitin to bind to other proteins, it must go through an activation process by E1, an ATP-dependent ubiquitin activating enzyme. The carboxyl terminal (C-terminus) of ubiquitin is linked to the cysteine residue of the E1 protein by a
1162:
was first discovered in reticuloendothelial tissues and mucosal-associated lymphoid immunological systems as one of the genes at the human major histocompatibility complex class I locus on chromosome 6. The UBD gene encodes an 18 kDa protein containing an N- and C-terminus with 29 and 36% identity
1146:
In general, the proteasome is responsible for removing structurally abnormal proteins, but also contributes to regulating the lifespan of specific proteins according to the intracellular environment. For example, mitotic cyclins required for the induction of mitosis (or mitosis) remain long-lived
2208:
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,
1150:
Then, how does this regulation of protein degradation occur? Activation of E3, a ubiquitin linking enzyme, can be achieved by phosphorylation or allosteric transition following ligand or subunit binding. For example, the anaphase-promoting complex (APC) is a multiubiquitin-linking enzyme that is
1130:
About a dozen E2 proteins are known to exist in yeast as transfer proteins that transfer ubiquitin from E1 to E3 or substrates, and it has been confirmed that more types exist in higher eukaryotes than yeast. E3 enzyme, also called E3 ligase, is an enzyme that acts in the final step of attaching
1142:
About 30 different E2s exist in mammalian cells, and more than 300 specific E2-E3 complexes have been found. Thanks to the function of the E3 component, they can recognize specific degradation signals of target proteins. In general, E2 is called ubiquitin-linking enzyme, and E3 is traditionally
1138:
Activated ubiquitin bound to E1 is transferred to the cysteine residue of the E2 molecule (ubiquitin conjugating enzyme). E2 molecules form complexes with E3 protein molecules, which are accessory proteins. In the E2-E3 complex, called ubiquitin ligase, the E3 component binds to a specific
63:
2076:
Barrios-Rodiles M, Brown KR, Ozdamar B, Bose R, Liu Z, Donovan RS, Shinjo F, Liu Y, Dembowy J, Taylor IW, Luga V, Przulj N, Robinson M, Suzuki H, Hayashizaki Y, Jurisica I, Wrana JL (Mar 2005). "High-throughput mapping of a dynamic signaling network in mammalian cells".
1163:
with ubiquitin, respectively. Of the ubiquitin-like proteins that have been identified, UBD is the only one of that conjugate to target proteins by a free diglycine motif at the C-terminus and directly guides noncovalently bound proteins to proteasomal degradation.
2003:
Brès V, Kiernan RE, Linares LK, Chable-Bessia C, Plechakova O, Tréand C, Emiliani S, Peloponese JM, Jeang KT, Coux O, Scheffner M, Benkirane M (Aug 2003). "A non-proteolytic role for ubiquitin in Tat-mediated transactivation of the HIV-1 promoter".
1209:
ENSG00000231968, ENSG00000206468, ENSG00000206513, ENSG00000224654, ENSG00000213886, ENSG00000226898 GRCh38: Ensembl release 89: ENSG00000228913, ENSG00000231968, ENSG00000206468, ENSG00000206513, ENSG00000224654, ENSG00000213886,
1143:
called ubiquitin-linking enzyme. Functionally, however, it is more accurate to call the E2-E3 complex a ubiquitin ligase. Multi-ubiquitin chains on target proteins are recognized by specific receptors on the proteasome.
2209:
Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network".
1126:
E1, E2 proteins and E3 enzymes are essential for attaching ubiquitin to matrix proteins. Among them, only one type of E1 protein exists in an individual, and it is known that the number is the highest.
1647:"Ubiquitin is covalently attached to the p6Gag proteins of human immunodeficiency virus type 1 and simian immunodeficiency virus and to the p12Gag protein of Moloney murine leukemia virus"
1118:
eukaryotic cells, the proteolysis process by the binding of ubiquitin composed of 76 amino acids plays an important role in regulating the half-life and function of proteins.
1151:
activated during mitosis by the addition of subunits along the cell cycle. Activated APC promotes proteolysis of mitotic cyclins and metaphase-late transition regulators.
323:
222:
1330:
Fan W, Cai W, Parimoo S, Schwarz DC, Lennon GG, Weissman SM (Aug 1996). "Identification of seven new human MHC class I region genes around the HLA-F locus".
790:
771:
145:
1287:, Lebecque S (Oct 1997). "Identification and analysis of a novel member of the ubiquitin family expressed in dendritic cells and mature B cells".
1265:
1247:
2264:
309:
1970:"Expression of the FAT10 gene is highly upregulated in hepatocellular carcinoma and other gastrointestinal and gynecological cancers"
1023:
1016:
286:
1109:
high energy thioester linkage and activated. This reaction requires ATP and proceeds through a covalent AMP-ubiquitin intermediate.
1373:
1464:"Ubiquitin D is correlated with colon cancer progression and predicts recurrence for stage II-III disease after curative surgery"
1234:
1213:
1131:
ubiquitin to a substrate protein. The specificity of the substrate protein to be ubiquitinated is determined by the E3 enzyme.
1645:
Ott DE, Coren LV, Copeland TD, Kane BP, Johnson DG, Sowder RC, Yoshinaka Y, Oroszlan S, Arthur LO, Henderson LE (Apr 1998).
1462:
Yan DW, Li DW, Yang YX, Xia J, Wang XL, Zhou CZ, Fan JW, Wen YG, Sun HC, Wang Q, Qiu GQ, Tang HM, Peng ZH (September 2010).
1230:
208:
183:
60:
1208:
1884:"Late assembly domain function can exhibit context dependence and involves ubiquitin residues implicated in endocytosis"
125:
1968:
Lee CG, Ren J, Cheong IS, Ban KH, Ooi LL, Yong Tan S, Kan A, Nuchprayoon I, Jin R, Lee KH, Choti M, Lee LA (May 2003).
1741:
Schubert U, Ott DE, Chertova EN, Welker R, Tessmer U, Princiotta MF, Bennink JR, Krausslich HG, Yewdell JW (Nov 2000).
1437:
1412:
1387:
1624:
Mazzé FM, Degrève L (2006). "The role of viral and cellular proteins in the budding of human immunodeficiency virus".
1176:
322:
221:
1690:"A MHC-encoded ubiquitin-like protein (FAT10) binds noncovalently to the spindle assembly checkpoint protein MAD2"
1562:"A MHC-encoded ubiquitin-like protein (FAT10) binds noncovalently to the spindle assembly checkpoint protein MAD2"
315:
214:
861:
133:
1743:"Proteasome inhibition interferes with gag polyprotein processing, release, and maturation of HIV-1 and HIV-2"
842:
838:
828:
824:
820:
816:
812:
2043:"NEDD8 ultimate buster-1L interacts with the ubiquitin-like protein FAT10 and accelerates its degradation"
1521:"NEDD8 ultimate buster-1L interacts with the ubiquitin-like protein FAT10 and accelerates its degradation"
2218:
2086:
1807:
1754:
1701:
1573:
197:
112:
2242:
2110:
2029:
1355:
1312:
1284:
157:
999:
978:
952:
931:
2234:
2196:
2153:
2102:
2064:
2021:
1991:
1956:
1913:
1870:
1835:
1782:
1729:
1676:
1633:
1601:
1542:
1501:
1483:
1347:
1304:
105:
53:
2226:
2186:
2178:
2143:
2135:
2094:
2054:
2013:
1981:
1946:
1938:
1903:
1895:
1860:
1825:
1815:
1772:
1762:
1719:
1709:
1666:
1658:
1591:
1581:
1532:
1491:
1475:
1339:
1296:
402:
333:
277:
232:
1147:
throughout the cell cycle, but are destined for abrupt degradation at the end of mitosis.
377:
1927:"Retroviruses have differing requirements for proteasome function in the budding process"
153:
2222:
2090:
1811:
1758:
1705:
1577:
2191:
2166:
2148:
2123:
1496:
1463:
1093:, by covalently modifying proteins and tagging them for destruction in the proteasome.
1951:
1926:
1908:
1883:
1671:
1646:
705:
700:
695:
690:
685:
680:
675:
670:
665:
660:
655:
650:
634:
629:
624:
619:
614:
598:
593:
2258:
2182:
1899:
1830:
1795:
1777:
1742:
1724:
1689:
1596:
1561:
1283:
Bates EE, Ravel O, Dieu MC, Ho S, Guret C, Bridon JM, Ait-Yahia S, Brière F, Caux C,
580:
2139:
2114:
1942:
1662:
1359:
1316:
1101:
137:
2246:
2033:
395:
174:
161:
1270:
National Center for
Biotechnology Information, U.S. National Library of Medicine
1252:
National Center for
Biotechnology Information, U.S. National Library of Medicine
1800:
Proceedings of the
National Academy of Sciences of the United States of America
1747:
Proceedings of the
National Academy of Sciences of the United States of America
1694:
Proceedings of the
National Academy of Sciences of the United States of America
1566:
Proceedings of the
National Academy of Sciences of the United States of America
478:
1688:
Liu YC, Pan J, Zhang C, Fan W, Collinge M, Bender JR, Weissman SM (Apr 1999).
1560:
Liu YC, Pan J, Zhang C, Fan W, Collinge M, Bender JR, Weissman SM (Apr 1999).
294:
191:
141:
1820:
1767:
1487:
2098:
1090:
735:
538:
416:
361:
348:
260:
247:
149:
2238:
2200:
2157:
2106:
2068:
2059:
2042:
2025:
1995:
1986:
1969:
1960:
1917:
1874:
1865:
1848:
1839:
1786:
1733:
1714:
1637:
1605:
1586:
1546:
1537:
1520:
1505:
1479:
1300:
1680:
1351:
1308:
1063:
1058:
17:
1047:
906:
887:
2230:
1343:
1079:
873:
802:
82:
1184:
1031:
757:
2167:"Analysis of human immunodeficiency virus type 1 Gag ubiquitination"
2017:
1847:
Ott DE, Coren LV, Chertova EN, Gagliardi TD, Schubert U (Dec 2000).
2124:"FAT10, a ubiquitin-independent signal for proteasomal degradation"
2122:
Hipp MS, Kalveram B, Raasi S, Groettrup M, Schmidtke G (May 2005).
1794:
Strack B, Calistri A, Accola MA, Palu G, Gottlinger HG (Nov 2000).
1100:
720:
716:
1180:
1086:
129:
1796:"A role for ubiquitin ligase recruitment in retrovirus release"
1925:
Ott DE, Coren LV, Sowder RC, Adams J, Schubert U (Mar 2003).
651:
positive regulation of I-kappaB kinase/NF-kappaB signaling
385:
2041:
Hipp MS, Raasi S, Groettrup M, Schmidtke G (Apr 2004).
1519:
Hipp MS, Raasi S, Groettrup M, Schmidtke G (Apr 2004).
550:
992:
971:
945:
924:
1226:
1224:
1222:
1204:
1202:
1200:
706:regulation of mitotic cell cycle phase transition
666:protein modification by small protein conjugation
332:
231:
1882:Strack B, Calistri A, Göttlinger HG (Jun 2002).
27:Protein-coding gene in the species Homo sapiens
1231:GRCm38: Ensembl release 89: ENSMUSG00000035186
676:ubiquitin-dependent protein catabolic process
8:
807:
731:
576:
373:
272:
169:
71:
2190:
2147:
2058:
1985:
1950:
1907:
1864:
1829:
1819:
1776:
1766:
1723:
1713:
1670:
1595:
1585:
1536:
1495:
1122:Ubiquitin-binding E1, E2, and E3 enzymes
696:positive regulation of apoptotic process
1196:
701:post-translational protein modification
2165:Gottwein E, Kräusslich HG (Jul 2005).
1849:"Ubiquitination of HIV-1 and MuLV Gag"
661:myeloid dendritic cell differentiation
31:
1089:, also known as FAT10. UBD acts like
337:
298:
293:
236:
195:
190:
7:
2047:The Journal of Biological Chemistry
1525:The Journal of Biological Chemistry
116:, FAT10, GABBR1, UBD-3, ubiquitin D
989:
968:
942:
921:
897:
878:
852:
781:
762:
555:
473:
411:
390:
25:
1082:that in humans is encoded by the
656:response to tumor necrosis factor
2183:10.1128/JVI.79.14.9134-9144.2005
1900:10.1128/JVI.76.11.5472-5479.2002
321:
314:
308:
285:
220:
213:
207:
182:
2140:10.1128/MCB.25.9.3483-3491.2005
1943:10.1128/JVI.77.6.3384-3393.2003
1663:10.1128/JVI.72.4.2962-2968.1998
2128:Molecular and Cellular Biology
1374:"Entrez Gene: UBD ubiquitin D"
1289:European Journal of Immunology
539:More reference expression data
455:olfactory zone of nasal mucosa
1:
306:
205:
681:response to interferon-gamma
2265:Genes on human chromosome 6
509:subcutaneous adipose tissue
2281:
1468:British Journal of Cancer
1266:"Mouse PubMed Reference:"
1248:"Human PubMed Reference:"
1062:
1057:
1053:
1046:
1030:
1011:
996:
975:
964:
949:
928:
917:
904:
900:
885:
881:
872:
859:
855:
836:
810:
801:
788:
784:
769:
765:
756:
741:
734:
730:
714:
579:
575:
563:
558:
549:
536:
485:
476:
423:
414:
384:
376:
372:
355:
342:
305:
284:
275:
271:
254:
241:
204:
181:
172:
168:
123:
120:
110:
103:
98:
79:
74:
57:
52:
47:
43:
39:
34:
1821:10.1073/pnas.97.24.13063
1768:10.1073/pnas.97.24.13057
2099:10.1126/science.1105776
1113:Importance of Ubiquitin
1024:Chr 17: 37.5 – 37.51 Mb
1017:Chr 6: 29.56 – 29.56 Mb
2060:10.1074/jbc.M310114200
1987:10.1038/sj.onc.1206337
1866:10.1006/viro.2000.0648
1715:10.1073/pnas.96.8.4313
1587:10.1073/pnas.96.8.4313
1538:10.1074/jbc.M310114200
1480:10.1038/sj.bjc.6605870
1301:10.1002/eji.1830271002
1175:UBD has been shown to
1105:
671:protein ubiquitination
501:mucous cell of stomach
493:mesenteric lymph nodes
1104:
300:Chromosome 17 (mouse)
198:Chromosome 6 (human)
75:List of PDB id codes
48:Available structures
2231:10.1038/nature04209
2223:2005Natur.437.1173R
2171:Journal of Virology
2091:2005Sci...307.1621B
2006:Nature Cell Biology
1931:Journal of Virology
1888:Journal of Virology
1812:2000PNAS...9713063S
1759:2000PNAS...9713057S
1706:1999PNAS...96.4313L
1651:Journal of Virology
1578:1999PNAS...96.4313L
435:islet of Langerhans
1344:10.1007/BF02660056
1106:
862:ENSMUSG00000035186
691:aggresome assembly
644:Biological process
608:Cellular component
594:proteasome binding
587:Molecular function
1073:
1072:
1069:
1068:
1042:
1041:
1007:
1006:
986:
985:
960:
959:
939:
938:
913:
912:
894:
893:
868:
867:
849:
848:
797:
796:
778:
777:
726:
725:
571:
570:
567:
566:
545:
544:
532:
531:
525:intestinal villus
505:lactiferous gland
470:
469:
368:
367:
267:
266:
94:
93:
90:
89:
58:Ortholog search:
16:(Redirected from
2272:
2250:
2217:(7062): 1173–8.
2204:
2194:
2161:
2151:
2118:
2085:(5715): 1621–5.
2072:
2062:
2053:(16): 16503–10.
2037:
1999:
1989:
1980:(17): 2592–603.
1964:
1954:
1921:
1911:
1878:
1868:
1843:
1833:
1823:
1790:
1780:
1770:
1753:(24): 13057–62.
1737:
1727:
1717:
1684:
1674:
1641:
1610:
1609:
1599:
1589:
1557:
1551:
1550:
1540:
1531:(16): 16503–10.
1516:
1510:
1509:
1499:
1459:
1453:
1452:
1450:
1449:
1434:
1428:
1427:
1425:
1424:
1409:
1403:
1402:
1400:
1399:
1384:
1378:
1377:
1370:
1364:
1363:
1327:
1321:
1320:
1280:
1274:
1273:
1262:
1256:
1255:
1244:
1238:
1228:
1217:
1206:
1055:
1054:
1026:
1019:
1002:
990:
981:
969:
965:RefSeq (protein)
955:
943:
934:
922:
898:
879:
853:
832:
808:
782:
763:
732:
630:fibrillar center
577:
556:
541:
481:
479:Top expressed in
474:
419:
417:Top expressed in
412:
391:
374:
364:
351:
340:
325:
318:
312:
301:
289:
273:
263:
250:
239:
224:
217:
211:
200:
186:
170:
164:
115:
108:
85:
72:
66:
45:
44:
32:
21:
2280:
2279:
2275:
2274:
2273:
2271:
2270:
2269:
2255:
2254:
2253:
2207:
2177:(14): 9134–44.
2164:
2121:
2075:
2040:
2018:10.1038/ncb1023
2002:
1967:
1924:
1881:
1846:
1806:(24): 13063–8.
1793:
1740:
1687:
1644:
1626:Acta Virologica
1623:
1619:
1617:Further reading
1614:
1613:
1559:
1558:
1554:
1518:
1517:
1513:
1461:
1460:
1456:
1447:
1445:
1442:terms.naver.com
1436:
1435:
1431:
1422:
1420:
1417:terms.naver.com
1411:
1410:
1406:
1397:
1395:
1392:terms.naver.com
1386:
1385:
1381:
1372:
1371:
1367:
1329:
1328:
1324:
1282:
1281:
1277:
1264:
1263:
1259:
1246:
1245:
1241:
1229:
1220:
1210:ENSG00000226898
1207:
1198:
1193:
1173:
1157:
1124:
1115:
1099:
1064:View/Edit Mouse
1059:View/Edit Human
1022:
1015:
1012:Location (UCSC)
998:
977:
951:
930:
843:ENSG00000226898
841:
839:ENSG00000213886
831:
829:ENSG00000224654
827:
825:ENSG00000206513
823:
821:ENSG00000206468
819:
817:ENSG00000231968
815:
813:ENSG00000228913
811:
710:
639:
603:
599:protein binding
537:
528:
523:
519:
515:
511:
507:
503:
499:
495:
491:
477:
466:
461:
457:
453:
449:
445:
441:
437:
433:
429:
415:
359:
346:
338:
328:
327:
326:
319:
299:
276:Gene location (
258:
245:
237:
227:
226:
225:
218:
196:
173:Gene location (
162:UBD - orthologs
124:
111:
104:
81:
59:
28:
23:
22:
15:
12:
11:
5:
2278:
2276:
2268:
2267:
2257:
2256:
2252:
2251:
2205:
2162:
2134:(9): 3483–91.
2119:
2073:
2038:
2000:
1965:
1937:(6): 3384–93.
1922:
1894:(11): 5472–9.
1879:
1844:
1791:
1738:
1685:
1642:
1620:
1618:
1615:
1612:
1611:
1552:
1511:
1474:(7): 961–969.
1454:
1429:
1404:
1379:
1365:
1332:Immunogenetics
1322:
1295:(10): 2471–7.
1275:
1257:
1239:
1218:
1195:
1194:
1192:
1189:
1172:
1169:
1156:
1153:
1123:
1120:
1114:
1111:
1098:
1095:
1071:
1070:
1067:
1066:
1061:
1051:
1050:
1044:
1043:
1040:
1039:
1037:
1035:
1028:
1027:
1020:
1013:
1009:
1008:
1005:
1004:
994:
993:
987:
984:
983:
973:
972:
966:
962:
961:
958:
957:
947:
946:
940:
937:
936:
926:
925:
919:
915:
914:
911:
910:
902:
901:
895:
892:
891:
883:
882:
876:
870:
869:
866:
865:
857:
856:
850:
847:
846:
834:
833:
805:
799:
798:
795:
794:
786:
785:
779:
776:
775:
767:
766:
760:
754:
753:
748:
743:
739:
738:
728:
727:
724:
723:
712:
711:
709:
708:
703:
698:
693:
688:
683:
678:
673:
668:
663:
658:
653:
647:
645:
641:
640:
638:
637:
632:
627:
622:
617:
611:
609:
605:
604:
602:
601:
596:
590:
588:
584:
583:
573:
572:
569:
568:
565:
564:
561:
560:
553:
547:
546:
543:
542:
534:
533:
530:
529:
527:
526:
522:
518:
514:
510:
506:
502:
498:
494:
490:
486:
483:
482:
471:
468:
467:
465:
464:
460:
456:
452:
448:
444:
440:
436:
432:
428:
424:
421:
420:
408:
407:
399:
388:
382:
381:
378:RNA expression
370:
369:
366:
365:
357:
353:
352:
344:
341:
336:
330:
329:
320:
313:
307:
303:
302:
297:
291:
290:
282:
281:
269:
268:
265:
264:
256:
252:
251:
243:
240:
235:
229:
228:
219:
212:
206:
202:
201:
194:
188:
187:
179:
178:
166:
165:
122:
118:
117:
109:
101:
100:
96:
95:
92:
91:
88:
87:
77:
76:
68:
67:
56:
50:
49:
41:
40:
37:
36:
26:
24:
14:
13:
10:
9:
6:
4:
3:
2:
2277:
2266:
2263:
2262:
2260:
2248:
2244:
2240:
2236:
2232:
2228:
2224:
2220:
2216:
2212:
2206:
2202:
2198:
2193:
2188:
2184:
2180:
2176:
2172:
2168:
2163:
2159:
2155:
2150:
2145:
2141:
2137:
2133:
2129:
2125:
2120:
2116:
2112:
2108:
2104:
2100:
2096:
2092:
2088:
2084:
2080:
2074:
2070:
2066:
2061:
2056:
2052:
2048:
2044:
2039:
2035:
2031:
2027:
2023:
2019:
2015:
2012:(8): 754–61.
2011:
2007:
2001:
1997:
1993:
1988:
1983:
1979:
1975:
1971:
1966:
1962:
1958:
1953:
1948:
1944:
1940:
1936:
1932:
1928:
1923:
1919:
1915:
1910:
1905:
1901:
1897:
1893:
1889:
1885:
1880:
1876:
1872:
1867:
1862:
1859:(1): 111–21.
1858:
1854:
1850:
1845:
1841:
1837:
1832:
1827:
1822:
1817:
1813:
1809:
1805:
1801:
1797:
1792:
1788:
1784:
1779:
1774:
1769:
1764:
1760:
1756:
1752:
1748:
1744:
1739:
1735:
1731:
1726:
1721:
1716:
1711:
1707:
1703:
1700:(8): 4313–8.
1699:
1695:
1691:
1686:
1682:
1678:
1673:
1668:
1664:
1660:
1657:(4): 2962–8.
1656:
1652:
1648:
1643:
1639:
1635:
1631:
1627:
1622:
1621:
1616:
1607:
1603:
1598:
1593:
1588:
1583:
1579:
1575:
1572:(8): 4313–8.
1571:
1567:
1563:
1556:
1553:
1548:
1544:
1539:
1534:
1530:
1526:
1522:
1515:
1512:
1507:
1503:
1498:
1493:
1489:
1485:
1481:
1477:
1473:
1469:
1465:
1458:
1455:
1443:
1439:
1433:
1430:
1418:
1414:
1408:
1405:
1393:
1389:
1383:
1380:
1375:
1369:
1366:
1361:
1357:
1353:
1349:
1345:
1341:
1338:(2): 97–103.
1337:
1333:
1326:
1323:
1318:
1314:
1310:
1306:
1302:
1298:
1294:
1290:
1286:
1279:
1276:
1271:
1267:
1261:
1258:
1253:
1249:
1243:
1240:
1236:
1232:
1227:
1225:
1223:
1219:
1215:
1211:
1205:
1203:
1201:
1197:
1190:
1188:
1186:
1182:
1178:
1170:
1168:
1164:
1161:
1154:
1152:
1148:
1144:
1140:
1136:
1132:
1128:
1121:
1119:
1112:
1110:
1103:
1096:
1094:
1092:
1088:
1085:
1081:
1077:
1065:
1060:
1056:
1052:
1049:
1045:
1038:
1036:
1033:
1029:
1025:
1021:
1018:
1014:
1010:
1003:
1001:
995:
991:
988:
982:
980:
974:
970:
967:
963:
956:
954:
948:
944:
941:
935:
933:
927:
923:
920:
918:RefSeq (mRNA)
916:
909:
908:
903:
899:
896:
890:
889:
884:
880:
877:
875:
871:
864:
863:
858:
854:
851:
845:
844:
840:
835:
830:
826:
822:
818:
814:
809:
806:
804:
800:
793:
792:
787:
783:
780:
774:
773:
768:
764:
761:
759:
755:
752:
749:
747:
744:
740:
737:
733:
729:
722:
718:
713:
707:
704:
702:
699:
697:
694:
692:
689:
687:
684:
682:
679:
677:
674:
672:
669:
667:
664:
662:
659:
657:
654:
652:
649:
648:
646:
643:
642:
636:
633:
631:
628:
626:
623:
621:
618:
616:
613:
612:
610:
607:
606:
600:
597:
595:
592:
591:
589:
586:
585:
582:
581:Gene ontology
578:
574:
562:
557:
554:
552:
548:
540:
535:
524:
520:
516:
512:
508:
504:
500:
496:
492:
488:
487:
484:
480:
475:
472:
462:
458:
454:
450:
446:
442:
438:
434:
430:
426:
425:
422:
418:
413:
410:
409:
406:
404:
400:
398:
397:
393:
392:
389:
387:
383:
379:
375:
371:
363:
358:
354:
350:
345:
339:17|17 B1
335:
331:
324:
317:
311:
304:
296:
292:
288:
283:
279:
274:
270:
262:
257:
253:
249:
244:
234:
230:
223:
216:
210:
203:
199:
193:
189:
185:
180:
176:
171:
167:
163:
159:
155:
151:
147:
143:
139:
135:
131:
127:
119:
114:
107:
102:
97:
86:
84:
78:
73:
70:
69:
65:
62:
55:
51:
46:
42:
38:
33:
30:
19:
2214:
2210:
2174:
2170:
2131:
2127:
2082:
2078:
2050:
2046:
2009:
2005:
1977:
1973:
1934:
1930:
1891:
1887:
1856:
1852:
1803:
1799:
1750:
1746:
1697:
1693:
1654:
1650:
1632:(2): 75–85.
1629:
1625:
1569:
1565:
1555:
1528:
1524:
1514:
1471:
1467:
1457:
1446:. Retrieved
1441:
1432:
1421:. Retrieved
1416:
1407:
1396:. Retrieved
1391:
1382:
1368:
1335:
1331:
1325:
1292:
1288:
1285:Banchereau J
1278:
1269:
1260:
1251:
1242:
1174:
1171:Interactions
1165:
1159:
1158:
1149:
1145:
1141:
1137:
1133:
1129:
1125:
1116:
1107:
1083:
1075:
1074:
997:
976:
950:
929:
905:
886:
860:
837:
789:
770:
750:
745:
447:human kidney
401:
394:
121:External IDs
80:
29:
1444:(in Korean)
1419:(in Korean)
1394:(in Korean)
1076:Ubiquitin D
686:proteolysis
443:gallbladder
360:37,506,986
347:37,504,783
259:29,559,732
246:29,555,515
99:Identifiers
1448:2023-04-27
1423:2023-04-27
1398:2023-04-27
1237:, May 2017
1216:, May 2017
1191:References
431:lymph node
405:(ortholog)
142:HomoloGene
18:UBD (gene)
1488:1532-1827
1097:Ubiquitin
1091:ubiquitin
1000:NP_075626
979:NP_006389
953:NM_023137
932:NM_006398
736:Orthologs
620:aggresome
615:cytoplasm
150:GeneCards
2259:Category
2239:16189514
2201:15994808
2158:15831455
2115:39457788
2107:15761153
2069:14757770
2026:12883554
1996:12730673
1974:Oncogene
1961:12610113
1918:11991975
1875:11112487
1853:Virology
1840:11087860
1787:11087859
1734:10200259
1638:16808324
1606:10200259
1547:14757770
1506:20808312
1360:21628804
1317:21652482
1233:–
1212:–
1177:interact
1048:Wikidata
715:Sources:
517:duodenum
427:appendix
2247:4427026
2219:Bibcode
2192:1168789
2149:1084302
2087:Bibcode
2079:Science
2034:8414608
1808:Bibcode
1755:Bibcode
1702:Bibcode
1681:9525617
1574:Bibcode
1497:2965875
1352:8662070
1309:9368598
1235:Ensembl
1214:Ensembl
1080:protein
874:UniProt
803:Ensembl
742:Species
721:QuickGO
635:cytosol
625:nucleus
497:jejunum
380:pattern
138:1344410
106:Aliases
2245:
2237:
2211:Nature
2199:
2189:
2156:
2146:
2113:
2105:
2067:
2032:
2024:
1994:
1959:
1952:149504
1949:
1916:
1909:137019
1906:
1873:
1838:
1828:
1785:
1775:
1732:
1722:
1679:
1672:109742
1669:
1636:
1604:
1594:
1545:
1504:
1494:
1486:
1438:"유비퀴틴"
1413:"유비퀴틴"
1388:"유비퀴틴"
1358:
1350:
1315:
1307:
1185:MAD2L1
1034:search
1032:PubMed
907:P63072
888:O15205
758:Entrez
551:BioGPS
521:spleen
513:embryo
489:thymus
463:spleen
451:tonsil
439:rectum
238:6p22.1
130:606050
2243:S2CID
2111:S2CID
2030:S2CID
1831:27178
1778:27177
1725:16329
1597:16329
1356:S2CID
1313:S2CID
1179:with
1078:is a
791:24108
772:10537
751:Mouse
746:Human
717:Amigo
459:liver
403:Mouse
396:Human
343:Start
278:Mouse
242:Start
175:Human
2235:PMID
2197:PMID
2154:PMID
2103:PMID
2065:PMID
2022:PMID
1992:PMID
1957:PMID
1914:PMID
1871:PMID
1836:PMID
1783:PMID
1730:PMID
1677:PMID
1634:PMID
1602:PMID
1543:PMID
1502:PMID
1484:ISSN
1348:PMID
1305:PMID
1183:and
1181:NUB1
1087:gene
386:Bgee
334:Band
295:Chr.
233:Band
192:Chr.
146:4665
126:OMIM
83:2MBE
64:RCSB
61:PDBe
2227:doi
2215:437
2187:PMC
2179:doi
2144:PMC
2136:doi
2095:doi
2083:307
2055:doi
2051:279
2014:doi
1982:doi
1947:PMC
1939:doi
1904:PMC
1896:doi
1861:doi
1857:278
1826:PMC
1816:doi
1773:PMC
1763:doi
1720:PMC
1710:doi
1667:PMC
1659:doi
1592:PMC
1582:doi
1533:doi
1529:279
1492:PMC
1476:doi
1472:103
1340:doi
1297:doi
1160:UBD
1155:UBD
1084:UBD
559:n/a
356:End
255:End
158:OMA
154:UBD
134:MGI
113:UBD
54:PDB
35:UBD
2261::
2241:.
2233:.
2225:.
2213:.
2195:.
2185:.
2175:79
2173:.
2169:.
2152:.
2142:.
2132:25
2130:.
2126:.
2109:.
2101:.
2093:.
2081:.
2063:.
2049:.
2045:.
2028:.
2020:.
2008:.
1990:.
1978:22
1976:.
1972:.
1955:.
1945:.
1935:77
1933:.
1929:.
1912:.
1902:.
1892:76
1890:.
1886:.
1869:.
1855:.
1851:.
1834:.
1824:.
1814:.
1804:97
1802:.
1798:.
1781:.
1771:.
1761:.
1751:97
1749:.
1745:.
1728:.
1718:.
1708:.
1698:96
1696:.
1692:.
1675:.
1665:.
1655:72
1653:.
1649:.
1630:50
1628:.
1600:.
1590:.
1580:.
1570:96
1568:.
1564:.
1541:.
1527:.
1523:.
1500:.
1490:.
1482:.
1470:.
1466:.
1440:.
1415:.
1390:.
1354:.
1346:.
1336:44
1334:.
1311:.
1303:.
1293:27
1291:.
1268:.
1250:.
1221:^
1199:^
1187:.
719:/
362:bp
349:bp
261:bp
248:bp
156:;
152::
148:;
144::
140:;
136::
132:;
128::
2249:.
2229::
2221::
2203:.
2181::
2160:.
2138::
2117:.
2097::
2089::
2071:.
2057::
2036:.
2016::
2010:5
1998:.
1984::
1963:.
1941::
1920:.
1898::
1877:.
1863::
1842:.
1818::
1810::
1789:.
1765::
1757::
1736:.
1712::
1704::
1683:.
1661::
1640:.
1608:.
1584::
1576::
1549:.
1535::
1508:.
1478::
1451:.
1426:.
1401:.
1376:.
1362:.
1342::
1319:.
1299::
1272:.
1254:.
280:)
177:)
160::
20:)
Text is available under the Creative Commons Attribution-ShareAlike License. Additional terms may apply.
