1206:
acids for new synthesis; in parallel, some key regulatory proteins fulfill their biological functions via selective degradation; furthermore, proteins are digested into peptides for MHC class I antigen presentation. To meet such complicated demands in biological process via spatial and temporal proteolysis, protein substrates have to be recognized, recruited, and eventually hydrolyzed in a well controlled fashion. Thus, 19S regulatory particle pertains a series of important capabilities to address these functional challenges. To recognize protein as designated substrate, 19S complex has subunits that are capable to recognize proteins with a special degradative tag, the ubiquitinylation. It also have subunits that can bind with nucleotides (e.g., ATPs) in order to facilitate the association between 19S and 20S particles, as well as to cause confirmation changes of alpha subunit C-terminals that form the substrate entrance of 20S complex. Rpn13 is one essential subunit of 19S regulatory particle and it contributes to the assembly of the "base" subcomplex. In the base sub complex, Rpn13, as a ubiquitin receptor, offers a docking position for ubiquitinated substrate. Evidence showed that ubiquitination of Rpn13 subunit can significantly reduced the proteasome's ability to bind and degrade ubiquitin-conjugated proteins. Investigation employing biochemical and unbiased AQUA-MS methodologies offered evidences showing that, although the vast majority (if not all) of the double-capped 26S proteasomes, both 19S complexes, contain the ubiquitin receptor
1185:
complex presents three types proteolytic activities, including caspase-like, trypsin-like, and chymotrypsin-like activities. These proteolytic active sites located in the inner side of a chamber formed by 4 stacked rings of 20S subunits, preventing random protein-enzyme encounter and uncontrolled protein degradation. The 19S regulatory particles can recognize ubiquitin-labeled protein as degradation substrate, unfold the protein to linear, open the gate of 20S core particle, and guide the substrate into the proteolytic chamber. To meet such functional complexity, 19S regulatory particle contains at least 18 constitutive subunits. These subunits can be categorized into two classes based on the ATP dependence of subunits, ATP-dependent subunits and ATP-independent subunits. According to the protein interaction and topological characteristics of this multisubunit complex, the 19S regulatory particle is composed of a base and a lid subcomplex. The base consists of a ring of six AAA ATPases (Subunit Rpt1-6, systematic nomenclature) and four non-ATPase subunits (
1197:. Thus, Proteasomal ubiquitin receptor ADRM1 (Rpn13) is an important component of forming the base subcomplex of 19S regulatory particle. Traditional view of Rpn13 is that it is rather an associating partner of proteasome complex than a constitutive subunit. However, emerging evidences suggested that Rpn13 is a novel subunit of 19S. A recent study provided new evidences of 19S complex structure via an integrative approach combining data from cryoelectron microscopy, X-ray crystallography, residue-specific chemical cross-linking, and several proteomics techniques. In the newly established sub complex model of 19S base, Rpn2 is rigid protein located on the side of ATPase ring, supporting as the connection between the lid and base. Rpn1 is conformationally variable, positioned at the periphery of the ATPase ring. The ubiquitin receptors Rpn10 and Rpn13 are located further in the distal part of the 19S complex, indicating that they were recruited to the complex late during the assembly process.
334:
311:
208:
233:
585:
340:
239:
29:
1205:
As the degradation machinery that is responsible for ~70% of intracellular proteolysis, proteasome complex (26S proteasome) plays a critical roles in maintaining the homeostasis of cellular proteome. Accordingly, misfolded proteins and damaged protein need to be continuously removed to recycle amino
1184:
complex is usually consisted of a 20S core particle (CP, or 20S proteasome) and one or two 19S regulatory particles (RP, or 19S proteasome) on either one side or both side of the barrel-shaped 20S. The CP and RPs pertain distinct structural characteristics and biological functions. In brief, 20S sub
1938:
Gandhi TK, Zhong J, Mathivanan S, Karthick L, Chandrika KN, Mohan SS, Sharma S, Pinkert S, Nagaraju S, Periaswamy B, Mishra G, Nandakumar K, Shen B, Deshpande N, Nayak R, Sarker M, Boeke JD, Parmigiani G, Schultz J, Bader JS, Pandey A (Mar 2006). "Analysis of the human protein interactome and
55:
1210:, only one of these 19S particles contains the additional ubiquitin receptor Rpn13, thereby defining asymmetry in the 26S proteasome. Such structural asymmetry might be the molecular foundation for the one-directional substrate feeding process of proteasome complex.
1304:
Shimada S, Ogawa M, Takahashi M, Schlom J, Greiner JW (Jul 1994). "Molecular cloning and characterization of the complementary DNA of an M(r) 110,000 antigen expressed by human gastric carcinoma cells and upregulated by gamma-interferon".
1631:
Rock KL, Gramm C, Rothstein L, Clark K, Stein R, Dick L, Hwang D, Goldberg AL (Sep 1994). "Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules".
2049:
Yao T, Song L, Xu W, DeMartino GN, Florens L, Swanson SK, Washburn MP, Conaway RC, Conaway JW, Cohen RE (Sep 2006). "Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1".
2019:
Jørgensen JP, Lauridsen AM, Kristensen P, Dissing K, Johnsen AH, Hendil KB, Hartmann-Petersen R (Jul 2006). "Adrm1, a putative cell adhesion regulating protein, is a novel proteasome-associated factor".
1140:
encodes one of the non-ATPase subunits of the 19S regulator base, subunit Rpn13. The human PSMD4 gene has 10 exons and locates at chromosome band 20q13.33.The human protein
347:
246:
1805:
Simins AB, Weighardt H, Weidner KM, Weidle UH, Holzmann B (2000). "Functional cloning of ARM-1, an adhesion-regulating molecule upregulated in metastatic tumor cells".
1128:, also known in yeast as 26S Proteasome regulatory subunit Rpn13 (systematic nomenclature for proteasome subunits), is a subunit of 19S proteasome complex.
823:
804:
169:
2226:
1286:
1268:
333:
1778:
1054:
1047:
310:
1335:
1976:
Lim J, Hao T, Shaw C, Patel AJ, Szabó G, Rual JF, Fisk CJ, Li N, Smolyar A, Hill DE, Barabási AL, Vidal M, Zoghbi HY (May 2006).
1255:
1234:
232:
207:
1251:
1784:
52:
1352:
Lasker K, Förster F, Bohn S, Walzthoeni T, Villa E, Unverdorben P, Beck F, Aebersold R, Sali A, Baumeister W (Jan 2012).
1230:
149:
1675:
Besche HC, Sha Z, Kukushkin NV, Peth A, Hock EM, Kim W, Gygi S, Gutierrez JA, Liao H, Dick L, Goldberg AL (May 2014).
346:
245:
339:
238:
1153:
1978:"A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration"
1574:
Husnjak K, Elsasser S, Zhang N, Chen X, Randles L, Shi Y, Hofmann K, Walters KJ, Finley D, Dikic I (May 2008).
868:
157:
849:
1144:
is 42 kDa in size and composed of 407 amino acids. The calculated theoretical pI of this protein is 4.95.
221:
2089:"A novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes"
1855:
1587:
140:, ARM-1, ARM1, GP110, adhesion regulating molecule 1, PSMD16, ADRM1 26S proteasome ubiquitin receptor
136:
1790:
1001:
997:
942:
938:
2161:
2075:
2007:
1964:
1926:
1830:
1657:
1507:
181:
2175:"hRpn13/ADRM1/GP110 is a novel proteasome subunit that binds the deubiquitinating enzyme, UCH37"
1527:"hRpn13/ADRM1/GP110 is a novel proteasome subunit that binds the deubiquitinating enzyme, UCH37"
1354:"Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach"
1030:
1009:
1005:
971:
950:
946:
1677:"Autoubiquitination of the 26S proteasome on Rpn13 regulates breakdown of ubiquitin conjugates"
2231:
2204:
2153:
2118:
2067:
2037:
1999:
1956:
1918:
1883:
1822:
1757:
1706:
1649:
1613:
1556:
1499:
1436:
1385:
1314:
129:
45:
2194:
2186:
2143:
2108:
2100:
2059:
2029:
1989:
1948:
1908:
1873:
1863:
1814:
1747:
1737:
1696:
1688:
1641:
1603:
1595:
1546:
1538:
1489:
1481:
1426:
1416:
1375:
1365:
1165:
426:
357:
301:
256:
1724:
Berko D, Herkon O, Braunstein I, Isakov E, David Y, Ziv T, Navon A, Stanhill A (Feb 2014).
584:
177:
401:
1859:
1591:
1494:
1469:
2199:
2174:
2113:
2088:
1752:
1725:
1701:
1676:
1608:
1575:
1551:
1526:
1431:
1404:
1380:
1353:
28:
1878:
1843:
1645:
738:
733:
728:
723:
718:
702:
697:
692:
687:
682:
677:
672:
667:
662:
646:
641:
636:
631:
626:
2220:
1913:
1896:
1726:"Inherent asymmetry in the 26S proteasome is defined by the ubiquitin receptor RPN13"
1161:
1157:
613:
2079:
2011:
1930:
1897:"Adhesion properties of adhesion-regulating molecule 1 protein on endothelial cells"
1834:
1661:
1511:
161:
2165:
2132:"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks"
1968:
1172:. Two transcript variants encoding the same protein have been found for this gene.
419:
198:
185:
1291:
National Center for
Biotechnology Information, U.S. National Library of Medicine
1273:
National Center for
Biotechnology Information, U.S. National Library of Medicine
1169:
2148:
2131:
2130:
Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (Nov 2006).
1994:
1977:
1848:
Proceedings of the
National Academy of Sciences of the United States of America
1844:"Human Elongator facilitates RNA polymerase II transcription through chromatin"
1358:
Proceedings of the
National Academy of Sciences of the United States of America
502:
2033:
1818:
1485:
1181:
1121:
318:
215:
165:
2190:
2104:
2087:
Hamazaki J, Iemura S, Natsume T, Yashiroda H, Tanaka K, Murata S (Oct 2006).
1542:
1742:
1421:
1370:
768:
562:
440:
385:
372:
284:
271:
173:
2208:
2157:
2122:
2071:
2041:
2003:
1960:
1922:
1887:
1868:
1826:
1761:
1710:
1692:
1617:
1560:
1503:
1440:
1389:
1653:
1318:
1094:
1089:
1454:
1078:
913:
894:
1599:
1110:
880:
835:
106:
102:
98:
94:
90:
86:
82:
78:
74:
1405:"Rpn1 and Rpn2 coordinate ubiquitin processing factors at proteasome"
1403:
Rosenzweig R, Bronner V, Zhang D, Fushman D, Glickman MH (Apr 2012).
1062:
790:
2063:
1952:
2173:
Qiu XB, Ouyang SY, Li CJ, Miao S, Wang L, Goldberg AL (Dec 2006).
1525:
Qiu XB, Ouyang SY, Li CJ, Miao S, Wang L, Goldberg AL (Dec 2006).
1207:
1194:
1190:
1186:
753:
749:
1117:
593:
153:
1124:
complex structure confirmed that the protein encoded by gene
1939:
comparison with yeast, worm and fly interaction datasets".
1164:. Expression of this gene has been shown to be induced by
1576:"Proteasome subunit Rpn13 is a novel ubiquitin receptor"
719:
transcription elongation from RNA polymerase II promoter
409:
1160:. The encoded protein is thought to undergo O-linked
574:
1336:"Entrez Gene: ADRM1 adhesion regulating molecule 1"
1023:
990:
964:
931:
1247:
1245:
1243:
1226:
1224:
1222:
356:
255:
16:Protein-coding gene in the species Homo sapiens
1252:GRCm38: Ensembl release 89: ENSMUSG00000039041
703:proteasome regulatory particle, lid subcomplex
734:ubiquitin-dependent protein catabolic process
729:positive regulation of endopeptidase activity
8:
1347:
1345:
1231:GRCh38: Ensembl release 89: ENSG00000130706
764:
609:
397:
296:
193:
63:
2198:
2147:
2112:
1993:
1912:
1877:
1867:
1751:
1741:
1700:
1607:
1550:
1493:
1430:
1420:
1379:
1369:
1842:Kim JH, Lane WS, Reinberg D (Feb 2002).
1330:
1328:
1218:
1152:The protein encoded by this gene is an
1807:Clinical & Experimental Metastasis
18:
673:integral component of plasma membrane
361:
322:
317:
260:
219:
214:
7:
1474:Cellular and Molecular Life Sciences
1142:Proteasomal ubiquitin receptor ADRM1
1107:Proteasomal ubiquitin receptor ADRM1
1730:The Journal of Biological Chemistry
1409:The Journal of Biological Chemistry
1020:
987:
961:
928:
904:
885:
859:
840:
814:
795:
579:
497:
435:
414:
14:
1113:that in humans is encoded by the
1914:10.1111/j.1742-4658.2005.04613.x
1895:Lamerant N, Kieda C (Apr 2005).
1154:integral plasma membrane protein
627:endopeptidase activator activity
583:
345:
338:
332:
309:
244:
237:
231:
206:
27:
1455:"Uniprot: Q16186 - ADRM1_HUMAN"
594:More reference expression data
563:More reference expression data
471:right hemisphere of cerebellum
1:
1646:10.1016/s0092-8674(94)90462-6
1468:Gu ZC, Enenkel C (Dec 2014).
330:
229:
2227:Genes on human chromosome 20
2022:Journal of Molecular Biology
2248:
2149:10.1016/j.cell.2006.09.026
1995:10.1016/j.cell.2006.03.032
1789:gene details page in the
2034:10.1016/j.jmb.2006.06.011
1486:10.1007/s00018-014-1699-8
1287:"Mouse PubMed Reference:"
1269:"Human PubMed Reference:"
1093:
1088:
1084:
1077:
1061:
1055:Chr 2: 179.81 – 179.82 Mb
1042:
1027:
994:
983:
968:
935:
924:
911:
907:
892:
888:
879:
866:
862:
847:
843:
834:
821:
817:
802:
798:
789:
774:
767:
763:
747:
612:
608:
591:
582:
573:
560:
509:
500:
447:
438:
408:
400:
396:
379:
366:
329:
308:
299:
295:
278:
265:
228:
205:
196:
192:
147:
144:
134:
127:
122:
71:
66:
49:
44:
39:
35:
26:
21:
2191:10.1038/sj.emboj.7601450
2105:10.1038/sj.emboj.7601338
1543:10.1038/sj.emboj.7601450
739:protein deubiquitination
1819:10.1023/A:1006790912877
1743:10.1074/jbc.M113.509380
1422:10.1074/jbc.M111.316323
1371:10.1073/pnas.1120559109
1048:Chr 20: 62.3 – 62.31 Mb
1869:10.1073/pnas.251672198
1693:10.1002/embj.201386906
1120:. Recent evidences on
537:skeletal muscle tissue
1470:"Proteasome assembly"
222:Chromosome 20 (human)
1783:genome location and
483:right adrenal cortex
451:gastrocnemius muscle
324:Chromosome 2 (mouse)
67:List of PDB id codes
40:Available structures
2052:Nature Cell Biology
1860:2002PNAS...99.1241K
1791:UCSC Genome Browser
1600:10.1038/nature06926
1592:2008Natur.453..481H
724:proteasome assembly
475:right adrenal gland
869:ENSMUSG00000039041
712:Biological process
663:proteasome complex
656:Cellular component
637:proteasome binding
620:Molecular function
487:left adrenal gland
1480:(24): 4729–4745.
1104:
1103:
1100:
1099:
1073:
1072:
1038:
1037:
1017:
1016:
979:
978:
958:
957:
920:
919:
901:
900:
875:
874:
856:
855:
830:
829:
811:
810:
759:
758:
647:ubiquitin binding
604:
603:
600:
599:
569:
568:
556:
555:
494:
493:
392:
391:
291:
290:
186:ADRM1 - orthologs
118:
117:
114:
113:
50:Ortholog search:
2239:
2212:
2202:
2179:The EMBO Journal
2169:
2151:
2126:
2116:
2093:The EMBO Journal
2083:
2045:
2015:
1997:
1972:
1934:
1916:
1901:The FEBS Journal
1891:
1881:
1871:
1838:
1766:
1765:
1755:
1745:
1721:
1715:
1714:
1704:
1681:The EMBO Journal
1672:
1666:
1665:
1628:
1622:
1621:
1611:
1571:
1565:
1564:
1554:
1531:The EMBO Journal
1522:
1516:
1515:
1497:
1465:
1459:
1458:
1451:
1445:
1444:
1434:
1424:
1415:(18): 14659–71.
1400:
1394:
1393:
1383:
1373:
1349:
1340:
1339:
1332:
1323:
1322:
1301:
1295:
1294:
1283:
1277:
1276:
1265:
1259:
1249:
1238:
1228:
1176:Complex assembly
1166:gamma interferon
1086:
1085:
1057:
1050:
1033:
1021:
1012:
988:
984:RefSeq (protein)
974:
962:
953:
929:
905:
886:
860:
841:
815:
796:
765:
632:protease binding
610:
596:
587:
580:
565:
505:
503:Top expressed in
498:
443:
441:Top expressed in
436:
415:
398:
388:
375:
364:
349:
342:
336:
325:
313:
297:
287:
274:
263:
248:
241:
235:
224:
210:
194:
188:
139:
132:
109:
64:
58:
37:
36:
31:
19:
2247:
2246:
2242:
2241:
2240:
2238:
2237:
2236:
2217:
2216:
2215:
2185:(24): 5742–53.
2172:
2129:
2099:(19): 4524–36.
2086:
2064:10.1038/ncb1460
2058:(9): 994–1002.
2048:
2018:
1975:
1941:Nature Genetics
1937:
1894:
1841:
1804:
1800:
1798:Further reading
1774:
1769:
1723:
1722:
1718:
1687:(10): 1159–76.
1674:
1673:
1669:
1630:
1629:
1625:
1586:(7194): 481–8.
1573:
1572:
1568:
1537:(24): 5742–53.
1524:
1523:
1519:
1467:
1466:
1462:
1453:
1452:
1448:
1402:
1401:
1397:
1351:
1350:
1343:
1334:
1333:
1326:
1307:Cancer Research
1303:
1302:
1298:
1285:
1284:
1280:
1267:
1266:
1262:
1250:
1241:
1229:
1220:
1216:
1203:
1178:
1156:which promotes
1150:
1134:
1095:View/Edit Mouse
1090:View/Edit Human
1053:
1046:
1043:Location (UCSC)
1029:
1008:
1004:
1000:
996:
970:
949:
945:
941:
937:
850:ENSG00000130706
743:
707:
668:plasma membrane
651:
642:protein binding
592:
561:
552:
547:
543:
539:
535:
531:
527:
523:
519:
517:proximal tubule
515:
513:muscle of thigh
501:
490:
485:
481:
477:
473:
469:
465:
463:muscle of thigh
461:
457:
453:
439:
383:
370:
362:
352:
351:
350:
343:
323:
300:Gene location (
282:
269:
261:
251:
250:
249:
242:
220:
197:Gene location (
148:
135:
128:
73:
51:
17:
12:
11:
5:
2245:
2243:
2235:
2234:
2229:
2219:
2218:
2214:
2213:
2170:
2127:
2084:
2046:
2028:(5): 1043–52.
2016:
1973:
1953:10.1038/ng1747
1935:
1907:(8): 1833–44.
1892:
1839:
1801:
1799:
1796:
1795:
1794:
1773:
1772:External links
1770:
1768:
1767:
1736:(9): 5609–18.
1716:
1667:
1623:
1566:
1517:
1460:
1446:
1395:
1341:
1324:
1313:(14): 3831–6.
1296:
1278:
1260:
1239:
1217:
1215:
1212:
1202:
1199:
1177:
1174:
1149:
1146:
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402:RNA expression
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280:
276:
275:
267:
264:
259:
253:
252:
243:
236:
230:
226:
225:
218:
212:
211:
203:
202:
190:
189:
146:
142:
141:
133:
125:
124:
120:
119:
116:
115:
112:
111:
69:
68:
60:
59:
48:
42:
41:
33:
32:
24:
23:
15:
13:
10:
9:
6:
4:
3:
2:
2244:
2233:
2230:
2228:
2225:
2224:
2222:
2210:
2206:
2201:
2196:
2192:
2188:
2184:
2180:
2176:
2171:
2167:
2163:
2159:
2155:
2150:
2145:
2142:(3): 635–48.
2141:
2137:
2133:
2128:
2124:
2120:
2115:
2110:
2106:
2102:
2098:
2094:
2090:
2085:
2081:
2077:
2073:
2069:
2065:
2061:
2057:
2053:
2047:
2043:
2039:
2035:
2031:
2027:
2023:
2017:
2013:
2009:
2005:
2001:
1996:
1991:
1988:(4): 801–14.
1987:
1983:
1979:
1974:
1970:
1966:
1962:
1958:
1954:
1950:
1947:(3): 285–93.
1946:
1942:
1936:
1932:
1928:
1924:
1920:
1915:
1910:
1906:
1902:
1898:
1893:
1889:
1885:
1880:
1875:
1870:
1865:
1861:
1857:
1854:(3): 1241–6.
1853:
1849:
1845:
1840:
1836:
1832:
1828:
1824:
1820:
1816:
1812:
1808:
1803:
1802:
1797:
1792:
1788:
1787:
1782:
1781:
1776:
1775:
1771:
1763:
1759:
1754:
1749:
1744:
1739:
1735:
1731:
1727:
1720:
1717:
1712:
1708:
1703:
1698:
1694:
1690:
1686:
1682:
1678:
1671:
1668:
1663:
1659:
1655:
1651:
1647:
1643:
1640:(5): 761–71.
1639:
1635:
1627:
1624:
1619:
1615:
1610:
1605:
1601:
1597:
1593:
1589:
1585:
1581:
1577:
1570:
1567:
1562:
1558:
1553:
1548:
1544:
1540:
1536:
1532:
1528:
1521:
1518:
1513:
1509:
1505:
1501:
1496:
1491:
1487:
1483:
1479:
1475:
1471:
1464:
1461:
1456:
1450:
1447:
1442:
1438:
1433:
1428:
1423:
1418:
1414:
1410:
1406:
1399:
1396:
1391:
1387:
1382:
1377:
1372:
1367:
1364:(5): 1380–7.
1363:
1359:
1355:
1348:
1346:
1342:
1337:
1331:
1329:
1325:
1320:
1316:
1312:
1308:
1300:
1297:
1292:
1288:
1282:
1279:
1274:
1270:
1264:
1261:
1257:
1253:
1248:
1246:
1244:
1240:
1236:
1232:
1227:
1225:
1223:
1219:
1213:
1211:
1209:
1200:
1198:
1196:
1192:
1188:
1183:
1175:
1173:
1171:
1167:
1163:
1162:glycosylation
1159:
1158:cell adhesion
1155:
1147:
1145:
1143:
1139:
1131:
1129:
1127:
1123:
1119:
1116:
1112:
1108:
1096:
1091:
1087:
1083:
1080:
1076:
1069:
1067:
1064:
1060:
1056:
1052:
1049:
1045:
1041:
1034:
1032:
1026:
1022:
1019:
1013:
1011:
1007:
1003:
999:
993:
989:
986:
982:
975:
973:
967:
963:
960:
954:
952:
948:
944:
940:
934:
930:
927:
925:RefSeq (mRNA)
923:
916:
915:
910:
906:
903:
897:
896:
891:
887:
884:
882:
878:
871:
870:
865:
861:
858:
852:
851:
846:
842:
839:
837:
833:
826:
825:
820:
816:
813:
807:
806:
801:
797:
794:
792:
788:
785:
782:
780:
777:
773:
770:
766:
762:
755:
751:
746:
740:
737:
735:
732:
730:
727:
725:
722:
720:
717:
716:
714:
711:
710:
704:
701:
699:
696:
694:
691:
689:
686:
684:
681:
679:
676:
674:
671:
669:
666:
664:
661:
660:
658:
655:
654:
648:
645:
643:
640:
638:
635:
633:
630:
628:
625:
624:
622:
619:
618:
615:
614:Gene ontology
611:
607:
595:
590:
586:
581:
578:
576:
572:
564:
559:
548:
544:
541:adrenal gland
540:
536:
532:
528:
525:muscle tissue
524:
520:
516:
512:
511:
508:
504:
499:
496:
486:
482:
478:
474:
470:
467:apex of heart
466:
462:
458:
454:
450:
449:
446:
442:
437:
434:
433:
430:
428:
424:
422:
421:
417:
416:
413:
411:
407:
403:
399:
395:
387:
382:
378:
374:
369:
359:
355:
348:
341:
335:
328:
320:
316:
312:
307:
303:
298:
294:
286:
281:
277:
273:
268:
258:
254:
247:
240:
234:
227:
223:
217:
213:
209:
204:
200:
195:
191:
187:
183:
179:
175:
171:
167:
163:
159:
155:
151:
143:
138:
131:
126:
121:
110:
108:
104:
100:
96:
92:
88:
84:
80:
76:
70:
65:
62:
61:
57:
54:
47:
43:
38:
34:
30:
25:
20:
2182:
2178:
2139:
2135:
2096:
2092:
2055:
2051:
2025:
2021:
1985:
1981:
1944:
1940:
1904:
1900:
1851:
1847:
1813:(8): 641–8.
1810:
1806:
1785:
1779:
1733:
1729:
1719:
1684:
1680:
1670:
1637:
1633:
1626:
1583:
1579:
1569:
1534:
1530:
1520:
1477:
1473:
1463:
1449:
1412:
1408:
1398:
1361:
1357:
1310:
1306:
1299:
1290:
1281:
1272:
1263:
1204:
1179:
1170:cancer cells
1151:
1141:
1137:
1135:
1125:
1114:
1106:
1105:
1028:
1002:NP_001268367
998:NP_001268366
995:
969:
943:NM_001281438
939:NM_001281437
936:
912:
893:
867:
848:
822:
803:
783:
778:
545:right kidney
455:right testis
425:
418:
384:179,818,079
371:179,813,278
145:External IDs
72:
688:nucleoplasm
529:neural tube
479:skin of leg
459:left testis
363:2|2 H4
283:62,308,862
270:62,302,093
123:Identifiers
2221:Categories
1258:, May 2017
1237:, May 2017
1214:References
1182:proteasome
1122:proteasome
429:(ortholog)
166:HomoloGene
1148:Structure
1136:The gene
1031:NP_062796
1010:NP_783163
1006:NP_008933
972:NM_019822
951:NM_175573
947:NM_007002
769:Orthologs
693:cytoplasm
174:GeneCards
2232:Proteins
2209:17139257
2158:17081983
2123:16990800
2080:25308728
2072:16906146
2042:16815440
2012:13709685
2004:16713569
1961:16501559
1931:23359211
1923:15819879
1888:11818576
1835:12042321
1827:10919708
1762:24429290
1711:24811749
1662:22262916
1618:18497817
1561:17139257
1512:15661805
1504:25107634
1495:11113775
1441:22318722
1390:22307589
1254:–
1233:–
1201:Function
1168:in some
1079:Wikidata
748:Sources:
678:membrane
533:yolk sac
262:20q13.33
2200:1698896
2166:7827573
2114:1589993
1969:1446423
1856:Bibcode
1753:3937637
1702:4193922
1654:8087844
1609:2839886
1588:Bibcode
1552:1698896
1432:3340268
1381:3277140
1319:8033103
1256:Ensembl
1235:Ensembl
1111:protein
881:UniProt
836:Ensembl
775:Species
754:QuickGO
698:cytosol
683:nucleus
404:pattern
162:1929289
130:Aliases
2207:
2197:
2164:
2156:
2121:
2111:
2078:
2070:
2040:
2010:
2002:
1967:
1959:
1929:
1921:
1886:
1879:122174
1876:
1833:
1825:
1777:Human
1760:
1750:
1709:
1699:
1660:
1652:
1616:
1606:
1580:Nature
1559:
1549:
1510:
1502:
1492:
1439:
1429:
1388:
1378:
1317:
1193:, and
1065:search
1063:PubMed
914:Q9JKV1
895:Q16186
791:Entrez
575:BioGPS
549:morula
154:610650
2162:S2CID
2076:S2CID
2008:S2CID
1965:S2CID
1927:S2CID
1831:S2CID
1786:ADRM1
1780:ADRM1
1658:S2CID
1508:S2CID
1208:Rpn10
1195:Rpn10
1138:ADRM1
1126:ADRM1
1115:ADRM1
1109:is a
824:56436
805:11047
784:Mouse
779:Human
750:Amigo
427:Mouse
420:Human
367:Start
302:Mouse
266:Start
199:Human
178:ADRM1
170:10513
137:ADRM1
22:ADRM1
2205:PMID
2154:PMID
2136:Cell
2119:PMID
2068:PMID
2038:PMID
2000:PMID
1982:Cell
1957:PMID
1919:PMID
1884:PMID
1823:PMID
1758:PMID
1707:PMID
1650:PMID
1634:Cell
1614:PMID
1557:PMID
1500:PMID
1437:PMID
1386:PMID
1315:PMID
1191:Rpn2
1187:Rpn1
1180:26S
1132:Gene
1118:gene
410:Bgee
358:Band
319:Chr.
257:Band
216:Chr.
150:OMIM
107:5IRS
103:4WLR
99:4WLQ
95:4UEM
91:4UEL
87:2MKZ
83:2L5V
79:2KR0
75:2KQZ
56:RCSB
53:PDBe
2195:PMC
2187:doi
2144:doi
2140:127
2109:PMC
2101:doi
2060:doi
2030:doi
2026:360
1990:doi
1986:125
1949:doi
1909:doi
1905:272
1874:PMC
1864:doi
1815:doi
1748:PMC
1738:doi
1734:289
1697:PMC
1689:doi
1642:doi
1604:PMC
1596:doi
1584:453
1547:PMC
1539:doi
1490:PMC
1482:doi
1427:PMC
1417:doi
1413:287
1376:PMC
1366:doi
1362:109
521:lip
380:End
279:End
182:OMA
158:MGI
46:PDB
2223::
2203:.
2193:.
2183:25
2181:.
2177:.
2160:.
2152:.
2138:.
2134:.
2117:.
2107:.
2097:25
2095:.
2091:.
2074:.
2066:.
2054:.
2036:.
2024:.
2006:.
1998:.
1984:.
1980:.
1963:.
1955:.
1945:38
1943:.
1925:.
1917:.
1903:.
1899:.
1882:.
1872:.
1862:.
1852:99
1850:.
1846:.
1829:.
1821:.
1811:17
1809:.
1756:.
1746:.
1732:.
1728:.
1705:.
1695:.
1685:33
1683:.
1679:.
1656:.
1648:.
1638:78
1636:.
1612:.
1602:.
1594:.
1582:.
1578:.
1555:.
1545:.
1535:25
1533:.
1529:.
1506:.
1498:.
1488:.
1478:71
1476:.
1472:.
1435:.
1425:.
1411:.
1407:.
1384:.
1374:.
1360:.
1356:.
1344:^
1327:^
1311:54
1309:.
1289:.
1271:.
1242:^
1221:^
1189:,
752:/
386:bp
373:bp
285:bp
272:bp
180:;
176::
172:;
168::
164:;
160::
156:;
152::
105:,
101:,
97:,
93:,
89:,
85:,
81:,
77:,
2211:.
2189::
2168:.
2146::
2125:.
2103::
2082:.
2062::
2056:8
2044:.
2032::
2014:.
1992::
1971:.
1951::
1933:.
1911::
1890:.
1866::
1858::
1837:.
1817::
1793:.
1764:.
1740::
1713:.
1691::
1664:.
1644::
1620:.
1598::
1590::
1563:.
1541::
1514:.
1484::
1457:.
1443:.
1419::
1392:.
1368::
1338:.
1321:.
1293:.
1275:.
304:)
201:)
184::
Text is available under the Creative Commons Attribution-ShareAlike License. Additional terms may apply.
