297:
274:
1227:(OSBP-related proteins) family of lipid transfer proteins. Mammals have 16 different ORPs, whereas the yeast S. cerevisiae genome encodes seven ORP homologues (Osh). ORP and Osh proteins contain a lipid transport domain called ORD (OSBP-related domain) encompassing the EQVSHHPP signature sequence. The ORD structure consists in a hydrophobic pocket. Because the EQVSHHPP sequence is crucial for PI4P binding to the ORD, but not for sterol binding, it has been proposed that PI4P transport is a common function of Osh/ORP proteins.
171:
196:
555:
548:
303:
202:
1215:, also bind 25-OH. In fact 25-OH is a potent suppressor of sterol synthesis in cultured cells and accelerates cholesterol esterification. In cellular studies it has been shown that OSBP, initially cytosolic, relocates to ER-Golgi membrane contact sites in the presence of 25-OH. 25-OH acts as an inhibitor of sterol transport mediated by OSBP in vitro.
1198:, which is an ER-resident protein. Therefore, OSBP acts as a negative regulator of its own attachment to the trans-Golgi (which requires the binding of its PH domain to PI4P). This negative feedback system might coordinate cholesterol transport out of the ER to PI4P level in the Golgi.
1123:
acts as a natural inhibitor of this exchange. OSBP regulates ER-Golgi membrane contact sites formation by bridging ER and Golgi membranes together. OSBP plays also a role as a sterol-regulated scaffolding protein for several cytosolic reactions including the phosphorylation of
50:
1139:(fatty acids and triglycerides biosynthesis). OSBP expression levels in transgenic mice affect liver and serum TG levels. OSBP is thought to be an essential scaffolding compound of the protein complex that regulates the activation state of the
1114:
Oxysterol-binding protein (OSBP) is an intracellular protein that was identified as a cytosolic 25-hydroxycholesterol-binding protein. OSBP is a lipid transfer protein that controls cholesterol/PI4P exchange at ER-Golgi
1861:
Levanon D, Hsieh CL, Francke U, Dawson PA, Ridgway ND, Brown MS, Goldstein JL (May 1990). "cDNA cloning of human oxysterol-binding protein and localization of the gene to human chromosome 11 and mouse chromosome 19".
1206:
OSBP is regulated by PKD mediated phosphorylation, and by the oxysterol 25-hydroxycholesterol (25-OH), a high-affinity ligand for OSBP (~30 nM). Several proteins involved in cholesterol homeostasis, such as
310:
209:
2049:"Oxysterol-binding protein and vesicle-associated membrane protein-associated protein are required for sterol-dependent activation of the ceramide transport protein"
1612:"Vesicle-associated membrane protein-associated protein-A (VAP-A) interacts with the oxysterol-binding protein to modify export from the endoplasmic reticulum"
833:
132:
814:
1140:
1125:
2100:
1303:
1285:
1212:
296:
1033:
1040:
273:
1442:
Wang PY, Weng J, Anderson RG (March 2005). "OSBP is a cholesterol-regulated scaffolding protein in control of ERK 1/2 activation".
1321:
1191:
1172:
1272:
1251:
1575:
Levine T (September 2004). "Short-range intracellular trafficking of small molecules across endoplasmic reticulum junctions".
195:
170:
1268:
47:
1702:"Sterol-regulated transport of SREBPs from endoplasmic reticulum to Golgi: oxysterols block transport by binding to Insig"
1247:
112:
1167:(two phenylalanines in an acidic track), and a C-terminal lipid transport domain (ORD). The PH domain binds the trans-
1928:"Molecular and biochemical characterization of a novel oxysterol-binding protein (OSBP2) highly expressed in retina"
309:
208:
1893:"Family of human oxysterol binding protein (OSBP) homologues. A novel member implicated in brain sterol metabolism"
1994:
Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (August 2004).
1224:
302:
201:
1808:
de Saint-Jean M, Delfosse V, Douguet D, Chicanne G, Payrastre B, Bourguet W, Antonny B, Drin G (December 2011).
878:
120:
1653:"Regulation of oxysterol-binding protein Golgi localization through protein kinase D-mediated phosphorylation"
1187:. OSBP bridges the Golgi and the ER by establishing contacts with all of these determinants simultaneously.
1176:
859:
1194:
backward (from the Golgi to the ER). Then, PI4P can be hydrolyzed by the phosphatidylinositide phosphatase
1400:"A Four-Step Cycle Driven by PI(4)P Hydrolysis Directs Sterol/PI(4)P Exchange by the ER-Golgi Tether OSBP"
1493:
Yan D, Lehto M, Rasilainen L, Metso J, Ehnholm C, Ylä-Herttuala S, Jauhiainen M, Olkkonen VM (May 2007).
1190:
OSBP is thought to transport cholesterol from the ER to the Golgi, and to transport the phosphoinositide
1120:
1116:
184:
2007:
1764:
1451:
99:
1160:
1016:
969:
1536:"Oxysterol and diabetes activate STAT3 and control endothelial expression of profilin-1 via OSBP1"
1475:
144:
995:
948:
2078:
2035:
1982:
1949:
1914:
1879:
1839:
1790:
1733:
1682:
1633:
1592:
1557:
1516:
1467:
1421:
1371:
92:
40:
1495:"Oxysterol binding protein induces upregulation of SREBP-1c and enhances hepatic lipogenesis"
2068:
2060:
2025:
2015:
1974:
1939:
1904:
1871:
1829:
1821:
1780:
1772:
1723:
1713:
1672:
1664:
1623:
1584:
1547:
1506:
1459:
1411:
1398:
Mesmin B, Bigay J, Moser von
Filseck J, Lacas-Gervais S, Drin G, Antonny B (November 2013).
1361:
1353:
554:
547:
389:
320:
264:
219:
1342:"Translocation of oxysterol binding protein to Golgi apparatus triggered by ligand binding"
1168:
364:
140:
2011:
1768:
1455:
2073:
2048:
1834:
1809:
1785:
1752:
1728:
1701:
1677:
1652:
1366:
1341:
2030:
1995:
1909:
1892:
748:
743:
738:
733:
717:
712:
707:
702:
697:
692:
687:
682:
677:
672:
667:
662:
657:
652:
647:
642:
626:
621:
616:
611:
606:
601:
596:
2094:
1875:
1810:"Osh4p exchanges sterols for phosphatidylinositol 4-phosphate between lipid bilayers"
583:
1479:
1651:
Nhek S, Ngo M, Yang X, Ng MM, Field SJ, Asara JM, Ridgway ND, Toker A (July 2010).
382:
161:
124:
148:
1753:"Structural mechanism for sterol sensing and transport by OSBP-related proteins"
1308:
National Center for
Biotechnology Information, U.S. National Library of Medicine
1290:
National Center for
Biotechnology Information, U.S. National Library of Medicine
1136:
1511:
1494:
1416:
1399:
465:
1588:
1180:
1164:
281:
178:
128:
2064:
2020:
1718:
1668:
1463:
1135:
is controlled by OSBP. SREBP-1c is a major transcription factor for hepatic
778:
525:
403:
348:
335:
247:
234:
136:
2082:
2039:
1986:
1978:
1953:
1944:
1927:
1918:
1843:
1794:
1737:
1686:
1637:
1628:
1611:
1596:
1561:
1552:
1535:
1520:
1471:
1425:
1883:
1825:
1375:
1357:
1080:
1075:
1064:
923:
904:
1776:
1700:
Radhakrishnan A, Ikeda Y, Kwon HJ, Brown MS, Goldstein JL (April 2007).
1208:
1096:
890:
845:
69:
1340:
Ridgway ND, Dawson PA, Ho YK, Brown MS, Goldstein JL (January 1992).
1195:
1048:
800:
1962:
1996:"Large-scale characterization of HeLa cell nuclear phosphoproteins"
1961:
Jaworski CJ, Moreira E, Li A, Lee R, Rodriguez IR (December 2001).
1148:
1132:
1963:"A family of 12 human genes containing oxysterol-binding domains"
763:
759:
1184:
1144:
1103:
116:
1143:
protein. OSBP also acts as a sterol-dependant scaffold for the
563:
1891:
Laitinen S, Olkkonen VM, Ehnholm C, Ikonen E (December 1999).
1751:
Im YJ, Raychaudhuri S, Prinz WA, Hurley JH (September 2005).
1159:
OSBP is a multi-domain protein consisting of an N-terminal
372:
1926:
Moreira EF, Jaworski C, Li A, Rodriguez IR (May 2001).
537:
1131:
It has been shown that expression and maturation of
1009:
988:
962:
941:
1264:
1262:
1260:
1243:
1241:
1239:
1610:Wyles JP, McMaster CR, Ridgway ND (August 2002).
319:
218:
16:Protein-coding gene in the species Homo sapiens
1269:GRCm38: Ensembl release 89: ENSMUSG00000024687
1322:"Entrez Gene: OSBP oxysterol binding protein"
8:
1248:GRCh38: Ensembl release 89: ENSG00000110048
774:
579:
360:
259:
156:
58:
2072:
2029:
2019:
1943:
1908:
1833:
1784:
1727:
1717:
1676:
1627:
1551:
1510:
1415:
1365:
1335:
1333:
1331:
1393:
1391:
1389:
1387:
1385:
713:intracellular membrane-bounded organelle
602:phosphatidylinositol-4-phosphate binding
434:Skeletal muscle tissue of biceps brachii
1235:
1437:
1435:
1183:binds the type II ER membrane protein
18:
1534:Romeo GR, Kazlauskas A (April 2008).
324:
285:
280:
223:
182:
177:
7:
1223:OSBP is the founding member of the
749:intracellular cholesterol transport
2047:Perry RJ, Ridgway ND (June 2006).
1175:and the activated small G protein
1006:
985:
959:
938:
914:
895:
869:
850:
824:
805:
542:
460:
398:
377:
103:, OSBP1, oxysterol binding protein
14:
1171:membrane by contacting the lipid
1099:that in humans is encoded by the
718:perinuclear endoplasmic reticulum
1499:Arterioscler. Thromb. Vasc. Biol
553:
546:
308:
301:
295:
272:
207:
200:
194:
169:
688:perinuclear region of cytoplasm
597:protein domain specific binding
744:bile acid biosynthetic process
653:endoplasmic reticulum membrane
564:More reference expression data
526:More reference expression data
1:
1910:10.1016/S0022-2275(20)32095-2
293:
192:
2101:Genes on human chromosome 11
2000:Proc. Natl. Acad. Sci. U.S.A
1876:10.1016/0888-7543(90)90519-Z
1706:Proc. Natl. Acad. Sci. U.S.A
1093:Oxysterol-binding protein 1
622:sterol transporter activity
2117:
1512:10.1161/ATVBAHA.106.138545
1417:10.1016/j.cell.2013.09.056
1589:10.1016/j.tcb.2004.07.017
1304:"Mouse PubMed Reference:"
1286:"Human PubMed Reference:"
1079:
1074:
1070:
1063:
1047:
1028:
1013:
992:
981:
966:
945:
934:
921:
917:
902:
898:
889:
876:
872:
857:
853:
844:
831:
827:
812:
808:
799:
784:
777:
773:
757:
582:
578:
561:
545:
536:
523:
472:
463:
410:
401:
371:
363:
359:
342:
329:
292:
271:
262:
258:
241:
228:
191:
168:
159:
155:
110:
107:
97:
90:
85:
66:
61:
44:
39:
34:
30:
26:
21:
1041:Chr 19: 11.94 – 11.97 Mb
1034:Chr 11: 59.57 – 59.62 Mb
2065:10.1091/mbc.E06-01-0060
2021:10.1073/pnas.0404720101
1719:10.1073/pnas.0700899104
1669:10.1091/mbc.E10-02-0090
1464:10.1126/science.1107710
1163:(PH) domain, a central
512:myocardium of ventricle
508:vastus lateralis muscle
1979:10.1006/geno.2001.6663
1945:10.1074/jbc.M011259200
1629:10.1074/jbc.M201191200
1553:10.1074/jbc.M710092200
1117:membrane contact sites
496:triceps brachii muscle
422:triceps brachii muscle
1826:10.1083/jcb.201104062
1358:10.1083/jcb.116.2.307
1121:25-hydroxycholesterol
683:endoplasmic reticulum
492:epithelium of stomach
287:Chromosome 19 (mouse)
185:Chromosome 11 (human)
1179:(-GTP), whereas the
430:right adrenal cortex
326:19 A|19 8.58 cM
62:List of PDB id codes
35:Available structures
2012:2004PNAS..10112130B
1777:10.1038/nature03923
1769:2005Natur.437..154I
1456:2005Sci...307.1472W
1161:pleckstrin homology
1155:Mechanism of action
703:trans-Golgi network
476:submandibular gland
450:left adrenal cortex
879:ENSMUSG00000024687
727:Biological process
636:Cellular component
590:Molecular function
442:left adrenal gland
1090:
1089:
1086:
1085:
1059:
1058:
1024:
1023:
1003:
1002:
977:
976:
956:
955:
930:
929:
911:
910:
885:
884:
866:
865:
840:
839:
821:
820:
769:
768:
612:oxysterol binding
574:
573:
570:
569:
532:
531:
519:
518:
457:
456:
426:corpus epididymis
355:
354:
254:
253:
81:
80:
77:
76:
45:Ortholog search:
2108:
2086:
2076:
2043:
2033:
2023:
1990:
1957:
1947:
1922:
1912:
1887:
1848:
1847:
1837:
1805:
1799:
1798:
1788:
1748:
1742:
1741:
1731:
1721:
1697:
1691:
1690:
1680:
1648:
1642:
1641:
1631:
1622:(33): 29908–18.
1607:
1601:
1600:
1577:Trends Cell Biol
1572:
1566:
1565:
1555:
1546:(15): 9595–605.
1531:
1525:
1524:
1514:
1490:
1484:
1483:
1450:(5714): 1472–6.
1439:
1430:
1429:
1419:
1395:
1380:
1379:
1369:
1337:
1326:
1325:
1318:
1312:
1311:
1300:
1294:
1293:
1282:
1276:
1266:
1255:
1245:
1072:
1071:
1043:
1036:
1019:
1007:
998:
986:
982:RefSeq (protein)
972:
960:
951:
939:
915:
896:
870:
851:
825:
806:
775:
739:sterol transport
580:
566:
557:
550:
543:
528:
468:
466:Top expressed in
461:
438:caput epididymis
406:
404:Top expressed in
399:
378:
361:
351:
338:
327:
312:
305:
299:
288:
276:
260:
250:
237:
226:
211:
204:
198:
187:
173:
157:
151:
149:OSBP - orthologs
102:
95:
72:
59:
53:
32:
31:
19:
2116:
2115:
2111:
2110:
2109:
2107:
2106:
2105:
2091:
2090:
2089:
2053:Mol. Biol. Cell
2046:
2006:(33): 12130–5.
1993:
1960:
1938:(21): 18570–8.
1925:
1903:(12): 2204–11.
1890:
1860:
1856:
1854:Further reading
1851:
1807:
1806:
1802:
1763:(7055): 154–8.
1750:
1749:
1745:
1699:
1698:
1694:
1663:(13): 2327–37.
1657:Mol. Biol. Cell
1650:
1649:
1645:
1609:
1608:
1604:
1574:
1573:
1569:
1533:
1532:
1528:
1492:
1491:
1487:
1441:
1440:
1433:
1397:
1396:
1383:
1339:
1338:
1329:
1320:
1319:
1315:
1302:
1301:
1297:
1284:
1283:
1279:
1267:
1258:
1246:
1237:
1233:
1221:
1204:
1157:
1112:
1081:View/Edit Mouse
1076:View/Edit Human
1039:
1032:
1029:Location (UCSC)
1015:
994:
968:
947:
860:ENSG00000110048
753:
734:lipid transport
722:
708:plasma membrane
648:Golgi apparatus
631:
607:protein binding
562:
552:
551:
524:
515:
510:
506:
502:
498:
494:
490:
486:
482:
480:right ventricle
478:
464:
453:
448:
444:
440:
436:
432:
428:
424:
420:
416:
402:
346:
333:
325:
315:
314:
313:
306:
286:
263:Gene location (
245:
232:
224:
214:
213:
212:
205:
183:
160:Gene location (
111:
98:
91:
68:
46:
17:
12:
11:
5:
2114:
2112:
2104:
2103:
2093:
2092:
2088:
2087:
2059:(6): 2604–16.
2044:
1991:
1958:
1923:
1888:
1857:
1855:
1852:
1850:
1849:
1800:
1743:
1712:(16): 6511–8.
1692:
1643:
1602:
1567:
1526:
1505:(5): 1108–14.
1485:
1431:
1381:
1327:
1313:
1295:
1277:
1256:
1234:
1232:
1229:
1220:
1217:
1203:
1200:
1156:
1153:
1111:
1108:
1088:
1087:
1084:
1083:
1078:
1068:
1067:
1061:
1060:
1057:
1056:
1054:
1052:
1045:
1044:
1037:
1030:
1026:
1025:
1022:
1021:
1011:
1010:
1004:
1001:
1000:
990:
989:
983:
979:
978:
975:
974:
964:
963:
957:
954:
953:
943:
942:
936:
932:
931:
928:
927:
919:
918:
912:
909:
908:
900:
899:
893:
887:
886:
883:
882:
874:
873:
867:
864:
863:
855:
854:
848:
842:
841:
838:
837:
829:
828:
822:
819:
818:
810:
809:
803:
797:
796:
791:
786:
782:
781:
771:
770:
767:
766:
755:
754:
752:
751:
746:
741:
736:
730:
728:
724:
723:
721:
720:
715:
710:
705:
700:
695:
690:
685:
680:
675:
670:
665:
663:Golgi membrane
660:
655:
650:
645:
639:
637:
633:
632:
630:
629:
627:sterol binding
624:
619:
614:
609:
604:
599:
593:
591:
587:
586:
576:
575:
572:
571:
568:
567:
559:
558:
540:
534:
533:
530:
529:
521:
520:
517:
516:
514:
513:
509:
505:
501:
497:
493:
489:
485:
484:lacrimal gland
481:
477:
473:
470:
469:
458:
455:
454:
452:
451:
447:
443:
439:
435:
431:
427:
423:
419:
418:jejunal mucosa
415:
411:
408:
407:
395:
394:
386:
375:
369:
368:
365:RNA expression
357:
356:
353:
352:
344:
340:
339:
331:
328:
323:
317:
316:
307:
300:
294:
290:
289:
284:
278:
277:
269:
268:
256:
255:
252:
251:
243:
239:
238:
230:
227:
222:
216:
215:
206:
199:
193:
189:
188:
181:
175:
174:
166:
165:
153:
152:
109:
105:
104:
96:
88:
87:
83:
82:
79:
78:
75:
74:
64:
63:
55:
54:
43:
37:
36:
28:
27:
24:
23:
15:
13:
10:
9:
6:
4:
3:
2:
2113:
2102:
2099:
2098:
2096:
2084:
2080:
2075:
2070:
2066:
2062:
2058:
2054:
2050:
2045:
2041:
2037:
2032:
2027:
2022:
2017:
2013:
2009:
2005:
2001:
1997:
1992:
1988:
1984:
1980:
1976:
1973:(3): 185–96.
1972:
1968:
1964:
1959:
1955:
1951:
1946:
1941:
1937:
1933:
1932:J. Biol. Chem
1929:
1924:
1920:
1916:
1911:
1906:
1902:
1898:
1894:
1889:
1885:
1881:
1877:
1873:
1869:
1865:
1859:
1858:
1853:
1845:
1841:
1836:
1831:
1827:
1823:
1820:(6): 965–78.
1819:
1815:
1811:
1804:
1801:
1796:
1792:
1787:
1782:
1778:
1774:
1770:
1766:
1762:
1758:
1754:
1747:
1744:
1739:
1735:
1730:
1725:
1720:
1715:
1711:
1707:
1703:
1696:
1693:
1688:
1684:
1679:
1674:
1670:
1666:
1662:
1658:
1654:
1647:
1644:
1639:
1635:
1630:
1625:
1621:
1617:
1616:J. Biol. Chem
1613:
1606:
1603:
1598:
1594:
1590:
1586:
1583:(9): 483–90.
1582:
1578:
1571:
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1541:
1540:J. Biol. Chem
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1438:
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1427:
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1418:
1413:
1410:(4): 830–43.
1409:
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1394:
1392:
1390:
1388:
1386:
1382:
1377:
1373:
1368:
1363:
1359:
1355:
1352:(2): 307–19.
1351:
1347:
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991:
987:
984:
980:
973:
971:
965:
961:
958:
952:
950:
944:
940:
937:
935:RefSeq (mRNA)
933:
926:
925:
920:
916:
913:
907:
906:
901:
897:
894:
892:
888:
881:
880:
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673:cell junction
671:
669:
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664:
661:
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651:
649:
646:
644:
641:
640:
638:
635:
634:
628:
625:
623:
620:
618:
617:lipid binding
615:
613:
610:
608:
605:
603:
600:
598:
595:
594:
592:
589:
588:
585:
584:Gene ontology
581:
577:
565:
560:
556:
549:
544:
541:
539:
535:
527:
522:
511:
507:
503:
499:
495:
491:
488:parotid gland
487:
483:
479:
475:
474:
471:
467:
462:
459:
449:
446:renal medulla
445:
441:
437:
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429:
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126:
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118:
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106:
101:
94:
89:
84:
73:
71:
65:
60:
57:
56:
52:
49:
42:
38:
33:
29:
25:
20:
2056:
2052:
2003:
1999:
1970:
1966:
1935:
1931:
1900:
1897:J. Lipid Res
1896:
1870:(1): 65–74.
1867:
1863:
1817:
1814:J. Cell Biol
1813:
1803:
1760:
1756:
1746:
1709:
1705:
1695:
1660:
1656:
1646:
1619:
1615:
1605:
1580:
1576:
1570:
1543:
1539:
1529:
1502:
1498:
1488:
1447:
1443:
1407:
1403:
1349:
1346:J. Cell Biol
1345:
1316:
1307:
1298:
1289:
1280:
1222:
1205:
1189:
1158:
1130:
1113:
1100:
1092:
1091:
1017:NP_001028346
1014:
993:
970:NM_001033174
967:
946:
922:
903:
877:
858:
832:
813:
793:
788:
388:
381:
108:External IDs
67:
1137:lipogenesis
668:nucleoplasm
347:11,971,476
334:11,943,305
246:59,615,774
233:59,574,398
86:Identifiers
1275:, May 2017
1254:, May 2017
1231:References
1202:Regulation
1181:FFAT motif
1165:FFAT motif
1151:proteins.
392:(ortholog)
129:HomoloGene
996:NP_002547
949:NM_002556
779:Orthologs
678:nucleolus
643:cytoplasm
414:beta cell
137:GeneCards
2095:Category
2083:16571669
2040:15302935
1987:11735225
1967:Genomics
1954:11278871
1919:10588946
1864:Genomics
1844:22162133
1795:16136145
1738:17428920
1687:20444975
1638:12023275
1597:15350976
1562:18230613
1521:17303778
1480:24956100
1472:15746430
1426:24209621
1271:–
1250:–
1219:Isoforms
1133:SREBP-1c
1110:Function
1065:Wikidata
758:Sources:
658:membrane
2074:1474796
2008:Bibcode
1884:1970801
1835:3241724
1786:1431608
1765:Bibcode
1729:1851665
1678:2893995
1452:Bibcode
1444:Science
1376:1730758
1367:2289278
1273:Ensembl
1252:Ensembl
1209:INSIG-1
1126:ERK 1/2
1097:protein
891:UniProt
846:Ensembl
785:Species
764:QuickGO
698:cytosol
693:nucleus
367:pattern
225:11q12.1
93:Aliases
2081:
2071:
2038:
2031:514446
2028:
1985:
1952:
1917:
1882:
1842:
1832:
1793:
1783:
1757:Nature
1736:
1726:
1685:
1675:
1636:
1595:
1560:
1519:
1478:
1470:
1424:
1374:
1364:
1051:search
1049:PubMed
924:Q3B7Z2
905:P22059
801:Entrez
538:BioGPS
117:167040
1476:S2CID
1185:VAP-A
1169:Golgi
1149:STAT3
1095:is a
834:76303
794:Mouse
789:Human
760:Amigo
504:ankle
500:molar
390:Mouse
383:Human
330:Start
265:Mouse
229:Start
162:Human
133:97668
125:97447
2079:PMID
2036:PMID
1983:PMID
1950:PMID
1915:PMID
1880:PMID
1840:PMID
1791:PMID
1734:PMID
1683:PMID
1634:PMID
1593:PMID
1558:PMID
1517:PMID
1468:PMID
1422:PMID
1404:Cell
1372:PMID
1213:ACAT
1196:SAC1
1192:PI4P
1177:Arf1
1173:PI4P
1147:and
1145:JAK2
1104:gene
1101:OSBP
815:5007
373:Bgee
321:Band
282:Chr.
220:Band
179:Chr.
141:OSBP
113:OMIM
100:OSBP
70:2RR3
51:RCSB
48:PDBe
22:OSBP
2069:PMC
2061:doi
2026:PMC
2016:doi
2004:101
1975:doi
1940:doi
1936:276
1905:doi
1872:doi
1830:PMC
1822:doi
1818:195
1781:PMC
1773:doi
1761:437
1724:PMC
1714:doi
1710:104
1673:PMC
1665:doi
1624:doi
1620:277
1585:doi
1548:doi
1544:283
1507:doi
1460:doi
1448:307
1412:doi
1408:155
1362:PMC
1354:doi
1350:116
1225:ORP
1211:or
1141:ERK
343:End
242:End
145:OMA
121:MGI
41:PDB
2097::
2077:.
2067:.
2057:17
2055:.
2051:.
2034:.
2024:.
2014:.
2002:.
1998:.
1981:.
1971:78
1969:.
1965:.
1948:.
1934:.
1930:.
1913:.
1901:40
1899:.
1895:.
1878:.
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1838:.
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1708:.
1704:.
1681:.
1671:.
1661:21
1659:.
1655:.
1632:.
1618:.
1614:.
1591:.
1581:14
1579:.
1556:.
1542:.
1538:.
1515:.
1503:27
1501:.
1497:.
1474:.
1466:.
1458:.
1446:.
1434:^
1420:.
1406:.
1402:.
1384:^
1370:.
1360:.
1348:.
1344:.
1330:^
1306:.
1288:.
1259:^
1238:^
1128:.
1119:.
1106:.
762:/
349:bp
336:bp
248:bp
235:bp
143:;
139::
135:;
131::
127:;
123::
119:;
115::
2085:.
2063::
2042:.
2018::
2010::
1989:.
1977::
1956:.
1942::
1921:.
1907::
1886:.
1874::
1868:7
1846:.
1824::
1797:.
1775::
1767::
1740:.
1716::
1689:.
1667::
1640:.
1626::
1599:.
1587::
1564:.
1550::
1523:.
1509::
1482:.
1462::
1454::
1428:.
1414::
1378:.
1356::
1324:.
1310:.
1292:.
267:)
164:)
147::
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