355:
332:
229:
254:
606:
361:
260:
2346:
4133:
Corrigall VM, Bodman-Smith MD, Brunst M, Cornell H, Panayi GS (April 2004). "Inhibition of antigen-presenting cell function and stimulation of human peripheral blood mononuclear cells to express an antiinflammatory cytokine profile by the stress protein BiP: relevance to the treatment of inflammatory
1554:
is bound to the NBD, the SBDα lid is open, which leads to the conformation of SBD with low affinity to substrate. Upon ATP hydrolysis, ADP is bound to the NBD and the lid closes on the bound substrate. This creates a low off rate for high-affinity substrate binding and protects the bound substrate
1534:
The NBD consists of two large globular subdomains (I and II), each further divided into two small subdomains (A and B). The subdomains are separated by a cleft where the nucleotide, one Mg, and two K ions bind and connect all four domains (IA, IB, IIA, IIB). The SBD is divided into two subdomains:
2138:
Like many stress and heat shock proteins, BiP has potent immunological activity when released from the internal environment of the cell into the extracellular space. Specifically, it feeds anti-inflammatory and pro-resolutory signals into immune networks, thus helping to resolve
52:
5672:
1716:
BiP is highly conserved among eukaryotes, including mammals (Table 1). It is also widely expressed among all tissue types in human. In the human BiP, there are two highly conserved cysteines. These cysteines have been shown to undergo
1535:
SBDβ and SBDα. SBDβ serves as a binding pocket for client proteins or peptide and SBDα serves as a helical lid to cover the binding pocket. An inter-domain linker connects NBD and SBD, favoring the formation of an NBD–SBD interface.
5677:
1635:
As an ER molecular chaperone, BiP is also required to import polypeptide into the ER lumen or ER membrane in an ATP-dependent manner. ATPase mutants of BiP were found to cause a block in translocation of a number of proteins
1559:. Exchange of ADP for ATP results in the opening of the SBDα lid and subsequent release of the substrate, which then is free to fold. The ATPase cycle can be synergistically enhanced by protein disulfide isomerase (
1664:. BiP is the first chaperone that contacts CPY* and is required for CPY* degradation. ATPase mutants (including allosteric mutants) of BiP have been shown to significantly slow down the degradation rate of CPY*.
2143:. The mechanisms underlying BiP's immunological activity are incompletely understood. Nonetheless, it has been shown to induce anti-inflammatory cytokine secretion by binding to a receptor on the surface of
1622:
mutants of BiP with defective ATPase activity (called class I mutations) and mutants of BiP with defective peptide binding activity (called class II mutations) both fail to fold carboxypeptidase Y (CPY) at
2162:, a murine disease that resembles human rheumatoid arthritis. Prophylactic or therapeutic parenteral delivery of BiP has been shown to ameliorate clinical and histological signs of inflammatory arthritis.
2547:
Hendershot LM, Valentine VA, Lee AS, Morris SW, Shapiro DN (Mar 1994). "Localization of the gene encoding human BiP/GRP78, the endoplasmic reticulum cognate of the HSP70 family, to chromosome 9q34".
2330:
rely on host BiP to successfully replicate, largely by infecting cells through cell-surface BiP, stimulating BiP expression to chaperone viral proteins, and suppressing the ER stress death response.
4485:
Zhao L, Longo-Guess C, Harris BS, Lee JW, Ackerman SL (September 2005). "Protein accumulation and neurodegeneration in the woozy mutant mouse is caused by disruption of SIL1, a cochaperone of BiP".
1688:), effectively activating their respective UPR pathways. As a UPR target gene product, BiP is upregulated when UPR transcription factors associate with the UPR element in BiP's DNA promoter region.
4528:
Anttonen AK, Mahjneh I, Hämäläinen RH, Lagier-Tourenne C, Kopra O, Waris L, et al. (December 2005). "The gene disrupted in
Marinesco-Sjögren syndrome encodes SIL1, an HSPA5 cochaperone".
1582:
Substrate release and binding by BiP facilitates diverse functions in the ER such as folding and assembly of newly synthesized proteins, binding to misfolded proteins to prevent protein
4826:
4351:"Prolonged endoplasmic reticulum stress in hypertrophic and failing heart after aortic constriction: possible contribution of endoplasmic reticulum stress to cardiac myocyte apoptosis"
3614:
Okamura K, Kimata Y, Higashio H, Tsuru A, Kohno K (December 2000). "Dissociation of Kar2p/BiP from an ER sensory molecule, Ire1p, triggers the unfolded protein response in yeast".
1515:. BiP is an abundant protein under all growth conditions, but its synthesis is markedly induced under conditions that lead to the accumulation of unfolded polypeptides in the ER.
5079:
1579:) family and involved in the folding and assembly of proteins in the ER. The level of BiP is strongly correlated with the amount of secretory proteins (e.g. IgG) within the ER.
368:
267:
5692:
3544:
Nishikawa S, Brodsky JL, Nakatsukasa K (May 2005). "Roles of molecular chaperones in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD)".
2299:. As a result, these bacterial Hsp70 chaperones represent a promising set of targets for antibiotic development. Notably, the anticancer drug OSU-03012 re-sensitized
4261:"Treatment of murine collagen-induced arthritis by the stress protein BiP via interleukin-4-producing regulatory T cells: a novel function for an ancient protein"
1708:, which promote ATP hydrolysis. BiP is also a validated substrate of HYPE (Huntingtin Yeast Interacting Partner E), which can adenylate BiP at multiple residues.
4171:"Binding immunoglobulin protein-treated peripheral blood monocyte-derived dendritic cells are refractory to maturation and induce regulatory T-cell development"
1575:(GRPs), is markedly increased. GRP78 (HSPA5), also referred to as 'immunoglobulin heavy chain-binding protein' (BiP), is a member of the heat-shock protein-70 (
4819:
2509:
Ting J, Lee AS (May 1988). "Human gene encoding the 78,000-dalton glucose-regulated protein and its pseudogene: structure, conservation, and regulation".
4220:"The human endoplasmic reticulum molecular chaperone BiP is an autoantigen for rheumatoid arthritis and prevents the induction of experimental arthritis"
1179:
1160:
190:
3053:
Zuiderweg ER, Bertelsen EB, Rousaki A, Mayer MP, Gestwicki JE, Ahmad A (2012-01-01). "Allostery in the Hsp70 chaperone proteins". In
Jackson S (ed.).
2232:
death induced by ER stress by correcting misfolded proteins. Moreover, a chemical inducer of BiP, named BIX, reduced cerebral infarction in cerebral
1729:
upon oxidative stress. Both modifications enhance BiP's ability to prevent protein aggregation. In mice cells, the conserved cysteine pair forms a
4812:
5424:
3197:
Kober L, Zehe C, Bode J (Oct 2012). "Development of a novel ER stress based selection system for the isolation of highly productive clones".
3070:
2491:
2737:"Crystal structures of the ATPase domains of four human Hsp70 isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78"
2473:
5667:
2319:
3786:"hsp70 genes in the human genome: Conservation and differentiation patterns predict a wide array of overlapping and specialized functions"
1387:
354:
5642:
4777:
4715:"Differential unfolded protein response during Chikungunya and Sindbis virus infection: CHIKV nsP4 suppresses eIF2α phosphorylation"
3340:"Binding protein BiP is required for translocation of secretory proteins into the endoplasmic reticulum in Saccharomyces cerevisiae"
1394:
2636:"1H, 13C, and 15N backbone assignment and secondary structure of the receptor-binding domain of vascular endothelial growth factor"
331:
4049:
Panayi GS, Corrigall VM, Henderson B (August 2004). "Stress cytokines: pivotal proteins in immune regulatory networks; Opinion".
2158:
The potent immunomodulatory activities of BiP/GRP78 have also been demonstrated in animal models of autoimmune disease including
2855:"Structural basis for the inhibition of HSP70 and DnaK chaperones by small-molecule targeting of a C-terminal allosteric pocket"
4835:
2460:
2439:
1718:
1511:
machinery and plays a role in retrograde transport across the ER membrane of aberrant proteins destined for degradation by the
3735:"A novel link between Fic (filamentation induced by cAMP)-mediated adenylylation/AMPylation and the unfolded protein response"
1527:: a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The NBD binds and hydrolyzes ATP, and the SBD binds
4446:"Overexpression of endoplasmic reticulum-resident chaperone attenuates cardiomyocyte death induced by proteasome inhibition"
4302:"Oxidative activation of Ca(2+)/calmodulin-activated kinase II mediates ER stress-induced cardiac dysfunction and apoptosis"
2456:
4783:
3686:"XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor"
253:
228:
49:
5687:
1660:. The most studied ERAD substrate is CPY*, a constitutively misfolded CPY completely imported into the ER and modified by
2435:
5682:
5248:
4798:
provides an overview of all the structure information available in the PDB for Human
Endoplasmic reticulum chaperone BiP
3579:
Chapman R, Sidrauski C, Walter P (1998-01-01). "Intracellular signaling from the endoplasmic reticulum to the nucleus".
170:
3848:"Redox signaling via the molecular chaperone BiP protects cells against endoplasmic reticulum-derived oxidative stress"
5193:
4668:"Control of mRNA translation preserves endoplasmic reticulum function in beta cells and maintains glucose homeostasis"
1560:
161:, BIP, GRP78, HEL-S-89n, MIF2, Binding immunoglobulin protein, heat shock protein family A (Hsp70) member 5, GRP78/Bip
2353:
The 2016 version of this article was updated by an external expert under a dual publication model. The corresponding
367:
266:
2159:
1701:
3902:"Formation and Reversibility of BiP Cysteine Oxidation Facilitates Cell Survival During and Post Oxidative Stress"
360:
259:
1673:
1595:
1572:
895:
positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress
5133:
4770:
1676:, and an essential regulator of the UPR pathway. During ER stress, BiP dissociates from the three transducers (
1224:
178:
4002:"Loss of the oxidative stress sensor NPGPx compromises GRP78 chaperone activity and induces systemic disease"
3953:"Loss of the oxidative stress sensor NPGPx compromises GRP78 chaperone activity and induces systemic disease"
5458:
2202:
1205:
5630:
5499:
2904:"Allosteric coupling between the lid and interdomain linker in DnaK revealed by inhibitor binding studies"
2237:
2171:
1624:
1619:
1551:
3399:"A Sec63p-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposome"
4880:
3150:"BiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functions"
2354:
2307:
1492:
2953:"The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE"
2220:
cardiomyocytes, overexpression of BiP attenuates cardiomyocyte death induced by proteasome inhibition.
4259:
Brownlie RJ, Myers LK, Wooley PH, Corrigall VM, Bodman-Smith MD, Panayi GS, et al. (March 2006).
3797:
3500:
3351:
3019:
2964:
2807:
2748:
2300:
2213:
242:
157:
4843:
4789:
2229:
1611:
1583:
1556:
1488:
1366:
1315:
4766:
4666:
Scheuner D, Vander Mierde D, Song B, Flamez D, Creemers JW, Tsukamoto K, et al. (July 2005).
4218:
Corrigall VM, Bodman-Smith MD, Fife MS, Canas B, Myers LK, Wooley P, et al. (February 2001).
5489:
4857:
4695:
4553:
4510:
3715:
3526:
3489:"Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation"
3222:
2735:
Wisniewska M, Karlberg T, Lehtiö L, Johansson I, Kotenyova T, Moche M, et al. (2010-01-01).
202:
4086:"Resolution-associated molecular patterns (RAMP): RAMParts defending immunological homeostasis?"
1721:
in both yeast and mammalian cells. In yeast cells, the N-terminus cysteine has been shown to be
1370:
1345:
1319:
1294:
4349:
Okada K, Minamino T, Tsukamoto Y, Liao Y, Tsukamoto O, Takashima S, et al. (August 2004).
5159:
4746:
4687:
4648:
4594:
4545:
4502:
4467:
4426:
4372:
4331:
4282:
4241:
4200:
4151:
4115:
4066:
4031:
3982:
3933:
3879:
3825:
3766:
3707:
3666:
3631:
3596:
3561:
3518:
3469:
3428:
3379:
3320:
3271:
3214:
3179:
3127:
3086:
3066:
3035:
2992:
2933:
2884:
2835:
2776:
2717:
2665:
2616:
2564:
2526:
2403:
1591:
1587:
1544:
1508:
1496:
150:
42:
2587:"Close and Allosteric Opening of the Polypeptide-Binding Site in a Human Hsp70 Chaperone BiP"
2345:
5419:
5378:
5373:
5348:
5338:
5333:
5323:
5123:
4736:
4726:
4679:
4638:
4630:
4584:
4537:
4494:
4457:
4416:
4408:
4362:
4321:
4313:
4272:
4231:
4190:
4182:
4143:
4105:
4097:
4058:
4021:
4013:
3972:
3964:
3923:
3913:
3869:
3859:
3815:
3805:
3756:
3746:
3697:
3658:
3623:
3588:
3553:
3508:
3459:
3448:"Endoplasmic reticulum associated protein degradation: a chaperone assisted journey to hell"
3418:
3410:
3369:
3359:
3310:
3302:
3261:
3253:
3206:
3169:
3161:
3117:
3076:
3058:
3027:
2982:
2972:
2923:
2915:
2874:
2866:
2825:
2815:
2766:
2756:
2707:
2699:
2655:
2647:
2606:
2598:
2556:
2518:
2393:
2385:
2303:
2186:
447:
378:
322:
277:
5394:
5328:
4571:
Kudo T, Kanemoto S, Hara H, Morimoto N, Morihara T, Kimura R, et al. (February 2008).
3057:. Topics in Current Chemistry. Vol. 328. Springer Berlin Heidelberg. pp. 99–153.
3010:
Schmid D, Baici A, Gehring H, Christen P (1994). "Kinetics of molecular chaperone action".
605:
198:
5625:
4848:
3733:
Sanyal A, Chen AJ, Nakayasu ES, Lazar CS, Zbornik EA, Worby CA, et al. (March 2015).
3662:
2315:
2296:
2257:
2209:
2175:
1645:
1500:
422:
1618:). Intact ATPase activity and peptide binding activity are required to act as a foldase:
4444:
Fu HY, Minamino T, Tsukamoto O, Sawada T, Asai M, Kato H, et al. (September 2008).
3801:
3504:
3355:
3023:
2968:
2811:
2752:
5172:
5167:
4741:
4714:
4643:
4618:
4421:
4396:
4367:
4350:
4326:
4301:
4195:
4170:
4110:
4085:
4026:
4001:
3977:
3952:
3928:
3901:
3874:
3847:
3820:
3785:
3761:
3734:
3423:
3398:
3315:
3290:
3266:
3241:
3174:
3149:
3081:
2928:
2903:
2879:
2854:
2830:
2795:
2771:
2736:
2712:
2687:
2660:
2635:
2611:
2586:
2398:
2376:
2367:
2249:
2170:
Upregulation of BiP has been associated with ER stress-induced cardiac dysfunction and
2152:
1730:
1524:
4617:
Booth L, Roberts JL, Cash DR, Tavallai S, Jean S, Fidanza A, et al. (July 2015).
3702:
3685:
3242:"BiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeast"
1094:
1089:
1084:
1079:
1074:
1069:
1064:
1059:
1054:
1049:
1044:
1039:
1034:
1029:
1024:
1019:
1014:
1009:
1004:
999:
994:
989:
984:
979:
974:
969:
964:
959:
954:
949:
944:
939:
934:
929:
924:
919:
914:
909:
904:
899:
894:
889:
884:
879:
874:
869:
864:
848:
843:
838:
833:
828:
823:
818:
813:
808:
803:
798:
793:
788:
783:
778:
773:
768:
763:
758:
753:
748:
743:
738:
722:
717:
712:
707:
702:
697:
692:
687:
682:
677:
672:
667:
662:
657:
652:
647:
5661:
4795:
4186:
4101:
3592:
3374:
3339:
2987:
2952:
1722:
1661:
634:
4557:
4514:
3226:
5528:
5510:
4699:
4667:
3719:
3649:
Korennykh A, Walter P (2012). "Structural basis of the unfolded protein response".
3530:
2265:
2261:
2198:
2194:
2179:
2148:
2140:
1697:
1641:
1528:
440:
219:
4412:
2236:
mice. Conversely, enhanced BiP chaperone function has been strongly implicated in
182:
4804:
4017:
3968:
3464:
3447:
2761:
1571:
When K12 cells are starved of glucose, the synthesis of several proteins, called
915:
negative regulation of transforming growth factor beta receptor signaling pathway
206:
5604:
5472:
4317:
4236:
4219:
3291:"Loss of BiP/GRP78 function blocks translocation of secretory proteins in yeast"
2496:
National Center for
Biotechnology Information, U.S. National Library of Medicine
2478:
National Center for
Biotechnology Information, U.S. National Library of Medicine
2311:
2284:
2190:
1726:
3344:
Proceedings of the
National Academy of Sciences of the United States of America
2957:
Proceedings of the
National Academy of Sciences of the United States of America
2800:
Proceedings of the
National Academy of Sciences of the United States of America
2634:
Fairbrother WJ, Champe MA, Christinger HW, Keyt BA, Starovasnik MA (Oct 1997).
2389:
523:
5434:
4862:
4062:
4000:
Wei PC, Hsieh YH, Su MI, Jiang X, Hsu PH, Lo WT, et al. (December 2012).
3165:
2703:
2602:
1512:
339:
236:
186:
2977:
5182:
5128:
4731:
3918:
3751:
3031:
2820:
2323:
2288:
1637:
1124:
583:
461:
406:
393:
305:
292:
194:
5673:
Knowledge (XXG) articles with corresponding academic peer reviewed articles
4750:
4691:
4652:
4619:"GRP78/BiP/HSPA5/Dna K is a universal therapeutic target for human disease"
4598:
4589:
4572:
4549:
4506:
4471:
4430:
4376:
4335:
4286:
4245:
4204:
4155:
4119:
4070:
4035:
3986:
3937:
3883:
3829:
3810:
3770:
3711:
3670:
3635:
3627:
3565:
3473:
3414:
3364:
3306:
3218:
3183:
3131:
3122:
3105:
3090:
2937:
2888:
2839:
2780:
2721:
2651:
2620:
2560:
2522:
2407:
3600:
3522:
3432:
3383:
3324:
3275:
3039:
2996:
2796:"Substrate-binding domain conformational dynamics mediate Hsp70 allostery"
2669:
2568:
2530:
1737:(NPGPx). The disulfide bond enhances BiP's binding to denatured proteins.
1434:
1429:
5462:
5095:
5087:
4462:
4445:
3951:
Wei PC, Hsieh YH, Su MI, Jiang X, Hsu PH, Lo WT, et al. (Dec 2012).
3257:
3062:
2951:
Szabo A, Langer T, Schröder H, Flanagan J, Bukau B, Hartl FU (Oct 1994).
2264:
by upregulating protective ER stress pathways. BiP is also necessary for
2233:
2217:
2183:
2144:
1504:
1418:
1269:
1250:
3864:
3557:
2919:
5213:
5100:
5060:
4991:
4986:
4981:
4976:
4971:
4926:
3106:"BiP and PDI cooperate in the oxidative folding of antibodies in vitro"
2273:
2269:
2253:
2151:
activation, and modulate the differentiation pathway of monocytes into
1681:
1615:
1607:
1470:
1236:
1191:
5678:
Knowledge (XXG) articles with corresponding articles published in Gene
4634:
4277:
4260:
4147:
3210:
2870:
127:
123:
119:
115:
111:
107:
103:
99:
95:
91:
87:
83:
79:
75:
71:
5429:
5404:
5399:
5389:
5353:
5343:
5318:
5303:
5298:
5293:
5288:
5283:
5278:
5273:
5268:
5233:
5218:
5065:
5030:
5015:
5010:
5005:
4966:
4961:
4956:
4951:
4946:
4941:
4936:
4931:
4921:
4916:
4911:
4906:
4901:
1547:
1402:
1146:
1499:
into the ER, and maintains them in a state competent for subsequent
4683:
4541:
4498:
5620:
5610:
5600:
5585:
5567:
5562:
5557:
5552:
5484:
5444:
5409:
5383:
5368:
5363:
5358:
5313:
5308:
5263:
5258:
5253:
5223:
5208:
5105:
5074:
5055:
5050:
5045:
5040:
5025:
5020:
5000:
4896:
4889:
4885:
4875:
4870:
3684:
Yoshida H, Matsui T, Yamamoto A, Okada T, Mori K (December 2001).
3513:
3488:
2327:
1705:
1576:
1484:
3487:
Plemper RK, Böhmler S, Bordallo J, Sommer T, Wolf DH (Aug 1997).
2853:
Leu JI, Zhang P, Murphy ME, Marmorstein R, George DL (Nov 2014).
1109:
1105:
5635:
5615:
5595:
5590:
5540:
5523:
5479:
5467:
5449:
5439:
5238:
5228:
5203:
5198:
5143:
5138:
4306:
American
Journal of Physiology. Heart and Circulatory Physiology
2292:
2216:, have been associated with heart failure complications. In rat
1734:
1685:
1677:
1657:
1477:
174:
4808:
4573:"A molecular chaperone inducer protects neurons from ER stress"
2372:
Gene encoding Hsp70 chaperone BiP in the endoplasmic reticulum"
614:
2688:"Hsp70 chaperones: cellular functions and molecular mechanism"
2339:
1095:
posttranslational protein targeting to membrane, translocation
1090:
negative regulation of IRE1-mediated unfolded protein response
3452:
Biochimica et
Biophysica Acta (BBA) - Molecular Cell Research
3156:. Molecular Chaperones and Protein Quality Control (Part I).
3784:
Brocchieri L, Conway de Macario E, Macario AJ (2008-01-23).
2366:
Jie Wang, Jessica Lee, David Liem, Peipei Ping (June 2017).
2174:. BiP also has been proposed to suppress the development of
900:
maintenance of protein localization in endoplasmic reticulum
4397:"ER chaperones in mammalian development and human diseases"
3240:
Simons JF, Ferro-Novick S, Rose MD, Helenius A (Jul 1995).
1610:) or simply bind and restrict a substrate from folding or
985:
proteolysis involved in cellular protein catabolic process
2122:*Predicted: Predicted sequence according to NCBI protein
2201:
activity, all of which can contribute to the buildup of
980:
negative regulation of protein homodimerization activity
430:
1495:(ER) that binds newly synthesized proteins as they are
4084:
Shields AM, Panayi GS, Corrigall VM (September 2011).
3846:
Wang J, Pareja KA, Kaiser CA, Sevier CS (2014-07-22).
3104:
Mayer M, Kies U, Kammermeier R, Buchner J (Sep 2000).
880:
regulation of protein folding in endoplasmic reticulum
2252:
is proposed to protect against high fat diet-induced
2189:, inhibiting the activation of genes responsible for
1704:, which facilitate ATP binding upon ADP release, and
1000:
regulation of IRE1-mediated unfolded protein response
965:
regulation of PERK-mediated unfolded protein response
870:
regulation of ATF6-mediated unfolded protein response
595:
4169:
Corrigall VM, Vittecoq O, Panayi GS (October 2009).
1010:
positive regulation of neuron projection development
829:
endoplasmic reticulum-Golgi intermediate compartment
794:
integral component of endoplasmic reticulum membrane
5578:
5509:
5498:
5181:
5158:
5116:
4856:
4842:
4713:Rathore AP, Ng ML, Vasudevan SG (28 January 2013).
3616:
Biochemical and Biophysical Research Communications
1672:BiP is both a target of the ER stress response, or
1359:
1338:
1308:
1287:
2585:Yang J, Nune M, Zong Y, Zhou L, Liu Q (Dec 2015).
2452:
2450:
2448:
2431:
2429:
2427:
1606:BiP can actively fold its substrates (acting as a
2291:were found to interact with key proteins such as
1050:cellular response to nerve growth factor stimulus
377:
276:
3148:Behnke J, Feige MJ, Hendershot LM (April 2015).
1741:Table 1. Conservation of BiP in mammalian cells
4612:
4610:
4608:
4390:
4388:
4386:
3651:Annual Review of Cell and Developmental Biology
3581:Annual Review of Cell and Developmental Biology
945:endoplasmic reticulum unfolded protein response
16:Protein-coding gene in the species Homo sapiens
3143:
3141:
2457:GRCm38: Ensembl release 89: ENSMUSG00000026864
2147:, downregulate critical molecules involved in
1085:chaperone cofactor-dependent protein refolding
4820:
2542:
2540:
995:positive regulation of protein ubiquitination
8:
3895:
3893:
3841:
3839:
2681:
2679:
2197:biosynthesis, and suppressing tissue factor
2182:-induced ER stress, preventing apoptosis of
1507:. BiP is also an essential component of the
3338:Nguyen TH, Law DT, Williams DB (Feb 1991).
2580:
2578:
2436:GRCh38: Ensembl release 89: ENSG00000044574
2322:undermines host cell survival by producing
5506:
4853:
4827:
4813:
4805:
1120:
960:cerebellar Purkinje cell layer development
630:
418:
317:
214:
60:
4769:at the U.S. National Library of Medicine
4740:
4730:
4642:
4588:
4461:
4420:
4366:
4325:
4276:
4235:
4194:
4109:
4025:
3976:
3927:
3917:
3873:
3863:
3819:
3809:
3760:
3750:
3701:
3512:
3463:
3422:
3373:
3363:
3314:
3265:
3173:
3121:
3080:
2986:
2976:
2927:
2878:
2829:
2819:
2770:
2760:
2711:
2659:
2610:
2397:
2228:As an ER chaperone protein, BiP prevents
1696:BiP's ATPase cycle is facilitated by its
1045:response to methamphetamine hydrochloride
3289:Vogel JP, Misra LM, Rose MD (Jun 1990).
2902:Liebscher M, Roujeinikova A (Mar 2009).
1739:
1543:The activity of BiP is regulated by its
925:response to endoplasmic reticulum stress
910:protein folding in endoplasmic reticulum
905:negative regulation of apoptotic process
849:intracellular membrane-bounded organelle
5693:Endoplasmic reticulum resident proteins
2423:
955:IRE1-mediated unfolded protein response
950:ATF6-mediated unfolded protein response
930:PERK-mediated unfolded protein response
875:cellular response to glucose starvation
784:endoplasmic reticulum chaperone complex
2794:Zhuravleva A, Gierasch LM (Jun 2015).
20:
3663:10.1146/annurev-cellbio-101011-155826
890:positive regulation of cell migration
382:
343:
338:
281:
240:
235:
7:
4090:Clinical and Experimental Immunology
2692:Cellular and Molecular Life Sciences
1055:cellular response to gamma radiation
554:endothelial cell of lymphatic vessel
538:vestibular membrane of cochlear duct
3906:The Journal of Biological Chemistry
3739:The Journal of Biological Chemistry
3397:Brodsky JL, Schekman R (Dec 1993).
3110:The Journal of Biological Chemistry
1987:Balaenoptera acutorostrata scammoni
5643:Prokaryotic ubiquitin-like protein
4368:10.1161/01.CIR.0000137836.95625.D4
2326:to inhibit host BiP. In contrast,
1356:
1335:
1305:
1284:
1260:
1241:
1215:
1196:
1170:
1151:
990:cellular response to manganese ion
935:cerebellum structural organization
865:cellular response to interleukin-4
723:protein folding chaperone activity
600:
518:
456:
435:
14:
1702:nucleotide binding factors (NEFs)
1473:that in humans is encoded by the
4187:10.1111/j.1365-2567.2009.03103.x
4102:10.1111/j.1365-2249.2011.04433.x
3593:10.1146/annurev.cellbio.14.1.459
3199:Biotechnology and Bioengineering
2344:
2320:Shiga toxigenic Escherichia coli
1719:post-translational modifications
1652:ER-associated degradation (ERAD)
1455:78 kDa glucose-regulated protein
1030:cellular response to calcium ion
970:ubiquitin-dependent ERAD pathway
698:ubiquitin protein ligase binding
604:
366:
359:
353:
330:
265:
258:
252:
227:
1757:Conservation of BiP's cysteine
975:cellular response to antibiotic
663:protein domain specific binding
5173:Mitochondrial targeting signal
4836:Posttranslational modification
4623:Journal of Cellular Physiology
4577:Cell Death and Differentiation
3900:Wang J, Sevier CS (Feb 2016).
2686:Mayer MP, Bukau B (Mar 2005).
2295:, which is vital to bacterial
1447:Binding immunoglobulin protein
749:endoplasmic reticulum membrane
615:More reference expression data
584:More reference expression data
1:
4413:10.1016/j.febslet.2007.04.045
4051:Current Opinion in Immunology
3703:10.1016/s0092-8674(01)00611-0
3446:Stolz A, Wolf DH (Jun 2010).
1712:Conservation of BiP cysteines
534:vestibular sensory epithelium
351:
250:
5249:Ubiquitin-conjugating enzyme
4300:Roe ND, Ren J (March 2013).
4018:10.1016/j.molcel.2012.10.007
3969:10.1016/j.molcel.2012.10.007
3465:10.1016/j.bbamcr.2010.02.005
3154:Journal of Molecular Biology
2762:10.1371/journal.pone.0008625
2310:to several standard-of-care
1523:BiP contains two functional
1491:located in the lumen of the
1065:response to unfolded protein
1040:stress response to metal ion
885:substantia nigra development
779:smooth endoplasmic reticulum
5668:Genes on human chromosome 9
5537:E2 SUMO-conjugating enzyme
5194:Ubiquitin-activating enzyme
4318:10.1152/ajpheart.00752.2012
4237:10.4049/jimmunol.166.3.1492
3403:The Journal of Cell Biology
3295:The Journal of Cell Biology
3246:The Journal of Cell Biology
1602:Protein folding and holding
1463:heat shock 70 kDa protein 5
744:endoplasmic reticulum lumen
5709:
5520:E1 SUMO-activating enzyme
4788:gene details page in the
4395:Ni M, Lee AS (July 2007).
2390:10.1016/j.gene.2017.03.005
2160:collagen-induced arthritis
1625:non-permissive temperature
1573:glucose-regulated proteins
1555:from premature folding or
844:protein-containing complex
718:heat shock protein binding
566:superior cervical ganglion
4063:10.1016/j.coi.2004.05.017
3166:10.1016/j.jmb.2015.02.011
2704:10.1007/s00018-004-4464-6
2603:10.1016/j.str.2015.10.012
2492:"Mouse PubMed Reference:"
2474:"Human PubMed Reference:"
2357:article was published in
2224:Neurodegenerative disease
2121:
2080:
2020:
1960:
1843:
1764:
1656:BiP also plays a role in
1563:), and its cochaperones.
1433:
1428:
1424:
1417:
1401:
1388:Chr 9: 125.23 – 125.24 Mb
1382:
1363:
1342:
1331:
1312:
1291:
1280:
1267:
1263:
1248:
1244:
1235:
1222:
1218:
1203:
1199:
1190:
1177:
1173:
1158:
1154:
1145:
1130:
1123:
1119:
1103:
1075:Unfolded Protein Response
1070:cellular response to heat
1035:cellular response to cAMP
673:misfolded protein binding
633:
629:
612:
603:
594:
581:
530:
521:
468:
459:
429:
421:
417:
400:
387:
350:
329:
320:
316:
299:
286:
249:
226:
217:
213:
168:
165:
155:
148:
143:
68:
63:
46:
41:
36:
32:
28:
23:
5134:Survival of motor neuron
4771:Medical Subject Headings
4265:Arthritis and Rheumatism
4136:Arthritis and Rheumatism
3790:BMC Evolutionary Biology
2978:10.1073/pnas.91.22.10345
1751:Species scientific name
1594:, and initiation of the
1025:neuron apoptotic process
703:unfolded protein binding
5500:Ubiquitin-like proteins
5459:Deubiquitinating enzyme
4732:10.1186/1743-422X-10-36
4450:Cardiovascular Research
3919:10.1074/jbc.M115.694810
3752:10.1074/jbc.M114.618348
3546:Journal of Biochemistry
3032:10.1126/science.8310296
2908:Journal of Bacteriology
2821:10.1073/pnas.1506692112
2203:atherosclerotic plaques
1395:Chr 2: 34.66 – 34.67 Mb
492:mucosa of sigmoid colon
4590:10.1038/sj.cdd.4402276
3811:10.1186/1471-2148-8-19
3628:10.1006/bbrc.2000.3987
3415:10.1083/jcb.123.6.1355
3365:10.1073/pnas.88.4.1565
3307:10.1083/jcb.110.6.1885
3123:10.1074/jbc.M002655200
2652:10.1002/pro.5560061020
2561:10.1006/geno.1994.1166
2523:10.1089/dna.1988.7.275
2355:academic peer reviewed
2172:dilated cardiomyopathy
2166:Cardiovascular disease
1640:, carboxypeptidase Y,
1015:neuron differentiation
4224:Journal of Immunology
2308:Neisseria gonorrhoeae
2214:proteasome inhibitors
2129:Clinical significance
2088:Monodelphis domestica
2066:Mustela putorius furo
1927:Oryctolagus cuniculus
1908:Heterocephalus glaber
1620:temperature-sensitive
1493:endoplasmic reticulum
1005:response to radiation
819:extracellular exosome
804:endoplasmic reticulum
542:mandibular prominence
5688:Molecular chaperones
4782:genome location and
4767:HSPA5+protein,+human
3258:10.1083/jcb.130.1.41
3063:10.1007/128_2012_323
3055:Molecular Chaperones
2859:ACS Chemical Biology
2363:and can be cited as:
2178:through alleviating
2107:Sarcophilus harrisii
1754:Conservation of BiP
1748:Species common name
940:ER overload response
834:extracellular matrix
546:maxillary prominence
345:Chromosome 2 (mouse)
243:Chromosome 9 (human)
64:List of PDB id codes
37:Available structures
5683:Heat shock proteins
4858:Heat shock proteins
4790:UCSC Genome Browser
3865:10.7554/eLife.03496
3802:2008BMCEE...8...19B
3505:1997Natur.388..891P
3409:(6 Pt 1): 1355–63.
3356:1991PNAS...88.1565N
3024:1994Sci...263..971S
2969:1994PNAS...9110345S
2920:10.1128/JB.01131-08
2812:2015PNAS..112E2865Z
2753:2010PLoSO...5.8625W
2238:Alzheimer's disease
1810:Chlorocebus sabaeus
1742:
1733:upon activation of
1020:response to cocaine
653:calcium ion binding
384:2 B|2 22.94 cM
4463:10.1093/cvr/cvn128
2280:Infectious disease
2134:Autoimmune disease
1829:Callithrix jacchus
1740:
1592:secretory proteins
1225:ENSMUSG00000026864
858:Biological process
732:Cellular component
713:hydrolase activity
648:nucleotide binding
641:Molecular function
500:lower lobe of lung
5655:
5654:
5651:
5650:
5160:Protein targeting
5154:
5153:
4635:10.1002/jcp.24919
4278:10.1002/art.21654
4148:10.1002/art.20134
3558:10.1093/jb/mvi068
3211:10.1002/bit.24527
3072:978-3-642-34551-7
2871:10.1021/cb500236y
2416:
2415:
2244:Metabolic disease
2187:endothelial cells
2126:
2125:
1870:Rattus norvegicus
1444:
1443:
1440:
1439:
1413:
1412:
1378:
1377:
1353:
1352:
1327:
1326:
1302:
1301:
1276:
1275:
1257:
1256:
1231:
1230:
1212:
1211:
1186:
1185:
1167:
1166:
1115:
1114:
1080:protein refolding
658:chaperone binding
625:
624:
621:
620:
590:
589:
577:
576:
515:
514:
488:corpus epididymis
413:
412:
312:
311:
207:HSPA5 - orthologs
139:
138:
135:
134:
47:Ortholog search:
5700:
5507:
5420:Ubiquitin ligase
5186:(ubiquitylation)
5124:Alpha crystallin
4854:
4829:
4822:
4815:
4806:
4755:
4754:
4744:
4734:
4719:Virology Journal
4710:
4704:
4703:
4663:
4657:
4656:
4646:
4614:
4603:
4602:
4592:
4568:
4562:
4561:
4525:
4519:
4518:
4482:
4476:
4475:
4465:
4441:
4435:
4434:
4424:
4392:
4381:
4380:
4370:
4346:
4340:
4339:
4329:
4297:
4291:
4290:
4280:
4256:
4250:
4249:
4239:
4215:
4209:
4208:
4198:
4166:
4160:
4159:
4130:
4124:
4123:
4113:
4081:
4075:
4074:
4046:
4040:
4039:
4029:
3997:
3991:
3990:
3980:
3948:
3942:
3941:
3931:
3921:
3897:
3888:
3887:
3877:
3867:
3843:
3834:
3833:
3823:
3813:
3781:
3775:
3774:
3764:
3754:
3730:
3724:
3723:
3705:
3681:
3675:
3674:
3646:
3640:
3639:
3611:
3605:
3604:
3576:
3570:
3569:
3541:
3535:
3534:
3516:
3484:
3478:
3477:
3467:
3443:
3437:
3436:
3426:
3394:
3388:
3387:
3377:
3367:
3335:
3329:
3328:
3318:
3286:
3280:
3279:
3269:
3237:
3231:
3230:
3205:(10): 2599–611.
3194:
3188:
3187:
3177:
3145:
3136:
3135:
3125:
3101:
3095:
3094:
3084:
3050:
3044:
3043:
3007:
3001:
3000:
2990:
2980:
2948:
2942:
2941:
2931:
2899:
2893:
2892:
2882:
2850:
2844:
2843:
2833:
2823:
2806:(22): E2865–73.
2791:
2785:
2784:
2774:
2764:
2732:
2726:
2725:
2715:
2683:
2674:
2673:
2663:
2631:
2625:
2624:
2614:
2597:(12): 2191–203.
2582:
2573:
2572:
2544:
2535:
2534:
2506:
2500:
2499:
2488:
2482:
2481:
2470:
2464:
2454:
2443:
2433:
2411:
2401:
2348:
2340:
2210:anticancer drugs
2103:Tasmanian Devil
2047:Felis silvestris
2028:Canis familiaris
1946:Tupaia chinensis
1760:Cysteine number
1743:
1727:glutathionylated
1631:ER translocation
1453:) also known as
1426:
1425:
1397:
1390:
1373:
1357:
1348:
1336:
1332:RefSeq (protein)
1322:
1306:
1297:
1285:
1261:
1242:
1216:
1197:
1171:
1152:
1121:
814:COP9 signalosome
708:cadherin binding
668:ribosome binding
631:
617:
608:
601:
586:
558:seminal vesicula
550:primitive streak
526:
524:Top expressed in
519:
508:caput epididymis
464:
462:Top expressed in
457:
436:
419:
409:
396:
385:
370:
363:
357:
346:
334:
318:
308:
295:
284:
269:
262:
256:
245:
231:
215:
209:
160:
153:
130:
61:
55:
34:
33:
21:
5708:
5707:
5703:
5702:
5701:
5699:
5698:
5697:
5658:
5657:
5656:
5647:
5574:
5549:E3 SUMO ligase
5513:
5502:
5494:
5185:
5177:
5150:
5112:
5091:
5083:
4861:
4849:protein folding
4847:
4838:
4833:
4802:
4763:
4758:
4712:
4711:
4707:
4672:Nature Medicine
4665:
4664:
4660:
4616:
4615:
4606:
4570:
4569:
4565:
4536:(12): 1309–11.
4530:Nature Genetics
4527:
4526:
4522:
4487:Nature Genetics
4484:
4483:
4479:
4443:
4442:
4438:
4407:(19): 3641–51.
4394:
4393:
4384:
4348:
4347:
4343:
4299:
4298:
4294:
4258:
4257:
4253:
4217:
4216:
4212:
4168:
4167:
4163:
4132:
4131:
4127:
4083:
4082:
4078:
4048:
4047:
4043:
3999:
3998:
3994:
3950:
3949:
3945:
3912:(14): 7541–57.
3899:
3898:
3891:
3845:
3844:
3837:
3783:
3782:
3778:
3745:(13): 8482–99.
3732:
3731:
3727:
3683:
3682:
3678:
3648:
3647:
3643:
3613:
3612:
3608:
3578:
3577:
3573:
3543:
3542:
3538:
3499:(6645): 891–5.
3486:
3485:
3481:
3445:
3444:
3440:
3396:
3395:
3391:
3337:
3336:
3332:
3288:
3287:
3283:
3239:
3238:
3234:
3196:
3195:
3191:
3160:(7): 1589–608.
3147:
3146:
3139:
3116:(38): 29421–5.
3103:
3102:
3098:
3073:
3052:
3051:
3047:
3018:(5149): 971–3.
3009:
3008:
3004:
2963:(22): 10345–9.
2950:
2949:
2945:
2901:
2900:
2896:
2865:(11): 2508–16.
2852:
2851:
2847:
2793:
2792:
2788:
2734:
2733:
2729:
2685:
2684:
2677:
2646:(10): 2250–60.
2640:Protein Science
2633:
2632:
2628:
2584:
2583:
2576:
2546:
2545:
2538:
2508:
2507:
2503:
2490:
2489:
2485:
2472:
2471:
2467:
2455:
2446:
2434:
2425:
2421:
2412:
2365:
2364:
2349:
2336:
2316:virulent strain
2314:. Meanwhile, a
2297:DNA replication
2282:
2272:homeostasis in
2258:type 2 diabetes
2246:
2226:
2176:atherosclerosis
2168:
2153:dendritic cells
2136:
2131:
1904:Naked mole rat
1889:Cavia porcellus
1714:
1694:
1670:
1654:
1633:
1604:
1569:
1541:
1521:
1505:oligomerization
1435:View/Edit Mouse
1430:View/Edit Human
1393:
1386:
1383:Location (UCSC)
1369:
1365:
1344:
1318:
1314:
1293:
1206:ENSG00000044574
1099:
920:toxin transport
853:
774:plasma membrane
727:
683:protein binding
678:ATPase activity
613:
582:
573:
568:
564:
560:
556:
552:
548:
544:
540:
536:
522:
511:
506:
502:
498:
494:
490:
486:
482:
478:
474:
460:
404:
391:
383:
373:
372:
371:
364:
344:
321:Gene location (
303:
290:
282:
272:
271:
270:
263:
241:
218:Gene location (
169:
156:
149:
70:
48:
17:
12:
11:
5:
5706:
5704:
5696:
5695:
5690:
5685:
5680:
5675:
5670:
5660:
5659:
5653:
5652:
5649:
5648:
5646:
5645:
5639:
5638:
5633:
5628:
5623:
5618:
5613:
5608:
5598:
5593:
5588:
5582:
5580:
5576:
5575:
5573:
5572:
5571:
5570:
5565:
5560:
5555:
5546:
5545:
5544:
5543:
5534:
5533:
5532:
5531:
5526:
5517:
5515:
5504:
5496:
5495:
5493:
5492:
5487:
5482:
5476:
5475:
5470:
5465:
5455:
5454:
5453:
5452:
5447:
5442:
5437:
5432:
5427:
5415:
5414:
5413:
5412:
5407:
5402:
5397:
5392:
5387:
5381:
5376:
5371:
5366:
5361:
5356:
5351:
5346:
5341:
5336:
5331:
5326:
5321:
5316:
5311:
5306:
5301:
5296:
5291:
5286:
5281:
5276:
5271:
5266:
5261:
5256:
5244:
5243:
5242:
5241:
5236:
5231:
5226:
5221:
5216:
5211:
5206:
5201:
5189:
5187:
5179:
5178:
5176:
5175:
5170:
5168:Signal peptide
5164:
5162:
5156:
5155:
5152:
5151:
5149:
5148:
5147:
5146:
5141:
5131:
5126:
5120:
5118:
5114:
5113:
5111:
5110:
5109:
5108:
5103:
5098:
5093:
5089:
5085:
5081:
5071:
5070:
5069:
5068:
5063:
5058:
5053:
5048:
5043:
5038:
5033:
5028:
5023:
5018:
5013:
5008:
4997:
4996:
4995:
4994:
4989:
4984:
4979:
4974:
4969:
4964:
4959:
4954:
4949:
4944:
4939:
4934:
4929:
4924:
4919:
4914:
4909:
4904:
4893:
4892:
4883:
4878:
4873:
4867:
4865:
4851:
4840:
4839:
4834:
4832:
4831:
4824:
4817:
4809:
4800:
4799:
4793:
4774:
4762:
4761:External links
4759:
4757:
4756:
4705:
4684:10.1038/nm1259
4658:
4629:(7): 1661–76.
4604:
4563:
4542:10.1038/ng1677
4520:
4499:10.1038/ng1620
4477:
4436:
4382:
4341:
4312:(6): H828–39.
4292:
4251:
4210:
4161:
4142:(4): 1164–71.
4125:
4096:(3): 292–300.
4076:
4041:
4006:Molecular Cell
3992:
3957:Molecular Cell
3943:
3889:
3835:
3776:
3725:
3676:
3641:
3606:
3571:
3536:
3479:
3458:(6): 694–705.
3438:
3389:
3330:
3301:(6): 1885–95.
3281:
3232:
3189:
3137:
3096:
3071:
3045:
3002:
2943:
2914:(5): 1456–62.
2894:
2845:
2786:
2727:
2675:
2626:
2574:
2536:
2501:
2483:
2465:
2444:
2422:
2420:
2417:
2414:
2413:
2352:
2350:
2343:
2335:
2332:
2281:
2278:
2250:heterozygosity
2245:
2242:
2225:
2222:
2167:
2164:
2135:
2132:
2130:
2127:
2124:
2123:
2119:
2118:
2115:
2112:
2109:
2104:
2100:
2099:
2096:
2093:
2090:
2085:
2082:
2078:
2077:
2074:
2071:
2068:
2063:
2059:
2058:
2055:
2052:
2049:
2044:
2040:
2039:
2036:
2033:
2030:
2025:
2022:
2018:
2017:
2014:
2011:
2008:
2003:
1999:
1998:
1995:
1992:
1989:
1984:
1980:
1979:
1976:
1973:
1970:
1965:
1962:
1958:
1957:
1954:
1951:
1948:
1943:
1939:
1938:
1935:
1932:
1929:
1924:
1920:
1919:
1916:
1913:
1910:
1905:
1901:
1900:
1897:
1894:
1891:
1886:
1882:
1881:
1878:
1875:
1872:
1867:
1863:
1862:
1859:
1856:
1853:
1848:
1845:
1841:
1840:
1837:
1834:
1831:
1826:
1822:
1821:
1818:
1815:
1812:
1807:
1803:
1802:
1799:
1796:
1793:
1791:Macaca fuscata
1788:
1784:
1783:
1780:
1777:
1774:
1769:
1766:
1762:
1761:
1758:
1755:
1752:
1749:
1746:
1731:disulfide bond
1713:
1710:
1693:
1690:
1669:
1666:
1653:
1650:
1632:
1629:
1603:
1600:
1568:
1565:
1540:
1537:
1520:
1517:
1442:
1441:
1438:
1437:
1432:
1422:
1421:
1415:
1414:
1411:
1410:
1408:
1406:
1399:
1398:
1391:
1384:
1380:
1379:
1376:
1375:
1361:
1360:
1354:
1351:
1350:
1340:
1339:
1333:
1329:
1328:
1325:
1324:
1310:
1309:
1303:
1300:
1299:
1289:
1288:
1282:
1278:
1277:
1274:
1273:
1265:
1264:
1258:
1255:
1254:
1246:
1245:
1239:
1233:
1232:
1229:
1228:
1220:
1219:
1213:
1210:
1209:
1201:
1200:
1194:
1188:
1187:
1184:
1183:
1175:
1174:
1168:
1165:
1164:
1156:
1155:
1149:
1143:
1142:
1137:
1132:
1128:
1127:
1117:
1116:
1113:
1112:
1101:
1100:
1098:
1097:
1092:
1087:
1082:
1077:
1072:
1067:
1062:
1057:
1052:
1047:
1042:
1037:
1032:
1027:
1022:
1017:
1012:
1007:
1002:
997:
992:
987:
982:
977:
972:
967:
962:
957:
952:
947:
942:
937:
932:
927:
922:
917:
912:
907:
902:
897:
892:
887:
882:
877:
872:
867:
861:
859:
855:
854:
852:
851:
846:
841:
836:
831:
826:
821:
816:
811:
806:
801:
796:
791:
786:
781:
776:
771:
766:
761:
759:focal adhesion
756:
751:
746:
741:
735:
733:
729:
728:
726:
725:
720:
715:
710:
705:
700:
695:
690:
688:enzyme binding
685:
680:
675:
670:
665:
660:
655:
650:
644:
642:
638:
637:
627:
626:
623:
622:
619:
618:
610:
609:
598:
592:
591:
588:
587:
579:
578:
575:
574:
572:
571:
570:lacrimal gland
567:
563:
559:
555:
551:
547:
543:
539:
535:
531:
528:
527:
516:
513:
512:
510:
509:
505:
501:
497:
493:
489:
485:
481:
480:olfactory bulb
477:
473:
469:
466:
465:
453:
452:
444:
433:
427:
426:
423:RNA expression
415:
414:
411:
410:
402:
398:
397:
389:
386:
381:
375:
374:
365:
358:
352:
348:
347:
342:
336:
335:
327:
326:
314:
313:
310:
309:
301:
297:
296:
288:
285:
280:
274:
273:
264:
257:
251:
247:
246:
239:
233:
232:
224:
223:
211:
210:
167:
163:
162:
154:
146:
145:
141:
140:
137:
136:
133:
132:
66:
65:
57:
56:
45:
39:
38:
30:
29:
26:
25:
15:
13:
10:
9:
6:
4:
3:
2:
5705:
5694:
5691:
5689:
5686:
5684:
5681:
5679:
5676:
5674:
5671:
5669:
5666:
5665:
5663:
5644:
5641:
5640:
5637:
5634:
5632:
5629:
5627:
5624:
5622:
5619:
5617:
5614:
5612:
5609:
5606:
5602:
5599:
5597:
5594:
5592:
5589:
5587:
5584:
5583:
5581:
5577:
5569:
5566:
5564:
5561:
5559:
5556:
5554:
5551:
5550:
5548:
5547:
5542:
5539:
5538:
5536:
5535:
5530:
5527:
5525:
5522:
5521:
5519:
5518:
5516:
5514:(SUMOylation)
5512:
5508:
5505:
5501:
5497:
5491:
5488:
5486:
5483:
5481:
5478:
5477:
5474:
5471:
5469:
5466:
5464:
5460:
5457:
5456:
5451:
5448:
5446:
5443:
5441:
5438:
5436:
5433:
5431:
5428:
5426:
5423:
5422:
5421:
5417:
5416:
5411:
5408:
5406:
5403:
5401:
5398:
5396:
5393:
5391:
5388:
5385:
5382:
5380:
5377:
5375:
5372:
5370:
5367:
5365:
5362:
5360:
5357:
5355:
5352:
5350:
5347:
5345:
5342:
5340:
5337:
5335:
5332:
5330:
5327:
5325:
5322:
5320:
5317:
5315:
5312:
5310:
5307:
5305:
5302:
5300:
5297:
5295:
5292:
5290:
5287:
5285:
5282:
5280:
5277:
5275:
5272:
5270:
5267:
5265:
5262:
5260:
5257:
5255:
5252:
5251:
5250:
5246:
5245:
5240:
5237:
5235:
5232:
5230:
5227:
5225:
5222:
5220:
5217:
5215:
5212:
5210:
5207:
5205:
5202:
5200:
5197:
5196:
5195:
5191:
5190:
5188:
5184:
5180:
5174:
5171:
5169:
5166:
5165:
5163:
5161:
5157:
5145:
5142:
5140:
5137:
5136:
5135:
5132:
5130:
5127:
5125:
5122:
5121:
5119:
5115:
5107:
5104:
5102:
5099:
5097:
5094:
5092:
5086:
5084:
5078:
5077:
5076:
5073:
5072:
5067:
5064:
5062:
5059:
5057:
5054:
5052:
5049:
5047:
5044:
5042:
5039:
5037:
5034:
5032:
5029:
5027:
5024:
5022:
5019:
5017:
5014:
5012:
5009:
5007:
5004:
5003:
5002:
4999:
4998:
4993:
4990:
4988:
4985:
4983:
4980:
4978:
4975:
4973:
4970:
4968:
4965:
4963:
4960:
4958:
4955:
4953:
4950:
4948:
4945:
4943:
4940:
4938:
4935:
4933:
4930:
4928:
4925:
4923:
4920:
4918:
4915:
4913:
4910:
4908:
4905:
4903:
4900:
4899:
4898:
4895:
4894:
4891:
4887:
4884:
4882:
4879:
4877:
4874:
4872:
4869:
4868:
4866:
4864:
4859:
4855:
4852:
4850:
4845:
4841:
4837:
4830:
4825:
4823:
4818:
4816:
4811:
4810:
4807:
4803:
4797:
4794:
4791:
4787:
4786:
4781:
4780:
4775:
4772:
4768:
4765:
4764:
4760:
4752:
4748:
4743:
4738:
4733:
4728:
4724:
4720:
4716:
4709:
4706:
4701:
4697:
4693:
4689:
4685:
4681:
4678:(7): 757–64.
4677:
4673:
4669:
4662:
4659:
4654:
4650:
4645:
4640:
4636:
4632:
4628:
4624:
4620:
4613:
4611:
4609:
4605:
4600:
4596:
4591:
4586:
4583:(2): 364–75.
4582:
4578:
4574:
4567:
4564:
4559:
4555:
4551:
4547:
4543:
4539:
4535:
4531:
4524:
4521:
4516:
4512:
4508:
4504:
4500:
4496:
4492:
4488:
4481:
4478:
4473:
4469:
4464:
4459:
4456:(4): 600–10.
4455:
4451:
4447:
4440:
4437:
4432:
4428:
4423:
4418:
4414:
4410:
4406:
4402:
4398:
4391:
4389:
4387:
4383:
4378:
4374:
4369:
4364:
4361:(6): 705–12.
4360:
4356:
4352:
4345:
4342:
4337:
4333:
4328:
4323:
4319:
4315:
4311:
4307:
4303:
4296:
4293:
4288:
4284:
4279:
4274:
4271:(3): 854–63.
4270:
4266:
4262:
4255:
4252:
4247:
4243:
4238:
4233:
4230:(3): 1492–8.
4229:
4225:
4221:
4214:
4211:
4206:
4202:
4197:
4192:
4188:
4184:
4181:(2): 218–26.
4180:
4176:
4172:
4165:
4162:
4157:
4153:
4149:
4145:
4141:
4137:
4129:
4126:
4121:
4117:
4112:
4107:
4103:
4099:
4095:
4091:
4087:
4080:
4077:
4072:
4068:
4064:
4060:
4056:
4052:
4045:
4042:
4037:
4033:
4028:
4023:
4019:
4015:
4012:(5): 747–59.
4011:
4007:
4003:
3996:
3993:
3988:
3984:
3979:
3974:
3970:
3966:
3963:(5): 747–59.
3962:
3958:
3954:
3947:
3944:
3939:
3935:
3930:
3925:
3920:
3915:
3911:
3907:
3903:
3896:
3894:
3890:
3885:
3881:
3876:
3871:
3866:
3861:
3857:
3853:
3849:
3842:
3840:
3836:
3831:
3827:
3822:
3817:
3812:
3807:
3803:
3799:
3795:
3791:
3787:
3780:
3777:
3772:
3768:
3763:
3758:
3753:
3748:
3744:
3740:
3736:
3729:
3726:
3721:
3717:
3713:
3709:
3704:
3699:
3696:(7): 881–91.
3695:
3691:
3687:
3680:
3677:
3672:
3668:
3664:
3660:
3656:
3652:
3645:
3642:
3637:
3633:
3629:
3625:
3622:(2): 445–50.
3621:
3617:
3610:
3607:
3602:
3598:
3594:
3590:
3586:
3582:
3575:
3572:
3567:
3563:
3559:
3555:
3551:
3547:
3540:
3537:
3532:
3528:
3524:
3520:
3515:
3514:10.1038/42276
3510:
3506:
3502:
3498:
3494:
3490:
3483:
3480:
3475:
3471:
3466:
3461:
3457:
3453:
3449:
3442:
3439:
3434:
3430:
3425:
3420:
3416:
3412:
3408:
3404:
3400:
3393:
3390:
3385:
3381:
3376:
3371:
3366:
3361:
3357:
3353:
3350:(4): 1565–9.
3349:
3345:
3341:
3334:
3331:
3326:
3322:
3317:
3312:
3308:
3304:
3300:
3296:
3292:
3285:
3282:
3277:
3273:
3268:
3263:
3259:
3255:
3251:
3247:
3243:
3236:
3233:
3228:
3224:
3220:
3216:
3212:
3208:
3204:
3200:
3193:
3190:
3185:
3181:
3176:
3171:
3167:
3163:
3159:
3155:
3151:
3144:
3142:
3138:
3133:
3129:
3124:
3119:
3115:
3111:
3107:
3100:
3097:
3092:
3088:
3083:
3078:
3074:
3068:
3064:
3060:
3056:
3049:
3046:
3041:
3037:
3033:
3029:
3025:
3021:
3017:
3013:
3006:
3003:
2998:
2994:
2989:
2984:
2979:
2974:
2970:
2966:
2962:
2958:
2954:
2947:
2944:
2939:
2935:
2930:
2925:
2921:
2917:
2913:
2909:
2905:
2898:
2895:
2890:
2886:
2881:
2876:
2872:
2868:
2864:
2860:
2856:
2849:
2846:
2841:
2837:
2832:
2827:
2822:
2817:
2813:
2809:
2805:
2801:
2797:
2790:
2787:
2782:
2778:
2773:
2768:
2763:
2758:
2754:
2750:
2746:
2742:
2738:
2731:
2728:
2723:
2719:
2714:
2709:
2705:
2701:
2698:(6): 670–84.
2697:
2693:
2689:
2682:
2680:
2676:
2671:
2667:
2662:
2657:
2653:
2649:
2645:
2641:
2637:
2630:
2627:
2622:
2618:
2613:
2608:
2604:
2600:
2596:
2592:
2588:
2581:
2579:
2575:
2570:
2566:
2562:
2558:
2554:
2550:
2543:
2541:
2537:
2532:
2528:
2524:
2520:
2517:(4): 275–86.
2516:
2512:
2505:
2502:
2497:
2493:
2487:
2484:
2479:
2475:
2469:
2466:
2462:
2458:
2453:
2451:
2449:
2445:
2441:
2437:
2432:
2430:
2428:
2424:
2418:
2409:
2405:
2400:
2395:
2391:
2387:
2384:(30): 14–23.
2383:
2379:
2378:
2373:
2371:
2362:
2361:
2356:
2351:
2347:
2342:
2341:
2338:
2333:
2331:
2329:
2325:
2321:
2317:
2313:
2309:
2305:
2302:
2298:
2294:
2290:
2286:
2279:
2277:
2275:
2271:
2267:
2263:
2259:
2255:
2251:
2243:
2241:
2239:
2235:
2231:
2230:neuronal cell
2223:
2221:
2219:
2215:
2211:
2206:
2204:
2200:
2196:
2192:
2188:
2185:
2181:
2177:
2173:
2165:
2163:
2161:
2156:
2154:
2150:
2146:
2142:
2133:
2128:
2120:
2116:
2113:
2110:
2108:
2105:
2102:
2101:
2097:
2094:
2091:
2089:
2086:
2083:
2079:
2075:
2072:
2069:
2067:
2064:
2061:
2060:
2056:
2053:
2050:
2048:
2045:
2042:
2041:
2037:
2034:
2031:
2029:
2026:
2023:
2019:
2015:
2012:
2009:
2007:
2004:
2001:
2000:
1996:
1993:
1990:
1988:
1985:
1982:
1981:
1977:
1974:
1971:
1969:
1966:
1963:
1959:
1955:
1952:
1949:
1947:
1944:
1941:
1940:
1936:
1933:
1930:
1928:
1925:
1922:
1921:
1917:
1914:
1911:
1909:
1906:
1903:
1902:
1898:
1895:
1892:
1890:
1887:
1884:
1883:
1879:
1876:
1873:
1871:
1868:
1865:
1864:
1860:
1857:
1854:
1852:
1849:
1846:
1842:
1838:
1835:
1832:
1830:
1827:
1824:
1823:
1819:
1816:
1813:
1811:
1808:
1805:
1804:
1800:
1797:
1794:
1792:
1789:
1786:
1785:
1781:
1778:
1775:
1773:
1770:
1767:
1763:
1759:
1756:
1753:
1750:
1747:
1745:
1744:
1738:
1736:
1732:
1728:
1724:
1720:
1711:
1709:
1707:
1703:
1699:
1698:co-chaperones
1691:
1689:
1687:
1683:
1679:
1675:
1667:
1665:
1663:
1662:glycosylation
1659:
1651:
1649:
1647:
1643:
1639:
1630:
1628:
1626:
1621:
1617:
1614:(acting as a
1613:
1609:
1601:
1599:
1597:
1593:
1589:
1588:translocation
1585:
1580:
1578:
1574:
1566:
1564:
1562:
1558:
1553:
1549:
1546:
1538:
1536:
1532:
1530:
1526:
1518:
1516:
1514:
1510:
1509:translocation
1506:
1502:
1498:
1494:
1490:
1486:
1481:
1479:
1476:
1472:
1468:
1464:
1460:
1456:
1452:
1448:
1436:
1431:
1427:
1423:
1420:
1416:
1409:
1407:
1404:
1400:
1396:
1392:
1389:
1385:
1381:
1374:
1372:
1368:
1362:
1358:
1355:
1349:
1347:
1341:
1337:
1334:
1330:
1323:
1321:
1317:
1311:
1307:
1304:
1298:
1296:
1290:
1286:
1283:
1281:RefSeq (mRNA)
1279:
1272:
1271:
1266:
1262:
1259:
1253:
1252:
1247:
1243:
1240:
1238:
1234:
1227:
1226:
1221:
1217:
1214:
1208:
1207:
1202:
1198:
1195:
1193:
1189:
1182:
1181:
1176:
1172:
1169:
1163:
1162:
1157:
1153:
1150:
1148:
1144:
1141:
1138:
1136:
1133:
1129:
1126:
1122:
1118:
1111:
1107:
1102:
1096:
1093:
1091:
1088:
1086:
1083:
1081:
1078:
1076:
1073:
1071:
1068:
1066:
1063:
1061:
1058:
1056:
1053:
1051:
1048:
1046:
1043:
1041:
1038:
1036:
1033:
1031:
1028:
1026:
1023:
1021:
1018:
1016:
1013:
1011:
1008:
1006:
1003:
1001:
998:
996:
993:
991:
988:
986:
983:
981:
978:
976:
973:
971:
968:
966:
963:
961:
958:
956:
953:
951:
948:
946:
943:
941:
938:
936:
933:
931:
928:
926:
923:
921:
918:
916:
913:
911:
908:
906:
903:
901:
898:
896:
893:
891:
888:
886:
883:
881:
878:
876:
873:
871:
868:
866:
863:
862:
860:
857:
856:
850:
847:
845:
842:
840:
837:
835:
832:
830:
827:
825:
822:
820:
817:
815:
812:
810:
809:mitochondrion
807:
805:
802:
800:
797:
795:
792:
790:
787:
785:
782:
780:
777:
775:
772:
770:
769:myelin sheath
767:
765:
762:
760:
757:
755:
752:
750:
747:
745:
742:
740:
737:
736:
734:
731:
730:
724:
721:
719:
716:
714:
711:
709:
706:
704:
701:
699:
696:
694:
691:
689:
686:
684:
681:
679:
676:
674:
671:
669:
666:
664:
661:
659:
656:
654:
651:
649:
646:
645:
643:
640:
639:
636:
635:Gene ontology
632:
628:
616:
611:
607:
602:
599:
597:
593:
585:
580:
569:
565:
561:
557:
553:
549:
545:
541:
537:
533:
532:
529:
525:
520:
517:
507:
503:
499:
495:
491:
487:
483:
479:
475:
471:
470:
467:
463:
458:
455:
454:
451:
449:
445:
443:
442:
438:
437:
434:
432:
428:
424:
420:
416:
408:
403:
399:
395:
390:
380:
376:
369:
362:
356:
349:
341:
337:
333:
328:
324:
319:
315:
307:
302:
298:
294:
289:
279:
275:
268:
261:
255:
248:
244:
238:
234:
230:
225:
221:
216:
212:
208:
204:
200:
196:
192:
188:
184:
180:
176:
172:
164:
159:
152:
147:
142:
131:
129:
125:
121:
117:
113:
109:
105:
101:
97:
93:
89:
85:
81:
77:
73:
67:
62:
59:
58:
54:
51:
44:
40:
35:
31:
27:
22:
19:
5511:SUMO protein
5035:
4801:
4784:
4778:
4722:
4718:
4708:
4675:
4671:
4661:
4626:
4622:
4580:
4576:
4566:
4533:
4529:
4523:
4493:(9): 974–9.
4490:
4486:
4480:
4453:
4449:
4439:
4404:
4401:FEBS Letters
4400:
4358:
4354:
4344:
4309:
4305:
4295:
4268:
4264:
4254:
4227:
4223:
4213:
4178:
4174:
4164:
4139:
4135:
4134:arthritis".
4128:
4093:
4089:
4079:
4057:(4): 531–4.
4054:
4050:
4044:
4009:
4005:
3995:
3960:
3956:
3946:
3909:
3905:
3855:
3851:
3793:
3789:
3779:
3742:
3738:
3728:
3693:
3689:
3679:
3654:
3650:
3644:
3619:
3615:
3609:
3584:
3580:
3574:
3552:(5): 551–5.
3549:
3545:
3539:
3496:
3492:
3482:
3455:
3451:
3441:
3406:
3402:
3392:
3347:
3343:
3333:
3298:
3294:
3284:
3249:
3245:
3235:
3202:
3198:
3192:
3157:
3153:
3113:
3109:
3099:
3054:
3048:
3015:
3011:
3005:
2960:
2956:
2946:
2911:
2907:
2897:
2862:
2858:
2848:
2803:
2799:
2789:
2747:(1): e8625.
2744:
2740:
2730:
2695:
2691:
2643:
2639:
2629:
2594:
2590:
2555:(2): 281–4.
2552:
2548:
2514:
2510:
2504:
2495:
2486:
2477:
2468:
2381:
2375:
2369:
2359:
2358:
2337:
2283:
2266:adipogenesis
2262:pancreatitis
2247:
2227:
2207:
2199:procoagulant
2195:triglyceride
2180:homocysteine
2169:
2157:
2149:T-lymphocyte
2141:inflammation
2137:
2106:
2087:
2065:
2046:
2027:
2005:
1986:
1983:Minke whale
1967:
1945:
1926:
1907:
1888:
1869:
1851:Mus musculus
1850:
1828:
1809:
1790:
1772:Homo sapiens
1771:
1723:sulfenylated
1715:
1695:
1692:Interactions
1671:
1655:
1634:
1605:
1581:
1570:
1550:cycle: when
1542:
1533:
1529:polypeptides
1522:
1497:translocated
1482:
1474:
1466:
1462:
1458:
1454:
1450:
1446:
1445:
1367:NP_001156906
1364:
1343:
1316:NM_001163434
1313:
1292:
1268:
1249:
1223:
1204:
1178:
1159:
1139:
1134:
789:cell surface
562:vas deferens
446:
439:
304:125,241,382
291:125,234,853
166:External IDs
69:
18:
5605:neddylation
4871:Hsp10/GroES
4863:Chaperonins
4355:Circulation
3252:(1): 41–9.
2312:antibiotics
2285:Prokaryotic
2191:cholesterol
2081:Marsupials
2021:Carnivores
1942:Tree shrew
1885:Guinea pig
1814:Predicted*
1668:UPR pathway
1648:of the ER.
1644:) into the
1612:aggregating
1584:aggregation
1557:aggregation
693:ATP binding
484:pericardium
405:34,667,559
392:34,661,982
144:Identifiers
5662:Categories
4897:Hsp40/DnaJ
4844:Chaperones
4175:Immunology
3858:: e03496.
3657:: 251–77.
3587:: 459–85.
2463:, May 2017
2442:, May 2017
2419:References
2212:, such as
2111:Predicted
2092:Predicted
2070:Predicted
2032:Predicted
2010:Predicted
2006:Sus scrofa
1968:Bos taurus
1961:Ungulates
1931:Predicted
1893:Predicted
1706:J proteins
1545:allosteric
1513:proteasome
1487:molecular
1060:luteolysis
764:melanosome
450:(ortholog)
187:HomoloGene
5183:Ubiquitin
5129:Clusterin
3796:(1): 19.
2591:Structure
2324:AB5 toxin
2289:orthologs
2276:tissues.
2145:monocytes
1825:Marmoset
1765:Primates
1638:invertase
1539:Mechanism
1519:Structure
1489:chaperone
1483:BiP is a
1371:NP_071705
1346:NP_005338
1320:NM_022310
1295:NM_005347
1125:Orthologs
739:cytoplasm
476:beta cell
472:vena cava
195:GeneCards
5463:Ataxin 3
4751:23356742
4692:15980866
4653:25546329
4599:18049481
4558:33094308
4550:16282978
4515:27489955
4507:16116427
4472:18508854
4431:17481612
4377:15289376
4336:23316062
4287:16508967
4246:11160188
4205:19740378
4156:15077298
4120:21671907
4071:15245751
4036:23123197
3987:23123197
3938:26865632
3884:25053742
3830:18215318
3771:25601083
3712:11779464
3671:23057742
3636:11118306
3566:15944407
3474:20219571
3227:25858120
3219:22510960
3184:25698114
3132:10893409
3091:22576356
2938:19103929
2889:25148104
2840:26038563
2781:20072699
2741:PLOS ONE
2722:15770419
2621:26655470
2549:Genomics
2459:–
2438:–
2408:28286085
2301:superbug
2234:ischemic
2218:neonatal
2184:vascular
2084:Opossum
1844:Rodents
1787:Macaque
1642:a-factor
1567:Function
1419:Wikidata
1104:Sources:
754:membrane
5386:(CDC34)
4796:PDBe-KB
4742:3605262
4700:2785104
4644:4402027
4422:2040386
4327:3602775
4196:2767311
4111:3170978
4027:3582359
3978:3582359
3929:4817183
3875:4132286
3821:2266713
3798:Bibcode
3762:4375499
3720:9460062
3601:9891790
3531:4431731
3523:9278052
3501:Bibcode
3433:8253836
3424:2290880
3384:1996357
3352:Bibcode
3325:2190988
3316:2116122
3276:7790376
3267:2120506
3175:4356644
3082:3623542
3040:8310296
3020:Bibcode
3012:Science
2997:7937953
2965:Bibcode
2929:2648196
2880:4241170
2831:4460500
2808:Bibcode
2772:2803158
2749:Bibcode
2713:2773841
2670:9336848
2661:2143562
2612:4680848
2569:8020977
2531:2840249
2461:Ensembl
2440:Ensembl
2399:5632570
2328:viruses
2304:strains
2274:adipose
2270:glucose
2254:obesity
2062:Ferret
1923:Rabbit
1806:Vervet
1700:, both
1616:holdase
1608:foldase
1525:domains
1501:folding
1471:protein
1469:) is a
1237:UniProt
1192:Ensembl
1131:Species
1110:QuickGO
839:cytosol
824:nucleus
799:midbody
504:trachea
496:pylorus
425:pattern
151:Aliases
5430:Cullin
4776:Human
4773:(MeSH)
4749:
4739:
4725:: 36.
4698:
4690:
4651:
4641:
4597:
4556:
4548:
4513:
4505:
4470:
4429:
4419:
4375:
4334:
4324:
4285:
4244:
4203:
4193:
4154:
4118:
4108:
4069:
4034:
4024:
3985:
3975:
3936:
3926:
3882:
3872:
3828:
3818:
3769:
3759:
3718:
3710:
3669:
3634:
3599:
3564:
3529:
3521:
3493:Nature
3472:
3431:
3421:
3382:
3372:
3323:
3313:
3274:
3264:
3225:
3217:
3182:
3172:
3130:
3089:
3079:
3069:
3038:
2995:
2985:
2936:
2926:
2887:
2877:
2838:
2828:
2779:
2769:
2720:
2710:
2668:
2658:
2619:
2609:
2567:
2529:
2406:
2396:
2260:, and
1847:Mouse
1768:Human
1684:, and
1548:ATPase
1459:GRP-78
1405:search
1403:PubMed
1270:P20029
1251:P11021
1147:Entrez
596:BioGPS
283:9q33.3
175:138120
5621:ATG12
5611:FAT10
5601:NEDD8
5586:ISG15
5579:Other
5568:PIAS4
5563:PIAS3
5558:PIAS2
5553:PIAS1
5503:(UBL)
5485:BIRC6
5445:FANCL
5117:Other
5106:TRAP1
5075:Hsp90
5001:Hsp70
4890:GroEL
4886:HSP60
4881:Hsp47
4876:Hsp27
4785:HSPA5
4779:HSPA5
4696:S2CID
4554:S2CID
4511:S2CID
3852:eLife
3716:S2CID
3527:S2CID
3375:51060
3223:S2CID
2988:45016
2370:HSPA5
2360:Gene
2334:Notes
2208:Some
1646:lumen
1577:HSP70
1485:HSP70
1475:HSPA5
1467:HSPA5
1461:) or
1180:14828
1140:Mouse
1135:Human
1106:Amigo
448:Mouse
441:Human
388:Start
323:Mouse
287:Start
220:Human
199:HSPA5
183:95835
158:HSPA5
24:HSPA5
5636:UBL5
5626:FUB1
5616:ATG8
5596:UFM1
5591:URM1
5541:UBC9
5529:SAE2
5524:SAE1
5490:UFC1
5480:ATG3
5473:CYLD
5468:USP6
5450:UBR1
5440:MDM2
5239:SAE1
5234:NAE1
5229:ATG7
5224:UBA7
5219:UBA6
5214:UBA5
5209:UBA3
5204:UBA2
5199:UBA1
5144:SMN2
5139:SMN1
4747:PMID
4688:PMID
4649:PMID
4595:PMID
4546:PMID
4503:PMID
4468:PMID
4427:PMID
4373:PMID
4332:PMID
4283:PMID
4242:PMID
4201:PMID
4152:PMID
4116:PMID
4067:PMID
4032:PMID
3983:PMID
3934:PMID
3880:PMID
3826:PMID
3767:PMID
3708:PMID
3690:Cell
3667:PMID
3632:PMID
3597:PMID
3562:PMID
3519:PMID
3470:PMID
3456:1803
3429:PMID
3380:PMID
3321:PMID
3272:PMID
3215:PMID
3180:PMID
3128:PMID
3087:PMID
3067:ISBN
3036:PMID
2993:PMID
2934:PMID
2885:PMID
2836:PMID
2777:PMID
2718:PMID
2666:PMID
2617:PMID
2565:PMID
2527:PMID
2404:PMID
2377:Gene
2293:RecA
2287:BiP
2268:and
2248:BiP
2114:Yes
2095:Yes
2073:Yes
2054:Yes
2051:Yes
2043:Cat
2035:Yes
2024:Dog
2013:Yes
2002:Pig
1994:Yes
1991:Yes
1975:Yes
1972:Yes
1964:Cow
1953:Yes
1950:Yes
1934:Yes
1915:Yes
1912:Yes
1896:Yes
1877:Yes
1874:Yes
1866:Rat
1858:Yes
1855:Yes
1836:Yes
1833:Yes
1817:Yes
1798:Yes
1795:Yes
1779:Yes
1776:Yes
1735:GPx7
1725:and
1686:ATF6
1682:PERK
1678:IRE1
1658:ERAD
1503:and
1478:gene
1451:BiPS
1161:3309
431:Bgee
379:Band
340:Chr.
278:Band
237:Chr.
191:3908
171:OMIM
128:5EXW
124:5EY4
120:5F0X
116:5F2R
112:5EVZ
108:5EX5
104:5F1X
100:5E85
96:5E86
92:5E84
88:3LDP
84:3LDO
80:3LDN
76:3LDL
72:3IUC
53:RCSB
50:PDBe
5631:MUB
5435:CBL
5425:VHL
5418:E3
5247:E2
5192:E1
5061:12A
4992:C19
4987:C14
4982:C13
4977:C11
4972:C10
4927:B11
4737:PMC
4727:doi
4680:doi
4639:PMC
4631:doi
4627:230
4585:doi
4538:doi
4495:doi
4458:doi
4417:PMC
4409:doi
4405:581
4363:doi
4359:110
4322:PMC
4314:doi
4310:304
4273:doi
4232:doi
4228:166
4191:PMC
4183:doi
4179:128
4144:doi
4106:PMC
4098:doi
4094:165
4059:doi
4022:PMC
4014:doi
3973:PMC
3965:doi
3924:PMC
3914:doi
3910:291
3870:PMC
3860:doi
3816:PMC
3806:doi
3757:PMC
3747:doi
3743:290
3698:doi
3694:107
3659:doi
3624:doi
3620:279
3589:doi
3554:doi
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