316:
293:
1294:. It is highly flexible and polar because of its negative charges. Probably it functions as a mediator of solubility for hydrophobic sHsps and it stabilizes the protein and protein/substrate complexes. This was shown by elimination of the C-terminal tail in Hsp27Δ182-205 and in Hsp25Δ18. In the case of Hsp27, the IxI/V motif corresponds to 181-Ile-Pro-Val-183, and this region of the protein plays a critical role, as the mutation of the central Pro residue causes the hereditary motor neuropathy
190:
215:
322:
221:
31:
1332:, dimerization by α-crystallin domains proceeds through the formation of a long β-strand at the interface. The amino acid sequences in this region, however, are predicted to be disordered Indeed, the α-crystallin domain of Hsp27 partially unfolds in its monomeric state and is less stable than the dimer.
3588:
Irobi J, Van Impe K, Seeman P, Jordanova A, Dierick I, Verpoorten N, Michalik A, De
Vriendt E, Jacobs A, Van Gerwen V, Vennekens K, Mazanec R, Tournev I, Hilton-Jones D, Talbot K, Kremensky I, Van Den Bosch L, Robberecht W, Van Vandekerckhove J, Van Broeckhoven C, Gettemans J, De Jonghe P, Timmerman
2251:
Evgrafov OV, Mersiyanova I, Irobi J, Van Den Bosch L, Dierick I, Leung CL, Schagina O, Verpoorten N, Van Impe K, Fedotov V, Dadali E, Auer-Grumbach M, Windpassinger C, Wagner K, Mitrovic Z, Hilton-Jones D, Talbot K, Martin JJ, Vasserman N, Tverskaya S, Polyakov A, Liem RK, Gettemans J, Robberecht W,
1635:
Protein kinase C-mediated HSPB1 phosphorylation protects against ferroptosis, an iron-dependent form of non-apoptotic cell death, by reducing iron-mediated production of lipid reactive oxygen species. These novel data support the development of Hsp-targeting strategies and, specifically, anti-HSP27
1601:
mutations throughout the amino acid sequence of Hsp27, and most disease-causing mutations present with adult-onset symptoms. One of the more severe Hsp27 mutants is the Pro182Leu mutant, which manifests symptomatically in the first few years of life and was additionally demonstrated in a transgenic
1289:
consists of a less conserved region, the so-called WD/EPF domain, followed by a short variable sequence with a rather conservative site near the end of this domain. The C-terminal region of sHsps consists of the above mentioned α-crystallin domain, followed by a variable sequence with high motility
1626:
Notably, phosphorylated Hsp27 increases human prostate cancer (PCa) cell invasion, enhances cell proliferation, and suppresses Fas-induced apoptosis in human PCa cells. Unphosphorylated Hsp27 has been shown to act as an actin capping protein, preventing actin reorganization and, consequently, cell
57:
3183:
d'Ydewalle C, Krishnan J, Chiheb DM, Van Damme P, Irobi J, Kozikowski AP, Vanden Berghe P, Timmerman V, Robberecht W, Van Den Bosch L (July 2011). "HDAC6 inhibitors reverse axonal loss in a mouse model of mutant HSPB1-induced
Charcot-Marie-Tooth disease".
2215:
Lindner RA, Carver JA, Ehrnsperger M, Buchner J, Esposito G, Behlke J, Lutsch G, Kotlyarov A, Gaestel M (April 2000). "Mouse Hsp25, a small shock protein. The role of its C-terminal extension in oligomerization and chaperone action".
1513:
and intermediate filaments. It prevents the formation of non-covalent filament/filament interactions of the intermediate filaments and protects actin filaments from fragmentation. It also preserves the focal contacts fixed at the
2942:
Qi Z, Shen L, Zhou H, Jiang Y, Lan L, Luo L, Yin Z (July 2014). "Phosphorylation of heat shock protein 27 antagonizes TNF-α induced HeLa cell apoptosis via regulating TAK1 ubiquitination and activation of p38 and ERK signaling".
1290:
and flexibility. Despite relatively low levels of global sequence conservation in the C-terminal region, many sHsps contain a locally conserved Ile-Xxx-Ile/Val (IxI/V) motif that plays a role in regulating the assembly of
1397:
In all probability, the oligomerization status is connected with the chaperone activity: aggregates of large oligomers have high chaperone activity, whereas dimers and monomers have relatively higher chaperone activity.
1505:
apoptotic protein and prevents the association of Daxx with Fas and Ask1. Moreover, Hsp27 phosphorylation leads to the activation of TAK1 and TAK1-p38/ERK pro-survival signaling, thus opposing TNF-α-induced apoptosis.
2724:
Gawlowski T, Stratmann B, Stork I, Engelbrecht B, Brodehl A, Niehaus K, Körfer R, Tschoepe D, Milting H (August 2009). "Heat shock protein 27 modification is increased in the human diabetic failing heart".
1378:, leads to the activation of MAPKAP kinases 2 and 3 which directly phosphorylate mammalian sHsps. The phosphorylation plays an important role for the formation of oligomers in exponentially growing cells
3227:
Gerasimovich ES, Strelkov SV, Gusev NB (November 2017). "Some properties of three αB-crystallin mutants carrying point substitutions in the C-terminal domain and associated with congenital diseases".
1572:
etc. The upregulation of Hsp27 correlates with the rate of phosphorylation and with an increase of large oligomers. It is possible that Hsp27 plays a crucial role in the termination of growth.
3710:
2681:
Bruey JM, Paul C, Fromentin A, Hilpert S, Arrigo AP, Solary E, Garrido C (October 2000). "Differential regulation of HSP27 oligomerization in tumor cells grown in vitro and in vivo".
3963:
3498:
Sinsimer KS, Gratacós FM, Knapinska AM, Lu J, Krause CD, Wierzbowski AV, Maher LR, Scrudato S, Rivera YM, Gupta S, Turrin DK, De La Cruz MP, Pestka S, Brewer G (September 2008).
1533:
pathway, that controls a lot of processes, such as cell growth and inflammatory and stress responses. The cytoprotective properties of Hsp27 result from its ability to modulate
329:
228:
2816:
Vargas-Roig LM, Fanelli MA, López LA, Gago FE, Tello O, Aznar JC, Ciocca DR (1997). "Heat shock proteins and cell proliferation in human breast cancer biopsy samples".
1269:
sHsps have some structural features in common: Very characteristic is a homologous and highly conserved amino acid sequence, the so-called α-crystallin domain near the
1426:. It is overexpressed during different stages of cell differentiation and development. This suggests an essential role for Hsp27 in the differentiation of tissues.
2095:
Gusev NB, Bogatcheva NV, Marston SB (May 2002). "Structure and properties of small heat shock proteins (sHsp) and their interaction with cytoskeleton proteins".
3703:
2599:"Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha by phosphorylation"
2843:
Rui Z, Jian-Guo J, Yuan-Peng T, Hai P, Bing-Gen R (April 2003). "Use of serological proteomic methods to find biomarkers associated with breast cancer".
941:
3027:
Arrigo AP (February 2005). "In search of the molecular mechanism by which small stress proteins counteract apoptosis during cellular differentiation".
1394:
is dependent on cell-cell contact, but not on the phosphorylation status. Furthermore, it was shown that HSP27 contains an
Argpyrimidine modification.
922:
151:
1951:
Van
Montfort R, Slingsby C, Vierling E (2001). "Structure and function of the small heat shock protein/α-crystallin family of molecular chaperones".
3362:"The functional landscape of Hsp27 reveals new cellular processes such as DNA repair and alternative splicing and proposes novel anticancer targets"
3360:
Katsogiannou M, Andrieu C, Baylot V, Baudot A, Dusetti NJ, Gayet O, Finetti P, Garrido C, Birnbaum D, Bertucci F, Brun C, Rocchi P (December 2014).
3696:
4308:
1788:
2978:
Parcellier A, Schmitt E, Gurbuxani S, Seigneurin-Berny D, Pance A, Chantôme A, Plenchette S, Khochbin S, Solary E, Garrido C (August 2003).
2786:
1770:
4551:
1590:
1477:-independent chaperone by inhibiting protein aggregation and by stabilizing partially denatured proteins, which ensures refolding by the
1627:
adhesion and motility. OGX-427, which targets HSP27 through an antisense mechanism, is currently undergoing testing in clinical trials.
1339:) consisting of 16 to 32 subunits and a high exchange rate of subunits. The oligomerization depends on the physiology of the cells, the
1277:, which are important for the formation of stable dimers. Hsp27 is rather unique among sHsps in that its α-crystallin domain contains a
2597:
Rogalla T, Ehrnsperger M, Preville X, Kotlyarov A, Lutsch G, Ducasse C, Paul C, Wieske M, Arrigo AP, Buchner J, Gaestel M (July 1999).
1610:
gene is also expressed alongside the mutated allele, the diseased cells contain a mixed populations of wild-type and mutant Hsp27, and
1544:
Probably Hsp27 – among other chaperones – is involved in the process of cell differentiation. Changes of Hsp27 levels were observed in
315:
4526:
1469:, cytoprotection, and support of cell survival under stress conditions. More specialized functions of Hsp27 are manifold and complex.
1148:
1141:
1968:
292:
802:
positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway
3719:
1757:
1736:
3919:
1753:
1328:
and wheat Hsp16.9. Therefore the first step in the oligomeric process involves dimerization of the α-crystallin domain. In
214:
189:
54:
2140:"C-terminal lysine truncation increases thermostability and enhances chaperone-like function of porcine alphaB-crystallin"
3072:"Refinement of evolutionary medicine predictions based on clinical evidence for the manifestations of Mendelian diseases"
2401:"Essential role of the NH2-terminal WD/EPF motif in the phosphorylation-activated protective function of mammalian Hsp27"
1732:
4556:
4132:
131:
4077:
1645:
1295:
2254:"Mutant small heat-shock protein 27 causes axonal Charcot-Marie-Tooth disease and distal hereditary motor neuropathy"
1335:
The oligomerization of Hsp27 is a dynamic process: There is a balance between stable dimers and oligomers (up to 800
328:
227:
1502:
1434:
321:
220:
4017:
3682:
1254:
986:
139:
3500:"Chaperone Hsp27, a novel subunit of AUF1 protein complexes, functions in AU-rich element-mediated mRNA decay"
2494:
Alderson TR, Roche J, Gastall HY, Dias DM, Pritišanac I, Ying J, Bax A, Benesch JL, Baldwin AJ (March 2019).
122:, CMT2F, HEL-S-102, HMN2B, HS.76067, HSP27, HSP28, Hsp25, SRP27, heat shock protein family B (small) member 1
4342:
1534:
1419:
967:
4514:
4383:
1474:
3418:"Detection of protein-protein interactions among lens crystallins in a mammalian two-hybrid system assay"
1857:"Assignment of the mouse Hsp25 and Hsp105 genes to the distal region of chromosome 5 by linkage analysis"
3764:
2298:
Jovcevski B, Kelly MA, Rote AP, Berg T, Gastall HY, Benesch JL, Aquilina JA, Ecroyd H (February 2015).
1273:. These domains consist of 80 to 100 residues with sequence homology between 20% and 60% and fold into
1953:
Structure and function of the small heat shock protein/alpha-crystallin family of molecular chaperones
3134:"Novel insights in the disease biology of mutant small heat shock proteins in neuromuscular diseases"
3083:
2507:
1906:
203:
2555:"The dynamics of Hsp25 quaternary structure. Structure and function of different oligomeric species"
2043:"1H NMR spectroscopy reveals that mouse Hsp25 has a flexible C-terminal extension of 18 amino acids"
1310:. The N-terminus of Hsp27, with its WD/EPF-region, is essential for the development of these large
118:
3727:
1594:
1549:
1258:
1249:, and others. The common functions of sHsps are chaperone activity, thermotolerance, inhibition of
1230:
3678:
4373:
3741:
3209:
3052:
2868:
2798:
2750:
2706:
2663:
2378:
2120:
2072:
1930:
1603:
1525:. It speeds up the degradation of irreversibly denatured proteins and junkproteins by binding to
1442:
1324:
1238:
163:
3264:"Heat shock protein 27 regulates human prostate cancer cell motility and metastatic progression"
1585:
At least 12 disease-causing mutations in this gene have been discovered. Heritable mutations in
1124:
1103:
1077:
1056:
3459:"Copurification of small heat shock protein with alpha B crystallin from human skeletal muscle"
2139:
4043:
3653:
3612:
3570:
3529:
3480:
3439:
3393:
3342:
3293:
3244:
3201:
3165:
3109:
3044:
3009:
2960:
2917:
2860:
2825:
2790:
2742:
2698:
2655:
2620:
2576:
2535:
2473:
2422:
2370:
2321:
2275:
2233:
2197:
2162:
2112:
2064:
2023:
1974:
1964:
1922:
1876:
1837:
1371:
111:
47:
4303:
4262:
4257:
4232:
4222:
4217:
4207:
4007:
3643:
3602:
3560:
3519:
3511:
3470:
3429:
3383:
3373:
3332:
3324:
3283:
3275:
3236:
3193:
3155:
3145:
3099:
3091:
3036:
2999:
2991:
2952:
2907:
2899:
2852:
2782:
2734:
2690:
2647:
2610:
2566:
2525:
2515:
2463:
2453:
2412:
2360:
2352:
2311:
2265:
2225:
2189:
2154:
2104:
2054:
2013:
2005:
1956:
1914:
1868:
1827:
1819:
408:
339:
283:
238:
4278:
4212:
2442:"Small Heat Shock Proteins, Big Impact on Protein Aggregation in Neurodegenerative Disease"
1347:(after hours) and phosphorylation (after several minutes) of Hsp27. Stimulation of the p38
159:
4509:
3732:
2180:
Lelj-Garolla B, Mauk AG (January 2005). "Self-association of a small heat shock protein".
1430:
1344:
1340:
383:
3087:
2980:"HSP27 is a ubiquitin-binding protein involved in I-kappaBalpha proteasomal degradation"
2511:
2365:
2340:
1910:
1897:
Kim KK, Kim R, Kim SH (August 1998). "Crystal structure of a small heat-shock protein".
4056:
4051:
3524:
3499:
3388:
3361:
3337:
3312:
3288:
3263:
3104:
3071:
2530:
2495:
2468:
2441:
2018:
1993:
1545:
3475:
3458:
3004:
2979:
2300:"Phosphomimics destabilize Hsp27 oligomeric assemblies and enhance chaperone activity"
2158:
1960:
1832:
1807:
856:
851:
846:
841:
836:
831:
826:
821:
816:
811:
806:
801:
796:
791:
786:
781:
776:
771:
766:
761:
756:
751:
746:
741:
725:
720:
715:
710:
705:
700:
695:
690:
685:
680:
675:
670:
665:
660:
655:
639:
634:
629:
624:
619:
614:
609:
604:
599:
4545:
3160:
2995:
2912:
2903:
2887:
2399:
Thériault JR, Lambert H, Chávez-Zobel AT, Charest G, Lavigne P, Landry J (May 2004).
2229:
2059:
2042:
1515:
1486:
1454:
1367:
1315:
797:
negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
586:
3213:
3056:
2872:
2802:
2710:
2382:
1429:
An affinity of high expression levels of different phosphorylated Hsp27 species and
4412:
4394:
2773:
Sarto C, Binz PA, Mocarelli P (April 2000). "Heat shock proteins in human cancer".
2754:
2316:
2299:
2124:
2076:
1934:
1565:
1490:
1450:
1423:
1356:
401:
180:
2956:
2667:
2638:
Garrido C (May 2002). "Size matters: of the small HSP27 and its large oligomers".
143:
3688:
3311:
Sun X, Ou Z, Xie M, Kang R, Fan Y, Niu X, Wang H, Cao L, Tang D (November 2015).
3262:
Voll EA, Ogden IM, Pavese JM, Huang X, Xu L, Jovanovic BD, Bergan RC (May 2014).
3240:
3132:
Adriaenssens E, Geuens T, Baets J, Echaniz-Laguna A, Timmerman V (October 2017).
167:
4488:
4356:
3632:"Identification and characterization of hic-5/ARA55 as an hsp27 binding protein"
3591:"Hot-spot residue in small heat-shock protein 22 causes distal motor neuropathy"
1994:"Structure of the α-crystallin domain from the redox-sensitive chaperone, HSPB1"
1793:
National Center for
Biotechnology Information, U.S. National Library of Medicine
1775:
National Center for
Biotechnology Information, U.S. National Library of Medicine
1538:
3095:
2787:
10.1002/(SICI)1522-2683(20000401)21:6<1218::AID-ELPS1218>3.0.CO;2-H
2520:
484:
4318:
3746:
3673:
3547:
Sun X, Fontaine JM, Rest JS, Shelden EA, Welsh MJ, Benndorf R (January 2004).
2193:
2108:
2009:
1561:
1522:
1446:
1348:
1336:
1286:
1274:
1270:
1242:
300:
197:
147:
3279:
2615:
2598:
2571:
2554:
2458:
1823:
1322:, which was first shown in crystal structures of the proteins MjHSP16.5 from
4066:
4012:
3378:
1615:
1526:
1482:
1407:
1363:
1359:
1329:
1311:
1291:
1282:
1250:
886:
544:
422:
367:
354:
266:
253:
155:
3657:
3648:
3631:
3616:
3574:
3565:
3548:
3533:
3457:
Kato K, Shinohara H, Goto S, Inaguma Y, Morishita R, Asano T (April 1992).
3443:
3434:
3417:
3397:
3346:
3297:
3248:
3205:
3169:
3150:
3133:
3113:
3048:
3013:
2964:
2921:
2864:
2856:
2794:
2746:
2738:
2702:
2694:
2659:
2651:
2624:
2580:
2539:
2477:
2426:
2417:
2400:
2374:
2325:
2279:
2237:
2201:
2166:
2116:
2027:
1978:
1872:
1441:
was observed. High expression levels possibly are in inverse relation with
3630:
Jia Y, Ransom RF, Shibanuma M, Liu C, Welsh MJ, Smoyer WE (October 2001).
3484:
2829:
2068:
1926:
1880:
1841:
1343:
status of Hsp27 and the exposure to stress. Stress induces an increase of
1188:
1183:
4346:
3979:
3971:
3549:"Interaction of human HSP22 (HSPB8) with other small heat shock proteins"
3515:
1695:
1598:
1557:
1530:
1529:
proteins and to the 26S proteasome. Hsp27 enhances the activation of the
1375:
1352:
1319:
1278:
1172:
1031:
1012:
3328:
1606:, meaning that only one allele contains a mutation. Since the wild-type
4097:
3984:
3944:
3875:
3870:
3865:
3860:
3855:
3810:
2356:
1707:
1659:
1553:
1498:
1438:
1415:
1306:
Hsp27 forms large, dynamic oligomers with an average mass near 500 kDa
1216:
998:
953:
3674:
GeneReviews/NCBI/NIH/UW entry on
Charcot-Marie-Tooth Neuropathy Type 2
3040:
88:
84:
80:
76:
4313:
4288:
4283:
4273:
4237:
4227:
4202:
4187:
4182:
4177:
4172:
4167:
4162:
4157:
4152:
4117:
4102:
3949:
3914:
3899:
3894:
3889:
3850:
3845:
3840:
3835:
3830:
3825:
3820:
3815:
3805:
3800:
3795:
3790:
3785:
1701:
1677:
1569:
1494:
1411:
1156:
908:
3197:
1856:
1281:
residue at its dimer interface, which can become oxidized to form a
3607:
3590:
2270:
2253:
4504:
4494:
4484:
4469:
4451:
4446:
4441:
4436:
4368:
4328:
4293:
4267:
4252:
4247:
4242:
4197:
4192:
4147:
4142:
4137:
4107:
4092:
3989:
3958:
3939:
3934:
3929:
3924:
3909:
3904:
3884:
3780:
3773:
3769:
3754:
2496:"Local unfolding of the HSP27 monome regulates chaperone activity"
1918:
1689:
1683:
1671:
1665:
1510:
1478:
1457:
patients; therefore Hsp27 could be a potential diagnostic marker.
1383:
1246:
1992:
Rajagopal P, Liu Y, Shi L, Clouser AF, Klevit RE (October 2015).
871:
867:
4519:
4499:
4479:
4474:
4424:
4407:
4363:
4351:
4333:
4323:
4122:
4112:
4087:
4082:
4027:
4022:
2888:"Inhibition of Daxx-mediated apoptosis by heat shock protein 27"
1955:. Advances in Protein Chemistry. Vol. 59. pp. 105–56.
1653:
1234:
1223:
752:
cellular response to vascular endothelial growth factor stimulus
135:
3692:
2440:
Webster JM, Darling AL, Uversky VN, Blair LJ (September 2019).
2041:
Carver JA, Esposito G, Schwedersky G, Gaestel M (August 1995).
757:
negative regulation of protein serine/threonine kinase activity
30:
1602:
mouse model. The genetic basis of these diseases is typically
1318:, which are formed by two α-crystallin-domains of neighboring
817:
positive regulation of blood vessel endothelial cell migration
3313:"HSPB1 as a novel regulator of ferroptotic cancer cell death"
812:
vascular endothelial growth factor receptor signaling pathway
2886:
Charette SJ, Lavoie JN, Lambert H, Landry J (October 2000).
1614:
experiments have shown that the two proteins can form heter-
1509:
A well documented function of Hsp27 is the interaction with
2553:
Ehrnsperger M, Lilie H, Gaestel M, Buchner J (May 1999).
1636:
agents for the treatment of ferroptosis-mediated cancer.
1465:
The main function of Hsp27 is to provide thermotolerance
391:
1497:/dATP complex and therefore inhibits the activation of
556:
807:
positive regulation of interleukin-1 beta production
4462:
4393:
4382:
4065:
4042:
4000:
3740:
3726:
2147:
1946:
1944:
1808:"cDNA sequence of a human heat shock protein HSP27"
1806:Carper SW, Rocheleau TA, Storm FK (November 1990).
1521:Another function of Hsp27 is the activation of the
1485:signalling pathway. Hsp27 interacts with the outer
1117:
1096:
1070:
1049:
1749:
1747:
1745:
1728:
1726:
1724:
1453:. High levels of Hsp27 were also found in sera of
787:negative regulation of apoptotic signaling pathway
762:positive regulation of endothelial cell chemotaxis
2394:
2392:
2293:
2291:
2289:
832:regulation of I-kappaB kinase/NF-kappaB signaling
338:
237:
2489:
2487:
1489:membranes and interferes with the activation of
3411:
3409:
3407:
2937:
2935:
2933:
2931:
2592:
2590:
2341:"sHsps and their role in the chaperone network"
18:Protein-coding gene in the species Homo sapiens
1855:Hunt CR, Goswami PC, Kozak CA (October 1997).
1754:GRCm38: Ensembl release 89: ENSMUSG00000004951
827:negative regulation of protein kinase activity
3704:
3127:
3125:
3123:
2768:
2766:
2764:
2090:
2088:
2086:
8:
2138:Liao JH, Lee JS, Chiou SH (September 2002).
1501:. The phosphorylated form of Hsp27 inhibits
1733:GRCh38: Ensembl release 89: ENSG00000106211
4390:
3737:
3711:
3697:
3689:
1892:
1890:
1285:bond that covalently links the dimer. The
882:
582:
453:Skeletal muscle tissue of rectus abdominis
379:
278:
175:
65:
3681:at the U.S. National Library of Medicine
3647:
3606:
3564:
3523:
3474:
3433:
3387:
3377:
3336:
3287:
3159:
3149:
3103:
3070:Šimčíková D, Heneberg P (December 2019).
3003:
2911:
2614:
2570:
2529:
2519:
2467:
2457:
2416:
2364:
2315:
2269:
2058:
2017:
1831:
1481:-complex. Hsp27 is also involved in the
842:negative regulation of apoptotic process
1720:
1418:, but also in the perinuclear region,
1253:, regulation of cell development, and
742:regulation of translational initiation
20:
1314:. Hsp27-oligomers consist of stable
847:regulation of protein phosphorylation
343:
304:
299:
242:
201:
196:
7:
2345:Cellular and Molecular Life Sciences
1591:distal hereditary motor neuropathies
857:anterograde axonal protein transport
3636:The Journal of Biological Chemistry
3553:The Journal of Biological Chemistry
3463:The Journal of Biological Chemistry
3422:The Journal of Biological Chemistry
3366:Molecular & Cellular Proteomics
2603:The Journal of Biological Chemistry
2559:The Journal of Biological Chemistry
2405:The Journal of Biological Chemistry
1414:cells. It is located mainly in the
1351:cascade by differentiating agents,
767:positive regulation of angiogenesis
600:protein kinase C inhibitor activity
4527:Prokaryotic ubiquitin-like protein
1114:
1093:
1067:
1046:
1022:
1003:
977:
958:
932:
913:
852:chaperone-mediated protein folding
671:intracellular anatomical structure
630:protein folding chaperone activity
561:
479:
417:
396:
14:
2252:De Jonghe P, Timmerman V (2004).
1219:that in humans is encoded by the
782:intracellular signal transduction
640:protein homodimerization activity
3416:Fu L, Liang JJ (February 2002).
3029:Journal of Cellular Biochemistry
2996:10.1128/MCB.23.16.5790-5802.2003
2904:10.1128/MCB.20.20.7602-7612.2000
2230:10.1046/j.1432-1327.2000.01188.x
2218:European Journal of Biochemistry
327:
320:
314:
291:
226:
219:
213:
188:
29:
2818:Cancer Detection and Prevention
4057:Mitochondrial targeting signal
3720:Posttranslational modification
3504:Molecular and Cellular Biology
2984:Molecular and Cellular Biology
2892:Molecular and Cellular Biology
2727:Hormone and Metabolic Research
2640:Cell Death and Differentiation
2317:10.1016/j.chembiol.2015.01.001
545:More reference expression data
1:
3476:10.1016/S0021-9258(18)42574-4
2957:10.1016/j.cellsig.2014.03.015
2159:10.1016/S0006-291X(02)02185-X
1961:10.1016/S0065-3233(01)59004-X
1382:, but the oligomerization in
1325:Methanocaldococcus jannaschii
312:
211:
4133:Ubiquitin-conjugating enzyme
3241:10.1016/j.biochi.2017.09.008
2182:Journal of Molecular Biology
2060:10.1016/0014-5793(95)00770-a
822:response to unfolded protein
747:regulation of mRNA stability
4552:Genes on human chromosome 7
4421:E2 SUMO-conjugating enzyme
4078:Ubiquitin-activating enzyme
2339:Haslbeck M (October 2002).
1998:Journal of Biomolecular NMR
1296:Charcot-Marie-Tooth disease
4573:
4404:E1 SUMO-activating enzyme
3096:10.1038/s41598-019-54976-4
2521:10.1038/s41467-019-08557-8
1435:neurodegenerative diseases
1410:, especially all types of
3161:10067/1468770151162165141
2446:Frontiers in Pharmacology
2194:10.1016/j.jmb.2004.10.056
2010:10.1007/s10858-015-9973-0
1789:"Mouse PubMed Reference:"
1771:"Human PubMed Reference:"
1593:and the motor neuropathy
1390:or growing at confluence
1257:. They also take part in
1209:heat shock protein beta-1
1187:
1182:
1178:
1171:
1155:
1149:Chr 5: 135.92 – 135.92 Mb
1136:
1121:
1100:
1089:
1074:
1053:
1042:
1029:
1025:
1010:
1006:
997:
984:
980:
965:
961:
952:
939:
935:
920:
916:
907:
892:
885:
881:
865:
625:identical protein binding
585:
581:
569:
564:
555:
542:
523:quadriceps femoris muscle
491:
482:
449:Descending thoracic aorta
429:
420:
390:
382:
378:
361:
348:
311:
290:
281:
277:
260:
247:
210:
187:
178:
174:
129:
126:
116:
109:
104:
73:
68:
51:
46:
41:
37:
28:
23:
4018:Survival of motor neuron
3683:Medical Subject Headings
3280:10.18632/oncotarget.1917
2616:10.1074/jbc.274.27.18947
2572:10.1074/jbc.274.21.14867
2459:10.3389/fphar.2019.01047
2097:Biochemistry. Biokhimiia
1644:Hsp27 has been shown to
615:protein kinase C binding
4384:Ubiquitin-like proteins
4343:Deubiquitinating enzyme
3379:10.1074/mcp.M114.041228
2109:10.1023/A:1015549725819
1535:reactive oxygen species
1420:endoplasmatic reticulum
792:regulation of autophagy
3649:10.1074/jbc.M103510200
3566:10.1074/jbc.M311324200
3435:10.1074/jbc.M110027200
2857:10.1002/pmic.200390058
2739:10.1055/s-0029-1216374
2695:10.1038/sj.onc.1203850
2652:10.1038/sj.cdd.4401005
2418:10.1074/jbc.M402325200
1873:10.1006/geno.1997.4973
1824:10.1093/nar/18.21.6457
1812:Nucleic Acids Research
1406:Hsp27 appears in many
605:protein kinase binding
2500:Nature Communications
1576:Clinical significance
1402:Cellular localization
1201:Heat shock protein 27
1142:Chr 7: 76.3 – 76.3 Mb
681:extracellular exosome
437:right coronary artery
3679:HSPB1+protein,+human
3516:10.1128/MCB.00431-08
3151:10.1093/brain/awx187
1550:embryonic stem cells
1449:, and resistance to
1255:cell differentiation
777:platelet aggregation
716:extracellular matrix
469:left coronary artery
345:5 G2|5 75.51 cM
306:Chromosome 5 (mouse)
204:Chromosome 7 (human)
69:List of PDB id codes
42:Available structures
4557:Heat shock proteins
3742:Heat shock proteins
3329:10.1038/onc.2015.32
3088:2019NatSR...918577S
2945:Cellular Signalling
2512:2019NatCo..10.1068A
1911:1998Natur.394..595K
1597:disease. There are
1595:Charcot-Marie-Tooth
1259:signal transduction
721:extracellular space
457:gingival epithelium
3076:Scientific Reports
2357:10.1007/PL00012492
1622:Roles in apoptosis
1604:autosomal dominant
1581:Motor neuropathies
1443:cell proliferation
1239:heat shock protein
987:ENSMUSG00000004951
772:retina homeostasis
735:Biological process
711:proteasome complex
649:Cellular component
593:Molecular function
4539:
4538:
4535:
4534:
4044:Protein targeting
4038:
4037:
3041:10.1002/jcb.20349
1372:hydrogen peroxide
1198:
1197:
1194:
1193:
1167:
1166:
1132:
1131:
1111:
1110:
1085:
1084:
1064:
1063:
1038:
1037:
1019:
1018:
993:
992:
974:
973:
948:
947:
929:
928:
877:
876:
837:response to virus
701:contractile fiber
620:ubiquitin binding
577:
576:
573:
572:
551:
550:
538:
537:
476:
475:
441:mucosa of pharynx
374:
373:
273:
272:
168:HSPB1 - orthologs
100:
99:
96:
95:
52:Ortholog search:
4564:
4391:
4304:Ubiquitin ligase
4070:(ubiquitylation)
4008:Alpha crystallin
3738:
3713:
3706:
3699:
3690:
3662:
3661:
3651:
3627:
3621:
3620:
3610:
3585:
3579:
3578:
3568:
3544:
3538:
3537:
3527:
3495:
3489:
3488:
3478:
3454:
3448:
3447:
3437:
3413:
3402:
3401:
3391:
3381:
3372:(12): 3585–601.
3357:
3351:
3350:
3340:
3308:
3302:
3301:
3291:
3259:
3253:
3252:
3224:
3218:
3217:
3180:
3174:
3173:
3163:
3153:
3129:
3118:
3117:
3107:
3067:
3061:
3060:
3024:
3018:
3017:
3007:
2990:(16): 5790–802.
2975:
2969:
2968:
2939:
2926:
2925:
2915:
2883:
2877:
2876:
2840:
2834:
2833:
2813:
2807:
2806:
2770:
2759:
2758:
2721:
2715:
2714:
2678:
2672:
2671:
2635:
2629:
2628:
2618:
2609:(27): 18947–56.
2594:
2585:
2584:
2574:
2565:(21): 14867–74.
2550:
2544:
2543:
2533:
2523:
2491:
2482:
2481:
2471:
2461:
2437:
2431:
2430:
2420:
2411:(22): 23463–71.
2396:
2387:
2386:
2368:
2336:
2330:
2329:
2319:
2295:
2284:
2283:
2273:
2248:
2242:
2241:
2212:
2206:
2205:
2177:
2171:
2170:
2144:
2135:
2129:
2128:
2092:
2081:
2080:
2062:
2038:
2032:
2031:
2021:
1989:
1983:
1982:
1948:
1939:
1938:
1894:
1885:
1884:
1852:
1846:
1845:
1835:
1803:
1797:
1796:
1785:
1779:
1778:
1767:
1761:
1751:
1740:
1730:
1241:) group among α-
1207:) also known as
1180:
1179:
1151:
1144:
1127:
1115:
1106:
1094:
1090:RefSeq (protein)
1080:
1068:
1059:
1047:
1023:
1004:
978:
959:
933:
914:
883:
583:
562:
547:
487:
485:Top expressed in
480:
461:popliteal artery
425:
423:Top expressed in
418:
397:
380:
370:
357:
346:
331:
324:
318:
307:
295:
279:
269:
256:
245:
230:
223:
217:
206:
192:
176:
170:
121:
114:
91:
66:
60:
39:
38:
33:
21:
4572:
4571:
4567:
4566:
4565:
4563:
4562:
4561:
4542:
4541:
4540:
4531:
4458:
4433:E3 SUMO ligase
4397:
4386:
4378:
4069:
4061:
4034:
3996:
3975:
3967:
3745:
3733:protein folding
3731:
3722:
3717:
3670:
3665:
3642:(43): 39911–8.
3629:
3628:
3624:
3595:Nature Genetics
3589:V (June 2004).
3587:
3586:
3582:
3559:(4): 2394–402.
3546:
3545:
3541:
3510:(17): 5223–37.
3497:
3496:
3492:
3469:(11): 7718–25.
3456:
3455:
3451:
3415:
3414:
3405:
3359:
3358:
3354:
3323:(45): 5617–25.
3310:
3309:
3305:
3261:
3260:
3256:
3226:
3225:
3221:
3198:10.1038/nm.2396
3186:Nature Medicine
3182:
3181:
3177:
3131:
3130:
3121:
3069:
3068:
3064:
3026:
3025:
3021:
2977:
2976:
2972:
2941:
2940:
2929:
2898:(20): 7602–12.
2885:
2884:
2880:
2842:
2841:
2837:
2815:
2814:
2810:
2775:Electrophoresis
2772:
2771:
2762:
2723:
2722:
2718:
2689:(42): 4855–63.
2680:
2679:
2675:
2637:
2636:
2632:
2596:
2595:
2588:
2552:
2551:
2547:
2493:
2492:
2485:
2439:
2438:
2434:
2398:
2397:
2390:
2351:(10): 1649–57.
2338:
2337:
2333:
2297:
2296:
2287:
2258:Nature Genetics
2250:
2249:
2245:
2214:
2213:
2209:
2179:
2178:
2174:
2142:
2137:
2136:
2132:
2094:
2093:
2084:
2053:(2–3): 305–10.
2040:
2039:
2035:
1991:
1990:
1986:
1971:
1950:
1949:
1942:
1905:(6693): 595–9.
1896:
1895:
1888:
1854:
1853:
1849:
1805:
1804:
1800:
1787:
1786:
1782:
1769:
1768:
1764:
1752:
1743:
1731:
1722:
1718:
1713:
1642:
1633:
1631:Roles in cancer
1624:
1583:
1578:
1463:
1404:
1341:phosphorylation
1304:
1302:Oligomerization
1267:
1189:View/Edit Mouse
1184:View/Edit Human
1147:
1140:
1137:Location (UCSC)
1123:
1102:
1076:
1055:
968:ENSG00000106211
861:
730:
686:plasma membrane
644:
610:protein binding
543:
534:
529:
525:
521:
517:
513:
511:urinary bladder
509:
507:muscle of thigh
505:
501:
497:
483:
472:
467:
465:tibial arteries
463:
459:
455:
451:
447:
443:
439:
435:
433:ascending aorta
421:
365:
352:
344:
334:
333:
332:
325:
305:
282:Gene location (
264:
251:
243:
233:
232:
231:
224:
202:
179:Gene location (
130:
117:
110:
75:
53:
19:
12:
11:
5:
4570:
4568:
4560:
4559:
4554:
4544:
4543:
4537:
4536:
4533:
4532:
4530:
4529:
4523:
4522:
4517:
4512:
4507:
4502:
4497:
4492:
4482:
4477:
4472:
4466:
4464:
4460:
4459:
4457:
4456:
4455:
4454:
4449:
4444:
4439:
4430:
4429:
4428:
4427:
4418:
4417:
4416:
4415:
4410:
4401:
4399:
4388:
4380:
4379:
4377:
4376:
4371:
4366:
4360:
4359:
4354:
4349:
4339:
4338:
4337:
4336:
4331:
4326:
4321:
4316:
4311:
4299:
4298:
4297:
4296:
4291:
4286:
4281:
4276:
4271:
4265:
4260:
4255:
4250:
4245:
4240:
4235:
4230:
4225:
4220:
4215:
4210:
4205:
4200:
4195:
4190:
4185:
4180:
4175:
4170:
4165:
4160:
4155:
4150:
4145:
4140:
4128:
4127:
4126:
4125:
4120:
4115:
4110:
4105:
4100:
4095:
4090:
4085:
4073:
4071:
4063:
4062:
4060:
4059:
4054:
4052:Signal peptide
4048:
4046:
4040:
4039:
4036:
4035:
4033:
4032:
4031:
4030:
4025:
4015:
4010:
4004:
4002:
3998:
3997:
3995:
3994:
3993:
3992:
3987:
3982:
3977:
3973:
3969:
3965:
3955:
3954:
3953:
3952:
3947:
3942:
3937:
3932:
3927:
3922:
3917:
3912:
3907:
3902:
3897:
3892:
3881:
3880:
3879:
3878:
3873:
3868:
3863:
3858:
3853:
3848:
3843:
3838:
3833:
3828:
3823:
3818:
3813:
3808:
3803:
3798:
3793:
3788:
3777:
3776:
3767:
3762:
3757:
3751:
3749:
3735:
3724:
3723:
3718:
3716:
3715:
3708:
3701:
3693:
3687:
3686:
3676:
3669:
3668:External links
3666:
3664:
3663:
3622:
3608:10.1038/ng1328
3601:(6): 597–601.
3580:
3539:
3490:
3449:
3428:(6): 4255–60.
3403:
3352:
3303:
3274:(9): 2648–63.
3254:
3219:
3175:
3144:(10): 2541–9.
3119:
3062:
3019:
2970:
2951:(7): 1616–25.
2927:
2878:
2835:
2808:
2781:(6): 1218–26.
2760:
2716:
2673:
2630:
2586:
2545:
2483:
2432:
2388:
2331:
2285:
2271:10.1038/ng1354
2243:
2224:(7): 1923–32.
2207:
2172:
2130:
2082:
2033:
1984:
1969:
1940:
1886:
1847:
1798:
1780:
1762:
1741:
1719:
1717:
1714:
1712:
1711:
1705:
1699:
1693:
1687:
1681:
1675:
1669:
1663:
1657:
1650:
1641:
1638:
1632:
1629:
1623:
1620:
1582:
1579:
1577:
1574:
1546:Ehrlich ascite
1473:it acts as an
1462:
1459:
1403:
1400:
1386:cells growing
1303:
1300:
1266:
1263:
1196:
1195:
1192:
1191:
1186:
1176:
1175:
1169:
1168:
1165:
1164:
1162:
1160:
1153:
1152:
1145:
1138:
1134:
1133:
1130:
1129:
1119:
1118:
1112:
1109:
1108:
1098:
1097:
1091:
1087:
1086:
1083:
1082:
1072:
1071:
1065:
1062:
1061:
1051:
1050:
1044:
1040:
1039:
1036:
1035:
1027:
1026:
1020:
1017:
1016:
1008:
1007:
1001:
995:
994:
991:
990:
982:
981:
975:
972:
971:
963:
962:
956:
950:
949:
946:
945:
937:
936:
930:
927:
926:
918:
917:
911:
905:
904:
899:
894:
890:
889:
879:
878:
875:
874:
863:
862:
860:
859:
854:
849:
844:
839:
834:
829:
824:
819:
814:
809:
804:
799:
794:
789:
784:
779:
774:
769:
764:
759:
754:
749:
744:
738:
736:
732:
731:
729:
728:
726:axon cytoplasm
723:
718:
713:
708:
706:focal adhesion
703:
698:
693:
688:
683:
678:
673:
668:
663:
658:
652:
650:
646:
645:
643:
642:
637:
632:
627:
622:
617:
612:
607:
602:
596:
594:
590:
589:
579:
578:
575:
574:
571:
570:
567:
566:
559:
553:
552:
549:
548:
540:
539:
536:
535:
533:
532:
528:
524:
520:
516:
512:
508:
504:
500:
496:
492:
489:
488:
477:
474:
473:
471:
470:
466:
462:
458:
454:
450:
446:
442:
438:
434:
430:
427:
426:
414:
413:
405:
394:
388:
387:
384:RNA expression
376:
375:
372:
371:
363:
359:
358:
350:
347:
342:
336:
335:
326:
319:
313:
309:
308:
303:
297:
296:
288:
287:
275:
274:
271:
270:
262:
258:
257:
249:
246:
241:
235:
234:
225:
218:
212:
208:
207:
200:
194:
193:
185:
184:
172:
171:
128:
124:
123:
115:
107:
106:
102:
101:
98:
97:
94:
93:
71:
70:
62:
61:
50:
44:
43:
35:
34:
26:
25:
17:
13:
10:
9:
6:
4:
3:
2:
4569:
4558:
4555:
4553:
4550:
4549:
4547:
4528:
4525:
4524:
4521:
4518:
4516:
4513:
4511:
4508:
4506:
4503:
4501:
4498:
4496:
4493:
4490:
4486:
4483:
4481:
4478:
4476:
4473:
4471:
4468:
4467:
4465:
4461:
4453:
4450:
4448:
4445:
4443:
4440:
4438:
4435:
4434:
4432:
4431:
4426:
4423:
4422:
4420:
4419:
4414:
4411:
4409:
4406:
4405:
4403:
4402:
4400:
4398:(SUMOylation)
4396:
4392:
4389:
4385:
4381:
4375:
4372:
4370:
4367:
4365:
4362:
4361:
4358:
4355:
4353:
4350:
4348:
4344:
4341:
4340:
4335:
4332:
4330:
4327:
4325:
4322:
4320:
4317:
4315:
4312:
4310:
4307:
4306:
4305:
4301:
4300:
4295:
4292:
4290:
4287:
4285:
4282:
4280:
4277:
4275:
4272:
4269:
4266:
4264:
4261:
4259:
4256:
4254:
4251:
4249:
4246:
4244:
4241:
4239:
4236:
4234:
4231:
4229:
4226:
4224:
4221:
4219:
4216:
4214:
4211:
4209:
4206:
4204:
4201:
4199:
4196:
4194:
4191:
4189:
4186:
4184:
4181:
4179:
4176:
4174:
4171:
4169:
4166:
4164:
4161:
4159:
4156:
4154:
4151:
4149:
4146:
4144:
4141:
4139:
4136:
4135:
4134:
4130:
4129:
4124:
4121:
4119:
4116:
4114:
4111:
4109:
4106:
4104:
4101:
4099:
4096:
4094:
4091:
4089:
4086:
4084:
4081:
4080:
4079:
4075:
4074:
4072:
4068:
4064:
4058:
4055:
4053:
4050:
4049:
4047:
4045:
4041:
4029:
4026:
4024:
4021:
4020:
4019:
4016:
4014:
4011:
4009:
4006:
4005:
4003:
3999:
3991:
3988:
3986:
3983:
3981:
3978:
3976:
3970:
3968:
3962:
3961:
3960:
3957:
3956:
3951:
3948:
3946:
3943:
3941:
3938:
3936:
3933:
3931:
3928:
3926:
3923:
3921:
3918:
3916:
3913:
3911:
3908:
3906:
3903:
3901:
3898:
3896:
3893:
3891:
3888:
3887:
3886:
3883:
3882:
3877:
3874:
3872:
3869:
3867:
3864:
3862:
3859:
3857:
3854:
3852:
3849:
3847:
3844:
3842:
3839:
3837:
3834:
3832:
3829:
3827:
3824:
3822:
3819:
3817:
3814:
3812:
3809:
3807:
3804:
3802:
3799:
3797:
3794:
3792:
3789:
3787:
3784:
3783:
3782:
3779:
3778:
3775:
3771:
3768:
3766:
3763:
3761:
3758:
3756:
3753:
3752:
3750:
3748:
3743:
3739:
3736:
3734:
3729:
3725:
3721:
3714:
3709:
3707:
3702:
3700:
3695:
3694:
3691:
3684:
3680:
3677:
3675:
3672:
3671:
3667:
3659:
3655:
3650:
3645:
3641:
3637:
3633:
3626:
3623:
3618:
3614:
3609:
3604:
3600:
3596:
3592:
3584:
3581:
3576:
3572:
3567:
3562:
3558:
3554:
3550:
3543:
3540:
3535:
3531:
3526:
3521:
3517:
3513:
3509:
3505:
3501:
3494:
3491:
3486:
3482:
3477:
3472:
3468:
3464:
3460:
3453:
3450:
3445:
3441:
3436:
3431:
3427:
3423:
3419:
3412:
3410:
3408:
3404:
3399:
3395:
3390:
3385:
3380:
3375:
3371:
3367:
3363:
3356:
3353:
3348:
3344:
3339:
3334:
3330:
3326:
3322:
3318:
3314:
3307:
3304:
3299:
3295:
3290:
3285:
3281:
3277:
3273:
3269:
3265:
3258:
3255:
3250:
3246:
3242:
3238:
3234:
3230:
3223:
3220:
3215:
3211:
3207:
3203:
3199:
3195:
3192:(8): 968–74.
3191:
3187:
3179:
3176:
3171:
3167:
3162:
3157:
3152:
3147:
3143:
3139:
3135:
3128:
3126:
3124:
3120:
3115:
3111:
3106:
3101:
3097:
3093:
3089:
3085:
3081:
3077:
3073:
3066:
3063:
3058:
3054:
3050:
3046:
3042:
3038:
3034:
3030:
3023:
3020:
3015:
3011:
3006:
3001:
2997:
2993:
2989:
2985:
2981:
2974:
2971:
2966:
2962:
2958:
2954:
2950:
2946:
2938:
2936:
2934:
2932:
2928:
2923:
2919:
2914:
2909:
2905:
2901:
2897:
2893:
2889:
2882:
2879:
2874:
2870:
2866:
2862:
2858:
2854:
2850:
2846:
2839:
2836:
2831:
2827:
2824:(5): 441–51.
2823:
2819:
2812:
2809:
2804:
2800:
2796:
2792:
2788:
2784:
2780:
2776:
2769:
2767:
2765:
2761:
2756:
2752:
2748:
2744:
2740:
2736:
2732:
2728:
2720:
2717:
2712:
2708:
2704:
2700:
2696:
2692:
2688:
2684:
2677:
2674:
2669:
2665:
2661:
2657:
2653:
2649:
2645:
2641:
2634:
2631:
2626:
2622:
2617:
2612:
2608:
2604:
2600:
2593:
2591:
2587:
2582:
2578:
2573:
2568:
2564:
2560:
2556:
2549:
2546:
2541:
2537:
2532:
2527:
2522:
2517:
2513:
2509:
2505:
2501:
2497:
2490:
2488:
2484:
2479:
2475:
2470:
2465:
2460:
2455:
2451:
2447:
2443:
2436:
2433:
2428:
2424:
2419:
2414:
2410:
2406:
2402:
2395:
2393:
2389:
2384:
2380:
2376:
2372:
2367:
2362:
2358:
2354:
2350:
2346:
2342:
2335:
2332:
2327:
2323:
2318:
2313:
2310:(2): 186–95.
2309:
2305:
2301:
2294:
2292:
2290:
2286:
2281:
2277:
2272:
2267:
2263:
2259:
2255:
2247:
2244:
2239:
2235:
2231:
2227:
2223:
2219:
2211:
2208:
2203:
2199:
2195:
2191:
2188:(3): 631–42.
2187:
2183:
2176:
2173:
2168:
2164:
2160:
2156:
2153:(2): 309–16.
2152:
2148:
2141:
2134:
2131:
2126:
2122:
2118:
2114:
2110:
2106:
2102:
2098:
2091:
2089:
2087:
2083:
2078:
2074:
2070:
2066:
2061:
2056:
2052:
2048:
2044:
2037:
2034:
2029:
2025:
2020:
2015:
2011:
2007:
2003:
1999:
1995:
1988:
1985:
1980:
1976:
1972:
1970:9780120342594
1966:
1962:
1958:
1954:
1947:
1945:
1941:
1936:
1932:
1928:
1924:
1920:
1919:10.1038/29106
1916:
1912:
1908:
1904:
1900:
1893:
1891:
1887:
1882:
1878:
1874:
1870:
1866:
1862:
1858:
1851:
1848:
1843:
1839:
1834:
1829:
1825:
1821:
1817:
1813:
1809:
1802:
1799:
1794:
1790:
1784:
1781:
1776:
1772:
1766:
1763:
1759:
1755:
1750:
1748:
1746:
1742:
1738:
1734:
1729:
1727:
1725:
1721:
1715:
1709:
1706:
1703:
1700:
1697:
1694:
1691:
1688:
1685:
1682:
1679:
1676:
1673:
1670:
1667:
1664:
1661:
1658:
1655:
1652:
1651:
1649:
1647:
1639:
1637:
1630:
1628:
1621:
1619:
1617:
1613:
1609:
1605:
1600:
1596:
1592:
1588:
1580:
1575:
1573:
1571:
1567:
1566:keratinocytes
1563:
1559:
1555:
1551:
1547:
1542:
1540:
1537:and to raise
1536:
1532:
1528:
1527:ubiquitinated
1524:
1519:
1517:
1516:cell membrane
1512:
1507:
1504:
1500:
1496:
1492:
1488:
1487:mitochondrial
1484:
1480:
1476:
1472:
1468:
1460:
1458:
1456:
1455:breast cancer
1452:
1448:
1444:
1440:
1436:
1432:
1427:
1425:
1421:
1417:
1413:
1409:
1401:
1399:
1395:
1393:
1389:
1385:
1381:
1377:
1373:
1369:
1365:
1361:
1358:
1354:
1350:
1346:
1342:
1338:
1333:
1331:
1327:
1326:
1321:
1317:
1313:
1309:
1301:
1299:
1297:
1293:
1288:
1284:
1280:
1276:
1272:
1264:
1262:
1260:
1256:
1252:
1248:
1244:
1240:
1236:
1232:
1227:
1225:
1222:
1218:
1214:
1210:
1206:
1202:
1190:
1185:
1181:
1177:
1174:
1170:
1163:
1161:
1158:
1154:
1150:
1146:
1143:
1139:
1135:
1128:
1126:
1120:
1116:
1113:
1107:
1105:
1099:
1095:
1092:
1088:
1081:
1079:
1073:
1069:
1066:
1060:
1058:
1052:
1048:
1045:
1043:RefSeq (mRNA)
1041:
1034:
1033:
1028:
1024:
1021:
1015:
1014:
1009:
1005:
1002:
1000:
996:
989:
988:
983:
979:
976:
970:
969:
964:
960:
957:
955:
951:
944:
943:
938:
934:
931:
925:
924:
919:
915:
912:
910:
906:
903:
900:
898:
895:
891:
888:
884:
880:
873:
869:
864:
858:
855:
853:
850:
848:
845:
843:
840:
838:
835:
833:
830:
828:
825:
823:
820:
818:
815:
813:
810:
808:
805:
803:
800:
798:
795:
793:
790:
788:
785:
783:
780:
778:
775:
773:
770:
768:
765:
763:
760:
758:
755:
753:
750:
748:
745:
743:
740:
739:
737:
734:
733:
727:
724:
722:
719:
717:
714:
712:
709:
707:
704:
702:
699:
697:
694:
692:
689:
687:
684:
682:
679:
677:
674:
672:
669:
667:
664:
662:
659:
657:
654:
653:
651:
648:
647:
641:
638:
636:
633:
631:
628:
626:
623:
621:
618:
616:
613:
611:
608:
606:
603:
601:
598:
597:
595:
592:
591:
588:
587:Gene ontology
584:
580:
568:
563:
560:
558:
554:
546:
541:
531:adrenal gland
530:
527:muscle tissue
526:
522:
518:
514:
510:
506:
502:
498:
494:
493:
490:
486:
481:
478:
468:
464:
460:
456:
452:
448:
444:
440:
436:
432:
431:
428:
424:
419:
416:
415:
412:
410:
406:
404:
403:
399:
398:
395:
393:
389:
385:
381:
377:
369:
364:
360:
356:
351:
341:
337:
330:
323:
317:
310:
302:
298:
294:
289:
285:
280:
276:
268:
263:
259:
255:
250:
240:
236:
229:
222:
216:
209:
205:
199:
195:
191:
186:
182:
177:
173:
169:
165:
161:
157:
153:
149:
145:
141:
137:
133:
125:
120:
113:
108:
103:
92:
90:
86:
82:
78:
72:
67:
64:
63:
59:
56:
49:
45:
40:
36:
32:
27:
22:
16:
4395:SUMO protein
3759:
3639:
3635:
3625:
3598:
3594:
3583:
3556:
3552:
3542:
3507:
3503:
3493:
3466:
3462:
3452:
3425:
3421:
3369:
3365:
3355:
3320:
3316:
3306:
3271:
3267:
3257:
3232:
3228:
3222:
3189:
3185:
3178:
3141:
3137:
3082:(1): 18577.
3079:
3075:
3065:
3035:(2): 241–6.
3032:
3028:
3022:
2987:
2983:
2973:
2948:
2944:
2895:
2891:
2881:
2851:(4): 433–9.
2848:
2844:
2838:
2821:
2817:
2811:
2778:
2774:
2733:(8): 594–9.
2730:
2726:
2719:
2686:
2682:
2676:
2646:(5): 483–5.
2643:
2639:
2633:
2606:
2602:
2562:
2558:
2548:
2503:
2499:
2449:
2445:
2435:
2408:
2404:
2348:
2344:
2334:
2307:
2303:
2264:(6): 602–6.
2261:
2257:
2246:
2221:
2217:
2210:
2185:
2181:
2175:
2150:
2146:
2133:
2103:(5): 511–9.
2100:
2096:
2050:
2047:FEBS Letters
2046:
2036:
2004:(2): 223–8.
2001:
1997:
1987:
1952:
1902:
1898:
1867:(2): 462–3.
1864:
1860:
1850:
1818:(21): 6457.
1815:
1811:
1801:
1792:
1783:
1774:
1765:
1643:
1640:Interactions
1634:
1625:
1611:
1607:
1586:
1584:
1543:
1520:
1508:
1499:procaspase-9
1491:cytochrome c
1470:
1466:
1464:
1451:chemotherapy
1437:and various
1428:
1405:
1396:
1391:
1387:
1379:
1357:inflammatory
1334:
1323:
1307:
1305:
1268:
1228:
1220:
1212:
1208:
1204:
1200:
1199:
1122:
1101:
1075:
1054:
1030:
1011:
985:
966:
940:
921:
901:
896:
661:cytoskeleton
503:zone of skin
407:
400:
366:135,918,417
353:135,916,773
127:External IDs
74:
15:
4489:neddylation
3755:Hsp10/GroES
3747:Chaperonins
2506:(1): 1068.
1562:osteoblasts
1539:glutathione
1229:Hsp27 is a
635:RNA binding
265:76,304,295
252:76,302,673
105:Identifiers
4546:Categories
3781:Hsp40/DnaJ
3728:Chaperones
3268:Oncotarget
3235:: 168–78.
2845:Proteomics
2304:Chem. Biol
1760:, May 2017
1739:, May 2017
1716:References
1523:proteasome
1447:metastasis
1408:cell types
1374:and other
1349:MAP kinase
1345:expression
1287:N-terminus
1271:C-terminus
1243:crystallin
691:Z discdkac
411:(ortholog)
148:HomoloGene
4067:Ubiquitin
4013:Clusterin
3229:Biochimie
1616:oligomers
1552:, normal
1483:apoptotic
1360:cytokines
1330:metazoans
1312:oligomers
1292:oligomers
1283:disulfide
1265:Structure
1251:apoptosis
1231:chaperone
1125:NP_038588
1104:NP_001531
1078:NM_013560
1057:NM_001540
887:Orthologs
696:cytoplasm
495:esophagus
156:GeneCards
4347:Ataxin 3
3658:11546764
3617:15122253
3575:14594798
3534:18573886
3444:11700327
3398:25277244
3347:25728673
3317:Oncogene
3298:24798191
3249:28919577
3214:17777551
3206:21785432
3170:28969372
3114:31819097
3057:12669980
3049:15546148
3014:12897149
2965:24686082
2922:11003656
2873:33723077
2865:12687611
2803:38332024
2795:10786894
2747:19384818
2711:11697388
2703:11039903
2683:Oncogene
2660:11973606
2625:10383393
2581:10329686
2540:30842409
2478:31619995
2452:: 1047.
2427:15033973
2383:31148963
2375:12475175
2366:11337447
2326:25699602
2280:15122254
2238:10727931
2202:15581903
2167:12237119
2117:12059769
2028:26243512
1979:11868270
1861:Genomics
1756:–
1735:–
1646:interact
1612:in vitro
1599:missense
1558:lymphoma
1541:levels.
1471:In vitro
1461:Function
1392:in vitro
1380:in vitro
1376:oxidants
1362:such as
1353:mitogens
1320:monomers
1308:in vitro
1279:cysteine
1275:β-sheets
1173:Wikidata
866:Sources:
515:placenta
4270:(CDC34)
3525:2519747
3485:1560006
3389:4256507
3338:4640181
3289:4058034
3105:6901466
3084:Bibcode
2830:9307847
2755:2344159
2531:6403371
2508:Bibcode
2469:6759932
2125:1486211
2077:8310260
2069:7649277
2019:4589510
1935:4431454
1927:9707123
1907:Bibcode
1881:9344682
1842:2243808
1758:Ensembl
1737:Ensembl
1708:TGFB1I1
1660:C2orf73
1570:neurons
1560:cells,
1554:B-cells
1548:cells,
1467:in vivo
1439:cancers
1424:nucleus
1416:cytosol
1388:in vivo
1237:(small
1233:of the
1217:protein
1215:) is a
999:UniProt
954:Ensembl
893:Species
872:QuickGO
676:cytosol
666:spindle
656:nucleus
386:pattern
244:7q11.23
112:Aliases
4314:Cullin
3685:(MeSH)
3656:
3615:
3573:
3532:
3522:
3483:
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3386:
3345:
3335:
3296:
3286:
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3168:
3112:
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3002:
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2871:
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2828:
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2745:
2709:
2701:
2668:445772
2666:
2658:
2623:
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2528:
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2425:
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2324:
2278:
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2165:
2123:
2115:
2075:
2067:
2026:
2016:
1977:
1967:
1933:
1925:
1899:Nature
1879:
1840:
1833:332574
1830:
1678:CRYBB2
1648:with:
1589:cause
1495:Apaf-1
1431:muscle
1422:, and
1412:muscle
1316:dimers
1159:search
1157:PubMed
1032:P14602
1013:P04792
909:Entrez
557:BioGPS
136:602195
4505:ATG12
4495:FAT10
4485:NEDD8
4470:ISG15
4463:Other
4452:PIAS4
4447:PIAS3
4442:PIAS2
4437:PIAS1
4387:(UBL)
4369:BIRC6
4329:FANCL
4001:Other
3990:TRAP1
3959:Hsp90
3885:Hsp70
3774:GroEL
3770:HSP60
3765:Hsp47
3760:Hsp27
3210:S2CID
3138:Brain
3053:S2CID
2913:86317
2869:S2CID
2799:S2CID
2751:S2CID
2707:S2CID
2664:S2CID
2379:S2CID
2143:(PDF)
2121:S2CID
2073:S2CID
1931:S2CID
1704:, and
1690:HSPB8
1684:HNRPD
1672:CRYAB
1666:CRYAA
1608:HSPB1
1587:HSPB1
1531:NF-κB
1511:actin
1479:Hsp70
1384:tumor
1368:IL-1β
1247:Hsp20
1221:HSPB1
1213:HSPB1
1205:Hsp27
942:15507
902:Mouse
897:Human
868:Amigo
519:heart
409:Mouse
402:Human
349:Start
284:Mouse
248:Start
181:Human
160:HSPB1
144:96240
119:HSPB1
24:HSPB1
4520:UBL5
4510:FUB1
4500:ATG8
4480:UFM1
4475:URM1
4425:UBC9
4413:SAE2
4408:SAE1
4374:UFC1
4364:ATG3
4357:CYLD
4352:USP6
4334:UBR1
4324:MDM2
4123:SAE1
4118:NAE1
4113:ATG7
4108:UBA7
4103:UBA6
4098:UBA5
4093:UBA3
4088:UBA2
4083:UBA1
4028:SMN2
4023:SMN1
3654:PMID
3613:PMID
3571:PMID
3530:PMID
3481:PMID
3440:PMID
3394:PMID
3343:PMID
3294:PMID
3245:PMID
3202:PMID
3166:PMID
3110:PMID
3045:PMID
3010:PMID
2961:PMID
2918:PMID
2861:PMID
2826:PMID
2791:PMID
2743:PMID
2699:PMID
2656:PMID
2621:PMID
2577:PMID
2536:PMID
2474:PMID
2423:PMID
2371:PMID
2322:PMID
2276:PMID
2234:PMID
2198:PMID
2163:PMID
2113:PMID
2065:PMID
2024:PMID
1975:PMID
1965:ISBN
1923:PMID
1877:PMID
1838:PMID
1702:TAK1
1654:ASK1
1556:, B-
1503:Daxx
1366:and
1364:TNFα
1235:sHsp
1224:gene
923:3315
445:gums
392:Bgee
340:Band
301:Chr.
239:Band
198:Chr.
152:1180
132:OMIM
89:2N3J
85:3Q9Q
81:3Q9P
77:4MJH
58:RCSB
55:PDBe
4515:MUB
4319:CBL
4309:VHL
4302:E3
4131:E2
4076:E1
3945:12A
3876:C19
3871:C14
3866:C13
3861:C11
3856:C10
3811:B11
3644:doi
3640:276
3603:doi
3561:doi
3557:279
3520:PMC
3512:doi
3471:doi
3467:267
3430:doi
3426:277
3384:PMC
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3333:PMC
3325:doi
3284:PMC
3276:doi
3237:doi
3233:142
3194:doi
3156:hdl
3146:doi
3142:140
3100:PMC
3092:doi
3037:doi
3000:PMC
2992:doi
2953:doi
2908:PMC
2900:doi
2853:doi
2783:doi
2735:doi
2691:doi
2648:doi
2611:doi
2607:274
2567:doi
2563:274
2526:PMC
2516:doi
2464:PMC
2454:doi
2413:doi
2409:279
2361:PMC
2353:doi
2312:doi
2266:doi
2226:doi
2222:267
2190:doi
2186:345
2155:doi
2151:297
2105:doi
2055:doi
2051:369
2014:PMC
2006:doi
1957:doi
1915:doi
1903:394
1869:doi
1828:PMC
1820:doi
1696:MK2
1475:ATP
1337:kDa
565:n/a
499:lip
362:End
261:End
164:OMA
140:MGI
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4289:V2
4284:V1
4274:R2
4268:R1
4263:Q2
4258:Q1
4238:L6
4233:L4
4228:L3
4223:L2
4218:L1
4208:J2
4203:J1
4188:G2
4183:G1
4178:E3
4173:E2
4168:E1
4163:D3
4158:D2
4153:D1
3985:ER
3950:14
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3895:1B
3890:1A
3851:C7
3846:C6
3841:C5
3836:C3
3831:C1
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