Summary: Chaperonin 10 Kd subunit
Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.
This is the Wikipedia entry entitled "GroES". More...
The Wikipedia text that you see displayed here is a download from Wikipedia. This means that the information we display is a copy of the information from the Wikipedia database. The button next to the article title ("Edit Wikipedia article") takes you to the edit page for the article directly within Wikipedia. You should be aware you are not editing our local copy of this information. Any changes that you make to the Wikipedia article will not be displayed here until we next download the article from Wikipedia. We currently download new content on a nightly basis.
Does Pfam agree with the content of the Wikipedia entry ?
Pfam has chosen to link families to Wikipedia articles. In some case we have created or edited these articles but in many other cases we have not made any direct contribution to the content of the article. The Wikipedia community does monitor edits to try to ensure that (a) the quality of article annotation increases, and (b) vandalism is very quickly dealt with. However, we would like to emphasise that Pfam does not curate the Wikipedia entries and we cannot guarantee the accuracy of the information on the Wikipedia page.
Editing Wikipedia articles
Before you edit for the first time
Wikipedia is a free, online encyclopedia. Although anyone can edit or contribute to an article, Wikipedia has some strong editing guidelines and policies, which promote the Wikipedia standard of style and etiquette. Your edits and contributions are more likely to be accepted (and remain) if they are in accordance with this policy.
You should take a few minutes to view the following pages:
How your contribution will be recorded
Anyone can edit a Wikipedia entry. You can do this either as a new user or you can register with Wikipedia and log on. When you click on the "Edit Wikipedia article" button, your browser will direct you to the edit page for this entry in Wikipedia. If you are a registered user and currently logged in, your changes will be recorded under your Wikipedia user name. However, if you are not a registered user or are not logged on, your changes will be logged under your computer's IP address. This has two main implications. Firstly, as a registered Wikipedia user your edits are more likely seen as valuable contribution (although all edits are open to community scrutiny regardless). Secondly, if you edit under an IP address you may be sharing this IP address with other users. If your IP address has previously been blocked (due to being flagged as a source of 'vandalism') your edits will also be blocked. You can find more information on this and creating a user account at Wikipedia.
If you have problems editing a particular page, contact us at email@example.com and we will try to help.
The community annotation is a new facility of the Pfam web site. If you have problems editing or experience problems with these pages please contact us.
GroES Edit Wikipedia article
|, heat shock 10kDa protein 1, CPN10, EPF, GROES, HSP10, heat shock protein family E (Hsp10) member 1|
gp31 co-chaperonin from bacteriophage t4
Heat shock 10 kDa protein 1 (Hsp10) also known as chaperonin 10 (cpn10) or early-pregnancy factor (EPF) is a protein that in humans is encoded by the HSPE1 gene. The homolog in E. coli is GroES that is a chaperonin which usually works in conjunction with GroEL.
Structure and function
GroES exists as a ring-shaped oligomer of between six and eight identical subunits, while the 60 kDa chaperonin (cpn60 - or groEL in bacteria) forms a structure comprising 2 stacked rings, each ring containing 7 identical subunits. These ring structures assemble by self-stimulation in the presence of Mg2+-ATP. The central cavity of the cylindrical cpn60 tetradecamer provides an isolated environment for protein folding whilst cpn-10 binds to cpn-60 and synchronizes the release of the folded protein in an Mg2+-ATP dependent manner. The binding of cpn10 to cpn60 inhibits the weak ATPase activity of cpn60.
Escherichia coli GroES has also been shown to bind ATP cooperatively, and with an affinity comparable to that of GroEL. Each GroEL subunit contains three structurally distinct domains: an apical, an intermediate and an equatorial domain. The apical domain contains the binding sites for both GroES and the unfolded protein substrate. The equatorial domain contains the ATP-binding site and most of the oligomeric contacts. The intermediate domain links the apical and equatorial domains and transfers allosteric information between them. The GroEL oligomer is a tetradecamer, cylindrically shaped, that is organised in two heptameric rings stacked back to back. Each GroEL ring contains a central cavity, known as the `Anfinsen cage', that provides an isolated environment for protein folding. The identical 10 kDa subunits of GroES form a dome-like heptameric oligomer in solution. ATP binding to GroES may be important in charging the seven subunits of the interacting GroEL ring with ATP, to facilitate cooperative ATP binding and hydrolysis for substrate protein release.
Early pregnancy factor is tested for rosette inhibition assay. EPF is present in the maternal serum (blood plasma) shortly after fertilization; EPF is also present in cervical mucus  and in amniotic fluid.
EPF may be detected in sheep within 72 hours of mating, in mice within 24 hours of mating, and in samples from media surrounding human embryos fertilized in vitro within 48 hours of fertilization (although another study failed to duplicate this finding for in vitro embryos). EPF has been detected as soon as within six hours of mating.
Because the rosette inhibition assay for EPF is indirect, substances that have similar effects may confound the test. Pig semen, like EPF, has been shown to inhibit rosette formation - the rosette inhibition test was positive for one day in sows mated with a vasectomized boar, but not in sows similarly stimulated without semen exposure. A number of studies in the years after the discovery of EPF were unable to reproduce the consistent detection of EPF in post-conception females, and the validity of the discovery experiments was questioned. However, progress in characterization of EPF has been made and its existence is well-accepted in the scientific community.
Early embryos are not believed to directly produce EPF. Rather, embryos are believed to produce some other chemical that induces the maternal system to create EPF. After implantation, EPF may be produced by the conceptus directly.
EPF is an immunosuppressant. Along with other substances associated with early embryos, EPF is believed to play a role in preventing the immune system of the pregnant female from attacking the embryo. Injecting anti-EPF antibodies into mice after mating significantly[quantify] reduced the number of successful pregnancies and number of pups; no effect on growth was seen when mice embryos were cultured in media containing anti-EPF antibodies. While some actions of EPF are the same in all mammals (namely rosette inhibition), other immunosuppressant mechanism vary between species.
In mice, EPF levels are high in early pregnancy, but on day 15 decline to levels found in non-pregnant mice. In humans, EPF levels are high for about the first twenty weeks, then decline, becoming undetectable within eight weeks of delivery.
It has been suggested that EPF could be used as a marker for a very early pregnancy test, and as a way to monitor the viability of ongoing pregnancies in livestock. Interest in EPF for this purpose has continued, although current test methods have not proved sufficiently accurate for the requirements of livestock management.
In humans, modern pregnancy tests detect human chorionic gonadotropin (hCG). hCG is not present until after implantation, which occurs six to twelve days after fertilization. In contrast, EPF is present within hours of fertilization. While several other pre-implantation signals have been identified, EPF is believed to be the earliest possible marker of pregnancy. The accuracy of EPF as a pregnancy test in humans has been found to be high by several studies.
Birth control research
EPF may also be used to determine whether pregnancy prevention mechanism of birth control methods act before or after fertilization. A 1982 study evaluating EPF levels in women with IUDs concluded that post-fertilization mechanisms contribute significantly[quantify] to the effectiveness of these devices. However, more recent evidence, such as tubal flushing studies indicates that IUDs work by inhibiting fertilization, acting earlier in the reproductive process than previously thought.
For groups that define pregnancy as beginning with fertilization, birth control methods that have postfertilization mechanisms are regarded as abortifacient. There is currently contention over whether hormonal contraception methods have post-fertilization methods, specifically the most popular hormonal method - the combined oral contraceptive pill (COCP). The group Pharmacists for Life has called for a large-scale clinical trial to evaluate EPF in women taking COCPs; this would be the most conclusive evidence available to determine whether COCPs have postfertilization mechanisms.
Infertility and early pregnancy loss
EPF is useful when investigating embryo loss prior to implantation. One study in healthy human women seeking pregnancy detected fourteen pregnancies with EPF. Of these, six were lost within ten days of ovulation (43% rate of early conceptus loss).
Use of EPF has been proposed to distinguish infertility caused by failure to conceive versus infertility caused by failure to implant. EPF has also been proposed as a marker of viable pregnancy, more useful in distinguishing ectopic or other nonviable pregnancies than other chemical markers such as hCG and progesterone.
As a tumour marker
Although almost exclusively associated with pregnancy, EPF-like activity has also been detected in tumors of germ cell origin and in other types of tumors. Its utility as a tumour marker, to evaluate the success of surgical treatment, has been suggested.
- GRCh38: Ensembl release 89: ENSG00000115541 - Ensembl, May 2017
- GRCm38: Ensembl release 89: ENSMUSG00000073676 - Ensembl, May 2017
- "Human PubMed Reference:".
- "Mouse PubMed Reference:".
- "Entrez Gene: HSPE1 heat shock 10kDa protein 1 (chaperonin 10)".
- Hemmingsen SM, Woolford C, van der Vies SM, Tilly K, Dennis DT, Georgopoulos CP, Hendrix RW, Ellis RJ (May 1988). "Homologous plant and bacterial proteins chaperone oligomeric protein assembly". Nature. 333 (6171): 330–4. doi:10.1038/333330a0. PMID 2897629.
- Schmidt A, Schiesswohl M, Völker U, Hecker M, Schumann W (June 1992). "Cloning, sequencing, mapping, and transcriptional analysis of the groESL operon from Bacillus subtilis". J. Bacteriol. 174 (12): 3993–9. PMC . PMID 1350777.
- Martin J, Geromanos S, Tempst P, Hartl FU (November 1993). "Identification of nucleotide-binding regions in the chaperonin proteins GroEL and GroES". Nature. 366 (6452): 279–82. doi:10.1038/366279a0. PMID 7901771.
- Samali A, Cai J, Zhivotovsky B, Jones DP, Orrenius S (April 1999). "Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of jurkat cells". EMBO J. 18 (8): 2040–8. doi:10.1093/emboj/18.8.2040. PMC . PMID 10205158.
- Lee KH, Kim HS, Jeong HS, Lee YS (October 2002). "Chaperonin GroESL mediates the protein folding of human liver mitochondrial aldehyde dehydrogenase in Escherichia coli". Biochem. Biophys. Res. Commun. 298 (2): 216–24. doi:10.1016/S0006-291X(02)02423-3. PMID 12387818.
- Cheng SJ, Zheng ZQ (Feb 2004). "Early pregnancy factor in cervical mucus of pregnant women". American Journal of Reproductive Immunology. 51 (2): 102–5. doi:10.1046/j.8755-8920.2003.00136.x. PMID 14748834.
- Zheng ZQ, Qin ZH, Ma AY, Qiao CX, Wang H (1990). "Detection of early pregnancy factor-like activity in human amniotic fluid". American Journal of Reproductive Immunology. 22 (1-2): 9–11. doi:10.1111/j.1600-0897.1990.tb01025.x. PMID 2346595.
- Morton H, Clunie GJ, Shaw FD (Mar 1979). "A test for early pregnancy in sheep". Research in Veterinary Science. 26 (2): 261–2. PMID 262615.
- Cavanagh AC, Morton H, Rolfe BE, Gidley-Baird AA (Apr 1982). "Ovum factor: a first signal of pregnancy?". American Journal of Reproductive Immunology. 2 (2): 97–101. doi:10.1111/j.1600-0897.1982.tb00093.x. PMID 7102890.
- Smart YC, Cripps AW, Clancy RL, Roberts TK, Lopata A, Shutt DA (Jan 1981). "Detection of an immunosuppressive factor in human preimplantation embryo cultures". The Medical Journal of Australia. 1 (2): 78–9. PMID 7231254.
- Nahhas F, Barnea E (1990). "Human embryonic origin early pregnancy factor before and after implantation". American Journal of Reproductive Immunology. 22 (3-4): 105–8. doi:10.1111/j.1600-0897.1990.tb00651.x. PMID 2375830.
- Shaw FD, Morton H (Mar 1980). "The immunological approach to pregnancy diagnosis: a review". The Veterinary Record. 106 (12): 268–70. doi:10.1136/vr.106.12.268. PMID 6966439.
- Koch E, Ellendorff F (May 1985). "Detection of activity similar to that of early pregnancy factor after mating sows with a vasectomized boar". Journal of Reproduction and Fertility. 74 (1): 39–46. doi:10.1530/jrf.0.0740039. PMID 4020773.
- Chard T, Grudzinskas JG (1987). "Early pregnancy factor". Biological Research in Pregnancy and Perinatology. 8 (2 2D Half): 53–6. PMID 3322417.
- Di Trapani G, Orosco C, Perkins A, Clarke F (Mar 1991). "Isolation from human placental extracts of a preparation possessing 'early pregnancy factor' activity and identification of the polypeptide components". Human Reproduction. 6 (3): 450–7. doi:10.1093/oxfordjournals.humrep.a137357. PMID 1955557.
- Cavanagh AC (Jan 1996). "Identification of early pregnancy factor as chaperonin 10: implications for understanding its role". Reviews of Reproduction. 1 (1): 28–32. doi:10.1530/ror.0.0010028. PMID 9414435.
- Orozco C, Perkins T, Clarke FM (Nov 1986). "Platelet-activating factor induces the expression of early pregnancy factor activity in female mice". Journal of Reproduction and Fertility. 78 (2): 549–55. doi:10.1530/jrf.0.0780549. PMID 3806515.
- Roberts TK, Adamson LM, Smart YC, Stanger JD, Murdoch RN (May 1987). "An evaluation of peripheral blood platelet enumeration as a monitor of fertilization and early pregnancy". Fertility and Sterility. 47 (5): 848–54. PMID 3569561.
- Sueoka K, Dharmarajan AM, Miyazaki T, Atlas SJ, Wallach EE (Dec 1988). "Platelet activating factor-induced early pregnancy factor activity from the perfused rabbit ovary and oviduct". American Journal of Obstetrics and Gynecology. 159 (6): 1580–4. doi:10.1016/0002-9378(88)90598-4. PMID 3207134.
- Cavanagh AC, Morton H, Athanasas-Platsis S, Quinn KA, Rolfe BE (Jan 1991). "Identification of a putative inhibitor of early pregnancy factor in mice". Journal of Reproduction and Fertility. 91 (1): 239–48. doi:10.1530/jrf.0.0910239. PMID 1995852.
- Cavanagh AC, Rolfe BE, Athanasas-Platsis S, Quinn KA, Morton H (Nov 1991). "Relationship between early pregnancy factor, mouse embryo-conditioned medium and platelet-activating factor". Journal of Reproduction and Fertility. 93 (2): 355–65. doi:10.1530/jrf.0.0930355. PMID 1787455.
- Bose R, Cheng H, Sabbadini E, McCoshen J, MaHadevan MM, Fleetham J (Apr 1989). "Purified human early pregnancy factor from preimplantation embryo possesses immunosuppresive properties". American Journal of Obstetrics and Gynecology. 160 (4): 954–60. doi:10.1016/0002-9378(89)90316-5. PMID 2712125.
- Igarashi S (Feb 1987). "[Significance of early pregnancy factor (EPF) on reproductive immunology]". Nihon Sanka Fujinka Gakkai Zasshi. 39 (2): 189–94. PMID 2950188.
- Athanasas-Platsis S, Quinn KA, Wong TY, Rolfe BE, Cavanagh AC, Morton H (Nov 1989). "Passive immunization of pregnant mice against early pregnancy factor causes loss of embryonic viability". Journal of Reproduction and Fertility. 87 (2): 495–502. doi:10.1530/jrf.0.0870495. PMID 2600905.
- Athanasas-Platsis S, Morton H, Dunglison GF, Kaye PL (Jul 1991). "Antibodies to early pregnancy factor retard embryonic development in mice in vivo". Journal of Reproduction and Fertility. 92 (2): 443–51. doi:10.1530/jrf.0.0920443. PMID 1886100.
- Rolfe BE, Cavanagh AC, Quinn KA, Morton H (Aug 1988). "Identification of two suppressor factors induced by early pregnancy factor". Clinical and Experimental Immunology. 73 (2): 219–25. PMC . PMID 3180511.
- Takimoto Y, Hishinuma M, Takahashi Y, Kanagawa H (Oct 1989). "Detection of early pregnancy factor in superovulated mice". Nihon Juigaku Zasshi. The Japanese Journal of Veterinary Science. 51 (5): 879–85. doi:10.1292/jvms1939.51.879. PMID 2607739.
- Qin ZH, Zheng ZQ (Jan 1987). "Detection of early pregnancy factor in human sera". American Journal of Reproductive Immunology and Microbiology. 13 (1): 15–8. doi:10.1111/j.1600-0897.1987.tb00082.x. PMID 2436493.
- Wang HN, Zheng ZQ (Jul 1990). "Detection of early pregnancy factor in fetal sera". American Journal of Reproductive Immunology. 23 (3): 69–72. doi:10.1111/j.1600-0897.1990.tb00674.x. PMID 2257053.
- Sakonju I, Enomoto S, Kamimura S, Hamana K (Apr 1993). "Monitoring bovine embryo viability with early pregnancy factor". The Journal of Veterinary Medical Science / the Japanese Society of Veterinary Science. 55 (2): 271–4. doi:10.1292/jvms.55.271. PMID 8513008.
- Greco CR, Vivas AB, Bosch RA (1992). "[Evaluation of the method for early pregnancy factor detection (EPF) in swine. Significance in early pregnancy diagnosis]". Acta Physiologica, Pharmacologica et Therapeutica Latinoamericana. 42 (1): 43–50. PMID 1294272.
- Sasser RG, Ruder CA (1987). "Detection of early pregnancy in domestic ruminants". Journal of Reproduction and Fertility. Supplement. 34: 261–71. PMID 3305923.
- Gandy B, Tucker W, Ryan P, Williams A, Tucker A, Moore A, Godfrey R, Willard S (Sep 2001). "Evaluation of the early conception factor (ECF) test for the detection of nonpregnancy in dairy cattle". Theriogenology. 56 (4): 637–47. doi:10.1016/S0093-691X(01)00595-7. PMID 11572444.
- Cordoba MC, Sartori R, Fricke PM (Aug 2001). "Assessment of a commercially available early conception factor (ECF) test for determining pregnancy status of dairy cattle". Journal of Dairy Science. 84 (8): 1884–9. doi:10.3168/jds.S0022-0302(01)74629-2. PMID 11518314.
- Wilcox AJ, Baird DD, Weinberg CR (Jun 1999). "Time of implantation of the conceptus and loss of pregnancy". The New England Journal of Medicine. 340 (23): 1796–9. doi:10.1056/NEJM199906103402304. PMID 10362823.
- Straube W (1989). "[Early embryonal signals]". Zentralblatt für Gynäkologie. 111 (10): 629–33. PMID 2665388.
- Smart YC, Roberts TK, Fraser IS, Cripps AW, Clancy RL (Jun 1982). "Validation of the rosette inhibition test for the detection of early pregnancy in women". Fertility and Sterility. 37 (6): 779–85. PMID 6177559.
- Bessho T, Taira S, Ikuma K, Shigeta M, Koyama K, Isojima S (Mar 1984). "[Detection of early pregnancy factor in the sera of conceived women before nidation]". Nihon Sanka Fujinka Gakkai Zasshi. 36 (3): 391–6. PMID 6715922.
- Straube W, Tiemann U, Loh M, Schütz M (1989). "Detection of early pregnancy factor (EPF) in pregnant and nonpregnant subjects with the rosette inhibition test". Archives of Gynecology and Obstetrics. 246 (3): 181–7. doi:10.1007/BF00934079. PMID 2619332.
- Fan XG, Zheng ZQ (May 1997). "A study of early pregnancy factor activity in preimplantation". American Journal of Reproductive Immunology. 37 (5): 359–64. doi:10.1111/j.1600-0897.1997.tb00244.x. PMID 9196793.
- Smart YC, Fraser IS, Clancy RL, Roberts TK, Cripps AW (Feb 1982). "Early pregnancy factor as a monitor for fertilization in women wearing intrauterine devices". Fertility and Sterility. 37 (2): 201–4. PMID 6174375.
- Grimes, David (2007). "Intrauterine Devices (IUDs)". In Hatcher, Robert A.; et al. Contraceptive Technology (19th rev. ed.). New York: Ardent Media. p. 120. ISBN 0-9664902-0-7.
- Lloyd J DuPlantis, Jr (2001). "Early Pregnancy Factor". Pharmacists for Life, Intl. Retrieved 2007-01-01.
- Smart YC, Fraser IS, Roberts TK, Clancy RL, Cripps AW (Sep 1982). "Fertilization and early pregnancy loss in healthy women attempting conception". Clinical Reproduction and Fertility. 1 (3): 177–84. PMID 6196101.
- Mesrogli M, Maas DH, Schneider J (1988). "[Early abortion rate in sterility patients: early pregnancy factor as a parameter]". Zentralblatt für Gynäkologie. 110 (9): 555–61. PMID 3407357.
- Straube W, Loh M, Leipe S (Dec 1988). "[Significance of the detection of early pregnancy factor for monitoring normal and disordered early pregnancy]". Geburtshilfe Und Frauenheilkunde. 48 (12): 854–8. doi:10.1055/s-2008-1026640. PMID 2466731.
- Gerhard I, Katzer E, Runnebaum B (1991). "The early pregnancy factor (EPF) in pregnancies of women with habitual abortions". Early Human Development. 26 (2): 83–92. doi:10.1016/0378-3782(91)90012-R. PMID 1720719.
- Shu-Xin H, Zhen-Qun Z (Mar 1993). "A study of early pregnancy factor activity in the sera of patients with unexplained spontaneous abortion". American Journal of Reproductive Immunology. 29 (2): 77–81. doi:10.1111/j.1600-0897.1993.tb00569.x. PMID 8329108.
- Shahani SK, Moniz CL, Bordekar AD, Gupta SM, Naik K (1994). "Early pregnancy factor as a marker for assessing embryonic viability in threatened and missed abortions". Gynecologic and Obstetric Investigation. 37 (2): 73–6. doi:10.1159/000292528. PMID 8150373.
- Rolfe BE, Morton H, Cavanagh AC, Gardiner RA (Mar 1983). "Detection of an early pregnancy factor-like substance in sera of patients with testicular germ cell tumors". American Journal of Reproductive Immunology. 3 (2): 97–100. doi:10.1111/j.1600-0897.1983.tb00223.x. PMID 6859385.
- Mehta AR, Shahani SK (Jul 1987). "Detection of early pregnancy factor-like activity in women with gestational trophoblastic tumors". American Journal of Reproductive Immunology and Microbiology. 14 (3): 67–9. doi:10.1111/j.1600-0897.1987.tb00122.x. PMID 2823620.
- Quinn KA, Athanasas-Platsis S, Wong TY, Rolfe BE, Cavanagh AC, Morton H (Apr 1990). "Monoclonal antibodies to early pregnancy factor perturb tumour cell growth". Clinical and Experimental Immunology. 80 (1): 100–8. doi:10.1111/j.1365-2249.1990.tb06448.x. PMC . PMID 2323098.
- Bojahr B, Straube W, Reddemann H (1993). "[Case observations on the significance of early pregnancy factor as a tumor marker]". Zentralblatt für Gynäkologie. 115 (3): 125–8. PMID 7682025.
- Czarnecka AM, Campanella C, Zummo G, Cappello F (2006). "Heat shock protein 10 and signal transduction: a "capsula eburnea" of carcinogenesis?". Cell Stress Chaperones. 11 (4): 287–94. doi:10.1379/CSC-200.1. PMC . PMID 17278877.
- Legname G, Fossati G, Gromo G, Monzini N, Marcucci F, Modena D (1995). "Expression in Escherichia coli, purification and functional activity of recombinant human chaperonin 10". FEBS Lett. 361 (2-3): 211–4. doi:10.1016/0014-5793(95)00184-B. PMID 7698325.
- Cavanagh AC, Morton H (1994). "The purification of early-pregnancy factor to homogeneity from human platelets and identification as chaperonin 10". Eur. J. Biochem. 222 (2): 551–60. doi:10.1111/j.1432-1033.1994.tb18897.x. PMID 7912672.
- Monzini N, Legname G, Marcucci F, Gromo G, Modena D (1994). "Identification and cloning of human chaperonin 10 homologue". Biochim. Biophys. Acta. 1218 (3): 478–80. doi:10.1016/0167-4781(94)90211-9. PMID 7914093.
- Chen JJ, McNealy DJ, Dalal S, Androphy EJ (1994). "Isolation, sequence analysis and characterization of a cDNA encoding human chaperonin 10". Biochim. Biophys. Acta. 1219 (1): 189–90. doi:10.1016/0167-4781(94)90268-2. PMID 7916212.
- Samali A, Cai J, Zhivotovsky B, Jones DP, Orrenius S (1999). "Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of jurkat cells". EMBO J. 18 (8): 2040–8. doi:10.1093/emboj/18.8.2040. PMC . PMID 10205158.
- Summers KM, Fletcher BH, Macaranas DD, Somodevilla-Torres MJ, Murphy RM, Osborne MJ, Spurr NK, Cassady AI, Cavanagh AC (1998). "Mapping and characterization of the eukaryotic early pregnancy factor/chaperonin 10 gene family". Somat. Cell Mol. Genet. 24 (6): 315–26. doi:10.1023/A:1024488422990. PMID 10763410.
- Richardson A, Schwager F, Landry SJ, Georgopoulos C (2001). "The importance of a mobile loop in regulating chaperonin/ co-chaperonin interaction: humans versus Escherichia coli". J. Biol. Chem. 276 (7): 4981–7. doi:10.1074/jbc.M008628200. PMID 11050098.
- Fletcher BH, Cassady AI, Summers KM, Cavanagh AC (2001). "The murine chaperonin 10 gene family contains an intronless, putative gene for early pregnancy factor, Cpn10-rs1". Mamm. Genome. 12 (2): 133–40. doi:10.1007/s003350010250. PMID 11210183.
- Parissi V, Calmels C, De Soultrait VR, Caumont A, Fournier M, Chaignepain S, Litvak S (2001). "Functional interactions of human immunodeficiency virus type 1 integrase with human and yeast HSP60". J. Virol. 75 (23): 11344–53. doi:10.1128/JVI.75.23.11344-11353.2001. PMC . PMID 11689615.
- Hansen JJ, Dürr A, Cournu-Rebeix I, Georgopoulos C, Ang D, Nielsen MN, Davoine CS, Brice A, Fontaine B, Gregersen N, Bross P (2002). "Hereditary spastic paraplegia SPG13 is associated with a mutation in the gene encoding the mitochondrial chaperonin Hsp60". Am. J. Hum. Genet. 70 (5): 1328–32. doi:10.1086/339935. PMC . PMID 11898127.
- Guidry JJ, Wittung-Stafshede P (2002). "Low stability for monomeric human chaperonin protein 10: interprotein interactions contribute majority of oligomer stability". Arch. Biochem. Biophys. 405 (2): 280–2. doi:10.1016/S0003-9861(02)00406-X. PMID 12220543.
- Lee KH, Kim HS, Jeong HS, Lee YS (2002). "Chaperonin GroESL mediates the protein folding of human liver mitochondrial aldehyde dehydrogenase in Escherichia coli". Biochem. Biophys. Res. Commun. 298 (2): 216–24. doi:10.1016/S0006-291X(02)02423-3. PMID 12387818.
- Hansen JJ, Bross P, Westergaard M, Nielsen MN, Eiberg H, Børglum AD, Mogensen J, Kristiansen K, Bolund L, Gregersen N (2003). "Genomic structure of the human mitochondrial chaperonin genes: HSP60 and HSP10 are localised head to head on chromosome 2 separated by a bidirectional promoter". Hum. Genet. 112 (1): 71–7. doi:10.1007/s00439-002-0837-9. PMID 12483302.
- Mansell JP, Yarram SJ, Brown NL, Sandy JR (2002). "Type I collagen synthesis by human osteoblasts in response to placental lactogen and chaperonin 10, a homolog of early-pregnancy factor". In Vitro Cell. Dev. Biol. Anim. 38 (9): 518–22. doi:10.1290/1071-2690(2002)038<0518:TICSBH>2.0.CO;2. PMID 12703979.
- Cappello F, Bellafiore M, David S, Anzalone R, Zummo G (2003). "Ten kilodalton heat shock protein (HSP10) is overexpressed during carcinogenesis of large bowel and uterine exocervix". Cancer Lett. 196 (1): 35–41. doi:10.1016/S0304-3835(03)00212-X. PMID 12860287.
- Shan YX, Liu TJ, Su HF, Samsamshariat A, Mestril R, Wang PH (2003). "Hsp10 and Hsp60 modulate Bcl-2 family and mitochondria apoptosis signaling induced by doxorubicin in cardiac muscle cells". J. Mol. Cell. Cardiol. 35 (9): 1135–43. doi:10.1016/S0022-2828(03)00229-3. PMID 12967636.
- Shan YX, Yang TL, Mestril R, Wang PH (2003). "Hsp10 and Hsp60 suppress ubiquitination of insulin-like growth factor-1 receptor and augment insulin-like growth factor-1 receptor signaling in cardiac muscle: implications on decreased myocardial protection in diabetic cardiomyopathy". J. Biol. Chem. 278 (46): 45492–8. doi:10.1074/jbc.M304498200. PMID 12970367.
- Guidry JJ, Shewmaker F, Maskos K, Landry S, Wittung-Stafshede P (2003). "Probing the interface in a human co-chaperonin heptamer: residues disrupting oligomeric unfolded state identified". BMC Biochem. 4: 14. doi:10.1186/1471-2091-4-14. PMC . PMID 14525625.
- GroES Protein at the US National Library of Medicine Medical Subject Headings (MeSH)
- 3D macromolecular structures of GroES in EMDB
This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Chaperonin 10 Kd subunit Provide feedback
This family contains GroES and Gp31-like chaperonins. Gp31 is a functional co-chaperonin that is required for the folding and assembly of Gp23, a major capsid protein, during phage morphogenesis .
Hunt JF, van der Vies SM, Henry L, Deisenhofer J; , Cell 1997;90:361-371.: Structural adaptations in the specialized bacteriophage T4 co-chaperonin Gp31 expand the size of the Anfinsen cage. PUBMED:9244309 EPMC:9244309
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR020818
The chaperonins are `helper' molecules required for correct folding and subsequent assembly of some proteins [PUBMED:1349837]. These are required for normal cell growth [PUBMED:2897629], and are stress-induced, acting to stabilise or protect disassembled polypeptides under heat-shock conditions. Type I chaperonins present in eubacteria, mitochondria and chloroplasts require the concerted action of 2 proteins, chaperonin 60 (cpn60) and chaperonin 10 (cpn10) [PUBMED:12354603].
The 10 kDa chaperonin (cpn10 - or groES in bacteria) exists as a ring-shaped oligomer of between six to eight identical subunits, while the 60 kDa chaperonin (cpn60 - or groEL in bacteria) forms a structure comprising 2 stacked rings, each ring containing 7 identical subunits [PUBMED:2897629]. These ring structures assemble by self-stimulation in the presence of Mg2+-ATP. The central cavity of the cylindrical cpn60 tetradecamer provides as isolated environment for protein folding whilst cpn-10 binds to cpn-60 and synchronizes the release of the folded protein in an Mg2+-ATP dependent manner [PUBMED:1350777]. The binding of cpn10 to cpn60 inhibits the weak ATPase activity of cpn60.
Escherichia coli GroES has also been shown to bind ATP cooperatively, and with an affinity comparable to that of GroEL [PUBMED:7901771]. Each GroEL subunit contains three structurally distinct domains: an apical, an intermediate and an equatorial domain. The apical domain contains the binding sites for both GroES and the unfolded protein substrate. The equatorial domain contains the ATP-binding site and most of the oligomeric contacts. The intermediate domain links the apical and equatorial domains and transfers allosteric information between them. The GroEL oligomer is a tetradecamer, cylindrically shaped, that is organised in two heptameric rings stacked back to back. Each GroEL ring contains a central cavity, known as the `Anfinsen cage', that provides an isolated environment for protein folding. The identical 10 kDa subunits of GroES form a dome-like heptameric oligomer in solution. ATP binding to GroES may be important in charging the seven subunits of the interacting GroEL ring with ATP, to facilitate cooperative ATP binding and hydrolysis for substrate protein release.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||cytoplasm (GO:0005737)|
|Biological process||protein folding (GO:0006457)|
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
The graphic that is shown by default represents the longest sequence with a given architecture. Each row contains the following information:
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- a link to the page in the Pfam site showing information about the sequence that the graphic describes
- the UniProt description of the protein sequence
- the number of residues in the sequence
- the Pfam graphic itself.
Note that you can see the family page for a particular domain by clicking on the graphic. You can also choose to see all sequences which have a given architecture by clicking on the Show link in each row.
Finally, because some families can be found in a very large number of architectures, we load only the first fifty architectures by default. If you want to see more architectures, click the button at the bottom of the page to load the next set.
Loading domain graphics...
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...
There are various ways to view or download the sequence alignments that we store. We provide several sequence viewers and a plain-text Stockholm-format file for download.
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the UniProtKB sequence database using the family HMM
- alignment generated by searching the NCBI sequence database using the family HMM
- alignment generated by searching the metagenomics sequence database using the family HMM
You can see the alignments as HTML or in three different sequence viewers:
- a Java applet developed at the University of Dundee. You will need Java installed before running jalview
- an HTML page showing the whole alignment.Please note: full Pfam alignments can be very large. These HTML views are extremely large and often cause problems for browsers. Please use either jalview or the Pfam viewer if you have trouble viewing the HTML version
- an HTML-based representation of the alignment, coloured according to the posterior-probability (PP) values from the HMM. As for the standard HTML view, heatmap alignments can also be very large and slow to render.
You can download (or view in your browser) a text representation of a Pfam alignment in various formats:
You can also change the order in which sequences are listed in the alignment, change how insertions are represented, alter the characters that are used to represent gaps in sequences and, finally, choose whether to download the alignment or to view it in your browser directly.
You may find that large alignments cause problems for the viewers and the reformatting tool, so we also provide all alignments in Stockholm format. You can download either the plain text alignment, or a gzipped version of it.
We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
Format an alignment
We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
If you find these logos useful in your own work, please consider citing the following article:
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
|Author:||Sonnhammer ELL, Finn RD|
|Number in seed:||39|
|Number in full:||6444|
|Average length of the domain:||91.10 aa|
|Average identity of full alignment:||42 %|
|Average coverage of the sequence by the domain:||86.52 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 26740544 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||20|
|Download:||download the raw HMM for this family|
Weight segments by...
Change the size of the sunburst
selected sequences to HMM
a FASTA-format file
- 0 sequences
- 0 species
This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the More....
This chart is a modified "sunburst" visualisation of the species tree for this family. It shows each node in the tree as a separate arc, arranged radially with the superkingdoms at the centre and the species arrayed around the outermost ring.
How the sunburst is generated
The tree is built by considering the taxonomic lineage of each sequence that has a match to this family. For each node in the resulting tree, we draw an arc in the sunburst. The radius of the arc, its distance from the root node at the centre of the sunburst, shows the taxonomic level ("superkingdom", "kingdom", etc). The length of the arc represents either the number of sequences represented at a given level, or the number of species that are found beneath the node in the tree. The weighting scheme can be changed using the sunburst controls.
In order to reduce the complexity of the representation, we reduce the number of taxonomic levels that we show. We consider only the following eight major taxonomic levels:
Colouring and labels
Segments of the tree are coloured approximately according to their superkingdom. For example, archeal branches are coloured with shades of orange, eukaryotes in shades of purple, etc. The colour assignments are shown under the sunburst controls. Where space allows, the name of the taxonomic level will be written on the arc itself.
As you move your mouse across the sunburst, the current node will be highlighted. In the top section of the controls panel we show a summary of the lineage of the currently highlighed node. If you pause over an arc, a tooltip will be shown, giving the name of the taxonomic level in the title and a summary of the number of sequences and species below that node in the tree.
Anomalies in the taxonomy tree
There are some situations that the sunburst tree cannot easily handle and for which we have work-arounds in place.
Missing taxonomic levels
Some species in the taxonomic tree may not have one or more of the main eight levels that we display. For example, Bos taurus is not assigned an order in the NCBI taxonomic tree. In such cases we mark the omitted level with, for example, "No order", in both the tooltip and the lineage summary.
Unmapped species names
The tree is built by looking at each sequence in the full alignment for the family. We take the name of the species given by UniProt and try to map that to the full taxonomic tree from NCBI. In some cases, the name chosen by UniProt does not map to any node in the NCBI tree, perhaps because the chosen name is listed as a synonym or a misspelling in the NCBI taxonomy.
So that these nodes are not simply omitted from the sunburst tree, we group them together in a separate branch (or segment of the sunburst tree). Since we cannot determine the lineage for these unmapped species, we show all levels between the superkingdom and the species as "uncategorised".
Since we reduce the species tree to only the eight main taxonomic levels, sequences that are mapped to the sub-species level in the tree would not normally be shown. Rather than leave out these species, we map them instead to their parent species. So, for example, for sequences belonging to one of the Vibrio cholerae sub-species in the NCBI taxonomy, we show them instead as belonging to the species Vibrio cholerae.
Too many species/sequences
For large species trees, you may see blank regions in the outer layers of the sunburst. These occur when there are large numbers of arcs to be drawn in a small space. If an arc is less than approximately one pixel wide, it will not be drawn and the space will be left blank. You may still be able to get some information about the species in that region by moving your mouse across the area, but since each arc will be very small, it will be difficult to accurately locate a particular species.
The tree shows the occurrence of this domain across different species. More...
We show the species tree in one of two ways. For smaller trees we try to show an interactive representation, which allows you to select specific nodes in the tree and view them as an alignment or as a set of Pfam domain graphics.
Unfortunately we have found that there are problems viewing the interactive tree when the it becomes larger than a certain limit. Furthermore, we have found that Internet Explorer can become unresponsive when viewing some trees, regardless of their size. We therefore show a text representation of the species tree when the size is above a certain limit or if you are using Internet Explorer to view the site.
If you are using IE you can still load the interactive tree by clicking the "Generate interactive tree" button, but please be aware of the potential problems that the interactive species tree can cause.
For all of the domain matches in a full alignment, we count the number that are found on all sequences in the alignment. This total is shown in the purple box.
We also count the number of unique sequences on which each domain is found, which is shown in green. Note that a domain may appear multiple times on the same sequence, leading to the difference between these two numbers.
Finally, we group sequences from the same organism according to the NCBI code that is assigned by UniProt, allowing us to count the number of distinct sequences on which the domain is found. This value is shown in the pink boxes.
We use the NCBI species tree to group organisms according to their taxonomy and this forms the structure of the displayed tree. Note that in some cases the trees are too large (have too many nodes) to allow us to build an interactive tree, but in most cases you can still view the tree in a plain text, non-interactive representation. Those species which are represented in the seed alignment for this domain are highlighted.
You can use the tree controls to manipulate how the interactive tree is displayed:
- show/hide the summary boxes
- highlight species that are represented in the seed alignment
- expand/collapse the tree or expand it to a given depth
- select a sub-tree or a set of species within the tree and view them graphically or as an alignment
- save a plain text representation of the tree
Please note: for large trees this can take some time. While the tree is loading, you can safely switch away from this tab but if you browse away from the family page entirely, the tree will not be loaded.
There are 2 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Cpn10 domain has been found. There are 200 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.
Loading structure mapping...