ID CH10_HUMAN Reviewed; 102 AA. AC P61604; O95421; Q04984; Q53X54; Q9UDH0; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 04-NOV-2026, entry version 184. DE RecName: Full=10 kDa heat shock protein, mitochondrial; DE Short=Hsp10; DE AltName: Full=10 kDa chaperonin; DE AltName: Full=Chaperonin 10; DE Short=CPN10; DE AltName: Full=Early-pregnancy factor; DE Short=EPF; DE AltName: Full=Heat shock protein family E member 1; GN Name=HSPE1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=7914093; DOI=10.1016/0167-4781(94)90211-9; RA Monzini N., Legname G., Marcucci F., Gromo G., Modena D.; RT "Identification and cloning of human chaperonin 10 homologue."; RL Biochim. Biophys. Acta 1218:478-480(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=7916212; DOI=10.1016/0167-4781(94)90268-2; RA Chen J.J., McNealy D.J., Dalal S., Androphy E.J.; RT "Isolation, sequence analysis and characterization of a cDNA encoding human RT chaperonin 10."; RL Biochim. Biophys. Acta 1219:189-190(1994). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=12483302; DOI=10.1007/s00439-002-0837-9; RA Hansen J.J., Bross P., Westergaard M., Nielsen M.N., Eiberg H., RA Boerglum A.D., Mogensen J., Kristiansen K., Bolund L., Gregersen N.; RT "Genomic structure of the human mitochondrial chaperonin genes: HSP60 and RT HSP10 are localised head to head on chromosome 2 separated by a RT bidirectional promoter."; RL Hum. Genet. 112:71-77(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-100. RX PubMed=10763410; DOI=10.1023/a:1024488422990; RA Summers K.M., Fletcher B.H., Macaranas D.D., Somodevilla-Torres M.J., RA Murphy R.M., Osborne M.J., Spurr N.K., Cassady A.I., Cavanagh A.C.; RT "Mapping and characterization of the eukaryotic early pregnancy RT factor/chaperonin 10 gene family."; RL Somat. Cell Mol. Genet. 24:315-326(1998). RN [10] RP PROTEIN SEQUENCE OF 2-15; 41-54; 57-66 AND 81-92, CLEAVAGE OF INITIATOR RP METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V.; RL Submitted (MAR-2005) to UniProtKB. RN [11] RP PROTEIN SEQUENCE OF 8-19; 28-54 AND 70-102, MASS SPECTROMETRY, AND RP FUNCTION. RC TISSUE=Platelet; RX PubMed=7912672; DOI=10.1111/j.1432-1033.1994.tb18897.x; RA Cavanagh A.C., Morton H.; RT "The purification of early-pregnancy factor to homogeneity from human RT platelets and identification as chaperonin 10."; RL Eur. J. Biochem. 222:551-560(1994). RN [12] RP FUNCTION. RX PubMed=1346131; DOI=10.1016/s0021-9258(18)48338-x; RA Viitanen P.V., Lorimer G.H., Seetharam R., Gupta R.S., Oppenheim J., RA Thomas J.O., Cowan N.J.; RT "Mammalian mitochondrial chaperonin 60 functions as a single toroidal RT ring."; RL J. Biol. Chem. 267:695-698(1992). RN [13] RP FUNCTION. RX PubMed=11422376; DOI=10.1046/j.1432-1327.2001.02243.x; RA Levy-Rimler G., Viitanen P., Weiss C., Sharkia R., Greenberg A., Niv A., RA Lustig A., Delarea Y., Azem A.; RT "The effect of nucleotides and mitochondrial chaperonin 10 on the structure RT and chaperone activity of mitochondrial chaperonin 60."; RL Eur. J. Biochem. 268:3465-3472(2001). RN [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-56; LYS-86 AND LYS-99, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-79, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [17] RP MALONYLATION AT LYS-40; LYS-54 AND LYS-56. RX PubMed=21908771; DOI=10.1074/mcp.m111.012658; RA Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y., He W., RA Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., Dai J., RA Verdin E., Ye Y., Zhao Y.; RT "The first identification of lysine malonylation substrates and its RT regulatory enzyme."; RL Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [20] RP X-RAY CRYSTALLOGRAPHY, SUBUNIT, AND FUNCTION. RX PubMed=25918392; DOI=10.1073/pnas.1411718112; RA Nisemblat S., Yaniv O., Parnas A., Frolow F., Azem A.; RT "Crystal structure of the human mitochondrial chaperonin symmetrical RT football complex."; RL Proc. Natl. Acad. Sci. U.S.A. 112:6044-6049(2015). CC -!- FUNCTION: Co-chaperonin implicated in mitochondrial protein import and CC macromolecular assembly. Together with Hsp60, facilitates the correct CC folding of imported proteins. May also prevent misfolding and promote CC the refolding and proper assembly of unfolded polypeptides generated CC under stress conditions in the mitochondrial matrix (PubMed:11422376, CC PubMed:1346131, PubMed:7912672). The functional units of these CC chaperonins consist of heptameric rings of the large subunit Hsp60, CC which function as a back-to-back double ring. In a cyclic reaction, CC Hsp60 ring complexes bind one unfolded substrate protein per ring, CC followed by the binding of ATP and association with 2 heptameric rings CC of the co-chaperonin Hsp10. This leads to sequestration of the CC substrate protein in the inner cavity of Hsp60 where, for a certain CC period of time, it can fold undisturbed by other cell components. CC Synchronous hydrolysis of ATP in all Hsp60 subunits results in the CC dissociation of the chaperonin rings and the release of ADP and the CC folded substrate protein (Probable). {ECO:0000269|PubMed:11422376, CC ECO:0000269|PubMed:1346131, ECO:0000269|PubMed:7912672, CC ECO:0000305|PubMed:25918392}. CC -!- SUBUNIT: Homoheptamer arranged in a ring structure (PubMed:25918392). 2 CC heptameric Hsp10 rings interact with a Hsp60 tetradecamer in the CC structure of a back-to-back double heptameric ring to form the CC symmetrical football complex (PubMed:25918392). CC {ECO:0000269|PubMed:25918392}. CC -!- INTERACTION: CC P61604; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-711483, EBI-741158; CC P61604; Q8WWX9: SELENOM; NbExp=3; IntAct=EBI-711483, EBI-10277687; CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. CC -!- INDUCTION: By stress. CC -!- MASS SPECTROMETRY: Mass=10843.5; Mass_error=0.2; Method=Electrospray; CC Evidence={ECO:0000269|PubMed:7912672}; CC -!- SIMILARITY: Belongs to the GroES chaperonin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X75821; CAA53455.1; -; mRNA. DR EMBL; U07550; AAA50953.1; -; mRNA. DR EMBL; AJ250915; CAB75425.1; -; Genomic_DNA. DR EMBL; AK312104; BAG35040.1; -; mRNA. DR EMBL; CR407688; CAG28616.1; -; mRNA. DR EMBL; AC020550; AAX93146.1; -; Genomic_DNA. DR EMBL; CH471063; EAW70163.1; -; Genomic_DNA. DR EMBL; BC023518; AAH23518.1; -; mRNA. DR EMBL; AH007060; AAC95387.1; -; Genomic_DNA. DR CCDS; CCDS2320.1; -. DR PIR; S47532; S47532. DR RefSeq; NP_002148.1; NM_002157.3. DR PDB; 4PJ1; X-ray; 3.15 A; 1/2/O/P/Q/R/S/T/U/V/W/X/Y/Z=1-102. DR PDB; 6HT7; X-ray; 3.70 A; 1/2/O/P/Q/R/S/T/U/V/W/X/Y/Z=1-102. DR PDB; 6MRC; EM; 3.08 A; 1/2/O/P/Q/R/S/T/U/V/W/X/Y/Z=3-102. DR PDB; 6MRD; EM; 3.82 A; O/P/Q/R/S/T/U=3-102. DR PDB; 8G7N; EM; 2.70 A; 1/2/M/O/P/Q/R/S/T/U/V/W/X/Z=1-102. DR PDB; 8G7O; EM; 3.40 A; H/I/J/K/L/M/N=3-102. DR PDB; 9ES0; EM; 2.58 A; a/b/c/d/e/f/g/h/i/j/k/l/m/n=1-102. DR PDB; 9ES1; EM; 2.95 A; a/b/c/d/e/f/g=1-102. DR PDB; 9ES4; EM; 2.91 A; a/b/c/d/e/f/g/h/i/j/k/l/m/n=1-102. DR PDB; 9ES5; EM; 3.50 A; a/b/c/d/e/f/g=1-102. DR PDB; 9H5S; EM; 2.98 A; a/b/c/d/e/f/g/h/i/j/k/l/m/n=1-102. DR PDB; 9H5T; EM; 3.44 A; a/b/c/d/e/f/g=1-102. DR PDB; 9L8P; EM; 7.30 A; 1/2/M/O/P/Q/R/S/T/U/V/W/X/Z=1-102. DR PDB; 9SHG; EM; 1.91 A; a/b/c/d/e/f/g/h/i/j/k/l/m/n=1-102. DR PDB; 9SHH; EM; 2.11 A; a/b/c/d/e/f/g=1-102. DR PDB; 9SHI; EM; 2.19 A; a/b/c/d/e/f/g=1-102. DR AlphaFoldDB; P61604; -. DR EMDB; EMD-19930; -. DR EMDB; EMD-19931; -. DR EMDB; EMD-19934; -. DR EMDB; EMD-19935; -. DR EMDB; EMD-29817; -. DR EMDB; EMD-29818; -. DR EMDB; EMD-51890; -. DR EMDB; EMD-51891; -. DR EMDB; EMD-54898; -. DR EMDB; EMD-54899; -. DR EMDB; EMD-54900; -. DR EMDB; EMD-9195; -. DR EMDB; EMD-9196; -. DR SMR; P61604; -. DR BioGRID; 109568; 344. DR FunCoup; P61604; 1351. DR IntAct; P61604; 119. DR NDEx; IQUERY-CP-HSPE1; 1 NDEx IQuery Curated Pathway. DR STRING; 9606.ENSP00000233893; -. DR BindingDB; P61604; -. DR ChEMBL; CHEMBL3808268; -. DR DrugBank; DB12695; Phenethyl Isothiocyanate. DR GlyCosmos; P61604; 1 site, 1 glycan. DR GlyGen; P61604; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P61604; -. DR MetOSite; P61604; -. DR PhosphoSitePlus; P61604; -. DR SwissPalm; P61604; -. DR BioMuta; HSPE1; -. DR DMDM; 47606335; -. DR jPOST; P61604; -. DR MassIVE; P61604; -. DR PaxDb; 9606-ENSP00000233893; -. DR PeptideAtlas; P61604; -. DR ProteomicsDB; 57325; -. DR Pumba; P61604; -. DR TopDownProteomics; P61604; -. DR Antibodypedia; 3376; 592 antibodies from 42 providers. DR DNASU; 3336; -. DR Ensembl; ENST00000233893.10; ENSP00000233893.5; ENSG00000115541.12. DR GeneID; 3336; -. DR KEGG; hsa:3336; -. DR MANE-Select; ENST00000233893.10; ENSP00000233893.5; NM_002157.3; NP_002148.1. DR UCSC; uc002uul.4; human. DR AGR; HGNC:5269; -. DR ClinPGx; PA29535; -. DR CTD; 3336; -. DR DisGeNET; 3336; -. DR GeneCards; HSPE1; -. DR HGNC; HGNC:5269; HSPE1. DR HPA; ENSG00000115541; Tissue enhanced (adrenal). DR MIM; 600141; gene. DR OpenTargets; ENSG00000115541; -. DR VEuPathDB; HostDB:ENSG00000115541; -. DR eggNOG; KOG1641; Eukaryota. DR GeneTree; ENSGT00390000006350; -. DR HOGENOM; CLU_132825_0_1_1; -. DR InParanoid; P61604; -. DR OMA; ACPLSHV; -. DR OrthoDB; 9525814at2759; -. DR PAN-GO; P61604; 6 GO annotations based on evolutionary models. DR PhylomeDB; P61604; -. DR PathwayCommons; P61604; -. DR Reactome; R-HSA-9013408; RHOG GTPase cycle. DR Reactome; R-HSA-9841251; Mitochondrial unfolded protein response (UPRmt). DR SignaLink; P61604; -. DR Agora; ENSG00000115541; -. DR BioGRID-ORCS; 3336; 731 hits in 1050 CRISPR screens. DR CD-CODE; 91857CE7; Nucleolus. DR ChiTaRS; HSPE1; human. DR EvolutionaryTrace; P61604; -. DR GeneWiki; GroES; -. DR GenomeRNAi; 3336; -. DR Pharos; P61604; Tbio. DR PRO; PR:P61604; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; P61604; protein. DR Bgee; ENSG00000115541; Expressed in adrenal tissue and 101 other cell types or tissues. DR ExpressionAtlas; P61604; baseline and differential. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IBA:GO_Central. DR GO; GO:0044183; F:protein folding chaperone; IEA:InterPro. DR GO; GO:0051087; F:protein-folding chaperone binding; IPI:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; NAS:UniProtKB. DR GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB. DR GO; GO:0006457; P:protein folding; IBA:GO_Central. DR GO; GO:0006986; P:response to unfolded protein; TAS:ProtInc. DR CDD; cd00320; cpn10; 1. DR FunFam; 2.30.33.40:FF:000002; 10 kDa chaperonin, mitochondrial; 1. DR Gene3D; 2.30.33.40; GroES chaperonin; 1. DR HAMAP; MF_00580; CH10; 1. DR InterPro; IPR020818; Chaperonin_GroES. DR InterPro; IPR037124; Chaperonin_GroES_sf. DR InterPro; IPR018369; Chaprnonin_Cpn10_CS. DR InterPro; IPR011032; GroES-like_sf. DR PANTHER; PTHR10772; 10 KDA HEAT SHOCK PROTEIN; 1. DR PANTHER; PTHR10772:SF0; 10 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL; 1. DR Pfam; PF00166; Cpn10; 1. DR PRINTS; PR00297; CHAPERONIN10. DR SMART; SM00883; Cpn10; 1. DR SUPFAM; SSF50129; GroES-like; 1. DR PROSITE; PS00681; CHAPERONINS_CPN10; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Chaperone; Direct protein sequencing; KW Mitochondrion; Phosphoprotein; Proteomics identification; KW Reference proteome; Stress response. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.10" FT CHAIN 2..102 FT /note="10 kDa heat shock protein, mitochondrial" FT /id="PRO_0000174917" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.10" FT MOD_RES 8 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q64433" FT MOD_RES 28 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q64433" FT MOD_RES 40 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q64433" FT MOD_RES 40 FT /note="N6-malonyllysine; alternate" FT /evidence="ECO:0000269|PubMed:21908771" FT MOD_RES 40 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q64433" FT MOD_RES 54 FT /note="N6-malonyllysine; alternate" FT /evidence="ECO:0000269|PubMed:21908771" FT MOD_RES 54 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q64433" FT MOD_RES 56 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 56 FT /note="N6-malonyllysine; alternate" FT /evidence="ECO:0000269|PubMed:21908771" FT MOD_RES 56 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q64433" FT MOD_RES 66 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q64433" FT MOD_RES 66 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q64433" FT MOD_RES 70 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q64433" FT MOD_RES 70 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q64433" FT MOD_RES 79 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 80 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q64433" FT MOD_RES 80 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q64433" FT MOD_RES 86 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 86 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q64433" FT MOD_RES 99 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT STRAND 6..8 FT /evidence="ECO:0007829|PDB:9SHG" FT STRAND 9..11 FT /evidence="ECO:0007829|PDB:8G7N" FT STRAND 15..20 FT /evidence="ECO:0007829|PDB:9SHG" FT HELIX 21..24 FT /evidence="ECO:0007829|PDB:9SHG" FT STRAND 28..30 FT /evidence="ECO:0007829|PDB:9SHH" FT TURN 35..37 FT /evidence="ECO:0007829|PDB:9SHH" FT STRAND 43..49 FT /evidence="ECO:0007829|PDB:9SHG" FT STRAND 56..59 FT /evidence="ECO:0007829|PDB:9SHG" FT HELIX 60..63 FT /evidence="ECO:0007829|PDB:9SHG" FT STRAND 70..72 FT /evidence="ECO:0007829|PDB:9SHG" FT STRAND 75..77 FT /evidence="ECO:0007829|PDB:9H5S" FT STRAND 79..85 FT /evidence="ECO:0007829|PDB:9SHG" FT STRAND 87..92 FT /evidence="ECO:0007829|PDB:9SHG" FT HELIX 93..95 FT /evidence="ECO:0007829|PDB:9SHG" FT STRAND 98..100 FT /evidence="ECO:0007829|PDB:9SHG" SQ SEQUENCE 102 AA; 10932 MW; 1F3192C81F6EDB78 CRC64; MAGQAFRKFL PLFDRVLVER SAAETVTKGG IMLPEKSQGK VLQATVVAVG SGSKGKGGEI QPVSVKVGDK VLLPEYGGTK VVLDDKDYFL FRDGDILGKY VD //