CH10_HUMAN
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 03-AUG-2022, entry version 164.
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;
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 (3.15 ANGSTROMS), 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:7912672,
CC PubMed:1346131, PubMed:11422376). 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}.
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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_002157.2.
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 PDBsum; 4PJ1; -.
DR PDBsum; 6HT7; -.
DR PDBsum; 6MRC; -.
DR PDBsum; 6MRD; -.
DR AlphaFoldDB; P61604; -.
DR SMR; P61604; -.
DR BioGRID; 109568; 261.
DR IntAct; P61604; 81.
DR MINT; P61604; -.
DR STRING; 9606.ENSP00000233893; -.
DR ChEMBL; CHEMBL4106131; -.
DR DrugBank; DB12695; Phenethyl Isothiocyanate.
DR GlyGen; P61604; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P61604; -.
DR MetOSite; P61604; -.
DR PhosphoSitePlus; P61604; -.
DR BioMuta; HSPE1; -.
DR DMDM; 47606335; -.
DR UCD-2DPAGE; P61604; -.
DR EPD; P61604; -.
DR jPOST; P61604; -.
DR MassIVE; P61604; -.
DR MaxQB; P61604; -.
DR PaxDb; P61604; -.
DR PeptideAtlas; P61604; -.
DR PRIDE; P61604; -.
DR ProteomicsDB; 57325; -.
DR TopDownProteomics; P61604; -.
DR Antibodypedia; 3376; 552 antibodies from 38 providers.
DR DNASU; 3336; -.
DR Ensembl; ENST00000233893.10; ENSP00000233893.5; ENSG00000115541.11.
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 CTD; 3336; -.
DR DisGeNET; 3336; -.
DR GeneCards; HSPE1; -.
DR HGNC; HGNC:5269; HSPE1.
DR HPA; ENSG00000115541; Low tissue specificity.
DR MIM; 600141; gene.
DR neXtProt; NX_P61604; -.
DR OpenTargets; ENSG00000115541; -.
DR PharmGKB; PA29535; -.
DR VEuPathDB; HostDB:ENSG00000115541; -.
DR eggNOG; KOG1641; Eukaryota.
DR GeneTree; ENSGT00390000006350; -.
DR HOGENOM; CLU_132825_0_1_1; -.
DR InParanoid; P61604; -.
DR OMA; EVKYSGE; -.
DR PhylomeDB; P61604; -.
DR TreeFam; TF313814; -.
DR PathwayCommons; P61604; -.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR SignaLink; P61604; -.
DR BioGRID-ORCS; 3336; 717 hits in 989 CRISPR screens.
DR ChiTaRS; HSPE1; human.
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 99 other tissues.
DR ExpressionAtlas; P61604; baseline and differential.
DR Genevisible; P61604; HS.
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:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051087; F:chaperone binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; NAS:UniProtKB.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB.
DR GO; GO:0006457; P:protein folding; TAS:ProtInc.
DR GO; GO:0006986; P:response to unfolded protein; TAS:ProtInc.
DR CDD; cd00320; cpn10; 1.
DR Gene3D; 2.30.33.40; -; 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; PTHR10772; 1.
DR Pfam; PF00166; Cpn10; 1.
DR PRINTS; PR00297; CHAPERONIN10.
DR SMART; SM00883; Cpn10; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR PROSITE; PS00681; CHAPERONINS_CPN10; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chaperone; Direct protein sequencing;
KW Mitochondrion; Phosphoprotein; 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 9..11
FT /evidence="ECO:0007829|PDB:6MRC"
FT STRAND 15..20
FT /evidence="ECO:0007829|PDB:6MRC"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:6MRC"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:6MRC"
FT STRAND 42..49
FT /evidence="ECO:0007829|PDB:6MRC"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:6MRC"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:6MRC"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:6MRC"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:6MRC"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:6MRC"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:4PJ1"
SQ SEQUENCE 102 AA; 10932 MW; 1F3192C81F6EDB78 CRC64;
MAGQAFRKFL PLFDRVLVER SAAETVTKGG IMLPEKSQGK VLQATVVAVG SGSKGKGGEI
QPVSVKVGDK VLLPEYGGTK VVLDDKDYFL FRDGDILGKY VD
