CH60_HUMAN
ID CH60_HUMAN Reviewed; 573 AA.
AC P10809; B2R5M6; B7Z712; Q38L19; Q9UCR6;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 2.
DT 03-AUG-2022, entry version 250.
DE RecName: Full=60 kDa heat shock protein, mitochondrial;
DE EC=5.6.1.7 {ECO:0000305};
DE AltName: Full=60 kDa chaperonin;
DE AltName: Full=Chaperonin 60;
DE Short=CPN60;
DE AltName: Full=Heat shock protein 60;
DE Short=HSP-60;
DE Short=Hsp60;
DE AltName: Full=HuCHA60;
DE AltName: Full=Mitochondrial matrix protein P1;
DE AltName: Full=P60 lymphocyte protein;
DE Flags: Precursor;
GN Name=HSPD1; Synonyms=HSP60;
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] (ISOFORM 1).
RX PubMed=2568584; DOI=10.1128/mcb.9.5.2279-2283.1989;
RA Jindal S., Dudani A.K., Singh B., Harley C.B., Gupta R.S.;
RT "Primary structure of a human mitochondrial protein homologous to the
RT bacterial and plant chaperonins and to the 65-kilodalton mycobacterial
RT antigen.";
RL Mol. Cell. Biol. 9:2279-2283(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1980192; DOI=10.1089/dna.1990.9.545;
RA Venner T.J., Singh B., Gupta R.S.;
RT "Nucleotide sequences and novel structural features of human and Chinese
RT hamster hsp60 (chaperonin) gene families.";
RL DNA Cell Biol. 9:545-552(1990).
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 [GENOMIC DNA].
RA Tan J., Ong R., Hibberd M.L., Seielstad M.;
RT "Genetic variation in immune response genes.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Adrenal gland, and Spleen;
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 [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 MRNA] (ISOFORM 1).
RC TISSUE=Lung, Skin, and 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 [8]
RP PROTEIN SEQUENCE OF 27-573.
RX PubMed=2907406; DOI=10.1515/bchm3.1988.369.2.1185;
RA Waldinger D., Eckerskorn C., Lottspeich F., Cleve H.;
RT "Amino-acid sequence homology of a polymorphic cellular protein from human
RT lymphocytes and the chaperonins from Escherichia coli (groEL) and
RT chloroplasts (Rubisco-binding protein).";
RL Biol. Chem. Hoppe-Seyler 369:1185-1189(1988).
RN [9]
RP PROTEIN SEQUENCE OF 27-55.
RC TISSUE=Colon carcinoma;
RX PubMed=2079031; DOI=10.1002/elps.1150111019;
RA Ward L.D., Hong J., Whitehead R.H., Simpson R.J.;
RT "Development of a database of amino acid sequences for human colon
RT carcinoma proteins separated by two-dimensional polyacrylamide gel
RT electrophoresis.";
RL Electrophoresis 11:883-891(1990).
RN [10]
RP PROTEIN SEQUENCE OF 27-55, AND INTERACTION WITH HTLV-1 P40TAX (MICROBIAL
RP INFECTION).
RX PubMed=1731090; DOI=10.1128/jvi.66.2.1040-1049.1992;
RA Nagata K., Ide Y., Takagi T., Ohtani K., Aoshima M., Tozawa H.,
RA Nakamura M., Sugamura K.;
RT "Complex formation of human T-cell leukemia virus type I p40tax
RT transactivator with cellular polypeptides.";
RL J. Virol. 66:1040-1049(1992).
RN [11]
RP PROTEIN SEQUENCE OF 27-50.
RC TISSUE=Mammary carcinoma;
RX PubMed=9150946; DOI=10.1002/elps.1150180342;
RA Rasmussen R.K., Ji H., Eddes J.S., Moritz R.L., Reid G.E., Simpson R.J.,
RA Dorow D.S.;
RT "Two-dimensional electrophoretic analysis of human breast carcinoma
RT proteins: mapping of proteins that bind to the SH3 domain of mixed lineage
RT kinase MLK2.";
RL Electrophoresis 18:588-598(1997).
RN [12]
RP PROTEIN SEQUENCE OF 27-46.
RC TISSUE=Heart;
RX PubMed=7895732; DOI=10.1002/elps.11501501209;
RA Corbett J.M., Wheeler C.H., Baker C.S., Yacoub M.H., Dunn M.J.;
RT "The human myocardial two-dimensional gel protein database: update 1994.";
RL Electrophoresis 15:1459-1465(1994).
RN [13]
RP PROTEIN SEQUENCE OF 27-37.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [14]
RP PROTEIN SEQUENCE OF 27-35.
RC TISSUE=Liver;
RX PubMed=1286669; DOI=10.1002/elps.11501301201;
RA Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F.,
RA Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R.,
RA Appel R.D., Hughes G.J.;
RT "Human liver protein map: a reference database established by
RT microsequencing and gel comparison.";
RL Electrophoresis 13:992-1001(1992).
RN [15]
RP PROTEIN SEQUENCE OF 61-72, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (OCT-2004) to UniProtKB.
RN [16]
RP PROTEIN SEQUENCE OF 61-72; 206-218; 237-249; 251-290; 430-446 AND 463-469,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [17]
RP PROTEIN SEQUENCE OF 97-121; 251-268 AND 430-446.
RC TISSUE=Adipocyte;
RX PubMed=15242332; DOI=10.1042/bj20040647;
RA Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.;
RT "Vectorial proteomics reveal targeting, phosphorylation and specific
RT fragmentation of polymerase I and transcript release factor (PTRF) at the
RT surface of caveolae in human adipocytes.";
RL Biochem. J. 383:237-248(2004).
RN [18]
RP PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Colon carcinoma;
RX PubMed=9150948; DOI=10.1002/elps.1150180344;
RA Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.;
RT "A two-dimensional gel database of human colon carcinoma proteins.";
RL Electrophoresis 18:605-613(1997).
RN [19]
RP MITOCHONDRIAL IMPORT.
RX PubMed=1972619; DOI=10.1016/0006-291x(90)90344-m;
RA Singh B., Patel H.V., Ridley R.G., Freeman K.B., Gupta R.S.;
RT "Mitochondrial import of the human chaperonin (HSP60) protein.";
RL Biochem. Biophys. Res. Commun. 169:391-396(1990).
RN [20]
RP FUNCTION, AND SUBUNIT.
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 [21]
RP FUNCTION, AND SUBUNIT.
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 [22]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [23]
RP INTERACTION WITH HBV PROTEIN X (MICROBIAL INFECTION).
RX PubMed=15120623; DOI=10.1016/j.bbrc.2004.04.046;
RA Tanaka Y., Kanai F., Kawakami T., Tateishi K., Ijichi H., Kawabe T.,
RA Arakawa Y., Kawakami T., Nishimura T., Shirakata Y., Koike K., Omata M.;
RT "Interaction of the hepatitis B virus X protein (HBx) with heat shock
RT protein 60 enhances HBx-mediated apoptosis.";
RL Biochem. Biophys. Res. Commun. 318:461-469(2004).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [28]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-82; LYS-125; LYS-130; LYS-202;
RP LYS-218; LYS-269; LYS-352; LYS-359; LYS-396 AND LYS-469, AND IDENTIFICATION
RP 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 [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, 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 [30]
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 [31]
RP MALONYLATION AT LYS-133.
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 [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [33]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22905912; DOI=10.1021/pr300539b;
RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P.,
RA Mariman E.C., Renes J.;
RT "Resveratrol-induced changes of the human adipocyte secretion profile.";
RL J. Proteome Res. 11:4733-4743(2012).
RN [34]
RP INTERACTION WITH ATAD3A.
RX PubMed=22664726; DOI=10.1016/j.mito.2012.05.005;
RA Merle N., Feraud O., Gilquin B., Hubstenberger A., Kieffer-Jacquinot S.,
RA Assard N., Bennaceur-Griscelli A., Honnorat J., Baudier J.;
RT "ATAD3B is a human embryonic stem cell specific mitochondrial protein, re-
RT expressed in cancer cells, that functions as dominant negative for the
RT ubiquitous ATAD3A.";
RL Mitochondrion 12:441-448(2012).
RN [35]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70 AND SER-488, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [36]
RP INTERACTION WITH ETFBKMT AND EEF1AKMT3.
RX PubMed=23349634; DOI=10.1371/journal.pgen.1003210;
RA Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.;
RT "A newly uncovered group of distantly related lysine methyltransferases
RT preferentially interact with molecular chaperones to regulate their
RT activity.";
RL PLoS Genet. 9:E1003210-E1003210(2013).
RN [37]
RP INTERACTION WITH MFHAS1.
RX PubMed=24286120; DOI=10.1111/febs.12593;
RA Dihanich S., Civiero L., Manzoni C., Mamais A., Bandopadhyay R.,
RA Greggio E., Lewis P.A.;
RT "GTP binding controls complex formation by the human ROCO protein MASL1.";
RL FEBS J. 281:261-274(2014).
RN [38]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67 AND TYR-90, AND
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 [39]
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 [40]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-551, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [41]
RP X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 27-556 IN COMPLEX WITH ADP,
RP 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).
RN [42]
RP VARIANT SPG13 ILE-98.
RX PubMed=11898127; DOI=10.1086/339935;
RA Hansen J.J., Durr A., Cournu-Rebeix I., Georgopoulos C., Ang D.,
RA Nielsen M.N., Davoine C.-S., Brice A., Fontaine B., Gregersen N., Bross P.;
RT "Hereditary spastic paraplegia SPG13 is associated with a mutation in the
RT gene encoding the mitochondrial chaperonin Hsp60.";
RL Am. J. Hum. Genet. 70:1328-1332(2002).
RN [43]
RP VARIANT HLD4 GLY-29, AND CHARACTERIZATION OF VARIANT HLD4 GLY-29.
RX PubMed=18571143; DOI=10.1016/j.ajhg.2008.05.016;
RA Magen D., Georgopoulos C., Bross P., Ang D., Segev Y., Goldsher D.,
RA Nemirovski A., Shahar E., Ravid S., Luder A., Heno B., Gershoni-Baruch R.,
RA Skorecki K., Mandel H.;
RT "Mitochondrial Hsp60 chaperonopathy causes an autosomal-recessive
RT neurodegenerative disorder linked to brain hypomyelination and
RT leukodystrophy.";
RL Am. J. Hum. Genet. 83:30-42(2008).
CC -!- FUNCTION: Chaperonin implicated in mitochondrial protein import and
CC macromolecular assembly. Together with Hsp10, 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:1346131,
CC PubMed:11422376). The functional units of these chaperonins consist of
CC heptameric rings of the large subunit Hsp60, which function as a back-
CC to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind
CC one unfolded substrate protein per ring, followed by the binding of ATP
CC and association with 2 heptameric rings of the co-chaperonin Hsp10.
CC This leads to sequestration of the substrate protein in the inner
CC cavity of Hsp60 where, for a certain period of time, it can fold
CC undisturbed by other cell components. Synchronous hydrolysis of ATP in
CC all Hsp60 subunits results in the dissociation of the chaperonin rings
CC and the release of ADP and the folded substrate protein (Probable).
CC {ECO:0000269|PubMed:11422376, ECO:0000269|PubMed:1346131,
CC ECO:0000305|PubMed:25918392}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + a folded polypeptide = ADP + phosphate + an
CC unfolded polypeptide.; EC=5.6.1.7; Evidence={ECO:0000305};
CC -!- SUBUNIT: Homoheptamer arranged in a ring structure (PubMed:1346131,
CC PubMed:11422376, PubMed:25918392). 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. Interacts with 2
CC heptameric Hsp10 rings to form the symmetrical football complex
CC (PubMed:25918392). Interacts with HRAS (By similarity). Interacts with
CC ATAD3A (PubMed:22664726). Interacts with ETFBKMT and EEF1AKMT3
CC (PubMed:23349634). Interacts with MFHAS1 (PubMed:24286120).
CC {ECO:0000250|UniProtKB:P63038, ECO:0000269|PubMed:11422376,
CC ECO:0000269|PubMed:1346131, ECO:0000269|PubMed:22664726,
CC ECO:0000269|PubMed:23349634, ECO:0000269|PubMed:24286120,
CC ECO:0000269|PubMed:25918392}.
CC -!- SUBUNIT: (Microbial infection) Interacts with hepatitis B virus/HBV
CC protein X. {ECO:0000269|PubMed:15120623}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HTLV-1 protein p40tax.
CC {ECO:0000269|PubMed:1731090}.
CC -!- INTERACTION:
CC P10809; P61158: ACTR3; NbExp=3; IntAct=EBI-352528, EBI-351428;
CC P10809; P05067: APP; NbExp=6; IntAct=EBI-352528, EBI-77613;
CC P10809; Q9NVI7: ATAD3A; NbExp=4; IntAct=EBI-352528, EBI-352007;
CC P10809; Q9UMX3: BOK; NbExp=3; IntAct=EBI-352528, EBI-7105206;
CC P10809; P38398: BRCA1; NbExp=2; IntAct=EBI-352528, EBI-349905;
CC P10809; Q8NHQ1: CEP70; NbExp=6; IntAct=EBI-352528, EBI-739624;
CC P10809; P28329-3: CHAT; NbExp=3; IntAct=EBI-352528, EBI-25837549;
CC P10809; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-352528, EBI-3867333;
CC P10809; Q6PI48: DARS2; NbExp=3; IntAct=EBI-352528, EBI-3917045;
CC P10809; Q9UBU7: DBF4; NbExp=3; IntAct=EBI-352528, EBI-372690;
CC P10809; A0A024RCP2: DOM3Z; NbExp=3; IntAct=EBI-352528, EBI-25847826;
CC P10809; Q99944: EGFL8; NbExp=3; IntAct=EBI-352528, EBI-3924130;
CC P10809; Q6NXG1: ESRP1; NbExp=3; IntAct=EBI-352528, EBI-10213520;
CC P10809; Q99504: EYA3; NbExp=3; IntAct=EBI-352528, EBI-9089567;
CC P10809; P22607: FGFR3; NbExp=3; IntAct=EBI-352528, EBI-348399;
CC P10809; Q14957: GRIN2C; NbExp=3; IntAct=EBI-352528, EBI-8285963;
CC P10809; P01112: HRAS; NbExp=3; IntAct=EBI-352528, EBI-350145;
CC P10809; Q0VD86: INCA1; NbExp=3; IntAct=EBI-352528, EBI-6509505;
CC P10809; P05412: JUN; NbExp=5; IntAct=EBI-352528, EBI-852823;
CC P10809; Q15323: KRT31; NbExp=3; IntAct=EBI-352528, EBI-948001;
CC P10809; O76011: KRT34; NbExp=3; IntAct=EBI-352528, EBI-1047093;
CC P10809; Q6A162: KRT40; NbExp=3; IntAct=EBI-352528, EBI-10171697;
CC P10809; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-352528, EBI-10171774;
CC P10809; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-352528, EBI-3958099;
CC P10809; Q14847-2: LASP1; NbExp=3; IntAct=EBI-352528, EBI-9088686;
CC P10809; Q6ZQX7-4: LIAT1; NbExp=3; IntAct=EBI-352528, EBI-25830459;
CC P10809; Q9BRK4: LZTS2; NbExp=7; IntAct=EBI-352528, EBI-741037;
CC P10809; Q9Y4C4: MFHAS1; NbExp=3; IntAct=EBI-352528, EBI-2864441;
CC P10809; P12036: NEFH; NbExp=3; IntAct=EBI-352528, EBI-2880271;
CC P10809; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-352528, EBI-945833;
CC P10809; A0A0C4DFM3: PRUNE2; NbExp=3; IntAct=EBI-352528, EBI-25830870;
CC P10809; O76081: RGS20; NbExp=3; IntAct=EBI-352528, EBI-1052678;
CC P10809; O76081-6: RGS20; NbExp=3; IntAct=EBI-352528, EBI-10178530;
CC P10809; Q8N6K7: SAMD3; NbExp=4; IntAct=EBI-352528, EBI-748741;
CC P10809; Q12888: TP53BP1; NbExp=3; IntAct=EBI-352528, EBI-396540;
CC P10809; Q9UBQ0-2: VPS29; NbExp=3; IntAct=EBI-352528, EBI-11141397;
CC P10809; Q9JJY3: Smpd3; Xeno; NbExp=3; IntAct=EBI-352528, EBI-9817007;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P10809-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P10809-2; Sequence=VSP_056144, VSP_056145;
CC -!- DISEASE: Spastic paraplegia 13, autosomal dominant (SPG13)
CC [MIM:605280]: A form of spastic paraplegia, a neurodegenerative
CC disorder characterized by a slow, gradual, progressive weakness and
CC spasticity of the lower limbs. Rate of progression and the severity of
CC symptoms are quite variable. Initial symptoms may include difficulty
CC with balance, weakness and stiffness in the legs, muscle spasms, and
CC dragging the toes when walking. In some forms of the disorder, bladder
CC symptoms (such as incontinence) may appear, or the weakness and
CC stiffness may spread to other parts of the body.
CC {ECO:0000269|PubMed:11898127}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Leukodystrophy, hypomyelinating, 4 (HLD4) [MIM:612233]: A
CC severe autosomal recessive hypomyelinating leukodystrophy. Clinically
CC characterized by infantile-onset rotary nystagmus, progressive spastic
CC paraplegia, neurologic regression, motor impairment, profound
CC intellectual disability. Death usually occurs within the first two
CC decades of life. {ECO:0000269|PubMed:18571143}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/HSPD1ID40888ch2q33.html";
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DR EMBL; M22382; AAA60127.1; -; mRNA.
DR EMBL; M34664; AAA36022.1; -; mRNA.
DR EMBL; AJ250915; CAB75426.1; -; Genomic_DNA.
DR EMBL; DQ217936; ABB01006.1; -; Genomic_DNA.
DR EMBL; AK301276; BAH13448.1; -; mRNA.
DR EMBL; AK312240; BAG35173.1; -; mRNA.
DR EMBL; AC010746; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC020550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC114809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002676; AAH02676.1; -; mRNA.
DR EMBL; BC003030; AAH03030.1; -; mRNA.
DR EMBL; BC067082; AAH67082.1; -; mRNA.
DR EMBL; BC073746; AAH73746.1; -; mRNA.
DR CCDS; CCDS33357.1; -. [P10809-1]
DR PIR; A32800; A32800.
DR RefSeq; NP_002147.2; NM_002156.4. [P10809-1]
DR RefSeq; NP_955472.1; NM_199440.1. [P10809-1]
DR PDB; 4PJ1; X-ray; 3.15 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=27-556.
DR PDB; 6HT7; X-ray; 3.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=27-573.
DR PDB; 6MRC; EM; 3.08 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=27-552.
DR PDB; 6MRD; EM; 3.82 A; A/B/C/D/E/F/G=27-552.
DR PDB; 7AZP; EM; 3.50 A; A/B/C/D/E/F/G=27-573.
DR PDB; 7L7S; EM; 3.50 A; H/I/J/K/L/M/N=27-550.
DR PDBsum; 4PJ1; -.
DR PDBsum; 6HT7; -.
DR PDBsum; 6MRC; -.
DR PDBsum; 6MRD; -.
DR PDBsum; 7AZP; -.
DR PDBsum; 7L7S; -.
DR AlphaFoldDB; P10809; -.
DR SMR; P10809; -.
DR BioGRID; 109561; 880.
DR CORUM; P10809; -.
DR DIP; DIP-58N; -.
DR IntAct; P10809; 556.
DR MINT; P10809; -.
DR STRING; 9606.ENSP00000373620; -.
DR BindingDB; P10809; -.
DR ChEMBL; CHEMBL4721; -.
DR DrugBank; DB09130; Copper.
DR MoonProt; P10809; -.
DR CarbonylDB; P10809; -.
DR GlyGen; P10809; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; P10809; -.
DR MetOSite; P10809; -.
DR PhosphoSitePlus; P10809; -.
DR SwissPalm; P10809; -.
DR BioMuta; HSPD1; -.
DR DMDM; 129379; -.
DR DOSAC-COBS-2DPAGE; P10809; -.
DR OGP; P10809; -.
DR REPRODUCTION-2DPAGE; IPI00784154; -.
DR REPRODUCTION-2DPAGE; P10809; -.
DR SWISS-2DPAGE; P10809; -.
DR UCD-2DPAGE; P10809; -.
DR CPTAC; CPTAC-391; -.
DR CPTAC; CPTAC-392; -.
DR EPD; P10809; -.
DR jPOST; P10809; -.
DR MassIVE; P10809; -.
DR MaxQB; P10809; -.
DR PaxDb; P10809; -.
DR PeptideAtlas; P10809; -.
DR PRIDE; P10809; -.
DR ProteomicsDB; 52653; -. [P10809-1]
DR ProteomicsDB; 6822; -.
DR TopDownProteomics; P10809-1; -. [P10809-1]
DR ABCD; P10809; 9 sequenced antibodies.
DR Antibodypedia; 869; 2392 antibodies from 51 providers.
DR CPTC; P10809; 3 antibodies.
DR DNASU; 3329; -.
DR Ensembl; ENST00000345042.6; ENSP00000340019.2; ENSG00000144381.18. [P10809-1]
DR Ensembl; ENST00000388968.8; ENSP00000373620.3; ENSG00000144381.18. [P10809-1]
DR Ensembl; ENST00000418022.2; ENSP00000412227.2; ENSG00000144381.18. [P10809-1]
DR Ensembl; ENST00000426480.2; ENSP00000414446.2; ENSG00000144381.18. [P10809-1]
DR Ensembl; ENST00000428204.6; ENSP00000396460.2; ENSG00000144381.18. [P10809-1]
DR Ensembl; ENST00000439605.2; ENSP00000402478.2; ENSG00000144381.18. [P10809-1]
DR Ensembl; ENST00000452200.6; ENSP00000412717.2; ENSG00000144381.18. [P10809-1]
DR Ensembl; ENST00000677913.1; ENSP00000503139.1; ENSG00000144381.18. [P10809-1]
DR Ensembl; ENST00000678761.1; ENSP00000503894.1; ENSG00000144381.18. [P10809-1]
DR GeneID; 3329; -.
DR KEGG; hsa:3329; -.
DR MANE-Select; ENST00000388968.8; ENSP00000373620.3; NM_002156.5; NP_002147.2.
DR UCSC; uc002uui.4; human. [P10809-1]
DR CTD; 3329; -.
DR DisGeNET; 3329; -.
DR GeneCards; HSPD1; -.
DR HGNC; HGNC:5261; HSPD1.
DR HPA; ENSG00000144381; Tissue enhanced (adrenal).
DR MalaCards; HSPD1; -.
DR MIM; 118190; gene.
DR MIM; 605280; phenotype.
DR MIM; 612233; phenotype.
DR neXtProt; NX_P10809; -.
DR OpenTargets; ENSG00000144381; -.
DR Orphanet; 100994; Autosomal dominant spastic paraplegia type 13.
DR Orphanet; 280288; Pelizaeus-Merzbacher-like disease due to HSPD1 mutation.
DR PharmGKB; PA29527; -.
DR VEuPathDB; HostDB:ENSG00000144381; -.
DR eggNOG; KOG0356; Eukaryota.
DR GeneTree; ENSGT00390000005727; -.
DR HOGENOM; CLU_016503_3_0_1; -.
DR InParanoid; P10809; -.
DR OMA; TDTDKME; -.
DR PhylomeDB; P10809; -.
DR TreeFam; TF300475; -.
DR PathwayCommons; P10809; -.
DR Reactome; R-HSA-1268020; Mitochondrial protein import.
DR Reactome; R-HSA-8869496; TFAP2A acts as a transcriptional repressor during retinoic acid induced cell differentiation.
DR SignaLink; P10809; -.
DR SIGNOR; P10809; -.
DR BioGRID-ORCS; 3329; 561 hits in 1017 CRISPR screens.
DR ChiTaRS; HSPD1; human.
DR GeneWiki; GroEL; -.
DR GenomeRNAi; 3329; -.
DR Pharos; P10809; Tbio.
DR PRO; PR:P10809; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P10809; protein.
DR Bgee; ENSG00000144381; Expressed in adrenal tissue and 150 other tissues.
DR ExpressionAtlas; P10809; baseline and differential.
DR Genevisible; P10809; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005905; C:clathrin-coated pit; IDA:BHF-UCL.
DR GO; GO:0030135; C:coated vesicle; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IDA:BHF-UCL.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0046696; C:lipopolysaccharide receptor complex; IDA:BHF-UCL.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:BHF-UCL.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:CAFA.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:CAFA.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0030141; C:secretory granule; ISS:BHF-UCL.
DR GO; GO:0097225; C:sperm midpiece; IMP:GO_Central.
DR GO; GO:0034186; F:apolipoprotein A-I binding; IPI:CAFA.
DR GO; GO:0034185; F:apolipoprotein binding; IPI:CAFA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:BHF-UCL.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051087; F:chaperone binding; IPI:UniProtKB.
DR GO; GO:0003688; F:DNA replication origin binding; ISS:BHF-UCL.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR GO; GO:0019899; F:enzyme binding; IPI:CAFA.
DR GO; GO:0008035; F:high-density lipoprotein particle binding; IDA:CAFA.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0001530; F:lipopolysaccharide binding; IDA:BHF-UCL.
DR GO; GO:0002039; F:p53 binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:BHF-UCL.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0051082; F:unfolded protein binding; ISS:BHF-UCL.
DR GO; GO:0006458; P:'de novo' protein folding; ISS:BHF-UCL.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:BHF-UCL.
DR GO; GO:0008637; P:apoptotic mitochondrial changes; IBA:GO_Central.
DR GO; GO:0042113; P:B cell activation; IDA:BHF-UCL.
DR GO; GO:0042100; P:B cell proliferation; IDA:BHF-UCL.
DR GO; GO:0051702; P:biological process involved in interaction with symbiont; IMP:CAFA.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; ISS:BHF-UCL.
DR GO; GO:0048291; P:isotype switching to IgG isotypes; IDA:BHF-UCL.
DR GO; GO:0034514; P:mitochondrial unfolded protein response; IBA:GO_Central.
DR GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:BHF-UCL.
DR GO; GO:0032727; P:positive regulation of interferon-alpha production; IDA:BHF-UCL.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IDA:BHF-UCL.
DR GO; GO:0032733; P:positive regulation of interleukin-10 production; IDA:BHF-UCL.
DR GO; GO:0032735; P:positive regulation of interleukin-12 production; IDA:BHF-UCL.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:BHF-UCL.
DR GO; GO:0043032; P:positive regulation of macrophage activation; IDA:BHF-UCL.
DR GO; GO:0050870; P:positive regulation of T cell activation; IDA:BHF-UCL.
DR GO; GO:0002842; P:positive regulation of T cell mediated immune response to tumor cell; IDA:BHF-UCL.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0045041; P:protein import into mitochondrial intermembrane space; IBA:GO_Central.
DR GO; GO:0051604; P:protein maturation; ISS:BHF-UCL.
DR GO; GO:0042026; P:protein refolding; IDA:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR GO; GO:0009409; P:response to cold; ISS:AgBase.
DR GO; GO:0006986; P:response to unfolded protein; IDA:BHF-UCL.
DR GO; GO:0042110; P:T cell activation; IDA:MGI.
DR CDD; cd03344; GroEL; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR HAMAP; MF_00600; CH60; 1.
DR InterPro; IPR018370; Chaperonin_Cpn60_CS.
DR InterPro; IPR001844; Cpn60/GroEL.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR027413; GROEL-like_equatorial_sf.
DR InterPro; IPR027410; TCP-1-like_intermed_sf.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00298; CHAPERONIN60.
DR SUPFAM; SSF48592; SSF48592; 1.
DR SUPFAM; SSF52029; SSF52029; 1.
DR SUPFAM; SSF54849; SSF54849; 1.
DR TIGRFAMs; TIGR02348; GroEL; 1.
DR PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Chaperone;
KW Direct protein sequencing; Disease variant; Hereditary spastic paraplegia;
KW Host-virus interaction; Isomerase; Isopeptide bond; Leukodystrophy;
KW Mitochondrion; Neurodegeneration; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transit peptide; Ubl conjugation.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0000269|PubMed:1286669, ECO:0000269|PubMed:1731090,
FT ECO:0000269|PubMed:2079031, ECO:0000269|PubMed:2907406,
FT ECO:0000269|PubMed:7895732, ECO:0000269|PubMed:9150946"
FT CHAIN 27..573
FT /note="60 kDa heat shock protein, mitochondrial"
FT /id="PRO_0000005026"
FT BINDING 75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25918392,
FT ECO:0007744|PDB:4PJ1"
FT BINDING 111..115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25918392,
FT ECO:0007744|PDB:4PJ1"
FT BINDING 440
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25918392,
FT ECO:0007744|PDB:4PJ1"
FT BINDING 520
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25918392,
FT ECO:0007744|PDB:4PJ1"
FT MOD_RES 31
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 75
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 82
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 82
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 87
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 90
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 91
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 125
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 125
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 130
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 133
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 133
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21908771"
FT MOD_RES 133
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 156
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 191
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 191
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 202
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 202
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 205
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 205
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 218
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 218
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 236
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 236
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 249
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 250
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 250
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 269
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 292
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 301
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 314
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 352
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 352
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 359
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 389
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 396
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 396
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 469
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 481
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 481
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 551
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 144..158
FT /note="VMLAVDAVIAELKKQ -> RNVCCHHSVLNFSVL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056144"
FT VAR_SEQ 159..573
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056145"
FT VARIANT 29
FT /note="D -> G (in HLD4; transfection with the mutant
FT protein impairs cell growth that worsens with increasing
FT temperature; dbSNP:rs72466451)"
FT /evidence="ECO:0000269|PubMed:18571143"
FT /id="VAR_054785"
FT VARIANT 98
FT /note="V -> I (in SPG13; dbSNP:rs66468541)"
FT /evidence="ECO:0000269|PubMed:11898127"
FT /id="VAR_026748"
FT CONFLICT 67
FT /note="S -> G (in Ref. 2; AAA36022)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="D -> N (in Ref. 5; BAG35173)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="N -> S (in Ref. 5; BAG35173)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="K -> KAS (in Ref. 4; ABB01006)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="A -> T (in Ref. 5; BAG35173)"
FT /evidence="ECO:0000305"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:6MRC"
FT HELIX 34..52
FT /evidence="ECO:0007829|PDB:6MRC"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:7L7S"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:6MRC"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:6MRC"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:6MRC"
FT HELIX 79..83
FT /evidence="ECO:0007829|PDB:6MRC"
FT HELIX 89..109
FT /evidence="ECO:0007829|PDB:6MRC"
FT HELIX 113..127
FT /evidence="ECO:0007829|PDB:6MRC"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:7L7S"
FT HELIX 137..158
FT /evidence="ECO:0007829|PDB:6MRC"
FT HELIX 165..175
FT /evidence="ECO:0007829|PDB:6MRC"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:4PJ1"
FT HELIX 180..191
FT /evidence="ECO:0007829|PDB:6MRC"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:6MRC"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:6MRC"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:6MRC"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:6MRC"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:4PJ1"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:6MRC"
FT STRAND 237..249
FT /evidence="ECO:0007829|PDB:6MRC"
FT HELIX 254..267
FT /evidence="ECO:0007829|PDB:6MRC"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:6MRC"
FT HELIX 280..291
FT /evidence="ECO:0007829|PDB:6MRC"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:6MRC"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:6MRC"
FT HELIX 308..320
FT /evidence="ECO:0007829|PDB:6MRC"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:4PJ1"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:6MRC"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:6MRC"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:6MRC"
FT STRAND 342..350
FT /evidence="ECO:0007829|PDB:6MRC"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:6MRC"
FT HELIX 364..380
FT /evidence="ECO:0007829|PDB:6MRC"
FT HELIX 386..395
FT /evidence="ECO:0007829|PDB:6MRC"
FT TURN 397..399
FT /evidence="ECO:0007829|PDB:4PJ1"
FT STRAND 401..406
FT /evidence="ECO:0007829|PDB:6MRC"
FT HELIX 411..431
FT /evidence="ECO:0007829|PDB:6MRC"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:6MRC"
FT TURN 439..441
FT /evidence="ECO:0007829|PDB:4PJ1"
FT HELIX 442..445
FT /evidence="ECO:0007829|PDB:6MRC"
FT HELIX 448..451
FT /evidence="ECO:0007829|PDB:6MRC"
FT HELIX 459..471
FT /evidence="ECO:0007829|PDB:6MRC"
FT HELIX 474..482
FT /evidence="ECO:0007829|PDB:6MRC"
FT HELIX 487..496
FT /evidence="ECO:0007829|PDB:6MRC"
FT STRAND 499..504
FT /evidence="ECO:0007829|PDB:6MRC"
FT TURN 505..508
FT /evidence="ECO:0007829|PDB:6MRC"
FT STRAND 509..513
FT /evidence="ECO:0007829|PDB:6MRC"
FT TURN 514..517
FT /evidence="ECO:0007829|PDB:6MRC"
FT STRAND 519..521
FT /evidence="ECO:0007829|PDB:6MRC"
FT HELIX 522..539
FT /evidence="ECO:0007829|PDB:6MRC"
FT STRAND 542..548
FT /evidence="ECO:0007829|PDB:6MRC"
SQ SEQUENCE 573 AA; 61055 MW; E51E1BAD9615899C CRC64;
MLRLPTVFRQ MRPVSRVLAP HLTRAYAKDV KFGADARALM LQGVDLLADA VAVTMGPKGR
TVIIEQSWGS PKVTKDGVTV AKSIDLKDKY KNIGAKLVQD VANNTNEEAG DGTTTATVLA
RSIAKEGFEK ISKGANPVEI RRGVMLAVDA VIAELKKQSK PVTTPEEIAQ VATISANGDK
EIGNIISDAM KKVGRKGVIT VKDGKTLNDE LEIIEGMKFD RGYISPYFIN TSKGQKCEFQ
DAYVLLSEKK ISSIQSIVPA LEIANAHRKP LVIIAEDVDG EALSTLVLNR LKVGLQVVAV
KAPGFGDNRK NQLKDMAIAT GGAVFGEEGL TLNLEDVQPH DLGKVGEVIV TKDDAMLLKG
KGDKAQIEKR IQEIIEQLDV TTSEYEKEKL NERLAKLSDG VAVLKVGGTS DVEVNEKKDR
VTDALNATRA AVEEGIVLGG GCALLRCIPA LDSLTPANED QKIGIEIIKR TLKIPAMTIA
KNAGVEGSLI VEKIMQSSSE VGYDAMAGDF VNMVEKGIID PTKVVRTALL DAAGVASLLT
TAEVVVTEIP KEEKDPGMGA MGGMGGGMGG GMF
