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60 kDa heat shock protein, mitochondrial (EC 3.6.4.9) (60 kDa chaperonin) (Chaperonin 60) (CPN60) (Heat shock protein 60) (HSP-60) (Hsp60) (HuCHA60) (Mitochondrial matrix protein P1) (P60 lymphocyte protein)

 CH60_HUMAN              Reviewed;         573 AA.
P10809; B2R5M6; B7Z712; Q38L19; Q9UCR6;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-AUG-1990, sequence version 2.
27-SEP-2017, entry version 214.
RecName: Full=60 kDa heat shock protein, mitochondrial;
EC=3.6.4.9;
AltName: Full=60 kDa chaperonin;
AltName: Full=Chaperonin 60;
Short=CPN60;
AltName: Full=Heat shock protein 60;
Short=HSP-60;
Short=Hsp60;
AltName: Full=HuCHA60;
AltName: Full=Mitochondrial matrix protein P1;
AltName: Full=P60 lymphocyte protein;
Flags: Precursor;
Name=HSPD1; Synonyms=HSP60;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2568584; DOI=10.1128/MCB.9.5.2279;
Jindal S., Dudani A.K., Singh B., Harley C.B., Gupta R.S.;
"Primary structure of a human mitochondrial protein homologous to the
bacterial and plant chaperonins and to the 65-kilodalton mycobacterial
antigen.";
Mol. Cell. Biol. 9:2279-2283(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1980192; DOI=10.1089/dna.1990.9.545;
Venner T.J., Singh B., Gupta R.S.;
"Nucleotide sequences and novel structural features of human and
Chinese hamster hsp60 (chaperonin) gene families.";
DNA Cell Biol. 9:545-552(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=12483302; DOI=10.1007/s00439-002-0837-9;
Hansen J.J., Bross P., Westergaard M., Nielsen M.N., Eiberg H.,
Boerglum A.D., Mogensen J., Kristiansen K., Bolund L., Gregersen N.;
"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. 112:71-77(2003).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tan J., Ong R., Hibberd M.L., Seielstad M.;
"Genetic variation in immune response genes.";
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Adrenal gland, and Spleen;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung, Skin, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 27-573.
PubMed=2907406;
Waldinger D., Eckerskorn C., Lottspeich F., Cleve H.;
"Amino-acid sequence homology of a polymorphic cellular protein from
human lymphocytes and the chaperonins from Escherichia coli (groEL)
and chloroplasts (Rubisco-binding protein).";
Biol. Chem. Hoppe-Seyler 369:1185-1189(1988).
[9]
PROTEIN SEQUENCE OF 27-55.
TISSUE=Colon carcinoma;
PubMed=2079031; DOI=10.1002/elps.1150111019;
Ward L.D., Hong J., Whitehead R.H., Simpson R.J.;
"Development of a database of amino acid sequences for human colon
carcinoma proteins separated by two-dimensional polyacrylamide gel
electrophoresis.";
Electrophoresis 11:883-891(1990).
[10]
PROTEIN SEQUENCE OF 27-55, AND INTERACTION WITH HTLV-1 P40TAX.
PubMed=1731090;
Nagata K., Ide Y., Takagi T., Ohtani K., Aoshima M., Tozawa H.,
Nakamura M., Sugamura K.;
"Complex formation of human T-cell leukemia virus type I p40tax
transactivator with cellular polypeptides.";
J. Virol. 66:1040-1049(1992).
[11]
PROTEIN SEQUENCE OF 27-50.
TISSUE=Mammary carcinoma;
PubMed=9150946; DOI=10.1002/elps.1150180342;
Rasmussen R.K., Ji H., Eddes J.S., Moritz R.L., Reid G.E.,
Simpson R.J., Dorow D.S.;
"Two-dimensional electrophoretic analysis of human breast carcinoma
proteins: mapping of proteins that bind to the SH3 domain of mixed
lineage kinase MLK2.";
Electrophoresis 18:588-598(1997).
[12]
PROTEIN SEQUENCE OF 27-46.
TISSUE=Heart;
PubMed=7895732; DOI=10.1002/elps.11501501209;
Corbett J.M., Wheeler C.H., Baker C.S., Yacoub M.H., Dunn M.J.;
"The human myocardial two-dimensional gel protein database: update
1994.";
Electrophoresis 15:1459-1465(1994).
[13]
PROTEIN SEQUENCE OF 27-37.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[14]
PROTEIN SEQUENCE OF 27-35.
TISSUE=Liver;
PubMed=1286669; DOI=10.1002/elps.11501301201;
Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F.,
Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R.,
Appel R.D., Hughes G.J.;
"Human liver protein map: a reference database established by
microsequencing and gel comparison.";
Electrophoresis 13:992-1001(1992).
[15]
PROTEIN SEQUENCE OF 61-72, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (OCT-2004) to UniProtKB.
[16]
PROTEIN SEQUENCE OF 61-72; 206-218; 237-249; 251-290; 430-446 AND
463-469, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[17]
PROTEIN SEQUENCE OF 97-121; 251-268 AND 430-446.
TISSUE=Adipocyte;
PubMed=15242332; DOI=10.1042/BJ20040647;
Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.;
"Vectorial proteomics reveal targeting, phosphorylation and specific
fragmentation of polymerase I and transcript release factor (PTRF) at
the surface of caveolae in human adipocytes.";
Biochem. J. 383:237-248(2004).
[18]
PARTIAL PROTEIN SEQUENCE.
TISSUE=Colon carcinoma;
PubMed=9150948; DOI=10.1002/elps.1150180344;
Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.;
"A two-dimensional gel database of human colon carcinoma proteins.";
Electrophoresis 18:605-613(1997).
[19]
MITOCHONDRIAL IMPORT.
PubMed=1972619; DOI=10.1016/0006-291X(90)90344-M;
Singh B., Patel H.V., Ridley R.G., Freeman K.B., Gupta R.S.;
"Mitochondrial import of the human chaperonin (HSP60) protein.";
Biochem. Biophys. Res. Commun. 169:391-396(1990).
[20]
FUNCTION, AND SUBUNIT.
PubMed=1346131;
Viitanen P.V., Lorimer G.H., Seetharam R., Gupta R.S., Oppenheim J.,
Thomas J.O., Cowan N.J.;
"Mammalian mitochondrial chaperonin 60 functions as a single toroidal
ring.";
J. Biol. Chem. 267:695-698(1992).
[21]
FUNCTION, AND SUBUNIT.
PubMed=11422376; DOI=10.1046/j.1432-1327.2001.02243.x;
Levy-Rimler G., Viitanen P., Weiss C., Sharkia R., Greenberg A.,
Niv A., Lustig A., Delarea Y., Azem A.;
"The effect of nucleotides and mitochondrial chaperonin 10 on the
structure and chaperone activity of mitochondrial chaperonin 60.";
Eur. J. Biochem. 268:3465-3472(2001).
[22]
INTERACTION WITH HBV PROTEIN X (MICROBIAL INFECTION).
PubMed=15120623; DOI=10.1016/j.bbrc.2004.04.046;
Tanaka Y., Kanai F., Kawakami T., Tateishi K., Ijichi H., Kawabe T.,
Arakawa Y., Kawakami T., Nishimura T., Shirakata Y., Koike K.,
Omata M.;
"Interaction of the hepatitis B virus X protein (HBx) with heat shock
protein 60 enhances HBx-mediated apoptosis.";
Biochem. Biophys. Res. Commun. 318:461-469(2004).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[27]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-82; LYS-125; LYS-130;
LYS-202; LYS-218; LYS-269; LYS-352; LYS-359; LYS-396 AND LYS-469, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[30]
MALONYLATION AT LYS-133.
PubMed=21908771; DOI=10.1074/mcp.M111.012658;
Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,
He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,
Dai J., Verdin E., Ye Y., Zhao Y.;
"The first identification of lysine malonylation substrates and its
regulatory enzyme.";
Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[32]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22905912; DOI=10.1021/pr300539b;
Rosenow A., Noben J.P., Jocken J., Kallendrusch S.,
Fischer-Posovszky P., Mariman E.C., Renes J.;
"Resveratrol-induced changes of the human adipocyte secretion
profile.";
J. Proteome Res. 11:4733-4743(2012).
[33]
INTERACTION WITH ATAD3A.
PubMed=22664726; DOI=10.1016/j.mito.2012.05.005;
Merle N., Feraud O., Gilquin B., Hubstenberger A.,
Kieffer-Jacquinot S., Assard N., Bennaceur-Griscelli A., Honnorat J.,
Baudier J.;
"ATAD3B is a human embryonic stem cell specific mitochondrial protein,
re-expressed in cancer cells, that functions as dominant negative for
the ubiquitous ATAD3A.";
Mitochondrion 12:441-448(2012).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70 AND SER-488, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[35]
INTERACTION WITH ETFBKMT AND METTL21B.
PubMed=23349634; DOI=10.1371/journal.pgen.1003210;
Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.;
"A newly uncovered group of distantly related lysine
methyltransferases preferentially interact with molecular chaperones
to regulate their activity.";
PLoS Genet. 9:E1003210-E1003210(2013).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67 AND TYR-90, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[37]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[38]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-551, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[39]
X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 27-556 IN COMPLEX WITH ADP,
SUBUNIT, AND FUNCTION.
PubMed=25918392; DOI=10.1073/pnas.1411718112;
Nisemblat S., Yaniv O., Parnas A., Frolow F., Azem A.;
"Crystal structure of the human mitochondrial chaperonin symmetrical
football complex.";
Proc. Natl. Acad. Sci. U.S.A. 112:6044-6049(2015).
[40]
VARIANT SPG13 ILE-98.
PubMed=11898127; DOI=10.1086/339935;
Hansen J.J., Durr A., Cournu-Rebeix I., Georgopoulos C., Ang D.,
Nielsen M.N., Davoine C.-S., Brice A., Fontaine B., Gregersen N.,
Bross P.;
"Hereditary spastic paraplegia SPG13 is associated with a mutation in
the gene encoding the mitochondrial chaperonin Hsp60.";
Am. J. Hum. Genet. 70:1328-1332(2002).
[41]
VARIANT HLD4 GLY-29, AND CHARACTERIZATION OF VARIANT HLD4 GLY-29.
PubMed=18571143; DOI=10.1016/j.ajhg.2008.05.016;
Magen D., Georgopoulos C., Bross P., Ang D., Segev Y., Goldsher D.,
Nemirovski A., Shahar E., Ravid S., Luder A., Heno B.,
Gershoni-Baruch R., Skorecki K., Mandel H.;
"Mitochondrial Hsp60 chaperonopathy causes an autosomal-recessive
neurodegenerative disorder linked to brain hypomyelination and
leukodystrophy.";
Am. J. Hum. Genet. 83:30-42(2008).
-!- FUNCTION: Chaperonin implicated in mitochondrial protein import
and macromolecular assembly. Together with Hsp10, facilitates the
correct folding of imported proteins. May also prevent misfolding
and promote the refolding and proper assembly of unfolded
polypeptides generated under stress conditions in the
mitochondrial matrix (PubMed:1346131, PubMed:11422376). The
functional units of these chaperonins consist of heptameric rings
of the large subunit Hsp60, which function as a back-to-back
double ring. In a cyclic reaction, Hsp60 ring complexes bind one
unfolded substrate protein per ring, followed by the binding of
ATP and association with 2 heptameric rings of the co-chaperonin
Hsp10. This leads to sequestration of the substrate protein in the
inner cavity of Hsp60 where, for a certain period of time, it can
fold undisturbed by other cell components. Synchronous hydrolysis
of ATP in all Hsp60 subunits results in the dissociation of the
chaperonin rings and the release of ADP and the folded substrate
protein (Probable). {ECO:0000269|PubMed:11422376,
ECO:0000269|PubMed:1346131, ECO:0000305|PubMed:25918392}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. {ECO:0000305}.
-!- SUBUNIT: Homoheptamer arranged in a ring structure
(PubMed:1346131, PubMed:11422376, PubMed:25918392). The functional
units of these chaperonins consist of heptameric rings of the
large subunit Hsp60, which function as a back-to-back double ring.
Interacts with 2 heptameric Hsp10 rings to form the symmetrical
football complex (PubMed:25918392). Interacts with HRAS (By
similarity). Interacts with ATAD3A (PubMed:22664726). Interacts
with ETFBKMT and METTL21B (PubMed:23349634).
{ECO:0000250|UniProtKB:P63038, ECO:0000269|PubMed:11422376,
ECO:0000269|PubMed:1346131, ECO:0000269|PubMed:15120623,
ECO:0000269|PubMed:22664726, ECO:0000269|PubMed:23349634,
ECO:0000269|PubMed:25918392}.
-!- SUBUNIT: (Microbial infection) Interacts with HBV protein X and
HTLV-1 protein p40tax (PubMed:15120623, PubMed:1731090).
{ECO:0000269|PubMed:1731090}.
-!- INTERACTION:
P38398:BRCA1; NbExp=2; IntAct=EBI-352528, EBI-349905;
Q8NHQ1:CEP70; NbExp=3; IntAct=EBI-352528, EBI-739624;
P49789:FHIT; NbExp=5; IntAct=EBI-352528, EBI-741760;
Q15323:KRT31; NbExp=3; IntAct=EBI-352528, EBI-948001;
Q6A162:KRT40; NbExp=3; IntAct=EBI-352528, EBI-10171697;
P60410:KRTAP10-8; NbExp=3; IntAct=EBI-352528, EBI-10171774;
P26371:KRTAP5-9; NbExp=3; IntAct=EBI-352528, EBI-3958099;
Q9BRK4:LZTS2; NbExp=7; IntAct=EBI-352528, EBI-741037;
Q9Y4C4:MFHAS1; NbExp=3; IntAct=EBI-352528, EBI-2864441;
Q7Z3S9:NOTCH2NL; NbExp=3; IntAct=EBI-352528, EBI-945833;
O76081:RGS20; NbExp=3; IntAct=EBI-352528, EBI-1052678;
O76081-6:RGS20; NbExp=3; IntAct=EBI-352528, EBI-10178530;
Q8N6K7:SAMD3; NbExp=3; IntAct=EBI-352528, EBI-748741;
Q9JJY3:Smpd3 (xeno); NbExp=3; IntAct=EBI-352528, EBI-9817007;
O75069-4:TMCC2; NbExp=6; IntAct=EBI-352528, EBI-10177480;
-!- SUBCELLULAR LOCATION: Mitochondrion matrix.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P10809-1; Sequence=Displayed;
Name=2;
IsoId=P10809-2; Sequence=VSP_056144, VSP_056145;
Note=No experimental confirmation available.;
-!- DISEASE: Spastic paraplegia 13, autosomal dominant (SPG13)
[MIM:605280]: A form of spastic paraplegia, a neurodegenerative
disorder characterized by a slow, gradual, progressive weakness
and spasticity of the lower limbs. Rate of progression and the
severity of symptoms are quite variable. Initial symptoms may
include difficulty with balance, weakness and stiffness in the
legs, muscle spasms, and dragging the toes when walking. In some
forms of the disorder, bladder symptoms (such as incontinence) may
appear, or the weakness and stiffness may spread to other parts of
the body. {ECO:0000269|PubMed:11898127}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: Leukodystrophy, hypomyelinating, 4 (HLD4) [MIM:612233]: A
severe autosomal recessive hypomyelinating leukodystrophy.
Clinically characterized by infantile-onset rotary nystagmus,
progressive spastic paraplegia, neurologic regression, motor
impairment, profound mental retardation. Death usually occurs
within the first two decades of life.
{ECO:0000269|PubMed:18571143}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/HSPD1ID40888ch2q33.html";
-----------------------------------------------------------------------
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EMBL; M22382; AAA60127.1; -; mRNA.
EMBL; M34664; AAA36022.1; -; mRNA.
EMBL; AJ250915; CAB75426.1; -; Genomic_DNA.
EMBL; DQ217936; ABB01006.1; -; Genomic_DNA.
EMBL; AK301276; BAH13448.1; -; mRNA.
EMBL; AK312240; BAG35173.1; -; mRNA.
EMBL; AC010746; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC020550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC114809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC002676; AAH02676.1; -; mRNA.
EMBL; BC003030; AAH03030.1; -; mRNA.
EMBL; BC067082; AAH67082.1; -; mRNA.
EMBL; BC073746; AAH73746.1; -; mRNA.
CCDS; CCDS33357.1; -. [P10809-1]
PIR; A32800; A32800.
RefSeq; NP_002147.2; NM_002156.4. [P10809-1]
RefSeq; NP_955472.1; NM_199440.1. [P10809-1]
UniGene; Hs.595053; -.
UniGene; Hs.727543; -.
PDB; 4PJ1; X-ray; 3.15 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=27-556.
PDBsum; 4PJ1; -.
ProteinModelPortal; P10809; -.
SMR; P10809; -.
BioGrid; 109561; 289.
CORUM; P10809; -.
DIP; DIP-58N; -.
IntAct; P10809; 119.
MINT; MINT-1162735; -.
STRING; 9606.ENSP00000340019; -.
ChEMBL; CHEMBL4721; -.
iPTMnet; P10809; -.
PhosphoSitePlus; P10809; -.
SwissPalm; P10809; -.
BioMuta; HSPD1; -.
DMDM; 129379; -.
DOSAC-COBS-2DPAGE; P10809; -.
OGP; P10809; -.
REPRODUCTION-2DPAGE; IPI00784154; -.
REPRODUCTION-2DPAGE; P10809; -.
SWISS-2DPAGE; P10809; -.
UCD-2DPAGE; P10809; -.
EPD; P10809; -.
MaxQB; P10809; -.
PaxDb; P10809; -.
PeptideAtlas; P10809; -.
PRIDE; P10809; -.
TopDownProteomics; P10809-1; -. [P10809-1]
DNASU; 3329; -.
Ensembl; ENST00000345042; ENSP00000340019; ENSG00000144381. [P10809-1]
Ensembl; ENST00000388968; ENSP00000373620; ENSG00000144381. [P10809-1]
GeneID; 3329; -.
KEGG; hsa:3329; -.
UCSC; uc002uui.4; human. [P10809-1]
CTD; 3329; -.
DisGeNET; 3329; -.
EuPathDB; HostDB:ENSG00000144381.16; -.
GeneCards; HSPD1; -.
HGNC; HGNC:5261; HSPD1.
HPA; CAB002775; -.
HPA; CAB072816; -.
HPA; HPA001523; -.
HPA; HPA050025; -.
MalaCards; HSPD1; -.
MIM; 118190; gene.
MIM; 605280; phenotype.
MIM; 612233; phenotype.
neXtProt; NX_P10809; -.
OpenTargets; ENSG00000144381; -.
Orphanet; 100994; Autosomal dominant spastic paraplegia type 13.
Orphanet; 280288; Pelizaeus-Merzbacher-like disease due to HSPD1 mutation.
PharmGKB; PA29527; -.
eggNOG; KOG0356; Eukaryota.
eggNOG; COG0459; LUCA.
GeneTree; ENSGT00390000005727; -.
HOGENOM; HOG000076290; -.
HOVERGEN; HBG001982; -.
InParanoid; P10809; -.
KO; K04077; -.
OMA; TDTDKME; -.
OrthoDB; EOG091G04JM; -.
PhylomeDB; P10809; -.
TreeFam; TF300475; -.
Reactome; R-HSA-1268020; Mitochondrial protein import.
Reactome; R-HSA-8869496; TFAP2A acts as a transcriptional repressor during retinoic acid induced cell differentiation.
ChiTaRS; HSPD1; human.
GeneWiki; GroEL; -.
GenomeRNAi; 3329; -.
PRO; PR:P10809; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000144381; -.
CleanEx; HS_HSPD1; -.
ExpressionAtlas; P10809; baseline and differential.
Genevisible; P10809; HS.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005905; C:clathrin-coated pit; IDA:BHF-UCL.
GO; GO:0030135; C:coated vesicle; IDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005769; C:early endosome; IDA:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0046696; C:lipopolysaccharide receptor complex; IDA:BHF-UCL.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005743; C:mitochondrial inner membrane; ISS:BHF-UCL.
GO; GO:0005759; C:mitochondrial matrix; IDA:CAFA.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:CAFA.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0030141; C:secretory granule; ISS:BHF-UCL.
GO; GO:0034186; F:apolipoprotein A-I binding; IPI:CAFA.
GO; GO:0034185; F:apolipoprotein binding; IPI:CAFA.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; ISS:BHF-UCL.
GO; GO:0051087; F:chaperone binding; IPI:UniProtKB.
GO; GO:0003688; F:DNA replication origin binding; ISS:BHF-UCL.
GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
GO; GO:0019899; F:enzyme binding; IPI:CAFA.
GO; GO:0008035; F:high-density lipoprotein particle binding; IDA:CAFA.
GO; GO:0001530; F:lipopolysaccharide binding; IDA:BHF-UCL.
GO; GO:0002039; F:p53 binding; IPI:UniProtKB.
GO; GO:0044183; F:protein binding involved in protein folding; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0003697; F:single-stranded DNA binding; ISS:BHF-UCL.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0051082; F:unfolded protein binding; ISS:BHF-UCL.
GO; GO:0006458; P:'de novo' protein folding; ISS:BHF-UCL.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:BHF-UCL.
GO; GO:0008637; P:apoptotic mitochondrial changes; IBA:GO_Central.
GO; GO:0042113; P:B cell activation; IDA:BHF-UCL.
GO; GO:0002368; P:B cell cytokine production; IDA:BHF-UCL.
GO; GO:0042100; P:B cell proliferation; IDA:BHF-UCL.
GO; GO:0051131; P:chaperone-mediated protein complex assembly; ISS:BHF-UCL.
GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
GO; GO:0051702; P:interaction with symbiont; IMP:CAFA.
GO; GO:0048291; P:isotype switching to IgG isotypes; IDA:BHF-UCL.
GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:BHF-UCL.
GO; GO:0032727; P:positive regulation of interferon-alpha production; IDA:BHF-UCL.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IDA:BHF-UCL.
GO; GO:0032733; P:positive regulation of interleukin-10 production; IDA:BHF-UCL.
GO; GO:0032735; P:positive regulation of interleukin-12 production; IDA:BHF-UCL.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:BHF-UCL.
GO; GO:0043032; P:positive regulation of macrophage activation; IDA:BHF-UCL.
GO; GO:0050870; P:positive regulation of T cell activation; IDA:BHF-UCL.
GO; GO:0002842; P:positive regulation of T cell mediated immune response to tumor cell; IDA:BHF-UCL.
GO; GO:0045041; P:protein import into mitochondrial intermembrane space; IBA:GO_Central.
GO; GO:0051604; P:protein maturation; ISS:BHF-UCL.
GO; GO:0042026; P:protein refolding; IDA:UniProtKB.
GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0009409; P:response to cold; ISS:AgBase.
GO; GO:0006986; P:response to unfolded protein; IDA:BHF-UCL.
GO; GO:0042110; P:T cell activation; IDA:MGI.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd03344; GroEL; 1.
Gene3D; 1.10.560.10; -; 2.
Gene3D; 3.50.7.10; -; 1.
HAMAP; MF_00600; CH60; 1.
InterPro; IPR018370; Chaperonin_Cpn60_CS.
InterPro; IPR001844; Chaprnin_Cpn60.
InterPro; IPR002423; Cpn60/TCP-1.
InterPro; IPR027409; GroEL-like_apical_dom.
InterPro; IPR027413; GROEL-like_equatorial.
Pfam; PF00118; Cpn60_TCP1; 1.
PRINTS; PR00298; CHAPERONIN60.
SUPFAM; SSF52029; SSF52029; 1.
TIGRFAMs; TIGR02348; GroEL; 1.
PROSITE; PS00296; CHAPERONINS_CPN60; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding;
Chaperone; Complete proteome; Direct protein sequencing;
Disease mutation; Hereditary spastic paraplegia;
Host-virus interaction; Hydrolase; Isopeptide bond; Leukodystrophy;
Mitochondrion; Neurodegeneration; Nucleotide-binding; Phosphoprotein;
Reference proteome; Transit peptide; Ubl conjugation.
TRANSIT 1 26 Mitochondrion.
{ECO:0000269|PubMed:12665801,
ECO:0000269|PubMed:1286669,
ECO:0000269|PubMed:1731090,
ECO:0000269|PubMed:2079031,
ECO:0000269|PubMed:2907406,
ECO:0000269|PubMed:7895732,
ECO:0000269|PubMed:9150946}.
CHAIN 27 573 60 kDa heat shock protein, mitochondrial.
/FTId=PRO_0000005026.
NP_BIND 111 115 ATP. {ECO:0000244|PDB:4PJ1,
ECO:0000269|PubMed:25918392}.
BINDING 75 75 ATP. {ECO:0000244|PDB:4PJ1,
ECO:0000269|PubMed:25918392}.
BINDING 440 440 ATP; via amide nitrogen and carbonyl
oxygen. {ECO:0000244|PDB:4PJ1,
ECO:0000269|PubMed:25918392}.
BINDING 520 520 ATP. {ECO:0000244|PDB:4PJ1,
ECO:0000269|PubMed:25918392}.
MOD_RES 31 31 N6-succinyllysine.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 67 67 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 70 70 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 75 75 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 82 82 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 82 82 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 87 87 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 90 90 Phosphotyrosine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 91 91 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 125 125 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 125 125 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 130 130 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 133 133 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 133 133 N6-malonyllysine; alternate.
{ECO:0000269|PubMed:21908771}.
MOD_RES 133 133 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 156 156 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 191 191 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 191 191 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 202 202 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 202 202 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 205 205 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 205 205 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 218 218 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 218 218 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 236 236 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 236 236 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 249 249 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 250 250 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 250 250 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 269 269 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 292 292 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 301 301 N6-succinyllysine.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 314 314 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 352 352 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 352 352 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 359 359 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 389 389 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 396 396 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 396 396 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 410 410 Phosphoserine.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 469 469 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 481 481 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 481 481 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 488 488 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 551 551 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 144 158 VMLAVDAVIAELKKQ -> RNVCCHHSVLNFSVL (in
isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056144.
VAR_SEQ 159 573 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056145.
VARIANT 29 29 D -> G (in HLD4; transfection with the
mutant protein impairs cell growth that
worsens with increasing temperature;
dbSNP:rs72466451).
{ECO:0000269|PubMed:18571143}.
/FTId=VAR_054785.
VARIANT 98 98 V -> I (in SPG13; dbSNP:rs66468541).
{ECO:0000269|PubMed:11898127}.
/FTId=VAR_026748.
CONFLICT 67 67 S -> G (in Ref. 2; AAA36022).
{ECO:0000305}.
CONFLICT 111 111 D -> N (in Ref. 5; BAG35173).
{ECO:0000305}.
CONFLICT 177 177 N -> S (in Ref. 5; BAG35173).
{ECO:0000305}.
CONFLICT 202 202 K -> KAS (in Ref. 4; ABB01006).
{ECO:0000305}.
CONFLICT 260 260 A -> T (in Ref. 5; BAG35173).
{ECO:0000305}.
STRAND 27 32 {ECO:0000244|PDB:4PJ1}.
HELIX 34 51 {ECO:0000244|PDB:4PJ1}.
HELIX 52 54 {ECO:0000244|PDB:4PJ1}.
STRAND 61 64 {ECO:0000244|PDB:4PJ1}.
STRAND 67 70 {ECO:0000244|PDB:4PJ1}.
STRAND 72 74 {ECO:0000244|PDB:4PJ1}.
HELIX 77 83 {ECO:0000244|PDB:4PJ1}.
HELIX 89 108 {ECO:0000244|PDB:4PJ1}.
HELIX 113 130 {ECO:0000244|PDB:4PJ1}.
HELIX 137 158 {ECO:0000244|PDB:4PJ1}.
HELIX 165 175 {ECO:0000244|PDB:4PJ1}.
TURN 176 178 {ECO:0000244|PDB:4PJ1}.
HELIX 180 193 {ECO:0000244|PDB:4PJ1}.
STRAND 197 203 {ECO:0000244|PDB:4PJ1}.
STRAND 205 208 {ECO:0000244|PDB:4PJ1}.
STRAND 210 214 {ECO:0000244|PDB:4PJ1}.
STRAND 216 220 {ECO:0000244|PDB:4PJ1}.
HELIX 226 228 {ECO:0000244|PDB:4PJ1}.
STRAND 232 235 {ECO:0000244|PDB:4PJ1}.
STRAND 237 249 {ECO:0000244|PDB:4PJ1}.
HELIX 254 266 {ECO:0000244|PDB:4PJ1}.
STRAND 271 276 {ECO:0000244|PDB:4PJ1}.
HELIX 280 292 {ECO:0000244|PDB:4PJ1}.
STRAND 297 301 {ECO:0000244|PDB:4PJ1}.
STRAND 305 307 {ECO:0000244|PDB:4PJ1}.
HELIX 308 320 {ECO:0000244|PDB:4PJ1}.
STRAND 324 326 {ECO:0000244|PDB:4PJ1}.
STRAND 328 330 {ECO:0000244|PDB:4PJ1}.
HELIX 339 341 {ECO:0000244|PDB:4PJ1}.
STRAND 344 350 {ECO:0000244|PDB:4PJ1}.
STRAND 355 360 {ECO:0000244|PDB:4PJ1}.
HELIX 364 378 {ECO:0000244|PDB:4PJ1}.
HELIX 387 396 {ECO:0000244|PDB:4PJ1}.
TURN 397 399 {ECO:0000244|PDB:4PJ1}.
STRAND 401 406 {ECO:0000244|PDB:4PJ1}.
HELIX 411 433 {ECO:0000244|PDB:4PJ1}.
STRAND 436 438 {ECO:0000244|PDB:4PJ1}.
TURN 439 441 {ECO:0000244|PDB:4PJ1}.
HELIX 442 445 {ECO:0000244|PDB:4PJ1}.
HELIX 448 452 {ECO:0000244|PDB:4PJ1}.
HELIX 459 471 {ECO:0000244|PDB:4PJ1}.
HELIX 474 483 {ECO:0000244|PDB:4PJ1}.
HELIX 487 496 {ECO:0000244|PDB:4PJ1}.
STRAND 501 504 {ECO:0000244|PDB:4PJ1}.
TURN 505 508 {ECO:0000244|PDB:4PJ1}.
STRAND 509 512 {ECO:0000244|PDB:4PJ1}.
HELIX 513 516 {ECO:0000244|PDB:4PJ1}.
STRAND 519 521 {ECO:0000244|PDB:4PJ1}.
HELIX 522 539 {ECO:0000244|PDB:4PJ1}.
STRAND 542 548 {ECO:0000244|PDB:4PJ1}.
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


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