TRAP1_HUMAN
ID TRAP1_HUMAN Reviewed; 704 AA.
AC Q12931; B4DR68; D3DUC8; F5H897; O43642; O75235; Q9UHL5;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 3.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Heat shock protein 75 kDa, mitochondrial;
DE Short=HSP 75;
DE AltName: Full=TNFR-associated protein 1;
DE AltName: Full=Tumor necrosis factor type 1 receptor-associated protein;
DE Short=TRAP-1;
DE Flags: Precursor;
GN Name=TRAP1; Synonyms=HSP75;
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], AND VARIANT GLY-307.
RX PubMed=10545594; DOI=10.1093/hmg/8.12.2155;
RA Simmons A.D., Musy M.M., Lopes C.S., Hwang L.-Y., Yang Y.-P., Lovett M.;
RT "A direct interaction between EXT proteins and glycosyltransferases is
RT defective in hereditary multiple exostoses.";
RL Hum. Mol. Genet. 8:2155-2164(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Eye;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 16-704, AND VARIANT GLY-307.
RX PubMed=7876093; DOI=10.1074/jbc.270.28.16630;
RA Song H.Y., Dunbar J.D., Zhang Y.X., Guo D., Donner D.B.;
RT "Identification of a protein with homology to hsp90 that binds the type 1
RT tumor necrosis factor receptor.";
RL J. Biol. Chem. 270:3574-3581(1995).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 53-704, AND VARIANT GLU-395.
RX PubMed=8756626; DOI=10.1128/mcb.16.9.4691;
RA Chen C.-F., Chen Y., Dai K., Chen P.-L., Riley D.J., Lee W.-H.;
RT "A new member of the hsp90 family of molecular chaperones interacts with
RT the retinoblastoma protein during mitosis and after heat shock.";
RL Mol. Cell. Biol. 16:4691-4699(1996).
RN [8]
RP CHARACTERIZATION.
RX PubMed=10652318; DOI=10.1074/jbc.275.5.3305;
RA Felts S.J., Owen B.A.L., Nguyen P., Trepel J., Donner D.B., Toft D.O.;
RT "The hsp90-related protein TRAP1 is a mitochondrial protein with distinct
RT functional properties.";
RL J. Biol. Chem. 275:3305-3312(2000).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-494, 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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-332; LYS-424 AND LYS-466, 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 [11]
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 [12]
RP FUNCTION AS NEGATIVE REGULATOR OF MITOCHONDRIAL RESPIRATION, AND
RP INTERACTION WITH SDHA.
RX PubMed=23747254; DOI=10.1016/j.cmet.2013.04.019;
RA Sciacovelli M., Guzzo G., Morello V., Frezza C., Zheng L., Nannini N.,
RA Calabrese F., Laudiero G., Esposito F., Landriscina M., Defilippi P.,
RA Bernardi P., Rasola A.;
RT "The mitochondrial chaperone TRAP1 promotes neoplastic growth by inhibiting
RT succinate dehydrogenase.";
RL Cell Metab. 17:988-999(2013).
RN [13]
RP FUNCTION.
RX PubMed=23525905; DOI=10.1093/hmg/ddt132;
RA Zhang L., Karsten P., Hamm S., Pogson J.H., Muller-Rischart A.K., Exner N.,
RA Haass C., Whitworth A.J., Winklhofer K.F., Schulz J.B., Voigt A.;
RT "TRAP1 rescues PINK1 loss-of-function phenotypes.";
RL Hum. Mol. Genet. 22:2829-2841(2013).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, AND IDENTIFICATION BY
RP 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 [15]
RP FUNCTION AS NEGATIVE REGULATOR OF MITOCHONDRIAL RESPIRATION, INTERACTION
RP WITH SRC, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=23564345; DOI=10.1073/pnas.1220659110;
RA Yoshida S., Tsutsumi S., Muhlebach G., Sourbier C., Lee M.J., Lee S.,
RA Vartholomaiou E., Tatokoro M., Beebe K., Miyajima N., Mohney R.P., Chen Y.,
RA Hasumi H., Xu W., Fukushima H., Nakamura K., Koga F., Kihara K., Trepel J.,
RA Picard D., Neckers L.;
RT "Molecular chaperone TRAP1 regulates a metabolic switch between
RT mitochondrial respiration and aerobic glycolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E1604-E1612(2013).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568, AND IDENTIFICATION BY
RP 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 [17]
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).
CC -!- FUNCTION: Chaperone that expresses an ATPase activity. Involved in
CC maintaining mitochondrial function and polarization, downstream of
CC PINK1 and mitochondrial complex I. Is a negative regulator of
CC mitochondrial respiration able to modulate the balance between
CC oxidative phosphorylation and aerobic glycolysis. The impact of TRAP1
CC on mitochondrial respiration is probably mediated by modulation of
CC mitochondrial SRC and inhibition of SDHA. {ECO:0000269|PubMed:23525905,
CC ECO:0000269|PubMed:23564345, ECO:0000269|PubMed:23747254}.
CC -!- SUBUNIT: Binds to the intracellular domain of tumor necrosis factor
CC type 1 receptor. Binds to RB1. Interacts with SRC. Interacts with SDHA.
CC {ECO:0000269|PubMed:23564345, ECO:0000269|PubMed:23747254}.
CC -!- INTERACTION:
CC Q12931; Q99714: HSD17B10; NbExp=3; IntAct=EBI-1055869, EBI-79964;
CC Q12931; Q9BXM7-1: PINK1; NbExp=4; IntAct=EBI-1055869, EBI-15643376;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:23564345}.
CC Mitochondrion inner membrane {ECO:0000269|PubMed:23564345}.
CC Mitochondrion matrix {ECO:0000269|PubMed:23564345}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q12931-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q12931-2; Sequence=VSP_055061;
CC -!- TISSUE SPECIFICITY: Found in skeletal muscle, liver, heart, brain,
CC kidney, pancreas, lung, placenta and bladder. Expression is highly
CC reduced in bladder cancer and renal cell carcinoma specimens compared
CC to healthy tissues, but it is increased in other type of tumors.
CC {ECO:0000269|PubMed:23564345}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA87704.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/TRAP1ID42692ch16p13.html";
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DR EMBL; AF154108; AAF15314.1; -; mRNA.
DR EMBL; AK299127; BAG61180.1; -; mRNA.
DR EMBL; AC005203; AAC24722.1; -; Genomic_DNA.
DR EMBL; AC006111; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85338.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85340.1; -; Genomic_DNA.
DR EMBL; BC018950; AAH18950.1; -; mRNA.
DR EMBL; BC023585; AAH23585.1; -; mRNA.
DR EMBL; U12595; AAA87704.1; ALT_FRAME; mRNA.
DR EMBL; AF043254; AAC02679.1; -; mRNA.
DR CCDS; CCDS10508.1; -. [Q12931-1]
DR CCDS; CCDS61824.1; -. [Q12931-2]
DR RefSeq; NP_001258978.1; NM_001272049.1. [Q12931-2]
DR RefSeq; NP_057376.2; NM_016292.2. [Q12931-1]
DR PDB; 4Z1F; X-ray; 2.70 A; A=60-561.
DR PDB; 4Z1G; X-ray; 3.10 A; A=60-561.
DR PDB; 4Z1H; X-ray; 2.90 A; A=60-561.
DR PDB; 4Z1I; X-ray; 3.30 A; A/B/C/D=60-561.
DR PDB; 5F3K; X-ray; 1.82 A; A/B=60-294.
DR PDB; 5F5R; X-ray; 1.85 A; A/B=60-294.
DR PDB; 5HPH; X-ray; 2.43 A; A/B=60-554.
DR PDB; 5Y3N; X-ray; 2.40 A; A=60-561.
DR PDB; 5Y3O; X-ray; 2.70 A; A=60-561.
DR PDB; 6XG6; EM; 3.20 A; A/B=60-704.
DR PDB; 7C04; X-ray; 1.70 A; A=60-294.
DR PDB; 7C05; X-ray; 2.59 A; A=60-561.
DR PDB; 7C7B; X-ray; 1.50 A; A=60-294.
DR PDB; 7C7C; X-ray; 3.00 A; A=60-561.
DR PDB; 7KCK; EM; 3.26 A; A/B=60-704.
DR PDB; 7KCL; EM; 3.14 A; A/B=60-704.
DR PDB; 7KCM; EM; 3.43 A; A/B=60-704.
DR PDB; 7KLU; EM; 3.50 A; A/B/C/D=60-704.
DR PDB; 7KLV; EM; 3.10 A; A/B=60-704.
DR PDBsum; 4Z1F; -.
DR PDBsum; 4Z1G; -.
DR PDBsum; 4Z1H; -.
DR PDBsum; 4Z1I; -.
DR PDBsum; 5F3K; -.
DR PDBsum; 5F5R; -.
DR PDBsum; 5HPH; -.
DR PDBsum; 5Y3N; -.
DR PDBsum; 5Y3O; -.
DR PDBsum; 6XG6; -.
DR PDBsum; 7C04; -.
DR PDBsum; 7C05; -.
DR PDBsum; 7C7B; -.
DR PDBsum; 7C7C; -.
DR PDBsum; 7KCK; -.
DR PDBsum; 7KCL; -.
DR PDBsum; 7KCM; -.
DR PDBsum; 7KLU; -.
DR PDBsum; 7KLV; -.
DR AlphaFoldDB; Q12931; -.
DR BMRB; Q12931; -.
DR SMR; Q12931; -.
DR BioGRID; 115435; 393.
DR CORUM; Q12931; -.
DR DIP; DIP-6250N; -.
DR IntAct; Q12931; 81.
DR MINT; Q12931; -.
DR STRING; 9606.ENSP00000246957; -.
DR BindingDB; Q12931; -.
DR ChEMBL; CHEMBL1075132; -.
DR DrugCentral; Q12931; -.
DR GuidetoPHARMACOLOGY; 2909; -.
DR GlyGen; Q12931; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q12931; -.
DR MetOSite; Q12931; -.
DR PhosphoSitePlus; Q12931; -.
DR SwissPalm; Q12931; -.
DR BioMuta; TRAP1; -.
DR DMDM; 67477458; -.
DR REPRODUCTION-2DPAGE; IPI00030275; -.
DR CPTAC; CPTAC-288; -.
DR CPTAC; CPTAC-289; -.
DR EPD; Q12931; -.
DR jPOST; Q12931; -.
DR MassIVE; Q12931; -.
DR MaxQB; Q12931; -.
DR PaxDb; Q12931; -.
DR PeptideAtlas; Q12931; -.
DR PRIDE; Q12931; -.
DR ProteomicsDB; 27722; -.
DR ProteomicsDB; 59034; -. [Q12931-1]
DR Antibodypedia; 3798; 729 antibodies from 42 providers.
DR DNASU; 10131; -.
DR Ensembl; ENST00000246957.10; ENSP00000246957.5; ENSG00000126602.11. [Q12931-1]
DR Ensembl; ENST00000538171.5; ENSP00000442070.1; ENSG00000126602.11. [Q12931-2]
DR GeneID; 10131; -.
DR KEGG; hsa:10131; -.
DR MANE-Select; ENST00000246957.10; ENSP00000246957.5; NM_016292.3; NP_057376.2.
DR UCSC; uc002cvt.4; human. [Q12931-1]
DR CTD; 10131; -.
DR DisGeNET; 10131; -.
DR GeneCards; TRAP1; -.
DR HGNC; HGNC:16264; TRAP1.
DR HPA; ENSG00000126602; Low tissue specificity.
DR MIM; 606219; gene.
DR neXtProt; NX_Q12931; -.
DR OpenTargets; ENSG00000126602; -.
DR PharmGKB; PA36781; -.
DR VEuPathDB; HostDB:ENSG00000126602; -.
DR eggNOG; KOG0019; Eukaryota.
DR GeneTree; ENSGT01020000230401; -.
DR HOGENOM; CLU_006684_3_1_1; -.
DR InParanoid; Q12931; -.
DR OMA; YTRKVLI; -.
DR PhylomeDB; Q12931; -.
DR TreeFam; TF315234; -.
DR PathwayCommons; Q12931; -.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR SignaLink; Q12931; -.
DR BioGRID-ORCS; 10131; 6 hits in 1075 CRISPR screens.
DR ChiTaRS; TRAP1; human.
DR GeneWiki; TRAP1; -.
DR GenomeRNAi; 10131; -.
DR Pharos; Q12931; Tchem.
DR PRO; PR:Q12931; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q12931; protein.
DR Bgee; ENSG00000126602; Expressed in hindlimb stylopod muscle and 202 other tissues.
DR ExpressionAtlas; Q12931; baseline and differential.
DR Genevisible; Q12931; HS.
DR GO; GO:0071944; C:cell periphery; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0005164; F:tumor necrosis factor receptor binding; NAS:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0061077; P:chaperone-mediated protein folding; TAS:ParkinsonsUK-UCL.
DR GO; GO:1901856; P:negative regulation of cellular respiration; IMP:UniProtKB.
DR GO; GO:1903751; P:negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide; ISS:ParkinsonsUK-UCL.
DR GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; TAS:ParkinsonsUK-UCL.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0009386; P:translational attenuation; IMP:CACAO.
DR Gene3D; 1.20.120.790; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR HAMAP; MF_00505; HSP90; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR PANTHER; PTHR11528; PTHR11528; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF110942; SSF110942; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Chaperone;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1..59
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 60..704
FT /note="Heat shock protein 75 kDa, mitochondrial"
FT /id="PRO_0000013604"
FT BINDING 119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 402
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5XHZ0"
FT MOD_RES 174
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5XHZ0"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 262
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQN1"
FT MOD_RES 324
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQN1"
FT MOD_RES 332
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 424
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 431
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQN1"
FT MOD_RES 466
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 494
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 568
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 30..82
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055061"
FT VARIANT 307
FT /note="R -> G (in dbSNP:rs13926)"
FT /evidence="ECO:0000269|PubMed:10545594,
FT ECO:0000269|PubMed:7876093"
FT /id="VAR_016108"
FT VARIANT 395
FT /note="D -> E (in dbSNP:rs1136948)"
FT /evidence="ECO:0000269|PubMed:8756626"
FT /id="VAR_049625"
FT VARIANT 572
FT /note="E -> K (in dbSNP:rs55766649)"
FT /id="VAR_061272"
FT VARIANT 692
FT /note="R -> H (in dbSNP:rs2791)"
FT /id="VAR_049626"
FT CONFLICT 17..19
FT /note="PLL -> ALR (in Ref. 6; AAA87704)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="L -> M (in Ref. 7; AAC02679)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="G -> D (in Ref. 2; BAG61180)"
FT /evidence="ECO:0000305"
FT CONFLICT 475..476
FT /note="Missing (in Ref. 7; AAC02679)"
FT /evidence="ECO:0000305"
FT CONFLICT 488..491
FT /note="SRMR -> AHW (in Ref. 7; AAC02679)"
FT /evidence="ECO:0000305"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:7C7B"
FT HELIX 94..105
FT /evidence="ECO:0007829|PDB:7C7B"
FT HELIX 106..110
FT /evidence="ECO:0007829|PDB:7C7B"
FT HELIX 111..134
FT /evidence="ECO:0007829|PDB:7C7B"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:7C7B"
FT TURN 149..152
FT /evidence="ECO:0007829|PDB:7C7B"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:7C7B"
FT HELIX 165..170
FT /evidence="ECO:0007829|PDB:7C7B"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:7C7B"
FT HELIX 174..178
FT /evidence="ECO:0007829|PDB:7C7B"
FT HELIX 181..189
FT /evidence="ECO:0007829|PDB:7C7B"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:7KLV"
FT HELIX 194..200
FT /evidence="ECO:0007829|PDB:7C7B"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:5F3K"
FT HELIX 206..210
FT /evidence="ECO:0007829|PDB:7C7B"
FT STRAND 212..220
FT /evidence="ECO:0007829|PDB:7C7B"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:5HPH"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:7C7B"
FT STRAND 235..246
FT /evidence="ECO:0007829|PDB:7C7B"
FT STRAND 249..257
FT /evidence="ECO:0007829|PDB:7C7B"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:7C7B"
FT HELIX 267..274
FT /evidence="ECO:0007829|PDB:7C7B"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:7C7B"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:7C7B"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:7C7B"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:7KLV"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:5HPH"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:5Y3N"
FT HELIX 308..319
FT /evidence="ECO:0007829|PDB:5Y3N"
FT STRAND 325..337
FT /evidence="ECO:0007829|PDB:5Y3N"
FT STRAND 339..348
FT /evidence="ECO:0007829|PDB:5Y3N"
FT TURN 352..354
FT /evidence="ECO:0007829|PDB:7KLV"
FT STRAND 364..367
FT /evidence="ECO:0007829|PDB:5Y3N"
FT STRAND 370..374
FT /evidence="ECO:0007829|PDB:5Y3N"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:7C05"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:5Y3N"
FT STRAND 388..392
FT /evidence="ECO:0007829|PDB:5Y3N"
FT STRAND 402..405
FT /evidence="ECO:0007829|PDB:5HPH"
FT HELIX 411..432
FT /evidence="ECO:0007829|PDB:5Y3N"
FT HELIX 435..454
FT /evidence="ECO:0007829|PDB:5Y3N"
FT HELIX 458..465
FT /evidence="ECO:0007829|PDB:5Y3N"
FT STRAND 470..472
FT /evidence="ECO:0007829|PDB:5Y3N"
FT HELIX 483..489
FT /evidence="ECO:0007829|PDB:5Y3N"
FT STRAND 497..501
FT /evidence="ECO:0007829|PDB:5Y3N"
FT HELIX 505..509
FT /evidence="ECO:0007829|PDB:5Y3N"
FT HELIX 512..515
FT /evidence="ECO:0007829|PDB:5Y3N"
FT TURN 516..518
FT /evidence="ECO:0007829|PDB:5Y3N"
FT STRAND 519..521
FT /evidence="ECO:0007829|PDB:5Y3N"
FT STRAND 525..527
FT /evidence="ECO:0007829|PDB:5Y3N"
FT HELIX 530..539
FT /evidence="ECO:0007829|PDB:5Y3N"
FT STRAND 541..544
FT /evidence="ECO:0007829|PDB:4Z1H"
FT STRAND 547..549
FT /evidence="ECO:0007829|PDB:5Y3N"
FT HELIX 550..556
FT /evidence="ECO:0007829|PDB:7KLV"
FT HELIX 577..589
FT /evidence="ECO:0007829|PDB:7KLV"
FT TURN 590..593
FT /evidence="ECO:0007829|PDB:7KLV"
FT STRAND 595..599
FT /evidence="ECO:0007829|PDB:7KLV"
FT STRAND 607..611
FT /evidence="ECO:0007829|PDB:7KLV"
FT HELIX 615..627
FT /evidence="ECO:0007829|PDB:7KLV"
FT HELIX 631..635
FT /evidence="ECO:0007829|PDB:7KLV"
FT TURN 636..638
FT /evidence="ECO:0007829|PDB:7KLV"
FT STRAND 641..644
FT /evidence="ECO:0007829|PDB:7KLV"
FT HELIX 649..657
FT /evidence="ECO:0007829|PDB:7KLV"
FT TURN 658..660
FT /evidence="ECO:0007829|PDB:7KLV"
FT HELIX 662..680
FT /evidence="ECO:0007829|PDB:7KLV"
FT HELIX 686..689
FT /evidence="ECO:0007829|PDB:7KLV"
FT HELIX 690..700
FT /evidence="ECO:0007829|PDB:7KLV"
FT TURN 701..703
FT /evidence="ECO:0007829|PDB:7KLV"
SQ SEQUENCE 704 AA; 80110 MW; 4B16DE3D2B9E0285 CRC64;
MARELRALLL WGRRLRPLLR APALAAVPGG KPILCPRRTT AQLGPRRNPA WSLQAGRLFS
TQTAEDKEEP LHSIISSTES VQGSTSKHEF QAETKKLLDI VARSLYSEKE VFIRELISNA
SDALEKLRHK LVSDGQALPE MEIHLQTNAE KGTITIQDTG IGMTQEELVS NLGTIARSGS
KAFLDALQNQ AEASSKIIGQ FGVGFYSAFM VADRVEVYSR SAAPGSLGYQ WLSDGSGVFE
IAEASGVRTG TKIIIHLKSD CKEFSSEARV RDVVTKYSNF VSFPLYLNGR RMNTLQAIWM
MDPKDVREWQ HEEFYRYVAQ AHDKPRYTLH YKTDAPLNIR SIFYVPDMKP SMFDVSRELG
SSVALYSRKV LIQTKATDIL PKWLRFIRGV VDSEDIPLNL SRELLQESAL IRKLRDVLQQ
RLIKFFIDQS KKDAEKYAKF FEDYGLFMRE GIVTATEQEV KEDIAKLLRY ESSALPSGQL
TSLSEYASRM RAGTRNIYYL CAPNRHLAEH SPYYEAMKKK DTEVLFCFEQ FDELTLLHLR
EFDKKKLISV ETDIVVDHYK EEKFEDRSPA AECLSEKETE ELMAWMRNVL GSRVTNVKVT
LRLDTHPAMV TVLEMGAARH FLRMQQLAKT QEERAQLLQP TLEINPRHAL IKKLNQLRAS
EPGLAQLLVD QIYENAMIAA GLVDDPRAMV GRLNELLVKA LERH
