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 27-MAR-2024, entry version 222. 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="https://atlasgeneticsoncology.org/gene/42692/TRAP1"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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 PDB; 7U8U; X-ray; 3.06 A; A/B=70-552. DR PDB; 7U8V; X-ray; 1.45 A; A=70-552. DR PDB; 7U8W; X-ray; 1.71 A; A=70-552. DR PDB; 7U8X; X-ray; 1.60 A; A=70-552. DR PDB; 7ULK; X-ray; 2.34 A; A/B=60-561. 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 PDBsum; 7U8U; -. DR PDBsum; 7U8V; -. DR PDBsum; 7U8W; -. DR PDBsum; 7U8X; -. DR PDBsum; 7ULK; -. DR AlphaFoldDB; Q12931; -. DR BMRB; Q12931; -. DR EMDB; EMD-22811; -. DR EMDB; EMD-22812; -. DR EMDB; EMD-22813; -. DR EMDB; EMD-22814; -. DR EMDB; EMD-22815; -. DR EMDB; EMD-22816; -. DR EMDB; EMD-22918; -. DR EMDB; EMD-22919; -. DR SMR; Q12931; -. DR BioGRID; 115435; 452. DR CORUM; Q12931; -. DR DIP; DIP-6250N; -. DR IntAct; Q12931; 87. 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; 9606-ENSP00000246957; -. DR PeptideAtlas; Q12931; -. DR ProteomicsDB; 27722; -. DR ProteomicsDB; 59034; -. [Q12931-1] DR Pumba; Q12931; -. DR Antibodypedia; 3798; 790 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 AGR; HGNC:16264; -. DR CTD; 10131; -. DR DisGeNET; 10131; -. DR GeneCards; TRAP1; -. DR HGNC; HGNC:16264; TRAP1. DR HPA; ENSG00000126602; Low tissue specificity. DR MalaCards; TRAP1; -. 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; DHTQQNE; -. DR OrthoDB; 5485387at2759; -. DR PhylomeDB; Q12931; -. DR TreeFam; TF315234; -. DR PathwayCommons; Q12931; -. DR Reactome; R-HSA-611105; Respiratory electron transport. DR SignaLink; Q12931; -. DR BioGRID-ORCS; 10131; 9 hits in 1160 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 204 other cell types or tissues. DR ExpressionAtlas; Q12931; baseline and differential. 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:0140662; F:ATP-dependent protein folding chaperone; 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 CDD; cd16927; HATPase_Hsp90-like; 1. DR Gene3D; 3.30.230.80; -; 1. DR Gene3D; 3.40.50.11260; -; 1. DR Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1. DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 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_Su5_D2-typ_SF. DR PANTHER; PTHR11528:SF44; HEAT SHOCK PROTEIN 75 KDA, MITOCHONDRIAL; 1. DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1. DR Pfam; PF13589; HATPase_c_3; 1. DR Pfam; PF00183; HSP90; 1. DR PIRSF; PIRSF002583; Hsp90; 1. DR PRINTS; PR00775; HEATSHOCK90. DR SMART; SM00387; HATPase_c; 1. DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1. DR SUPFAM; SSF110942; HSP90 C-terminal domain; 1. DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1. DR Genevisible; Q12931; HS. 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 HELIX 298..300 FT /evidence="ECO:0007829|PDB:7ULK" FT TURN 303..305 FT /evidence="ECO:0007829|PDB:7ULK" FT HELIX 308..319 FT /evidence="ECO:0007829|PDB:7ULK" FT STRAND 325..333 FT /evidence="ECO:0007829|PDB:7ULK" FT STRAND 335..337 FT /evidence="ECO:0007829|PDB:7ULK" FT STRAND 339..348 FT /evidence="ECO:0007829|PDB:7ULK" FT HELIX 352..356 FT /evidence="ECO:0007829|PDB:7ULK" FT STRAND 363..367 FT /evidence="ECO:0007829|PDB:7ULK" FT STRAND 370..373 FT /evidence="ECO:0007829|PDB:7ULK" FT STRAND 377..380 FT /evidence="ECO:0007829|PDB:7ULK" FT HELIX 382..384 FT /evidence="ECO:0007829|PDB:7ULK" FT STRAND 388..392 FT /evidence="ECO:0007829|PDB:7ULK" FT STRAND 402..405 FT /evidence="ECO:0007829|PDB:5HPH" FT HELIX 412..432 FT /evidence="ECO:0007829|PDB:7ULK" FT HELIX 434..454 FT /evidence="ECO:0007829|PDB:7ULK" FT HELIX 458..465 FT /evidence="ECO:0007829|PDB:7ULK" FT STRAND 469..475 FT /evidence="ECO:0007829|PDB:7ULK" FT HELIX 483..489 FT /evidence="ECO:0007829|PDB:7ULK" FT STRAND 498..501 FT /evidence="ECO:0007829|PDB:7ULK" FT HELIX 505..510 FT /evidence="ECO:0007829|PDB:7ULK" FT HELIX 512..515 FT /evidence="ECO:0007829|PDB:7ULK" 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:7ULK" FT HELIX 530..538 FT /evidence="ECO:0007829|PDB:7ULK" 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 //