CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020537
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Heat shock protein 75 kDa, mitochondrial 
Protein Synonyms/Alias
 HSP 75; TNFR-associated protein 1; Tumor necrosis factor type 1 receptor-associated protein; TRAP-1 
Gene Name
 Trap1 
Gene Synonyms/Alias
 Hsp75 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
89AVRGSVSKHEFQAETacetylation[1, 2]
111ARSLYSEKEVFIRELacetylation[3]
152IHLQTDAKKGTITIQacetylation[3]
264IHLKSDCKDFASESRacetylation[2, 3, 4]
326YIAQAYDKPRFTLHYacetylation[2, 3, 5]
326YIAQAYDKPRFTLHYsuccinylation[5]
334PRFTLHYKTDAPLNIacetylation[2, 3, 4]
334PRFTLHYKTDAPLNIubiquitination[6]
351IFYVPEMKPSMFDVSacetylation[4]
426VLQQRLIKFFIDQSKacetylation[2, 3, 4, 5, 7]
426VLQQRLIKFFIDQSKsuccinylation[5]
433KFFIDQSKKDAEKYAacetylation[2, 3]
438QSKKDAEKYAKFFEDacetylation[3]
579ADERLSEKETEDLMAacetylation[4]
654NPRHTLIKKLCQLREacetylation[3]
Reference
 [1] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [2] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [3] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [4] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [5] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [6] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [7] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758
Functional Description
 Chaperone that expresses an ATPase activity (By similarity). 
Sequence Annotation
 BINDING 121 121 ATP (By similarity).
 BINDING 160 160 ATP (By similarity).
 BINDING 173 173 ATP (By similarity).
 BINDING 207 207 ATP; via amide nitrogen (By similarity).
 BINDING 404 404 ATP (By similarity).
 MOD_RES 89 89 N6-acetyllysine.
 MOD_RES 172 172 Phosphoserine (By similarity).
 MOD_RES 176 176 Phosphothreonine (By similarity).
 MOD_RES 334 334 N6-acetyllysine (By similarity).
 MOD_RES 403 403 Phosphoserine (By similarity).
 MOD_RES 426 426 N6-acetyllysine (By similarity).
 MOD_RES 468 468 N6-acetyllysine (By similarity).
 MOD_RES 496 496 Phosphothreonine (By similarity).  
Keyword
 Acetylation; ATP-binding; Chaperone; Complete proteome; Direct protein sequencing; Mitochondrion; Nucleotide-binding; Phosphoprotein; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 706 AA 
Protein Sequence
MACELRAVLL WGRGLQTVLR APALAGVRRG KPVLHLQKTT VQFRGPTQSL ASGISAGQLY 60
STQAAEDKEE ESLHSIISNT EAVRGSVSKH EFQAETKKLL DIVARSLYSE KEVFIRELIS 120
NASDALEKLR HKLVCEGQVL PEMEIHLQTD AKKGTITIQD TGIGMTQEEL VSNLGTIARS 180
GSKAFLEALQ NQAETSSKII GQFGVGFYSA FMVADKVEVY SRSAAPESPG YQWLSDGSGV 240
FEIAEASGVR PGTKIIIHLK SDCKDFASES RVQDVVTKYS NFVSFPLYLN GKRINTLQAI 300
WMMDPKDISE FQHEEFYRYI AQAYDKPRFT LHYKTDAPLN IRSIFYVPEM KPSMFDVSRE 360
LGSSVALYSR KVLIQTKAAD ILPKWLRFIR GVVDSEDIPL NLSRELLQES ALIRKLRDVL 420
QQRLIKFFID QSKKDAEKYA KFFEDYGLFM REGIVTTAEQ DIKEDIAKLL RYESSALPAG 480
QLTSLPDYAS RMQAGTRNIY YLCAPNRHLA EHSPYYEAMK QKHTEVLFCY EQFDELTLLH 540
LREFDKKKLI SVETDIVVDH YKEEKFEDTS PADERLSEKE TEDLMAWMRN ALGSRVTNVK 600
VTFRLDTHPA MVTVLEMGAA RHFLRMQQLA KTQEERAQLL QPTLEINPRH TLIKKLCQLR 660
ESEPELAQLL VDQIYENAMI AAGLVDDPRA MVGRLNDLLV KVLEKH 706 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0034599; P:cellular response to oxidative stress; IEA:Compara.
 GO:0006457; P:protein folding; IEA:InterPro. 
Interpro
 IPR003594; HATPase_ATP-bd.
 IPR001404; Hsp90.
 IPR020575; Hsp90_N.
 IPR020568; Ribosomal_S5_D2-typ_fold. 
Pfam
 PF00183; HSP90 
SMART
 SM00387; HATPase_c 
PROSITE
 PS00298; HSP90 
PRINTS
 PR00775; HEATSHOCK90.