CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002558
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Heat shock protein HSP 90-alpha 
Protein Synonyms/Alias
 Heat shock 86 kDa; HSP 86; HSP86; Tumor-specific transplantation 86 kDa antigen; TSTA 
Gene Name
 Hsp90aa1 
Gene Synonyms/Alias
 Hsp86; Hsp86-1; Hspca 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
58NSSDALDKIRYESLTubiquitination[1]
69ESLTDPSKLDSGKELubiquitination[1]
74PSKLDSGKELHINLIubiquitination[1]
84HINLIPSKQDRTLTIubiquitination[1]
112NNLGTIAKSGTKAFMubiquitination[1]
204YLEERRIKEIVKKHSacetylation[2]
208RRIKEIVKKHSQFIGacetylation[2]
209RIKEIVKKHSQFIGYacetylation[2, 3]
224PITLFVEKERDKEVSacetylation[3]
224PITLFVEKERDKEVSubiquitination[1]
295QEELNKTKPIWTRNPubiquitination[1]
411LQQSKILKVIRKNLVacetylation[3]
420IRKNLVKKCLELFTEubiquitination[1]
437EDKENYKKFYEQFSKacetylation[3, 4]
437EDKENYKKFYEQFSKsuccinylation[4]
437EDKENYKKFYEQFSKubiquitination[1]
444KFYEQFSKNIKLGIHacetylation[3, 5]
444KFYEQFSKNIKLGIHubiquitination[1]
459EDSQNRKKLSELLRYacetylation[3]
479GDEMVSLKDYCTRMKacetylation[3]
479GDEMVSLKDYCTRMKubiquitination[1]
486KDYCTRMKENQKHIYacetylation[3]
490TRMKENQKHIYFITGacetylation[3, 5, 6]
500YFITGETKDQVANSAacetylation[3]
514AFVERLRKHGLEVIYacetylation[3]
540QLKEFEGKTLVSVTKacetylation[4, 5]
540QLKEFEGKTLVSVTKubiquitination[1]
547KTLVSVTKEGLELPEacetylation[3]
547KTLVSVTKEGLELPEubiquitination[1]
559LPEDEEEKKKQEEKKacetylation[5]
566KKKQEEKKTKFENLCacetylation[3]
568KQEEKKTKFENLCKIacetylation[3]
577ENLCKIMKDILEKKVacetylation[3, 5]
583MKDILEKKVEKVVVSacetylation[3]
586ILEKKVEKVVVSNRLacetylation[3]
616ANMERIMKAQALRDNacetylation[3, 4]
616ANMERIMKAQALRDNsuccinylation[4]
616ANMERIMKAQALRDNubiquitination[1]
632TMGYMAAKKHLEINPacetylation[4]
632TMGYMAAKKHLEINPsuccinylation[4]
632TMGYMAAKKHLEINPubiquitination[1]
633MGYMAAKKHLEINPDacetylation[3, 4]
633MGYMAAKKHLEINPDubiquitination[1]
655RQKAEADKNDKSVKDacetylation[7]
Reference
 [1] 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]
 [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] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [4] 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]
 [5] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [6] 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]
 [7] 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] 
Functional Description
 Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (By similarity). 
Sequence Annotation
 REGION 683 733 Required for homodimerization (By
 MOTIF 729 733 TPR repeat-binding.
 BINDING 51 51 ATP (By similarity).
 BINDING 93 93 ATP (By similarity).
 BINDING 112 112 ATP (By similarity).
 BINDING 138 138 ATP; via amide nitrogen (By similarity).
 BINDING 401 401 ATP (By similarity).
 MOD_RES 5 5 Phosphothreonine; by PRKDC.
 MOD_RES 7 7 Phosphothreonine; by PRKDC.
 MOD_RES 224 224 N6-acetyllysine (By similarity).
 MOD_RES 231 231 Phosphoserine.
 MOD_RES 252 252 Phosphoserine (By similarity).
 MOD_RES 263 263 Phosphoserine.
 MOD_RES 314 314 Phosphotyrosine.
 MOD_RES 400 400 Phosphoserine (By similarity).
 MOD_RES 411 411 N6-acetyllysine (By similarity).
 MOD_RES 444 444 N6-acetyllysine (By similarity).
 MOD_RES 459 459 N6-acetyllysine (By similarity).
 MOD_RES 490 490 N6-acetyllysine (By similarity).
 MOD_RES 493 493 Phosphotyrosine.
 MOD_RES 577 577 N6-acetyllysine (By similarity).
 MOD_RES 586 586 N6-acetyllysine (By similarity).
 MOD_RES 599 599 S-nitrosocysteine (By similarity).  
Keyword
 Acetylation; ATP-binding; Chaperone; Complete proteome; Cytoplasm; Direct protein sequencing; Nucleotide-binding; Phosphoprotein; Reference proteome; S-nitrosylation; Stress response; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 733 AA 
Protein Sequence
MPEETQTQDQ PMEEEEVETF AFQAEIAQLM SLIINTFYSN KEIFLRELIS NSSDALDKIR 60
YESLTDPSKL DSGKELHINL IPSKQDRTLT IVDTGIGMTK ADLINNLGTI AKSGTKAFME 120
ALQAGADISM IGQFGVGFYS AYLVAEKVTV ITKHNDDEQY AWESSAGGSF TVRTDTGEPM 180
GRGTKVILHL KEDQTEYLEE RRIKEIVKKH SQFIGYPITL FVEKERDKEV SDDEAEEKEE 240
KEEEKEKEEK ESDDKPEIED VGSDEEEEEK KDGDKKKKKK IKEKYIDQEE LNKTKPIWTR 300
NPDDITNEEY GEFYKSLTND WEEHLAVKHF SVEGQLEFRA LLFVPRRAPF DLFENRKKKN 360
NIKLYVRRVF IMDNCEELIP EYLNFIRGVV DSEDLPLNIS REMLQQSKIL KVIRKNLVKK 420
CLELFTELAE DKENYKKFYE QFSKNIKLGI HEDSQNRKKL SELLRYYTSA SGDEMVSLKD 480
YCTRMKENQK HIYFITGETK DQVANSAFVE RLRKHGLEVI YMIEPIDEYC VQQLKEFEGK 540
TLVSVTKEGL ELPEDEEEKK KQEEKKTKFE NLCKIMKDIL EKKVEKVVVS NRLVTSPCCI 600
VTSTYGWTAN MERIMKAQAL RDNSTMGYMA AKKHLEINPD HSIIETLRQK AEADKNDKSV 660
KDLVILLYET ALLSSGFSLE DPQTHANRIY RMIKLGLGID EDDPTVDDTS AAVTEEMPPL 720
EGDDDTSRME EVD 733 
Gene Ontology
 GO:0016324; C:apical plasma membrane; IEA:Compara.
 GO:0016323; C:basolateral plasma membrane; IEA:Compara.
 GO:0031526; C:brush border membrane; IEA:Compara.
 GO:0009986; C:cell surface; IEA:Compara.
 GO:0005829; C:cytosol; TAS:UniProtKB.
 GO:0031012; C:extracellular matrix; IEA:Compara.
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0043005; C:neuron projection; IEA:Compara.
 GO:0043025; C:neuronal cell body; IEA:Compara.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:Compara.
 GO:0043234; C:protein complex; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0016887; F:ATPase activity; IEA:Compara.
 GO:0002135; F:CTP binding; IEA:Compara.
 GO:0032564; F:dATP binding; IEA:Compara.
 GO:0005525; F:GTP binding; IEA:Compara.
 GO:0003729; F:mRNA binding; IEA:Compara.
 GO:0030235; F:nitric-oxide synthase regulator activity; IDA:UniProtKB.
 GO:0042803; F:protein homodimerization activity; IDA:MGI.
 GO:0030911; F:TPR domain binding; ISS:UniProtKB.
 GO:0051082; F:unfolded protein binding; TAS:UniProtKB.
 GO:0002134; F:UTP binding; IEA:Compara.
 GO:0010659; P:cardiac muscle cell apoptotic process; IEA:Compara.
 GO:0051131; P:chaperone-mediated protein complex assembly; IEA:Compara.
 GO:0001764; P:neuron migration; IEA:Compara.
 GO:0006809; P:nitric oxide biosynthetic process; TAS:UniProtKB.
 GO:0060452; P:positive regulation of cardiac muscle contraction; IEA:Compara.
 GO:0045793; P:positive regulation of cell size; IEA:Compara.
 GO:0045585; P:positive regulation of cytotoxic T cell differentiation; TAS:UniProtKB.
 GO:0010592; P:positive regulation of lamellipodium assembly; IEA:Compara.
 GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IDA:UniProtKB.
 GO:0033160; P:positive regulation of protein import into nucleus, translocation; IEA:Compara.
 GO:0045040; P:protein import into mitochondrial outer membrane; IEA:Compara.
 GO:0042026; P:protein refolding; TAS:UniProtKB.
 GO:0043627; P:response to estrogen stimulus; IEA:Compara.
 GO:0009408; P:response to heat; IEA:Compara.
 GO:0009651; P:response to salt stress; IEA:Compara.
 GO:0006986; P:response to unfolded protein; TAS:UniProtKB.
 GO:0003009; P:skeletal muscle contraction; IEA:Compara. 
Interpro
 IPR003594; HATPase_ATP-bd.
 IPR019805; Heat_shock_protein_90_CS.
 IPR001404; Hsp90.
 IPR020575; Hsp90_N.
 IPR020568; Ribosomal_S5_D2-typ_fold. 
Pfam
 PF02518; HATPase_c
 PF00183; HSP90 
SMART
 SM00387; HATPase_c 
PROSITE
 PS00298; HSP90 
PRINTS
 PR00775; HEATSHOCK90.