CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003841
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 60 kDa heat shock protein, mitochondrial 
Protein Synonyms/Alias
 60 kDa chaperonin; Chaperonin 60; CPN60; Heat shock protein 60; HSP-60; Hsp60; HuCHA60; Mitochondrial matrix protein P1; P60 lymphocyte protein 
Gene Name
 HSPD1 
Gene Synonyms/Alias
 HSP60 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
31RAYAKDVKFGADARAacetylation[1]
31RAYAKDVKFGADARAubiquitination[2, 3, 4]
58VAVTMGPKGRTVIIEubiquitination[2, 4, 5]
72EQSWGSPKVTKDGVTubiquitination[2, 4, 6, 7]
75WGSPKVTKDGVTVAKubiquitination[2, 4, 7]
82KDGVTVAKSIDLKDKacetylation[1]
82KDGVTVAKSIDLKDKubiquitination[2, 3, 4, 5, 7]
87VAKSIDLKDKYKNIGubiquitination[7]
89KSIDLKDKYKNIGAKubiquitination[6, 7]
96KYKNIGAKLVQDVANubiquitination[3, 7, 8]
125VLARSIAKEGFEKISacetylation[1]
125VLARSIAKEGFEKISubiquitination[2, 3, 4, 5, 7]
130IAKEGFEKISKGANPacetylation[1]
130IAKEGFEKISKGANPubiquitination[6, 7]
133EGFEKISKGANPVEImalonylation[9]
133EGFEKISKGANPVEIubiquitination[2, 3, 4, 5, 6, 7, 8]
156DAVIAELKKQSKPVTacetylation[1]
160AELKKQSKPVTTPEEubiquitination[2, 3, 4]
191NIISDAMKKVGRKGVubiquitination[2, 4]
196AMKKVGRKGVITVKDubiquitination[3, 7]
202RKGVITVKDGKTLNDacetylation[1]
202RKGVITVKDGKTLNDubiquitination[3]
205VITVKDGKTLNDELEubiquitination[3]
218LEIIEGMKFDRGYISacetylation[1]
218LEIIEGMKFDRGYISubiquitination[2, 3, 4, 7]
233PYFINTSKGQKCEFQubiquitination[2, 3, 4, 5, 6, 7, 10, 11]
236INTSKGQKCEFQDAYacetylation[11]
236INTSKGQKCEFQDAYubiquitination[7, 11]
249AYVLLSEKKISSIQSacetylation[1, 11]
249AYVLLSEKKISSIQSubiquitination[6]
250YVLLSEKKISSIQSIubiquitination[2, 4, 7, 11]
269EIANAHRKPLVIIAEacetylation[1, 12]
292TLVLNRLKVGLQVVAubiquitination[2, 4, 7, 13]
301GLQVVAVKAPGFGDNubiquitination[3, 11]
352VGEVIVTKDDAMLLKacetylation[1, 11, 12, 14]
352VGEVIVTKDDAMLLKubiquitination[2, 3, 4, 5, 7, 8]
359KDDAMLLKGKGDKAQacetylation[1, 11, 12]
359KDDAMLLKGKGDKAQubiquitination[2, 3, 4, 7, 8]
364LLKGKGDKAQIEKRIacetylation[11]
389TSEYEKEKLNERLAKacetylation[11]
396KLNERLAKLSDGVAVacetylation[1, 11, 14]
396KLNERLAKLSDGVAVubiquitination[3, 7, 11]
417SDVEVNEKKDRVTDAacetylation[11]
417SDVEVNEKKDRVTDAubiquitination[3, 7, 8]
418DVEVNEKKDRVTDALubiquitination[7]
469KIGIEIIKRTLKIPAacetylation[1, 11]
469KIGIEIIKRTLKIPAubiquitination[2, 3, 4, 7, 8, 11]
473EIIKRTLKIPAMTIAacetylation[1, 11]
473EIIKRTLKIPAMTIAubiquitination[5, 7, 11]
481IPAMTIAKNAGVEGSubiquitination[2, 3, 4, 7, 8]
516DFVNMVEKGIIDPTKacetylation[14]
516DFVNMVEKGIIDPTKmethylation[15]
523KGIIDPTKVVRTALLacetylation[1]
523KGIIDPTKVVRTALLubiquitination[3, 7, 11]
551VVVTEIPKEEKDPGMacetylation[1]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [6] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [7] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [8] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [9] The first identification of lysine malonylation substrates and its regulatory enzyme.
 Peng C, Lu Z, Xie Z, Cheng Z, Chen Y, Tan M, Luo H, Zhang Y, He W, Yang K, Zwaans BM, Tishkoff D, Ho L, Lombard D, He TC, Dai J, Verdin E, Ye Y, Zhao Y.
 Mol Cell Proteomics. 2011 Dec;10(12):M111.012658. [PMID: 21908771]
 [10] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [11] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [12] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [13] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [14] 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]
 [15] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510] 
Functional Description
 Implicated in mitochondrial protein import and macromolecular assembly. May facilitate 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. 
Sequence Annotation
 MOD_RES 70 70 Phosphoserine.
 MOD_RES 82 82 N6-acetyllysine.
 MOD_RES 125 125 N6-acetyllysine.
 MOD_RES 130 130 N6-acetyllysine.
 MOD_RES 133 133 N6-malonyllysine.
 MOD_RES 202 202 N6-acetyllysine.
 MOD_RES 218 218 N6-acetyllysine.
 MOD_RES 223 223 Phosphotyrosine (By similarity).
 MOD_RES 269 269 N6-acetyllysine.
 MOD_RES 352 352 N6-acetyllysine.
 MOD_RES 359 359 N6-acetyllysine.
 MOD_RES 396 396 N6-acetyllysine.
 MOD_RES 469 469 N6-acetyllysine.  
Keyword
 Acetylation; ATP-binding; Chaperone; Complete proteome; Direct protein sequencing; Disease mutation; Hereditary spastic paraplegia; Host-virus interaction; Leukodystrophy; Mitochondrion; Neurodegeneration; Nucleotide-binding; Phosphoprotein; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 573 AA 
Protein Sequence
MLRLPTVFRQ MRPVSRVLAP HLTRAYAKDV KFGADARALM LQGVDLLADA VAVTMGPKGR 60
TVIIEQSWGS PKVTKDGVTV AKSIDLKDKY KNIGAKLVQD VANNTNEEAG DGTTTATVLA 120
RSIAKEGFEK ISKGANPVEI RRGVMLAVDA VIAELKKQSK PVTTPEEIAQ VATISANGDK 180
EIGNIISDAM KKVGRKGVIT VKDGKTLNDE LEIIEGMKFD RGYISPYFIN TSKGQKCEFQ 240
DAYVLLSEKK ISSIQSIVPA LEIANAHRKP LVIIAEDVDG EALSTLVLNR LKVGLQVVAV 300
KAPGFGDNRK NQLKDMAIAT GGAVFGEEGL TLNLEDVQPH DLGKVGEVIV TKDDAMLLKG 360
KGDKAQIEKR IQEIIEQLDV TTSEYEKEKL NERLAKLSDG VAVLKVGGTS DVEVNEKKDR 420
VTDALNATRA AVEEGIVLGG GCALLRCIPA LDSLTPANED QKIGIEIIKR TLKIPAMTIA 480
KNAGVEGSLI VEKIMQSSSE VGYDAMAGDF VNMVEKGIID PTKVVRTALL DAAGVASLLT 540
TAEVVVTEIP KEEKDPGMGA MGGMGGGMGG GMF 573 
Gene Ontology
 GO:0009986; C:cell surface; IDA:UniProtKB.
 GO:0005905; C:coated pit; IDA:BHF-UCL.
 GO:0030135; C:coated vesicle; IDA:BHF-UCL.
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0005769; C:early endosome; IDA:BHF-UCL.
 GO:0005615; C:extracellular space; IDA:BHF-UCL.
 GO:0046696; C:lipopolysaccharide receptor complex; IDA:BHF-UCL.
 GO:0005743; C:mitochondrial inner membrane; ISS:BHF-UCL.
 GO:0005759; C:mitochondrial matrix; TAS:BHF-UCL.
 GO:0030141; C:secretory granule; ISS:BHF-UCL.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0016887; F:ATPase activity; ISS:BHF-UCL.
 GO:0003688; F:DNA replication origin binding; ISS:BHF-UCL.
 GO:0001530; F:lipopolysaccharide binding; IDA:BHF-UCL.
 GO:0003697; F:single-stranded DNA binding; ISS:BHF-UCL.
 GO:0051082; F:unfolded protein binding; IC:UniProtKB.
 GO:0006458; P:'de novo' protein folding; ISS:BHF-UCL.
 GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:BHF-UCL.
 GO:0002368; P:B cell cytokine production; IDA:BHF-UCL.
 GO:0042100; P:B cell proliferation; IDA:BHF-UCL.
 GO:0051131; P:chaperone-mediated protein complex assembly; ISS:BHF-UCL.
 GO:0048291; P:isotype switching to IgG isotypes; IDA:BHF-UCL.
 GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; IDA:BHF-UCL.
 GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
 GO:0043065; P:positive regulation of apoptotic process; IMP:BHF-UCL.
 GO:0032727; P:positive regulation of interferon-alpha production; IDA:BHF-UCL.
 GO:0032729; P:positive regulation of interferon-gamma production; IDA:BHF-UCL.
 GO:0032733; P:positive regulation of interleukin-10 production; IDA:BHF-UCL.
 GO:0032735; P:positive regulation of interleukin-12 production; IDA:BHF-UCL.
 GO:0032755; P:positive regulation of interleukin-6 production; IDA:BHF-UCL.
 GO:0043032; P:positive regulation of macrophage activation; IDA:BHF-UCL.
 GO:0050870; P:positive regulation of T cell activation; IDA:BHF-UCL.
 GO:0002842; P:positive regulation of T cell mediated immune response to tumor cell; IDA:BHF-UCL.
 GO:0051604; P:protein maturation; ISS:BHF-UCL.
 GO:0042026; P:protein refolding; IDA:UniProtKB.
 GO:0050821; P:protein stabilization; IMP:UniProtKB.
 GO:0006986; P:response to unfolded protein; IDA:BHF-UCL.
 GO:0042110; P:T cell activation; IDA:MGI.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR018370; Chaperonin_Cpn60_CS.
 IPR001844; Chaprnin_Cpn60.
 IPR002423; Cpn60/TCP-1.
 IPR027409; GroEL-like_apical_dom.
 IPR027413; GROEL-like_equatorial. 
Pfam
 PF00118; Cpn60_TCP1 
SMART
  
PROSITE
 PS00296; CHAPERONINS_CPN60 
PRINTS
 PR00298; CHAPERONIN60.