CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008067
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 T-complex protein 1 subunit epsilon 
Protein Synonyms/Alias
 TCP-1-epsilon; CCT-epsilon 
Gene Name
 CCT5 
Gene Synonyms/Alias
 CCTE; KIAA0098 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
20GRPFLIIKDQDRKSRubiquitination[1, 2]
35LMGLEALKSHIMAAKubiquitination[1, 2, 3, 4, 5]
42KSHIMAAKAVANTMRubiquitination[1, 2, 4, 6]
59LGPNGLDKMMVDKDGubiquitination[1, 7]
64LDKMMVDKDGDVTVTubiquitination[1, 4]
150VAIEHLDKISDSVLVubiquitination[1, 2, 4, 8]
160DSVLVDIKDTEPLIQubiquitination[1, 2, 4, 6, 8]
170EPLIQTAKTTLGSKVubiquitination[1, 2, 4]
176AKTTLGSKVVNSCHRubiquitination[1, 6]
210DVDFELIKVEGKVGGubiquitination[1, 2, 4, 6]
214ELIKVEGKVGGRLEDubiquitination[1, 4]
223GGRLEDTKLIKGVIVacetylation[9]
223GGRLEDTKLIKGVIVubiquitination[1, 5, 6]
226LEDTKLIKGVIVDKDubiquitination[1, 2, 3, 4]
232IKGVIVDKDFSHPQMacetylation[9]
232IKGVIVDKDFSHPQMubiquitination[1, 3]
247PKKVEDAKIAILTCPubiquitination[5]
261PFEPPKPKTKHKLDVubiquitination[1]
263EPPKPKTKHKLDVTSubiquitination[1, 5]
265PKPKTKHKLDVTSVEubiquitination[1, 2, 3, 4, 5, 8]
275VTSVEDYKALQKYEKubiquitination[1, 2, 3, 4, 5, 7, 10]
282KALQKYEKEKFEEMIubiquitination[1]
284LQKYEKEKFEEMIQQubiquitination[1, 3]
352FSELTAEKLGFAGLVubiquitination[2, 6]
368EISFGTTKDKMLVIEubiquitination[1, 2, 4, 5]
370SFGTTKDKMLVIEQCubiquitination[1]
378MLVIEQCKNSRAVTIubiquitination[1, 2, 4, 6]
392IFIRGGNKMIIEEAKubiquitination[1, 2, 4]
399KMIIEEAKRSLHDALacetylation[9]
399KMIIEEAKRSLHDALubiquitination[1, 2, 4, 5, 6]
439AVSQEADKCPTLEQYubiquitination[1]
483EVRARQVKEMNPALGubiquitination[1, 3, 5, 7]
496LGIDCLHKGTNDMKQubiquitination[1, 6]
502HKGTNDMKQQHVIETubiquitination[1, 2, 4, 6]
513VIETLIGKKQQISLAubiquitination[1, 2, 4]
514IETLIGKKQQISLATubiquitination[1, 2, 3, 4, 5]
529QMVRMILKIDDIRKPubiquitination[1, 2, 3, 4, 6, 7]
535LKIDDIRKPGESEE*ubiquitination[1, 2, 4]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [7] 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]
 [8] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [9] 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]
 [10] 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] 
Functional Description
 Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin. 
Sequence Annotation
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 26 26 Phosphoserine.  
Keyword
 Acetylation; ATP-binding; Chaperone; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease mutation; Neuropathy; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 541 AA 
Protein Sequence
MASMGTLAFD EYGRPFLIIK DQDRKSRLMG LEALKSHIMA AKAVANTMRT SLGPNGLDKM 60
MVDKDGDVTV TNDGATILSM MDVDHQIAKL MVELSKSQDD EIGDGTTGVV VLAGALLEEA 120
EQLLDRGIHP IRIADGYEQA ARVAIEHLDK ISDSVLVDIK DTEPLIQTAK TTLGSKVVNS 180
CHRQMAEIAV NAVLTVADME RRDVDFELIK VEGKVGGRLE DTKLIKGVIV DKDFSHPQMP 240
KKVEDAKIAI LTCPFEPPKP KTKHKLDVTS VEDYKALQKY EKEKFEEMIQ QIKETGANLA 300
ICQWGFDDEA NHLLLQNNLP AVRWVGGPEI ELIAIATGGR IVPRFSELTA EKLGFAGLVQ 360
EISFGTTKDK MLVIEQCKNS RAVTIFIRGG NKMIIEEAKR SLHDALCVIR NLIRDNRVVY 420
GGGAAEISCA LAVSQEADKC PTLEQYAMRA FADALEVIPM ALSENSGMNP IQTMTEVRAR 480
QVKEMNPALG IDCLHKGTND MKQQHVIETL IGKKQQISLA TQMVRMILKI DDIRKPGESE 540
E 541 
Gene Ontology
 GO:0005813; C:centrosome; IDA:MGI.
 GO:0005832; C:chaperonin-containing T-complex; IEA:Compara.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005874; C:microtubule; IDA:UniProtKB.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0051084; P:'de novo' posttranslational protein folding; TAS:Reactome.
 GO:0009615; P:response to virus; IEP:UniProtKB. 
Interpro
 IPR012718; Chap_CCT_epsi.
 IPR017998; Chaperone_TCP-1.
 IPR002194; Chaperonin_TCP-1_CS.
 IPR002423; Cpn60/TCP-1.
 IPR027409; GroEL-like_apical_dom.
 IPR027413; GROEL-like_equatorial.
 IPR027410; TCP-1-like_intermed. 
Pfam
 PF00118; Cpn60_TCP1 
SMART
  
PROSITE
 PS00750; TCP1_1
 PS00751; TCP1_2
 PS00995; TCP1_3 
PRINTS
 PR00304; TCOMPLEXTCP1.