CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008343
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 T-complex protein 1 subunit theta 
Protein Synonyms/Alias
 TCP-1-theta; CCT-theta; Renal carcinoma antigen NY-REN-15 
Gene Name
 CCT8 
Gene Synonyms/Alias
 C21orf112; CCTQ; KIAA0002 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
7*MALHVPKAPGFAQMacetylation[1]
7*MALHVPKAPGFAQMubiquitination[2, 3, 4, 5, 6]
16PGFAQMLKEGAKHFSacetylation[7, 8]
16PGFAQMLKEGAKHFSubiquitination[2, 3, 4, 5, 6, 9, 10]
20QMLKEGAKHFSGLEEacetylation[11]
20QMLKEGAKHFSGLEEubiquitination[2, 3, 4, 5]
37YRNIQACKELAQTTRubiquitination[3, 4, 5]
54YGPNGMNKMVINHLEubiquitination[2, 4, 5]
62MVINHLEKLFVTNDAubiquitination[2, 3, 4, 5, 10, 12]
138GYEIACRKAHEILPNubiquitination[5]
152NLVCCSAKNLRDIDEubiquitination[2, 5]
171LRTSIMSKQYGNEVFubiquitination[2, 3, 4, 5]
225LHGMVFKKETEGDVTubiquitination[5, 13]
235EGDVTSVKDAKIAVYubiquitination[3, 5, 10, 13]
254DGMITETKGTVLIKTubiquitination[3, 5]
260TKGTVLIKTAEELMNubiquitination[2, 5, 10, 14]
270EELMNFSKGEENLMDubiquitination[3, 5, 10]
296NVVVTGGKVADMALHubiquitination[5]
307MALHYANKYNIMLVRubiquitination[4, 5]
318MLVRLNSKWDLRRLCacetylation[1]
318MLVRLNSKWDLRRLCubiquitination[5]
326WDLRRLCKTVGATALubiquitination[2, 3, 4, 5]
400DDGVNTFKVLTRDKRacetylation[1]
400DDGVNTFKVLTRDKRubiquitination[2, 3, 4, 5, 10]
421ATEIELAKQITSYGEubiquitination[2, 5]
439GLEQYAIKKFAEAFEubiquitination[5]
440LEQYAIKKFAEAFEAubiquitination[2, 3, 4, 5, 10]
459LAENSGVKANEVISKubiquitination[3, 5]
466KANEVISKLYAVHQEacetylation[1]
466KANEVISKLYAVHQEubiquitination[2, 5, 10]
528VDQIIMAKPAGGPKPubiquitination[2, 5]
534AKPAGGPKPPSGKKDubiquitination[5, 10]
539GPKPPSGKKDWDDDQubiquitination[3, 10]
540PKPPSGKKDWDDDQNubiquitination[3, 10]
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] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] 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]
 [11] 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]
 [12] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [13] Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry.
 Denis NJ, Vasilescu J, Lambert JP, Smith JC, Figeys D.
 Proteomics. 2007 Mar;7(6):868-74. [PMID: 17370265]
 [14] 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 23 23 Phosphoserine.
 MOD_RES 30 30 Phosphotyrosine.
 MOD_RES 318 318 N6-acetyllysine.
 MOD_RES 400 400 N6-acetyllysine.
 MOD_RES 466 466 N6-acetyllysine.
 MOD_RES 505 505 Phosphotyrosine.
 CROSSLNK 225 225 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 235 235 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Acetylation; ATP-binding; Chaperone; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Isopeptide bond; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 548 AA 
Protein Sequence
MALHVPKAPG FAQMLKEGAK HFSGLEEAVY RNIQACKELA QTTRTAYGPN GMNKMVINHL 60
EKLFVTNDAA TILRELEVQH PAAKMIVMAS HMQEQEVGDG TNFVLVFAGA LLELAEELLR 120
IGLSVSEVIE GYEIACRKAH EILPNLVCCS AKNLRDIDEV SSLLRTSIMS KQYGNEVFLA 180
KLIAQACVSI FPDSGHFNVD NIRVCKILGS GISSSSVLHG MVFKKETEGD VTSVKDAKIA 240
VYSCPFDGMI TETKGTVLIK TAEELMNFSK GEENLMDAQV KAIADTGANV VVTGGKVADM 300
ALHYANKYNI MLVRLNSKWD LRRLCKTVGA TALPRLTPPV LEEMGHCDSV YLSEVGDTQV 360
VVFKHEKEDG AISTIVLRGS TDNLMDDIER AVDDGVNTFK VLTRDKRLVP GGGATEIELA 420
KQITSYGETC PGLEQYAIKK FAEAFEAIPR ALAENSGVKA NEVISKLYAV HQEGNKNVGL 480
DIEAEVPAVK DMLEAGILDT YLGKYWAIKL ATNAAVTVLR VDQIIMAKPA GGPKPPSGKK 540
DWDDDQND 548 
Gene Ontology
 GO:0016235; C:aggresome; IDA:HPA.
 GO:0005813; C:centrosome; IDA:MGI.
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
 GO:0005874; C:microtubule; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0042623; F:ATPase activity, coupled; TAS:ProtInc.
 GO:0051084; P:'de novo' posttranslational protein folding; TAS:Reactome. 
Interpro
 IPR012721; Chap_CCT_theta.
 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.