CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-031916
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Chaperonin containing TCP1, subunit 7 (Eta), isoform CRA_a 
Protein Synonyms/Alias
 T-complex protein 1 subunit eta; cDNA FLJ59454, highly similar to T-complex protein 1 subunit eta 
Gene Name
 CCT7 
Gene Synonyms/Alias
 hCG_1997313 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
29EQRKLLEKCAMTALSacetylation[1]
29EQRKLLEKCAMTALSubiquitination[2, 3]
38AMTALSSKLISQQKAubiquitination[2, 3, 4, 5]
44SKLISQQKAFFAKMVacetylation[3]
44SKLISQQKAFFAKMVubiquitination[2, 3, 6]
71LKMIGIKKVQGGALEubiquitination[2]
89LVAGVAFKKTFSYAGubiquitination[3, 4, 7, 8]
90VAGVAFKKTFSYAGFubiquitination[2, 3, 4, 5, 6]
102AGFEMQPKKYHNPKIubiquitination[2, 3]
103GFEMQPKKYHNPKIAubiquitination[2, 3]
122ELELKAEKDNAEIRVacetylation[3]
122ELELKAEKDNAEIRVubiquitination[9]
159KIHHSGAKVVLSKLPacetylation[3]
159KIHHSGAKVVLSKLPubiquitination[2, 3]
164GAKVVLSKLPIGDVAacetylation[1]
164GAKVVLSKLPIGDVAubiquitination[2, 3, 4, 6, 7, 8]
192RVPEEDLKRTMMACGacetylation[3]
192RVPEEDLKRTMMACGubiquitination[2, 3, 4, 5]
238NFFTGCPKAKTCTFIubiquitination[2, 3, 4, 5, 6]
240FTGCPKAKTCTFILRubiquitination[2, 3, 5]
273MIVRRAIKNDSVVAGubiquitination[4]
290AIEMELSKYLRDYSRubiquitination[2, 3, 4, 6, 7, 8]
302YSRTIPGKQQLLIGAubiquitination[2, 3, 6]
312LLIGAYAKALEIIPRubiquitination[2, 3, 4, 6, 7, 8]
335DATNILNKLRARHAQacetylation[1, 3]
335DATNILNKLRARHAQubiquitination[2, 3, 4, 5, 6, 7, 9]
393VSVDETIKNPRSTVDubiquitination[2, 4, 9]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [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] 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]
 [7] 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]
 [8] 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]
 [9] 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
Functional Description
  
Sequence Annotation
  
Keyword
 ATP-binding; Chaperone; Complete proteome; Cytoplasm; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 415 AA 
Protein Sequence
MWRKVYTPRS SFELSAQPPS WEQRKLLEKC AMTALSSKLI SQQKAFFAKM VVDAVMMLDD 60
LLQLKMIGIK KVQGGALEDS QLVAGVAFKK TFSYAGFEMQ PKKYHNPKIA LLNVELELKA 120
EKDNAEIRVH TVEDYQAIVD AEWNILYDKL EKIHHSGAKV VLSKLPIGDV ATQYFADRDM 180
FCAGRVPEED LKRTMMACGG SIQTSVNALS ADVLGRCQVF EETQIGGERY NFFTGCPKAK 240
TCTFILRGGA EQFMEETERS LHDAIMIVRR AIKNDSVVAG GGAIEMELSK YLRDYSRTIP 300
GKQQLLIGAY AKALEIIPRQ LCDNAGFDAT NILNKLRARH AQGGTWYGVD INNEDIADNF 360
EAFVWEPAMV RINALTAASE AACLIVSVDE TIKNPRSTVD APTAAGRGRG RGRPH 415 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0006457; P:protein folding; IEA:InterPro. 
Interpro
 IPR012720; Chap_CCT_eta.
 IPR017998; Chaperone_TCP-1.
 IPR002423; Cpn60/TCP-1.
 IPR027409; GroEL-like_apical_dom.
 IPR027413; GROEL-like_equatorial.
 IPR027410; TCP-1-like_intermed. 
Pfam
 PF00118; Cpn60_TCP1 
SMART
  
PROSITE
  
PRINTS
 PR00304; TCOMPLEXTCP1.