CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019803
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 T-complex protein 1 subunit eta 
Protein Synonyms/Alias
 TCP-1-eta; CCT-eta; HIV-1 Nef-interacting protein 
Gene Name
 CCT7 
Gene Synonyms/Alias
 CCTH; NIP7-1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
47LGPRGMDKLIVDGRGubiquitination[1, 2, 3, 4, 5, 6, 7]
55LIVDGRGKATISNDGubiquitination[2, 3, 5, 6, 7]
67NDGATILKLLDVVHPacetylation[8]
67NDGATILKLLDVVHPubiquitination[2, 3, 6, 7]
77DVVHPAAKTLVDIAKubiquitination[2, 3, 5, 6, 7]
84KTLVDIAKSQDAEVGubiquitination[3, 6]
106LLAAEFLKQVKPYVEubiquitination[7]
109AEFLKQVKPYVEEGLubiquitination[6]
135ATQLAVNKIKEIAVTubiquitination[3, 5, 6]
137QLAVNKIKEIAVTVKubiquitination[6, 7]
144KEIAVTVKKADKVEQubiquitination[6]
145EIAVTVKKADKVEQRubiquitination[6]
157EQRKLLEKCAMTALSubiquitination[6]
166AMTALSSKLISQQKAubiquitination[3, 5, 6]
172SKLISQQKAFFAKMVubiquitination[2, 6]
199LKMIGIKKVQGGALEubiquitination[6]
217LVAGVAFKKTFSYAGubiquitination[3, 7]
218VAGVAFKKTFSYAGFubiquitination[2, 3, 5, 6]
230AGFEMQPKKYHNPKIubiquitination[6]
231GFEMQPKKYHNPKIAubiquitination[6]
250ELELKAEKDNAEIRVubiquitination[4]
287KIHHSGAKVVLSKLPubiquitination[6]
292GAKVVLSKLPIGDVAubiquitination[2, 3, 6, 7]
320RVPEEDLKRTMMACGacetylation[8]
320RVPEEDLKRTMMACGubiquitination[3, 5, 6]
366NFFTGCPKAKTCTFIubiquitination[2, 3, 5, 6]
368FTGCPKAKTCTFILRubiquitination[5, 6]
401MIVRRAIKNDSVVAGubiquitination[3]
418AIEMELSKYLRDYSRubiquitination[2, 3, 6, 7]
430YSRTIPGKQQLLIGAubiquitination[2, 6]
440LLIGAYAKALEIIPRubiquitination[2, 3, 6, 7]
463DATNILNKLRARHAQubiquitination[2, 3, 4, 5, 6, 9]
521VSVDETIKNPRSTVDubiquitination[3, 4, 6]
Reference
 [1] 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]
 [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] 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]
 [4] 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]
 [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] 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]
 [7] 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]
 [8] 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]
 [9] 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] 
Functional Description
 Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity). 
Sequence Annotation
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 67 67 N6-acetyllysine.
 MOD_RES 320 320 N6-acetyllysine.  
Keyword
 Acetylation; Alternative splicing; ATP-binding; Chaperone; Complete proteome; Cytoplasm; Direct protein sequencing; Nucleotide-binding; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 543 AA 
Protein Sequence
MMPTPVILLK EGTDSSQGIP QLVSNISACQ VIAEAVRTTL GPRGMDKLIV DGRGKATISN 60
DGATILKLLD VVHPAAKTLV DIAKSQDAEV GDGTTSVTLL AAEFLKQVKP YVEEGLHPQI 120
IIRAFRTATQ LAVNKIKEIA VTVKKADKVE QRKLLEKCAM TALSSKLISQ QKAFFAKMVV 180
DAVMMLDDLL QLKMIGIKKV QGGALEDSQL VAGVAFKKTF SYAGFEMQPK KYHNPKIALL 240
NVELELKAEK DNAEIRVHTV EDYQAIVDAE WNILYDKLEK IHHSGAKVVL SKLPIGDVAT 300
QYFADRDMFC AGRVPEEDLK RTMMACGGSI QTSVNALSAD VLGRCQVFEE TQIGGERYNF 360
FTGCPKAKTC TFILRGGAEQ FMEETERSLH DAIMIVRRAI KNDSVVAGGG AIEMELSKYL 420
RDYSRTIPGK QQLLIGAYAK ALEIIPRQLC DNAGFDATNI LNKLRARHAQ GGTWYGVDIN 480
NEDIADNFEA FVWEPAMVRI NALTAASEAA CLIVSVDETI KNPRSTVDAP TAAGRGRGRG 540
RPH 543 
Gene Ontology
 GO:0005832; C:chaperonin-containing T-complex; IEA:Compara.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005874; C:microtubule; IDA:UniProtKB.
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0051082; F:unfolded protein binding; TAS:ProtInc.
 GO:0051084; P:'de novo' posttranslational protein folding; TAS:Reactome. 
Interpro
 IPR012720; Chap_CCT_eta.
 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.