UniProt Accession

 B4DPJ8_HUMAN; B4DPJ8 

Genbank Protein ID

 AC092101; AC092579; AK298371; AK316230 

Genbank Nucleotide ID

 BAG60610.1; BAH14601.1 

Protein Name

 T-complex protein 1 subunit zeta 

Protein Synonyms/Alias

 cDNA FLJ52344, highly similar to T-complex protein 1 subunit zeta; cDNA, FLJ79129, highly similar to T-complex protein 1 subunit zeta 

Gene Name

 CCT6A 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
5	***MAAVKTLNPKGT	acetylation	[1, 2, 3]
5	***MAAVKTLNPKGT	ubiquitination	[3, 4, 5]
14	LNPKGTMKMLVSGAG	ubiquitination	[5]
24	VSGAGDIKLTKDGNV	ubiquitination	[5, 6]
27	AGDIKLTKDGNVLLH	ubiquitination	[5, 7, 8]
96	TEGFEAAKEKALQFL	acetylation	[2]
96	TEGFEAAKEKALQFL	ubiquitination	[3, 4, 5, 6, 8, 9]
98	GFEAAKEKALQFLEE	ubiquitination	[3, 4, 5, 6, 8, 9]
107	LQFLEEVKVSREMDR	ubiquitination	[5, 6, 8, 9]
128	ARTSLRTKVHAELAD	ubiquitination	[5]
168	EIMEMKHKSETDTSL	acetylation	[1, 2, 3]
168	EIMEMKHKSETDTSL	ubiquitination	[3, 5, 6, 9]
192	ARHPDMKKRVEDAYI	ubiquitination	[9]
220	VNSGFFYKSAEEREK	acetylation	[2]
220	VNSGFFYKSAEEREK	ubiquitination	[3, 5, 6, 7, 8, 9, 10]
234	KLVKAERKFIEDRVK	ubiquitination	[5]
249	KIIELKRKVCGDSDK	ubiquitination	[3, 4, 5]
256	KVCGDSDKGFVVINQ	acetylation	[2, 3]
256	KVCGDSDKGFVVINQ	ubiquitination	[7, 8]
264	GFVVINQKGIDPFSL	ubiquitination	[5, 6, 7, 8, 9]
276	FSLDALSKEGIVALR	ubiquitination	[3, 5, 6, 7, 8, 9]
334	EKFTFIEKCNNPRSV	acetylation	[1, 2, 3]
334	EKFTFIEKCNNPRSV	ubiquitination	[3, 5]
346	RSVTLLIKGPNKHTL	acetylation	[1, 2, 3]
346	RSVTLLIKGPNKHTL	ubiquitination	[3, 4, 5, 6, 7, 8, 9]
350	LLIKGPNKHTLTQIK	ubiquitination	[3, 5, 7]
357	KHTLTQIKDAVRDGL	acetylation	[1, 2, 3]
357	KHTLTQIKDAVRDGL	ubiquitination	[5, 8]
368	RDGLRAVKNAIDDGC	ubiquitination	[3, 5, 8]
393	AMAEALIKHKPSVKG	ubiquitination	[5]
395	AEALIKHKPSVKGRA	ubiquitination	[5]
499	RAGMSSLKG******	ubiquitination	[3, 4, 5, 6, 7, 8, 9]

Reference

 [1] 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]
 [2] 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]
 [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] 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]
 [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] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] 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

 500 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0006457; P:protein folding; IEA:InterPro. 

Interpro

 IPR012722; Chap_CCT_zeta.
 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

 PS00751; TCP1_2
 PS00995; TCP1_3 

PRINTS

 PR00304; TCOMPLEXTCP1.