UniProt Accession

 TCPZ_HUMAN; P40227; A6NCD2; Q3KP28; Q75LP4; Q96S46 

Genbank Protein ID

 L27706; AF385084; AB063318; AC092101; AC092579; BC106942; BU540578; M94083 

Genbank Nucleotide ID

 AAA61061.1; AAK61354.1; BAB61032.1; AAS07451.1; AAI06943.1; AAA58676.1 

Protein Name

 T-complex protein 1 subunit zeta 

Protein Synonyms/Alias

 TCP-1-zeta; Acute morphine dependence-related protein 2; CCT-zeta-1; HTR3; Tcp20 

Gene Name

 CCT6A 

Gene Synonyms/Alias

 CCT6; CCTZ 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
5	***MAAVKTLNPKAE	acetylation	[1]
5	***MAAVKTLNPKAE	ubiquitination	[2, 3, 4, 5]
10	AVKTLNPKAEVARAQ	acetylation	[1, 6, 7, 8]
10	AVKTLNPKAEVARAQ	ubiquitination	[2, 3, 4, 5, 8, 9, 10, 11]
41	LRTNLGPKGTMKMLV	ubiquitination	[4, 5, 8, 10]
45	LGPKGTMKMLVSGAG	ubiquitination	[5]
55	VSGAGDIKLTKDGNV	ubiquitination	[5, 9]
58	AGDIKLTKDGNVLLH	ubiquitination	[3, 5]
127	TEGFEAAKEKALQFL	ubiquitination	[4, 5, 9, 11, 12]
129	GFEAAKEKALQFLEE	ubiquitination	[4, 5, 9, 11]
138	LQFLEEVKVSREMDR	ubiquitination	[5, 9, 11]
159	ARTSLRTKVHAELAD	ubiquitination	[5]
199	EIMEMKHKSETDTSL	acetylation	[1]
199	EIMEMKHKSETDTSL	ubiquitination	[5, 9, 11]
223	ARHPDMKKRVEDAYI	ubiquitination	[11]
251	VNSGFFYKSAEEREK	ubiquitination	[3, 5, 9, 11]
265	KLVKAERKFIEDRVK	ubiquitination	[5]
278	VKKIIELKRKVCGDS	ubiquitination	[9]
280	KIIELKRKVCGDSDK	ubiquitination	[4, 5]
287	KVCGDSDKGFVVINQ	ubiquitination	[3]
295	GFVVINQKGIDPFSL	ubiquitination	[3, 5, 9, 11]
307	FSLDALSKEGIVALR	ubiquitination	[3, 5, 9, 11]
365	EKFTFIEKCNNPRSV	acetylation	[1]
365	EKFTFIEKCNNPRSV	ubiquitination	[5]
377	RSVTLLIKGPNKHTL	acetylation	[1]
377	RSVTLLIKGPNKHTL	ubiquitination	[3, 4, 5, 9, 11]
381	LLIKGPNKHTLTQIK	ubiquitination	[3, 5]
388	KHTLTQIKDAVRDGL	acetylation	[1]
388	KHTLTQIKDAVRDGL	ubiquitination	[5]
399	RDGLRAVKNAIDDGC	ubiquitination	[5]
424	AMAEALIKHKPSVKG	ubiquitination	[5]
426	AEALIKHKPSVKGRA	ubiquitination	[5]
530	RAGMSSLKG******	ubiquitination	[3, 4, 5, 9, 11]

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] 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]
 [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] 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] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] 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]
 [11] 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]
 [12] 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. 

Sequence Annotation

 MOD_RES 199 199 N6-acetyllysine.
 MOD_RES 365 365 N6-acetyllysine.
 MOD_RES 377 377 N6-acetyllysine.
 MOD_RES 388 388 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

 531 AA 

Protein Sequence

Gene Ontology

 GO:0005832; C:chaperonin-containing T-complex; IEA:Compara.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005874; C:microtubule; IDA:UniProtKB.
 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

 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

 PS00750; TCP1_1
 PS00751; TCP1_2
 PS00995; TCP1_3 

PRINTS

 PR00304; TCOMPLEXTCP1.