UniProt Accession

 B4DUR8_HUMAN; B4DUR8 

Genbank Protein ID

 AL589685; AK300765; AK315923; AK316387 

Genbank Nucleotide ID

 BAG62430.1; BAH14294.1; BAH14758.1 

Protein Name

 T-complex protein 1 subunit gamma 

Protein Synonyms/Alias

 cDNA FLJ57603, highly similar to T-complex protein 1 subunit gamma; cDNA, FLJ78822, highly similar to T-complex protein 1 subunit gamma; cDNA, FLJ79286, highly similar to T-complex protein 1 subunit gamma 

Gene Name

 CCT3 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
33	QVQHPAAKSMIEISR	ubiquitination	[1, 2, 3, 4, 5, 6, 7]
83	VVISAYRKALDDMIS	ubiquitination	[1, 5]
93	DDMISTLKKISIPVD	acetylation	[8]
93	DDMISTLKKISIPVD	ubiquitination	[1, 2, 3, 6, 9]
94	DMISTLKKISIPVDI	ubiquitination	[2, 3, 5]
118	INSSITTKAISRWSS	ubiquitination	[3, 6]
136	NIALDAVKMVQFEEN	ubiquitination	[5]
158	KKYARVEKIPGGIIE	ubiquitination	[5, 7]
177	LRGVMINKDVTHPRM	acetylation	[7, 8, 10]
177	LRGVMINKDVTHPRM	ubiquitination	[2, 3, 5, 6, 7]
189	PRMRRYIKNPRIVLL	ubiquitination	[5]
203	LDSSLEYKKGESQTD	acetylation	[7, 8, 10]
203	LDSSLEYKKGESQTD	ubiquitination	[1, 2, 3, 5, 6]
204	DSSLEYKKGESQTDI	ubiquitination	[2, 3, 4, 5, 6, 7, 9]
308	GAGLLEIKKIGDEYF	ubiquitination	[2, 3, 6]
309	AGLLEIKKIGDEYFT	ubiquitination	[3, 5, 7, 9]
322	FTFITDCKDPKACTI	ubiquitination	[3, 5, 7]
325	ITDCKDPKACTILLR	ubiquitination	[3, 5, 7]
336	ILLRGASKEILSEVE	acetylation	[8]
336	ILLRGASKEILSEVE	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 9]
380	VAHALTEKSKAMTGV	ubiquitination	[2, 3, 5, 6, 9]
382	HALTEKSKAMTGVEQ	ubiquitination	[2, 3, 5, 6, 7]
424	LLTSLRAKHTQENCE	ubiquitination	[3, 5, 7]
446	TGTLVDMKELGIWEP	ubiquitination	[3, 5]
457	IWEPLAVKLQTYKTA	ubiquitination	[1, 2, 3, 5, 6]
462	AVKLQTYKTAVETAV	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 9, 11]
482	DDIVSGHKKKGDDQS	ubiquitination	[2, 6]
483	DIVSGHKKKGDDQSR	ubiquitination	[5]

Reference

 [1] 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]
 [2] 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]
 [3] 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]
 [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] 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] 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]
 [7] 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]
 [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] 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]
 [10] 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]
 [11] 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] 

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:0005832; C:chaperonin-containing T-complex; IEA:Compara.
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0006457; P:protein folding; IEA:InterPro. 

Interpro

 IPR012719; Chap_CCT_gamma.
 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.