UniProt Accession

 TCPG_HUMAN; P49368; A6NE14; Q5SZY1; Q9BR64 

Genbank Protein ID

 AK293477; AL833197; AL589685; BC006501; BC008019; X74801; U17104 

Genbank Nucleotide ID

 BAG56968.1; CAI46192.1; CAI14167.1; AAH06501.3; AAH08019.1; CAA52808.1; AAC50068.1 

Protein Name

 T-complex protein 1 subunit gamma 

Protein Synonyms/Alias

 TCP-1-gamma; CCT-gamma; hTRiC5 

Gene Name

 CCT3 

Gene Synonyms/Alias

 CCTG; TRIC5 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
15	LVLSQNTKRESGRKV	ubiquitination	[1]
21	TKRESGRKVQSGNIN	acetylation	[2]
21	TKRESGRKVQSGNIN	ubiquitination	[1]
31	SGNINAAKTIADIIR	acetylation	[2]
31	SGNINAAKTIADIIR	ubiquitination	[1, 3, 4, 5]
44	IRTCLGPKSMMKMLL	acetylation	[2]
44	IRTCLGPKSMMKMLL	ubiquitination	[1, 3, 4]
78	QVQHPAAKSMIEISR	ubiquitination	[1, 3, 5, 6]
128	VVISAYRKALDDMIS	ubiquitination	[1, 3]
138	DDMISTLKKISIPVD	ubiquitination	[3, 4, 5]
139	DMISTLKKISIPVDI	ubiquitination	[1]
163	INSSITTKAISRWSS	ubiquitination	[5]
181	NIALDAVKMVQFEEN	ubiquitination	[1]
203	KKYARVEKIPGGIIE	ubiquitination	[1]
222	LRGVMINKDVTHPRM	acetylation	[7]
222	LRGVMINKDVTHPRM	ubiquitination	[1, 5]
234	PRMRRYIKNPRIVLL	ubiquitination	[1]
248	LDSSLEYKKGESQTD	acetylation	[7]
248	LDSSLEYKKGESQTD	ubiquitination	[1, 3, 5]
249	DSSLEYKKGESQTDI	ubiquitination	[1, 4, 5, 8]
353	GAGLLEIKKIGDEYF	ubiquitination	[5]
354	AGLLEIKKIGDEYFT	ubiquitination	[1, 4]
367	FTFITDCKDPKACTI	ubiquitination	[1]
370	ITDCKDPKACTILLR	ubiquitination	[1]
381	ILLRGASKEILSEVE	ubiquitination	[1, 3, 4, 5]
425	VAHALTEKSKAMTGV	ubiquitination	[1, 4, 5]
427	HALTEKSKAMTGVEQ	ubiquitination	[1, 5]
469	LLTSLRAKHTQENCE	ubiquitination	[1]
491	TGTLVDMKELGIWEP	ubiquitination	[1]
502	IWEPLAVKLQTYKTA	ubiquitination	[1, 3, 5]
507	AVKLQTYKTAVETAV	ubiquitination	[1, 3, 4, 5, 6, 8, 9]
527	DDIVSGHKKKGDDQS	ubiquitination	[5]
528	DIVSGHKKKGDDQSR	ubiquitination	[1]

Reference

 [1] 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]
 [2] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [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] 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]
 [6] 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]
 [7] 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]
 [8] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [9] 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

 Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin. 

Sequence Annotation

 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 222 222 N6-acetyllysine.
 MOD_RES 244 244 Phosphoserine.
 MOD_RES 252 252 Phosphoserine.
 DISULFID 366 372 By similarity.  

Keyword

 Acetylation; Alternative splicing; ATP-binding; Chaperone; Complete proteome; Cytoplasm; Direct protein sequencing; Disulfide bond; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 545 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:0005886; C:plasma membrane; IDA:HPA.
 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

 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

 PS00750; TCP1_1
 PS00751; TCP1_2
 PS00995; TCP1_3 

PRINTS

 PR00304; TCOMPLEXTCP1.