UniProt Accession

 TCPB_MOUSE; P80314; Q9R1U0 

Genbank Protein ID

 Z31553; AB022156; BC007470; BC026918 

Genbank Nucleotide ID

 CAA83428.1; BAA81874.1; AAH07470.1; AAH26918.1 

Protein Name

 T-complex protein 1 subunit beta 

Protein Synonyms/Alias

 TCP-1-beta; CCT-beta 

Gene Name

 Cct2 

Gene Synonyms/Alias

 Cctb 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
13	LAPVNIFKAGADEER	acetylation	[1]
13	LAPVNIFKAGADEER	ubiquitination	[2]
50	LGPKGMDKILLSSGR	acetylation	[1]
50	LGPKGMDKILLSSGR	ubiquitination	[2]
72	NDGATILKNIGVDNP	ubiquitination	[2]
191	VEAVLRLKGSGNLEA	acetylation	[1]
191	VEAVLRLKGSGNLEA	ubiquitination	[2]
203	LEAIHVIKKLGGSLA	acetylation	[1]
204	EAIHVIKKLGGSLAD	ubiquitination	[2]
222	DEGFLLDKKIGVNQP	acetylation	[3]
222	DEGFLLDKKIGVNQP	ubiquitination	[2]
248	NTGMDTDKIKIFGSR	acetylation	[1, 3]
248	NTGMDTDKIKIFGSR	ubiquitination	[2]
250	GMDTDKIKIFGSRVR	acetylation	[1]
250	GMDTDKIKIFGSRVR	ubiquitination	[2]
284	EKVERILKHGINCFI	acetylation	[1]
284	EKVERILKHGINCFI	ubiquitination	[2]
342	FDHPELVKLGSCKLI	ubiquitination	[2]
402	CVLAQTVKDPRTVYG	acetylation	[1]
441	VAMESFAKALRMLPT	acetylation	[1]
441	VAMESFAKALRMLPT	ubiquitination	[2]
522	LRVDNIIKAAPRKRV	acetylation	[1]
522	LRVDNIIKAAPRKRV	ubiquitination	[2]
527	IIKAAPRKRVPDHHP	ubiquitination	[2]

Reference

 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [3] 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] 

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 (By similarity). 

Sequence Annotation

 MOD_RES 2 2 N-acetylalanine (By similarity).
 MOD_RES 3 3 Phosphoserine (By similarity).
 MOD_RES 13 13 N6-acetyllysine (By similarity).
 MOD_RES 181 181 N6-acetyllysine (By similarity).
 MOD_RES 260 260 Phosphoserine (By similarity).
 MOD_RES 261 261 Phosphothreonine (By similarity).  

Keyword

 Acetylation; ATP-binding; Chaperone; Complete proteome; Cytoplasm; Direct protein sequencing; Nucleotide-binding; Phosphoprotein; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 535 AA 

Protein Sequence

Gene Ontology

 GO:0044297; C:cell body; IDA:MGI.
 GO:0005832; C:chaperonin-containing T-complex; IDA:MGI.
 GO:0005874; C:microtubule; IEA:Compara.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0002199; C:zona pellucida receptor complex; IDA:MGI.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0007339; P:binding of sperm to zona pellucida; IDA:MGI.
 GO:0051131; P:chaperone-mediated protein complex assembly; IEA:Compara.
 GO:0006457; P:protein folding; IEA:InterPro. 

Interpro

 IPR012716; Chap_CCT_beta.
 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.