UniProt Accession

 TCPA_MOUSE; P11983; P11984; Q3TJ96; Q3TKU1; Q3U5T8; Q3U7I8; Q3UAA8; Q3UB80; Q3UE48 

Genbank Protein ID

 M20130; M12899; D90344; D10606; S46763; AK149611; AK149755; AK151068; AK151445; AK152641; AK153430; AK165665; AK166828; AK166966; AK167529; BC003809 

Genbank Nucleotide ID

 AAA40337.1; AAA40338.1; BAA14356.1; BAA01461.1; AAB23855.1; BAE28989.1; BAE29063.1; BAE30084.1; BAE30407.1; BAE31381.1; BAE31988.1; BAE38327.1; BAE39052.1; BAE39149.1; BAE39599.1; AAH03809.1 

Protein Name

 T-complex protein 1 subunit alpha 

Protein Synonyms/Alias

 TCP-1-alpha; CCT-alpha; Tailless complex polypeptide 1A; TCP-1-A; Tailless complex polypeptide 1B; TCP-1-B 

Gene Name

 Tcp1 

Gene Synonyms/Alias

 Cct1; Ccta 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
43	FGPVGLDKMLVDDIG	ubiquitination	[1]
126	SGYRLACKEAVRYIN	ubiquitination	[1]
243	CLDFSLQKTKMKLGV	phosphoglycerylation	[2]
317	RVLKRDLKHVAKASG	acetylation	[3]
365	DDELILIKNTKARTS	acetylation	[4, 5]
365	DDELILIKNTKARTS	ubiquitination	[1]
400	HDALCVVKRVLELKS	acetylation	[4, 5, 6, 7, 8, 9]
400	HDALCVVKRVLELKS	succinylation	[9]
484	NPERKNLKWIGLDLV	acetylation	[4]
494	GLDLVHGKPRDNKQA	acetylation	[4, 5, 9]
494	GLDLVHGKPRDNKQA	ubiquitination	[1]
532	LRIDDLIKLHPESKD	acetylation	[4, 5]
532	LRIDDLIKLHPESKD	ubiquitination	[1]
538	IKLHPESKDDKHGSY	ubiquitination	[1]
541	HPESKDDKHGSYENA	ubiquitination	[1]

Reference

 [1] 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]
 [2] Functional lysine modification by an intrinsically reactive primary glycolytic metabolite.
 Moellering RE, Cravatt BF.
 Science. 2013 Aug 2;341(6145):549-53. [PMID: 23908237]
 [3] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [4] 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]
 [5] 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]
 [6] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [7] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
 Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
 Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599]
 [8] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [9] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337] 

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 1 1 N-acetylmethionine.
 MOD_RES 181 181 Phosphotyrosine (By similarity).
 MOD_RES 182 182 Phosphothreonine (By similarity).
 MOD_RES 199 199 N6-acetyllysine (By similarity).
 MOD_RES 400 400 N6-acetyllysine (By similarity).
 MOD_RES 544 544 Phosphoserine.
 MOD_RES 551 551 Phosphoserine.  

Keyword

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

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 556 AA 

Protein Sequence

Gene Ontology

 GO:0001669; C:acrosomal vesicle; IDA:MGI.
 GO:0044297; C:cell body; IDA:MGI.
 GO:0030054; C:cell junction; IEA:Compara.
 GO:0005832; C:chaperonin-containing T-complex; IDA:MGI.
 GO:0005794; C:Golgi apparatus; IDA:MGI.
 GO:0005874; C:microtubule; IEA:Compara.
 GO:0005720; C:nuclear heterochromatin; IDA:MGI.
 GO:0000242; C:pericentriolar material; IDA:MGI.
 GO:0005886; C:plasma membrane; 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:0006457; P:protein folding; IEA:InterPro. 

Interpro

 IPR012715; Chap_CCT_alpha.
 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.