CPLM-010417

Genbank Nucleotide ID

T-complex protein 1 subunit beta

Protein Synonyms/Alias

TCP-1-beta; CCT-beta

Homo sapiens (Human)

Position	Peptide	Type	References
13	LAPVNIFKAGADEER	acetylation	[1]
13	LAPVNIFKAGADEER	ubiquitination	[2, 3, 4, 5]
40	IAIGDLVKSTLGPKG	ubiquitination	[6]
46	VKSTLGPKGMDKILL	ubiquitination	[5]
50	LGPKGMDKILLSSGR	ubiquitination	[5]
72	NDGATILKNIGVDNP	ubiquitination	[2, 3, 5, 6, 7, 8]
82	GVDNPAAKVLVDMSR	ubiquitination	[2, 5, 6, 8]
119	EAESLIAKKIHPQTI	ubiquitination	[3, 5, 6]
120	AESLIAKKIHPQTII	ubiquitination	[2, 5]
154	DHGSDEVKFRQDLMN	acetylation	[1]
154	DHGSDEVKFRQDLMN	ubiquitination	[2, 3, 4, 5, 6, 8, 9]
170	AGTTLSSKLLTHHKD	ubiquitination	[5]
176	SKLLTHHKDHFTKLA	ubiquitination	[5]
181	HHKDHFTKLAVEAVL	acetylation	[1]
191	VEAVLRLKGSGNLEA	ubiquitination	[2, 5, 6]
203	LEAIHIIKKLGGSLA	ubiquitination	[2, 6]
204	EAIHIIKKLGGSLAD	ubiquitination	[5, 6]
222	DEGFLLDKKIGVNQP	ubiquitination	[3, 5, 6, 8]
223	EGFLLDKKIGVNQPK	ubiquitination	[5]
230	KIGVNQPKRIENAKI	ubiquitination	[5]
236	PKRIENAKILIANTG	ubiquitination	[2, 4]
248	NTGMDTDKIKIFGSR	ubiquitination	[2, 3, 4, 5, 6, 10]
250	GMDTDKIKIFGSRVR	ubiquitination	[2, 3, 4, 5]
263	VRVDSTAKVAEIEHA	ubiquitination	[5, 6]
272	AEIEHAEKEKMKEKV	ubiquitination	[5]
274	IEHAEKEKMKEKVER	ubiquitination	[5]
284	EKVERILKHGINCFI	ubiquitination	[2, 3, 5, 6]
342	FDHPELVKLGSCKLI	ubiquitination	[5, 6]
347	LVKLGSCKLIEEVMI	ubiquitination	[5]
402	CVLAQTVKDSRTVYG	ubiquitination	[3, 5, 6]
431	LANRTPGKEAVAMES	ubiquitination	[3, 5, 6]
441	VAMESYAKALRMLPT	ubiquitination	[2, 4, 5, 6, 7, 8]
500	ITESFQVKRQVLLSA	ubiquitination	[5]
522	LRVDNIIKAAPRKRV	ubiquitination	[2, 3, 4, 5, 6, 8, 11, 12]
527	IIKAAPRKRVPDHHP	ubiquitination	[3]

[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] 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]
[3] 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]
[4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
[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] 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]
[7] 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]
[8] 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]
[9] 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]
[10] 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]
[11] 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]
[12] 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]

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.

MOD_RES 2 2 N-acetylalanine.
MOD_RES 3 3 Phosphoserine.
MOD_RES 13 13 N6-acetyllysine.
MOD_RES 154 154 N6-acetyllysine.
MOD_RES 181 181 N6-acetyllysine.
MOD_RES 260 260 Phosphoserine.
MOD_RES 261 261 Phosphothreonine.

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

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005832; C:chaperonin-containing T-complex; IEA:Compara.
GO:0005829; C:cytosol; NAS:UniProtKB.
GO:0005874; C:microtubule; IDA:UniProtKB.
GO:0005634; C:nucleus; IDA:HPA.
GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO:0051082; F:unfolded protein binding; NAS:UniProtKB.
GO:0051084; P:'de novo' posttranslational protein folding; TAS:Reactome.
GO:0051131; P:chaperone-mediated protein complex assembly; IMP:MGI.

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.

PS00750; TCP1_1
PS00751; TCP1_2
PS00995; TCP1_3

PR00304; TCOMPLEXTCP1.