UniProt Accession

 TCPD_HUMAN; P50991; B2R6I3; B7Z8B1; F5H5W3; O14870; Q53QP9; Q96C51 

Genbank Protein ID

 U38846; AF026291; AK303082; AK312586; AC107081; BC014676; BC106934; BC106933 

Genbank Nucleotide ID

 AAC50384.1; AAC96010.1; BAH13897.1; BAG35480.1; AAY24140.1; AAH14676.1; AAI06935.1; AAI06934.1 

Protein Name

 T-complex protein 1 subunit delta 

Protein Synonyms/Alias

 TCP-1-delta; CCT-delta; Stimulator of TAR RNA-binding 

Gene Name

 CCT4 

Gene Synonyms/Alias

 CCTD; SRB 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
42	FSNISAAKAVADAIR	ubiquitination	[1, 2, 3]
55	IRTSLGPKGMDKMIQ	acetylation	[4]
55	IRTSLGPKGMDKMIQ	ubiquitination	[1, 3, 4, 5]
59	LGPKGMDKMIQDGKG	ubiquitination	[3]
65	DKMIQDGKGDVTITN	ubiquitination	[1, 2, 3, 5, 6, 7, 8]
79	NDGATILKQMQVLHP	ubiquitination	[1, 2, 3]
126	SCTKLLQKGIHPTII	ubiquitination	[1, 2, 3, 5, 8]
139	IISESFQKALEKGIE	acetylation	[9]
139	IISESFQKALEKGIE	ubiquitination	[1, 3, 5]
143	SFQKALEKGIEILTD	ubiquitination	[8]
213	RDIKIVKKLGGTIDD	ubiquitination	[3]
232	EGLVLTQKVSNSGIT	ubiquitination	[3]
245	ITRVEKAKIGLIQFC	ubiquitination	[3]
288	AYILNLVKQIKKTGC	acetylation	[9]
288	AYILNLVKQIKKTGC	ubiquitination	[1, 2, 3, 7, 8]
292	NLVKQIKKTGCNVLL	ubiquitination	[3]
302	CNVLLIQKSILRDAL	acetylation	[9]
302	CNVLLIQKSILRDAL	ubiquitination	[3]
319	LALHFLNKMKIMVIK	acetylation	[9]
319	LALHFLNKMKIMVIK	ubiquitination	[1, 6, 7, 8]
321	LHFLNKMKIMVIKDI	ubiquitination	[3]
326	KMKIMVIKDIEREDI	acetylation	[9]
343	ICKTIGTKPVAHIDQ	ubiquitination	[3]
375	NGSGKLLKITGCASP	ubiquitination	[3]
384	TGCASPGKTVTIVVR	ubiquitination	[3, 5]
395	IVVRGSNKLVIEEAE	ubiquitination	[3, 7]
489	NRHAQGEKTAGINVR	acetylation	[9]
489	NRHAQGEKTAGINVR	ubiquitination	[3, 7, 10]
531	ETVRSILKIDDVVNT	ubiquitination	[1, 2, 3, 7, 8]

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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [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] 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]
 [10] 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] 

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 288 288 N6-acetyllysine.
 MOD_RES 302 302 N6-acetyllysine.
 MOD_RES 319 319 N6-acetyllysine.
 MOD_RES 326 326 N6-acetyllysine.  

Keyword

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

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 539 AA 

Protein Sequence

Gene Ontology

 GO:0005813; C:centrosome; IDA:MGI.
 GO:0005832; C:chaperonin-containing T-complex; IEA:Compara.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 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; TAS:ProtInc.
 GO:0051084; P:'de novo' posttranslational protein folding; TAS:Reactome. 

Interpro

 IPR012717; Chap_CCT_delta.
 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.