CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004635
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 T-complex protein 1 subunit alpha 
Protein Synonyms/Alias
 TCP-1-alpha; CCT-alpha 
Gene Name
 TCP1 
Gene Synonyms/Alias
 CCT1; CCTA 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
33ASIANIVKSSLGPVGubiquitination[1]
63NDGATILKLLEVEHPubiquitination[1, 2]
73EVEHPAAKVLCELADubiquitination[3, 4]
109KNADELVKQKIHPTSubiquitination[1, 2, 5]
111ADELVKQKIHPTSVIubiquitination[1, 3, 4]
126SGYRLACKEAVRYINubiquitination[1, 2, 5, 6, 7]
153DCLINAAKTSMSSKIubiquitination[1]
199VNSVNILKAHGRSQMacetylation[8]
199VNSVNILKAHGRSQMubiquitination[1, 2, 5, 9]
233PKRIVNAKIACLDFSubiquitination[1]
243CLDFSLQKTKMKLGVubiquitination[1, 5]
245DFSLQKTKMKLGVQVubiquitination[1]
247SLQKTKMKLGVQVVIubiquitination[1]
259VVITDPEKLDQIRQRubiquitination[1, 2, 6]
365DDELILIKNTKARTSubiquitination[1, 5]
368LILIKNTKARTSASIubiquitination[1]
400HDALCVVKRVLESKSacetylation[8, 10]
400HDALCVVKRVLESKSubiquitination[1, 5]
466DSTDLVAKLRAFHNEubiquitination[1, 2, 9, 11]
484NPERKNLKWIGLDLSubiquitination[1, 3, 4, 5, 9]
494GLDLSNGKPRDNKQAubiquitination[1, 2, 3, 4, 5, 9]
499NGKPRDNKQAGVFEPubiquitination[1, 2, 5]
510VFEPTIVKVKSLKFAubiquitination[1]
512EPTIVKVKSLKFATEubiquitination[1]
515IVKVKSLKFATEAAIubiquitination[5, 9]
532LRIDDLIKLHPESKDacetylation[8]
532LRIDDLIKLHPESKDubiquitination[1, 2, 3, 4, 7, 9]
538IKLHPESKDDKHGSYubiquitination[1, 2, 3, 4, 9]
541HPESKDDKHGSYEDAubiquitination[1, 2, 3, 4, 5, 6, 9, 12]
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] 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]
 [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] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [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] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [11] 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]
 [12] 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 181 181 Phosphotyrosine.
 MOD_RES 182 182 Phosphothreonine.
 MOD_RES 199 199 N6-acetyllysine.
 MOD_RES 400 400 N6-acetyllysine.
 MOD_RES 544 544 Phosphoserine.
 MOD_RES 551 551 Phosphoserine.  
Keyword
 Acetylation; ATP-binding; Chaperone; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 556 AA 
Protein Sequence
MEGPLSVFGD RSTGETIRSQ NVMAAASIAN IVKSSLGPVG LDKMLVDDIG DVTITNDGAT 60
ILKLLEVEHP AAKVLCELAD LQDKEVGDGT TSVVIIAAEL LKNADELVKQ KIHPTSVISG 120
YRLACKEAVR YINENLIVNT DELGRDCLIN AAKTSMSSKI IGINGDFFAN MVVDAVLAIK 180
YTDIRGQPRY PVNSVNILKA HGRSQMESML ISGYALNCVV GSQGMPKRIV NAKIACLDFS 240
LQKTKMKLGV QVVITDPEKL DQIRQRESDI TKERIQKILA TGANVILTTG GIDDMCLKYF 300
VEAGAMAVRR VLKRDLKRIA KASGATILST LANLEGEETF EAAMLGQAEE VVQERICDDE 360
LILIKNTKAR TSASIILRGA NDFMCDEMER SLHDALCVVK RVLESKSVVP GGGAVEAALS 420
IYLENYATSM GSREQLAIAE FARSLLVIPN TLAVNAAQDS TDLVAKLRAF HNEAQVNPER 480
KNLKWIGLDL SNGKPRDNKQ AGVFEPTIVK VKSLKFATEA AITILRIDDL IKLHPESKDD 540
KHGSYEDAVH SGALND 556 
Gene Ontology
 GO:0030054; C:cell junction; IDA:HPA.
 GO:0005813; C:centrosome; IDA:MGI.
 GO:0005832; C:chaperonin-containing T-complex; IEA:Compara.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005794; C:Golgi apparatus; IDA:HPA.
 GO:0005874; C:microtubule; IDA:UniProtKB.
 GO:0005720; C:nuclear heterochromatin; IEA:Compara.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0000242; C:pericentriolar material; IEA:Compara.
 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.
 GO:0007021; P:tubulin complex assembly; NAS:UniProtKB. 
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.