CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010417
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 T-complex protein 1 subunit beta 
Protein Synonyms/Alias
 TCP-1-beta; CCT-beta 
Gene Name
 CCT2 
Gene Synonyms/Alias
 99D8.1; CCTB 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
13LAPVNIFKAGADEERacetylation[1]
13LAPVNIFKAGADEERubiquitination[2, 3, 4, 5]
40IAIGDLVKSTLGPKGubiquitination[6]
46VKSTLGPKGMDKILLubiquitination[5]
50LGPKGMDKILLSSGRubiquitination[5]
72NDGATILKNIGVDNPubiquitination[2, 3, 5, 6, 7, 8]
82GVDNPAAKVLVDMSRubiquitination[2, 5, 6, 8]
119EAESLIAKKIHPQTIubiquitination[3, 5, 6]
120AESLIAKKIHPQTIIubiquitination[2, 5]
154DHGSDEVKFRQDLMNacetylation[1]
154DHGSDEVKFRQDLMNubiquitination[2, 3, 4, 5, 6, 8, 9]
170AGTTLSSKLLTHHKDubiquitination[5]
176SKLLTHHKDHFTKLAubiquitination[5]
181HHKDHFTKLAVEAVLacetylation[1]
191VEAVLRLKGSGNLEAubiquitination[2, 5, 6]
203LEAIHIIKKLGGSLAubiquitination[2, 6]
204EAIHIIKKLGGSLADubiquitination[5, 6]
222DEGFLLDKKIGVNQPubiquitination[3, 5, 6, 8]
223EGFLLDKKIGVNQPKubiquitination[5]
230KIGVNQPKRIENAKIubiquitination[5]
236PKRIENAKILIANTGubiquitination[2, 4]
248NTGMDTDKIKIFGSRubiquitination[2, 3, 4, 5, 6, 10]
250GMDTDKIKIFGSRVRubiquitination[2, 3, 4, 5]
263VRVDSTAKVAEIEHAubiquitination[5, 6]
272AEIEHAEKEKMKEKVubiquitination[5]
274IEHAEKEKMKEKVERubiquitination[5]
284EKVERILKHGINCFIubiquitination[2, 3, 5, 6]
342FDHPELVKLGSCKLIubiquitination[5, 6]
347LVKLGSCKLIEEVMIubiquitination[5]
402CVLAQTVKDSRTVYGubiquitination[3, 5, 6]
431LANRTPGKEAVAMESubiquitination[3, 5, 6]
441VAMESYAKALRMLPTubiquitination[2, 4, 5, 6, 7, 8]
500ITESFQVKRQVLLSAubiquitination[5]
522LRVDNIIKAAPRKRVubiquitination[2, 3, 4, 5, 6, 8, 11, 12]
527IIKAAPRKRVPDHHPubiquitination[3]
Reference
 [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. 
Sequence Annotation
 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.  
Keyword
 Acetylation; Alternative splicing; 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
MASLSLAPVN IFKAGADEER AETARLTSFI GAIAIGDLVK STLGPKGMDK ILLSSGRDAS 60
LMVTNDGATI LKNIGVDNPA AKVLVDMSRV QDDEVGDGTT SVTVLAAELL REAESLIAKK 120
IHPQTIIAGW REATKAAREA LLSSAVDHGS DEVKFRQDLM NIAGTTLSSK LLTHHKDHFT 180
KLAVEAVLRL KGSGNLEAIH IIKKLGGSLA DSYLDEGFLL DKKIGVNQPK RIENAKILIA 240
NTGMDTDKIK IFGSRVRVDS TAKVAEIEHA EKEKMKEKVE RILKHGINCF INRQLIYNYP 300
EQLFGAAGVM AIEHADFAGV ERLALVTGGE IASTFDHPEL VKLGSCKLIE EVMIGEDKLI 360
HFSGVALGEA CTIVLRGATQ QILDEAERSL HDALCVLAQT VKDSRTVYGG GCSEMLMAHA 420
VTQLANRTPG KEAVAMESYA KALRMLPTII ADNAGYDSAD LVAQLRAAHS EGNTTAGLDM 480
REGTIGDMAI LGITESFQVK RQVLLSAAEA AEVILRVDNI IKAAPRKRVP DHHPC 535 
Gene Ontology
 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. 
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.