CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-036958
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 T-complex protein 1 subunit alpha 
Protein Synonyms/Alias
  
Gene Name
 TCP1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
44VNSVNILKAHGRSQMubiquitination[1, 2, 3, 4, 5, 6]
78PKRIVNAKIACLDFSubiquitination[4, 6]
88CLDFSLQKTKMKLGVubiquitination[3, 4]
90DFSLQKTKMKLGVQVubiquitination[4]
92SLQKTKMKLGVQVVIubiquitination[4]
104VVITDPEKLDQIRQRubiquitination[1, 4, 6, 7]
210DDELILIKNTKARTSacetylation[6, 8]
210DDELILIKNTKARTSubiquitination[3, 4, 6]
213LILIKNTKARTSASIubiquitination[4, 6]
245HDALCVVKRVLESKSacetylation[6, 8, 9, 10]
245HDALCVVKRVLESKSubiquitination[2, 3, 4, 6]
311DSTDLVAKLRAFHNEacetylation[8]
311DSTDLVAKLRAFHNEubiquitination[1, 4, 5, 6]
329NPERKNLKWIGLDLSacetylation[6]
329NPERKNLKWIGLDLSubiquitination[3, 4, 5, 6, 11]
339GLDLSNGKPRDNKQAubiquitination[1, 3, 4, 5, 6, 11]
344NGKPRDNKQAGVFEPubiquitination[1, 3, 4, 6]
355VFEPTIVKVKSLKFAubiquitination[4, 6]
357EPTIVKVKSLKFATEubiquitination[4]
360IVKVKSLKFATEAAIubiquitination[2, 3, 5]
377LRIDDLIKLHPESKDacetylation[6, 8]
377LRIDDLIKLHPESKDubiquitination[1, 2, 4, 5, 6, 11]
383IKLHPESKDDKHGSYacetylation[6]
383IKLHPESKDDKHGSYubiquitination[1, 2, 4, 5, 6, 11]
386HPESKDDKHGSYEDAacetylation[6, 8]
386HPESKDDKHGSYEDAubiquitination[1, 2, 3, 4, 5, 6, 7, 11, 12]
Reference
 [1] 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]
 [2] 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]
 [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] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224]
 [10] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [11] 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]
 [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
  
Sequence Annotation
  
Keyword
 ATP-binding; Chaperone; Complete proteome; Cytoplasm; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 401 AA 
Protein Sequence
MSSKIIGING DFFANMVVDA VLAIKYTDIR GQPRYPVNSV NILKAHGRSQ MESMLISGYA 60
LNCVVGSQGM PKRIVNAKIA CLDFSLQKTK MKLGVQVVIT DPEKLDQIRQ RESDITKERI 120
QKILATGANV ILTTGGIDDM CLKYFVEAGA MAVRRVLKRD LKRIAKASGA TILSTLANLE 180
GEETFEAAML GQAEEVVQER ICDDELILIK NTKARTSASI ILRGANDFMC DEMERSLHDA 240
LCVVKRVLES KSVVPGGGAV EAALSIYLEN YATSMGSREQ LAIAEFARSL LVIPNTLAVN 300
AAQDSTDLVA KLRAFHNEAQ VNPERKNLKW IGLDLSNGKP RDNKQAGVFE PTIVKVKSLK 360
FATEAAITIL RIDDLIKLHP ESKDDKHGSY EDAVHSGALN D 401 
Gene Ontology
 GO:0030054; C:cell junction; IDA:HPA.
 GO:0005832; C:chaperonin-containing T-complex; IEA:Compara.
 GO:0005794; C:Golgi apparatus; IDA:HPA.
 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:0006457; P:protein folding; IEA:InterPro. 
Interpro
 IPR012715; Chap_CCT_alpha.
 IPR017998; Chaperone_TCP-1.
 IPR002423; Cpn60/TCP-1.
 IPR027409; GroEL-like_apical_dom.
 IPR027413; GROEL-like_equatorial.
 IPR027410; TCP-1-like_intermed. 
Pfam
 PF00118; Cpn60_TCP1 
SMART
  
PROSITE
  
PRINTS
 PR00304; TCOMPLEXTCP1.