CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-031455
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Transketolase 
Protein Synonyms/Alias
 cDNA FLJ56274, highly similar to Transketolase (EC 2.2.1.1) 
Gene Name
 TKT 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
55AELLNLRKISSDLDGubiquitination[1, 2, 3, 4]
67LDGHPVPKQAFTDVAubiquitination[1, 3, 4]
93CGMAYTGKYFDKASYubiquitination[1, 3, 4]
97YTGKYFDKASYRVYCubiquitination[3]
157HQMDIYQKRCEAFGWacetylation[5]
157HQMDIYQKRCEAFGWubiquitination[1, 2, 3, 4, 6, 7, 8, 9]
185CKAFGQAKHQPTAIIacetylation[4, 5]
185CKAFGQAKHQPTAIIubiquitination[1, 3, 4, 6, 7]
194QPTAIIAKTFKGRGIubiquitination[1, 2, 3, 4, 7, 9]
207GITGVEDKESWHGKPacetylation[4, 5]
207GITGVEDKESWHGKPubiquitination[2, 3, 4, 6]
213DKESWHGKPLPKNMAacetylation[4]
213DKESWHGKPLPKNMAubiquitination[3, 4, 6, 7]
234IYSQIQSKKKILATPubiquitination[1, 3, 7, 9]
235YSQIQSKKKILATPPubiquitination[2, 3, 9]
236SQIQSKKKILATPPQubiquitination[3, 4, 6, 9]
263MPSLPSYKVGDKIATubiquitination[1, 3, 4, 6, 7, 9]
267PSYKVGDKIATRKAYacetylation[4]
267PSYKVGDKIATRKAYubiquitination[3]
272GDKIATRKAYGQALAubiquitination[1, 2, 3, 4, 6, 7, 9, 10]
280AYGQALAKLGHASDRubiquitination[3, 7]
296IALDGDTKNSTFSEIubiquitination[1, 3, 4, 7]
305STFSEIFKKEHPDRFubiquitination[1, 2, 3, 7, 9]
306TFSEIFKKEHPDRFIubiquitination[3]
409SDGVATEKAVELAANubiquitination[1, 3, 4, 7, 9]
418VELAANTKGICFIRTubiquitination[1, 3, 4, 6]
446DFQVGQAKVVLKSKDubiquitination[1, 3]
452AKVVLKSKDDQVTVIacetylation[4]
452AKVVLKSKDDQVTVIubiquitination[3]
476LAAAELLKKEKINIRubiquitination[9]
491VLDPFTIKPLDRKLIubiquitination[1, 3, 4, 6, 7, 9]
496TIKPLDRKLILDSARubiquitination[3]
550NRVPRSGKPAELLKMubiquitination[1, 2, 3, 4, 9]
556GKPAELLKMFGIDRDacetylation[5]
556GKPAELLKMFGIDRDubiquitination[1]
Reference
 [1] 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]
 [2] 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]
 [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] 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]
 [6] 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]
 [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] 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]
 [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] 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
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 576 AA 
Protein Sequence
MAVLFFHTMR YKSQDPRNPH NDRFVLSKGH AAPILYAVWA EAGFLAEAEL LNLRKISSDL 60
DGHPVPKQAF TDVATGSLGQ GLGAACGMAY TGKYFDKASY RVYCLLGDGE LSEGSVWEAM 120
AFASIYKLDN LVAILDINRL GQSDPAPLQH QMDIYQKRCE AFGWHAIIVD GHSVEELCKA 180
FGQAKHQPTA IIAKTFKGRG ITGVEDKESW HGKPLPKNMA EQIIQEIYSQ IQSKKKILAT 240
PPQEDAPSVD IANIRMPSLP SYKVGDKIAT RKAYGQALAK LGHASDRIIA LDGDTKNSTF 300
SEIFKKEHPD RFIECYIAEQ NMVSIAVGCA TRNRTVPFCS TFAAFFTRAF DQIRMAAISE 360
SNINLCGSHC GVSIGEDGPS QMALEDLAMF RSVPTSTVFY PSDGVATEKA VELAANTKGI 420
CFIRTSRPEN AIIYNNNEDF QVGQAKVVLK SKDDQVTVIG AGVTLHEALA AAELLKKEKI 480
NIRVLDPFTI KPLDRKLILD SARATKGRIL TVEDHYYEGG IGEAVSSAVV GEPGITVTHL 540
AVNRVPRSGK PAELLKMFGI DRDAIAQAVR GLITKA 576 
Gene Ontology
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0003824; F:catalytic activity; IEA:InterPro. 
Interpro
 IPR009014; Transketo_C/Pyr-ferredox_oxred.
 IPR015941; Transketolase-like_C.
 IPR005475; Transketolase-like_Pyr-bd.
 IPR020826; Transketolase_BS.
 IPR005476; Transketolase_C.
 IPR005474; Transketolase_N. 
Pfam
 PF02779; Transket_pyr
 PF02780; Transketolase_C
 PF00456; Transketolase_N 
SMART
 SM00861; Transket_pyr 
PROSITE
 PS00802; TRANSKETOLASE_2 
PRINTS