CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005779
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Transketolase 
Protein Synonyms/Alias
 TK 
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
6**MESYHKPDQQKLQacetylation[1]
6**MESYHKPDQQKLQubiquitination[2]
11YHKPDQQKLQALKDTacetylation[1]
11YHKPDQQKLQALKDTubiquitination[3, 4]
16QQKLQALKDTANRLRubiquitination[2, 3, 4, 5, 6, 7]
102AELLNLRKISSDLDGubiquitination[2, 7]
114LDGHPVPKQAFTDVAubiquitination[2]
140CGMAYTGKYFDKASYubiquitination[2]
144YTGKYFDKASYRVYCacetylation[1]
144YTGKYFDKASYRVYCubiquitination[2, 8]
204HQMDIYQKRCEAFGWacetylation[1]
204HQMDIYQKRCEAFGWubiquitination[2, 3, 5, 7, 8, 9]
232CKAFGQAKHQPTAIIacetylation[10, 11]
232CKAFGQAKHQPTAIIubiquitination[2, 3, 5, 8]
241QPTAIIAKTFKGRGIacetylation[1]
241QPTAIIAKTFKGRGIubiquitination[2, 5, 7, 9]
254GITGVEDKESWHGKPacetylation[1]
254GITGVEDKESWHGKPubiquitination[2, 3, 4, 7]
260DKESWHGKPLPKNMAacetylation[1]
260DKESWHGKPLPKNMAubiquitination[2, 3, 5]
281IYSQIQSKKKILATPubiquitination[2, 5, 9]
282YSQIQSKKKILATPPubiquitination[2, 7, 9]
283SQIQSKKKILATPPQubiquitination[2, 3, 8, 9]
310MPSLPSYKVGDKIATubiquitination[2, 3, 5, 6, 8, 9]
314PSYKVGDKIATRKAYacetylation[1]
314PSYKVGDKIATRKAYubiquitination[2]
319GDKIATRKAYGQALAubiquitination[2, 8, 9, 12]
327AYGQALAKLGHASDRubiquitination[2, 3, 4, 5, 7]
343IALDGDTKNSTFSEIubiquitination[2, 5]
352STFSEIFKKEHPDRFubiquitination[2, 5, 7, 9]
353TFSEIFKKEHPDRFIubiquitination[2]
456SDGVATEKAVELAANubiquitination[2, 5, 9]
465VELAANTKGICFIRTubiquitination[2, 3, 6, 8]
493DFQVGQAKVVLKSKDubiquitination[2]
499AKVVLKSKDDQVTVIubiquitination[2]
523LAAAELLKKEKINIRubiquitination[9]
538VLDPFTIKPLDRKLIubiquitination[2, 3, 5, 6, 8, 9]
543TIKPLDRKLILDSARubiquitination[2]
597NRVPRSGKPAELLKMacetylation[1, 11]
597NRVPRSGKPAELLKMubiquitination[2, 5, 7, 9]
603GKPAELLKMFGIDRDacetylation[1]
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] 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]
 [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] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [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] Proteome-wide prediction of acetylation substrates.
 Basu A, Rose KL, Zhang J, Beavis RC, Ueberheide B, Garcia BA, Chait B, Zhao Y, Hunt DF, Segal E, Allis CD, Hake SB.
 Proc Natl Acad Sci U S A. 2009 Aug 18;106(33):13785-90. [PMID: 19666589]
 [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
 Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate. 
Sequence Annotation
 NP_BIND 123 125 Thiamine pyrophosphate.
 ACT_SITE 366 366 Proton donor (By similarity).
 METAL 155 155 Magnesium.
 METAL 185 185 Magnesium.
 METAL 187 187 Magnesium; via carbonyl oxygen.
 BINDING 37 37 Substrate (By similarity).
 BINDING 40 40 Thiamine pyrophosphate.
 BINDING 77 77 Thiamine pyrophosphate.
 BINDING 156 156 Thiamine pyrophosphate; via amide
 BINDING 185 185 Thiamine pyrophosphate.
 BINDING 244 244 Thiamine pyrophosphate.
 BINDING 258 258 Substrate (By similarity).
 BINDING 258 258 Thiamine pyrophosphate.
 BINDING 318 318 Substrate (By similarity).
 BINDING 345 345 Substrate (By similarity).
 BINDING 392 392 Thiamine pyrophosphate.
 BINDING 416 416 Substrate (By similarity).
 BINDING 424 424 Substrate (By similarity).
 BINDING 428 428 Thiamine pyrophosphate.
 BINDING 474 474 Substrate (By similarity).
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 6 6 N6-acetyllysine.
 MOD_RES 11 11 N6-acetyllysine.
 MOD_RES 144 144 N6-acetyllysine.
 MOD_RES 204 204 N6-acetyllysine.
 MOD_RES 241 241 N6-acetyllysine.
 MOD_RES 260 260 N6-acetyllysine.
 MOD_RES 275 275 Phosphotyrosine.
 MOD_RES 287 287 Phosphothreonine.
 MOD_RES 295 295 Phosphoserine.
 MOD_RES 603 603 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Calcium; Complete proteome; Direct protein sequencing; Magnesium; Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; Thiamine pyrophosphate; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 623 AA 
Protein Sequence
MESYHKPDQQ KLQALKDTAN RLRISSIQAT TAAGSGHPTS CCSAAEIMAV LFFHTMRYKS 60
QDPRNPHNDR FVLSKGHAAP ILYAVWAEAG FLAEAELLNL RKISSDLDGH PVPKQAFTDV 120
ATGSLGQGLG AACGMAYTGK YFDKASYRVY CLLGDGELSE GSVWEAMAFA SIYKLDNLVA 180
ILDINRLGQS DPAPLQHQMD IYQKRCEAFG WHAIIVDGHS VEELCKAFGQ AKHQPTAIIA 240
KTFKGRGITG VEDKESWHGK PLPKNMAEQI IQEIYSQIQS KKKILATPPQ EDAPSVDIAN 300
IRMPSLPSYK VGDKIATRKA YGQALAKLGH ASDRIIALDG DTKNSTFSEI FKKEHPDRFI 360
ECYIAEQNMV SIAVGCATRN RTVPFCSTFA AFFTRAFDQI RMAAISESNI NLCGSHCGVS 420
IGEDGPSQMA LEDLAMFRSV PTSTVFYPSD GVATEKAVEL AANTKGICFI RTSRPENAII 480
YNNNEDFQVG QAKVVLKSKD DQVTVIGAGV TLHEALAAAE LLKKEKINIR VLDPFTIKPL 540
DRKLILDSAR ATKGRILTVE DHYYEGGIGE AVSSAVVGEP GITVTHLAVN RVPRSGKPAE 600
LLKMFGIDRD AIAQAVRGLI TKA 623 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0005777; C:peroxisome; ISS:UniProtKB.
 GO:0048037; F:cofactor binding; IDA:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
 GO:0004802; F:transketolase activity; IDA:UniProtKB.
 GO:0006112; P:energy reserve metabolic process; TAS:Reactome.
 GO:0046166; P:glyceraldehyde-3-phosphate biosynthetic process; IDA:UniProtKB.
 GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; NAS:UniProtKB.
 GO:0005999; P:xylulose biosynthetic process; TAS:Reactome. 
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
 PS00801; TRANSKETOLASE_1
 PS00802; TRANSKETOLASE_2 
PRINTS