Search Results

Overview

Uniprot IDP29401
Protein NameTransketolase
Gene NameTKT
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
102 AELLNLRKISSDLDG
11 YHKPDQQKLQALKDT
114 LDGHPVPKQAFTDVA
144 YTGKYFDKASYRVYC
16 QQKLQALKDTANRLR
204 HQMDIYQKRCEAFGW
232 CKAFGQAKHQPTAII
241 QPTAIIAKTFKGRGI
254 GITGVEDKESWHGKP
260 DKESWHGKPLPKNMA
281 IYSQIQSKKKILATP
283 SQIQSKKKILATPPQ
310 MPSLPSYKVGDKIAT
314 PSYKVGDKIATRKAY
319 GDKIATRKAYGQALA
327 AYGQALAKLGHASDR
352 STFSEIFKKEHPDRF
353 TFSEIFKKEHPDRFI
465 VELAANTKGICFIRT
493 DFQVGQAKVVLKSKD
499 AKVVLKSKDDQVTVI
538 VLDPFTIKPLDRKLI
543 TIKPLDRKLILDSAR
59 FFHTMRYKSQDPRNP
597 NRVPRSGKPAELLKM
6 **MESYHKPDQQKLQ

Function

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 (PubMed:20667822, PubMed:27259054, PubMed:31534226). Thus, catalyzes the reversible transfer of a two-carbon ketol group from sedoheptulose-7-phosphate to glyceraldehyde-3-phosphate, producing xylulose-5-phosphate and ribose-5-phosphate (PubMed:20667822, PubMed:27259054, PubMed:31534226). The phosphate group of the substrate plays a role in stabilizing the substrate-thiamine intermediate while preventing the formation of the reactive enamine intermediate (Ref.28). Can also use fructose-6-phosphate as a ketose donor (Probable)

Protein Sequence

10 MESYHKPDQQ 20 KLQALKDTAN 30 RLRISSIQAT 40 TAAGSGHPTS 50 CCSAAEIMAV 60 LFFHTMRYKS 70 QDPRNPHNDR 80 FVLSKGHAAP 90 ILYAVWAEAG 100 FLAEAELLNL 110 RKISSDLDGH 120 PVPKQAFTDV 130 ATGSLGQGLG 140 AACGMAYTGK 150 YFDKASYRVY 160 CLLGDGELSE 170 GSVWEAMAFA 180 SIYKLDNLVA 190 ILDINRLGQS 200 DPAPLQHQMD 210 IYQKRCEAFG 220 WHAIIVDGHS 230 VEELCKAFGQ 240 AKHQPTAIIA 250 KTFKGRGITG 260 VEDKESWHGK 270 PLPKNMAEQI 280 IQEIYSQIQS 290 KKKILATPPQ 300 EDAPSVDIAN 310 IRMPSLPSYK 320 VGDKIATRKA 330 YGQALAKLGH 340 ASDRIIALDG 350 DTKNSTFSEI 360 FKKEHPDRFI 370 ECYIAEQNMV 380 SIAVGCATRN 390 RTVPFCSTFA 400 AFFTRAFDQI 410 RMAAISESNI 420 NLCGSHCGVS 430 IGEDGPSQMA 440 LEDLAMFRSV 450 PTSTVFYPSD 460 GVATEKAVEL 470 AANTKGICFI 480 RTSRPENAII 490 YNNNEDFQVG 500 QAKVVLKSKD 510 DQVTVIGAGV 520 TLHEALAAAE 530 LLKKEKINIR 540 VLDPFTIKPL 550 DRKLILDSAR 560 ATKGRILTVE 570 DHYYEGGIGE 580 AVSSAVVGEP 590 GITVTHLAVN 600 RVPRSGKPAE 610 LLKMFGIDRD 620 AIAQAVRGLI TKA

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0016604 nuclear body
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005777 peroxisome
Cellular Component GO:0031982 vesicle
Molecular Function GO:0005509 calcium ion binding
Molecular Function GO:0000287 magnesium ion binding
Molecular Function GO:0042803 protein homodimerization activity
Molecular Function GO:0030976 thiamine pyrophosphate binding
Molecular Function GO:0004802 transketolase activity
Biological Process GO:1901159 D-xylulose 5-phosphate biosynthetic process
Biological Process GO:0046166 glyceraldehyde-3-phosphate biosynthetic process
Biological Process GO:0006098 pentose-phosphate shunt
Biological Process GO:0009052 pentose-phosphate shunt, non-oxidative branch

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[3] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[4] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[5] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[6] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[7] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[8] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[9] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.

[10] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.