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Overview

Uniprot IDP60174
Protein NameTriosephosphate isomerase
Gene NameTPI1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
131 VIACIGEKLDEREAG
142 REAGITEKVVFEQTK
149 KVVFEQTKVIADNVK
156 KVIADNVKDWSKVVL
175 VWAIGTGKTATPQQA
188 QAQEVHEKLRGWLKS
19 NWKMNGRKQSLGELI
194 EKLRGWLKSNVSDAV
59 ARQKLDPKIAVAAQN
6 **MAPSRKFFVGGNW
69 VAAQNCYKVTNGAFT

Function

Triosephosphate isomerase is an extremely efficient metabolic enzyme that catalyzes the interconversion between dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde-3-phosphate (G3P) in glycolysis and gluconeogenesis

Protein Sequence

10 MAPSRKFFVG 20 GNWKMNGRKQ 30 SLGELIGTLN 40 AAKVPADTEV 50 VCAPPTAYID 60 FARQKLDPKI 70 AVAAQNCYKV 80 TNGAFTGEIS 90 PGMIKDCGAT 100 WVVLGHSERR 110 HVFGESDELI 120 GQKVAHALAE 130 GLGVIACIGE 140 KLDEREAGIT 150 EKVVFEQTKV 160 IADNVKDWSK 170 VVLAYEPVWA 180 IGTGKTATPQ 190 QAQEVHEKLR 200 GWLKSNVSDA 210 VAQSTRIIYG 220 GSVTGATCKE 230 LASQPDVDGF 240 LVGGASLKPE FVDIINAKQ

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005615 extracellular space
Cellular Component GO:0005634 nucleus
Molecular Function GO:0008929 methylglyoxal synthase activity
Molecular Function GO:0042803 protein homodimerization activity
Molecular Function GO:0004807 triose-phosphate isomerase activity
Molecular Function GO:0031625 ubiquitin protein ligase binding
Biological Process GO:0061621 canonical glycolysis
Biological Process GO:0006094 gluconeogenesis
Biological Process GO:0046166 glyceraldehyde-3-phosphate biosynthetic process
Biological Process GO:0019563 glycerol catabolic process
Biological Process GO:0006096 glycolytic process
Biological Process GO:0019242 methylglyoxal biosynthetic process

Reference

[1] 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.

[2] 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.

[3] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[4] 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.

[5] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[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] 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.

[8] 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.