Search Results

Overview

Uniprot IDP37837
Protein NameTransaldolase
Gene NameTALDO1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
115 DARLSFDKDAMVARA
130 RRLIELYKEAGISKD
136 YKEAGISKDRILIKL
203 WHVANTDKKSYEPLE
204 HVANTDKKSYEPLED
219 PGVKSVTKIYNYYKK
225 TKIYNYYKKFSYKTI
277 LVPVLSAKAAQASDL
286 AQASDLEKIHLDEKS
292 EKIHLDEKSFRWLHN
307 EDQMAVEKLSDGIRK
314 KLSDGIRKFAADAVK
321 KFAADAVKLERMLTE
7 *MSSSPVKRQRMESA
71 EAIAYGRKLGGSQED
81 GSQEDQIKNAIDKLF

Function

Catalyzes the rate-limiting step of the non-oxidative phase in the pentose phosphate pathway. Catalyzes the reversible conversion of sedoheptulose-7-phosphate and D-glyceraldehyde 3-phosphate into erythrose-4-phosphate and beta-D-fructose 6-phosphate (PubMed:18687684, PubMed:8955144). Not only acts as a pentose phosphate pathway enzyme, but also affects other metabolite pathways by altering its subcellular localization between the nucleus and the cytoplasm (By similarity)

Protein Sequence

10 MSSSPVKRQR 20 MESALDQLKQ 30 FTTVVADTGD 40 FHAIDEYKPQ 50 DATTNPSLIL 60 AAAQMPAYQE 70 LVEEAIAYGR 80 KLGGSQEDQI 90 KNAIDKLFVL 100 FGAEILKKIP 110 GRVSTEVDAR 120 LSFDKDAMVA 130 RARRLIELYK 140 EAGISKDRIL 150 IKLSSTWEGI 160 QAGKELEEQH 170 GIHCNMTLLF 180 SFAQAVACAE 190 AGVTLISPFV 200 GRILDWHVAN 210 TDKKSYEPLE 220 DPGVKSVTKI 230 YNYYKKFSYK 240 TIVMGASFRN 250 TGEIKALAGC 260 DFLTISPKLL 270 GELLQDNAKL 280 VPVLSAKAAQ 290 ASDLEKIHLD 300 EKSFRWLHNE 310 DQMAVEKLSD 320 GIRKFAADAV 330 KLERMLTERM FNAENGK

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005634 nucleus
Molecular Function GO:0048029 monosaccharide binding
Molecular Function GO:0004801 transaldolase activity
Biological Process GO:0005975 carbohydrate metabolic process
Biological Process GO:0006002 fructose 6-phosphate metabolic process
Biological Process GO:0009052 pentose-phosphate shunt, non-oxidative branch

Reference

[1] 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.

[2] 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.

[3] 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.

[4] 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.

[5] 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.

[6] 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.

[7] 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.