Search Results

Overview

Uniprot IDP78417
Protein NameGlutathione S-transferase omega-1
Gene NameGSTO1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
101 DEAYPGKKLLPDDPY
11 ESARSLGKGSAPPGP
110 LPDDPYEKACQKMIL
136 SFIRSQNKEDYAGLK
143 KEDYAGLKEEFRKEF
152 EFRKEFTKLEEVLTN
160 LEEVLTNKKTTFFGG
161 EEVLTNKKTTFFGGN
188 FERLEAMKLNECVDH
198 ECVDHTPKLKLWMAA
57 EVININLKNKPEWFF
59 ININLKNKPEWFFKK

Function

Exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities. Has S-(phenacyl)glutathione reductase activity. Also has glutathione S-transferase activity. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) and dimethylarsonic acid

Protein Sequence

10 MSGESARSLG 20 KGSAPPGPVP 30 EGSIRIYSMR 40 FCPFAERTRL 50 VLKAKGIRHE 60 VININLKNKP 70 EWFFKKNPFG 80 LVPVLENSQG 90 QLIYESAITC 100 EYLDEAYPGK 110 KLLPDDPYEK 120 ACQKMILELF 130 SKVPSLVGSF 140 IRSQNKEDYA 150 GLKEEFRKEF 160 TKLEEVLTNK 170 KTTFFGGNSI 180 SMIDYLIWPW 190 FERLEAMKLN 200 ECVDHTPKLK 210 LWMAAMKEDP 220 TVSALLTSEK 230 DWQGFLELYL 240 QNSPEACDYG L

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Molecular Function GO:0045174 glutathione dehydrogenase (ascorbate) activity
Molecular Function GO:0004364 glutathione transferase activity
Molecular Function GO:0050610 methylarsonate reductase activity
Molecular Function GO:0016491 oxidoreductase activity
Biological Process GO:0071243 cellular response to arsenic-containing substance
Biological Process GO:0006749 glutathione metabolic process
Biological Process GO:0019852 L-ascorbic acid metabolic process
Biological Process GO:0051280 negative regulation of release of sequestered calcium ion into cytosol
Biological Process GO:0051281 positive regulation of release of sequestered calcium ion into cytosol
Biological Process GO:0014810 positive regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
Biological Process GO:0010881 regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
Biological Process GO:0010880 regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
Biological Process GO:0042178 xenobiotic catabolic process

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] 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] 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.

[5] 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.

[6] 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.