Search Results

Overview

Uniprot IDO43813
Protein NameGlutathione S-transferase LANCL1
Gene NameLANCL1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
128 YHKMNNEKQAEDCIT
142 TRLIHLNKIDPHAPN
52 QQMERGLKSADPRDG

Function

Functions as a glutathione transferase. Catalyzes conjugation of the glutathione (GSH) to artificial substrates 1-chloro-2,4-dinitrobenzene (CDNB) and p-nitrophenyl acetate. Mitigates neuronal oxidative stress during normal postnatal development and in response to oxidative stresses probably through GSH antioxidant defense mechanism (By similarity). May play a role in EPS8 signaling. Binds glutathione (PubMed:19528316)

Protein Sequence

10 MAQRAFPNPY 20 ADYNKSLAEG 30 YFDAAGRLTP 40 EFSQRLTNKI 50 RELLQQMERG 60 LKSADPRDGT 70 GYTGWAGIAV 80 LYLHLYDVFG 90 DPAYLQLAHG 100 YVKQSLNCLT 110 KRSITFLCGD 120 AGPLAVAAVL 130 YHKMNNEKQA 140 EDCITRLIHL 150 NKIDPHAPNE 160 MLYGRIGYIY 170 ALLFVNKNFG 180 VEKIPQSHIQ 190 QICETILTSG 200 ENLARKRNFT 210 AKSPLMYEWY 220 QEYYVGAAHG 230 LAGIYYYLMQ 240 PSLQVSQGKL 250 HSLVKPSVDY 260 VCQLKFPSGN 270 YPPCIGDNRD 280 LLVHWCHGAP 290 GVIYMLIQAY 300 KVFREEKYLC 310 DAYQCADVIW 320 QYGLLKKGYG 330 LCHGSAGNAY 340 AFLTLYNLTQ 350 DMKYLYRACK 360 FAEWCLEYGE 370 HGCRTPDTPF 380 SLFEGMAGTI 390 YFLADLLVPT KARFPAFEL

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005886 plasma membrane
Molecular Function GO:0004930 G protein-coupled receptor activity
Molecular Function GO:0043295 glutathione binding
Molecular Function GO:0004364 glutathione transferase activity
Molecular Function GO:0050750 low-density lipoprotein particle receptor binding
Molecular Function GO:0017124 SH3 domain binding
Molecular Function GO:0008270 zinc ion binding
Biological Process GO:0005975 carbohydrate metabolic process
Biological Process GO:1990748 cellular detoxification
Biological Process GO:0007186 G protein-coupled receptor signaling pathway
Biological Process GO:0031179 peptide modification

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] 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.

[4] 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.

[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] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.