Search Results

Overview

Uniprot ID	Q16881
Protein Name	Thioredoxin reductase 1, cytoplasmic
Gene Name	TXNRD1
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
126	DLPVVFVKQRKIGGH
129	VVFVKQRKIGGHGPT
138	GGHGPTLKAYQEGRL
150	GRLQKLLKMNGPEDL
218	NVGCIPKKLMHQAAL
274	RVALREKKVVYENAY
300	TNNKGKEKIYSAERF
449	GRDACTRKIGLETVG

Function

Reduces disulfide protein thioredoxin (Trx) to its dithiol-containing form (PubMed:8577704). Homodimeric flavoprotein involved in the regulation of cellular redox reactions, growth and differentiation. A selenocysteine residue at the C-terminal active site is essential for catalysis (Probable). Also has reductase activity on hydrogen peroxide (H2O2) (PubMed:10849437)

Protein Sequence

10 MGCAEGKAVA 20 AAAPTELQTK 30 GKNGDGRRRS 40 AKDHHPGKTL 50 PENPAGFTST 60 ATADSRALLQ 70 AYIDGHSVVI 80 FSRSTCTRCT 90 EVKKLFKSLC 100 VPYFVLELDQ 110 TEDGRALEGT 120 LSELAAETDL 130 PVVFVKQRKI 140 GGHGPTLKAY 150 QEGRLQKLLK 160 MNGPEDLPKS 170 YDYDLIIIGG 180 GSGGLAAAKE 190 AAQYGKKVMV 200 LDFVTPTPLG 210 TRWGLGGTCV 220 NVGCIPKKLM 230 HQAALLGQAL 240 QDSRNYGWKV 250 EETVKHDWDR 260 MIEAVQNHIG 270 SLNWGYRVAL 280 REKKVVYENA 290 YGQFIGPHRI 300 KATNNKGKEK 310 IYSAERFLIA 320 TGERPRYLGI 330 PGDKEYCISS 340 DDLFSLPYCP 350 GKTLVVGASY 360 VALECAGFLA 370 GIGLDVTVMV 380 RSILLRGFDQ 390 DMANKIGEHM 400 EEHGIKFIRQ 410 FVPIKVEQIE 420 AGTPGRLRVV 430 AQSTNSEEII 440 EGEYNTVMLA 450 IGRDACTRKI 460 GLETVGVKIN 470 EKTGKIPVTD 480 EEQTNVPYIY 490 AIGDILEDKV 500 ELTPVAIQAG 510 RLLAQRLYAG 520 STVKCDYENV 530 PTTVFTPLEY 540 GACGLSEEKA 550 VEKFGEENIE 560 VYHSYFWPLE 570 WTIPSRDNNK 580 CYAKIICNTK 590 DNERVVGFHV 600 LGPNAGEVTQ 610 GFAAALKCGL 620 TKKQLDSTIG 630 IHPVCAEVFT 640 TLSVTKRSGA SILQAGCUG

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:0005739	mitochondrion
Cellular Component	GO:0005654	nucleoplasm
Molecular Function	GO:0071949	FAD binding
Molecular Function	GO:0042802	identical protein binding
Molecular Function	GO:0050137	NADPH peroxidase activity
Molecular Function	GO:0004791	thioredoxin-disulfide reductase (NADPH) activity
Biological Process	GO:0045454	cell redox homeostasis
Biological Process	GO:0007165	signal transduction

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] 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.

[4] 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.

[5] 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.