Search Results

Overview

Uniprot ID	Q9BRA2
Protein Name	Thioredoxin domain-containing protein 17
Gene Name	TXNDC17
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
35	FAYFTGSKDAGGKSW
40	GSKDAGGKSWCPDCV
89	NDFRKNLKVTAVPTL
98	TAVPTLLKYGTPQKL

Function

Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Modulates TNF signaling and NF-kappa-B activation. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide

Protein Sequence

10 MARYEEVSVS 20 GFEEFHRAVE 30 QHNGKTIFAY 40 FTGSKDAGGK 50 SWCPDCVQAE 60 PVVREGLKHI 70 SEGCVFIYCQ 80 VGEKPYWKDP 90 NNDFRKNLKV 100 TAVPTLLKYG 110 TPQKLVESEC 120 LQANLVEMLF SED

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005829	cytosol
Cellular Component	GO:0070062	extracellular exosome
Molecular Function	GO:0047134	protein-disulfide reductase [NAD(P)H] activity
Biological Process	GO:0033209	tumor necrosis factor-mediated signaling pathway

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] 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.