Search Results

Overview

Uniprot IDP32119
Protein NamePeroxiredoxin-2
Gene NamePRDX2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
10 SGNARIGKPAPDFKA
119 SEDYGVLKTDEGIAY
135 GLFIIDGKGVLRQIT
177 EVCPAGWKPGSDTIK
26 AVVDGAFKEVKLSDY
29 DGAFKEVKLSDYKGK
67 NRAEDFRKLGCEVLG
92 AWINTPRKEGGLGPL

Function

Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2)

Protein Sequence

10 MASGNARIGK 20 PAPDFKATAV 30 VDGAFKEVKL 40 SDYKGKYVVL 50 FFYPLDFTFV 60 CPTEIIAFSN 70 RAEDFRKLGC 80 EVLGVSVDSQ 90 FTHLAWINTP 100 RKEGGLGPLN 110 IPLLADVTRR 120 LSEDYGVLKT 130 DEGIAYRGLF 140 IIDGKGVLRQ 150 ITVNDLPVGR 160 SVDEALRLVQ 170 AFQYTDEHGE 180 VCPAGWKPGS 190 DTIKPNVDDS KEYFSKHN

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:0016209 antioxidant activity
Molecular Function GO:0008379 thioredoxin peroxidase activity
Biological Process GO:0045454 cell redox homeostasis
Biological Process GO:0034599 cellular response to oxidative stress
Biological Process GO:0002357 defense response to tumor cell
Biological Process GO:0042744 hydrogen peroxide catabolic process
Biological Process GO:0045321 leukocyte activation
Biological Process GO:0043066 negative regulation of apoptotic process
Biological Process GO:0030194 positive regulation of blood coagulation
Biological Process GO:0042981 regulation of apoptotic process
Biological Process GO:0019430 removal of superoxide radicals
Biological Process GO:0006979 response to oxidative stress

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] 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] 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] 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.