Search Results

Overview

Uniprot IDQ06830
Protein NamePeroxiredoxin-1
Gene NamePRDX1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
109 IPLVSDPKRTIAQDY
120 AQDYGVLKADEGISF
136 GLFIIDDKGILRQIT
168 QAFQFTDKHGEVCPA
178 EVCPAGWKPGSDTIK
190 TIKPDVQKSKEYFSK
192 KPDVQKSKEYFSKQK
197 KSKEYFSKQK*****
27 VMPDGQFKDISLSDY
35 DISLSDYKGKYVVFF
68 DRAEEFKKLNCQVIG
7 *MSSGNAKIGHPAPN
92 LAWVNTPKKQGGLGP
93 AWVNTPKKQGGLGPM

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) (PubMed:9497357). Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (By similarity)

Protein Sequence

10 MSSGNAKIGH 20 PAPNFKATAV 30 MPDGQFKDIS 40 LSDYKGKYVV 50 FFFYPLDFTF 60 VCPTEIIAFS 70 DRAEEFKKLN 80 CQVIGASVDS 90 HFCHLAWVNT 100 PKKQGGLGPM 110 NIPLVSDPKR 120 TIAQDYGVLK 130 ADEGISFRGL 140 FIIDDKGILR 150 QITVNDLPVG 160 RSVDETLRLV 170 QAFQFTDKHG 180 EVCPAGWKPG 190 SDTIKPDVQK SKEYFSKQK

Gene Ontology

Classification GO ID Description
Biological Process GO:0019430 removal of superoxide radicals
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005615 extracellular space
Cellular Component GO:0042470 melanosome
Cellular Component GO:0005634 nucleus
Molecular Function GO:0045296 cadherin binding
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0004601 peroxidase activity
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0008379 thioredoxin peroxidase activity
Biological Process GO:0008283 cell population proliferation
Biological Process GO:0045454 cell redox homeostasis
Biological Process GO:0042744 hydrogen peroxide catabolic process
Biological Process GO:0045321 leukocyte activation
Biological Process GO:0030101 natural killer cell activation
Biological Process GO:0006979 response to oxidative stress
Biological Process GO:0001501 skeletal system development

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] 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.

[4] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[5] 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.

[6] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.

[7] 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.

[8] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[9] 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.

[10] 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.

[11] 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.

[12] 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.

[13] 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.