Search Results

Overview

Uniprot IDP04179
Protein NameSuperoxide dismutase [Mn], mitochondrial
Gene NameSOD2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
114 PNGGGEPKGELLEAI
122 GELLEAIKRDFGSFD
130 RDFGSFDKFKEKLTA
68 NLNVTEEKYQEALAK
75 KYQEALAKGDVTAQI

Function

Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems

Protein Sequence

10 MLSRAVCGTS 20 RQLAPVLGYL 30 GSRQKHSLPD 40 LPYDYGALEP 50 HINAQIMQLH 60 HSKHHAAYVN 70 NLNVTEEKYQ 80 EALAKGDVTA 90 QIALQPALKF 100 NGGGHINHSI 110 FWTNLSPNGG 120 GEPKGELLEA 130 IKRDFGSFDK 140 FKEKLTAASV 150 GVQGSGWGWL 160 GFNKERGHLQ 170 IAACPNQDPL 180 QGTTGLIPLL 190 GIDVWEHAYY 200 LQYKNVRPDY 210 LKAIWNVINW 220 ENVTERYMAC KK

Gene Ontology

Classification GO ID Description
Cellular Component GO:0070062 extracellular exosome
Biological Process GO:0030335 positive regulation of cell migration
Biological Process GO:0010729 positive regulation of hydrogen peroxide biosynthetic process
Biological Process GO:1905461 positive regulation of vascular associated smooth muscle cell apoptotic process
Biological Process GO:1905932 positive regulation of vascular associated smooth muscle cell differentiation involved in phenotypic switching
Biological Process GO:0051289 protein homotetramerization
Biological Process GO:0008217 regulation of blood pressure
Biological Process GO:0006357 regulation of transcription by RNA polymerase II
Biological Process GO:0001836 release of cytochrome c from mitochondria
Biological Process GO:0019430 removal of superoxide radicals
Biological Process GO:0014823 response to activity
Biological Process GO:0046686 response to cadmium ion
Biological Process GO:0051602 response to electrical stimulus
Biological Process GO:0042542 response to hydrogen peroxide
Biological Process GO:0001666 response to hypoxia
Biological Process GO:0035902 response to immobilization stress
Biological Process GO:0035900 response to isolation stress
Biological Process GO:0033591 response to L-ascorbic acid
Biological Process GO:0032496 response to lipopolysaccharide
Biological Process GO:0071000 response to magnetism
Biological Process GO:0010042 response to manganese ion
Biological Process GO:0010269 response to selenium ion
Biological Process GO:0034021 response to silicon dioxide
Biological Process GO:0000303 response to superoxide
Biological Process GO:0009410 response to xenobiotic stimulus
Biological Process GO:0010043 response to zinc ion
Biological Process GO:0006801 superoxide metabolic process
Cellular Component GO:0005759 mitochondrial matrix
Cellular Component GO:0042645 mitochondrial nucleoid
Cellular Component GO:0005739 mitochondrion
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0019899 enzyme binding
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0030145 manganese ion binding
Molecular Function GO:0019825 oxygen binding
Molecular Function GO:0004784 superoxide dismutase activity
Biological Process GO:0003069 acetylcholine-mediated vasodilation involved in regulation of systemic arterial blood pressure
Biological Process GO:0071361 cellular response to ethanol
Biological Process GO:0034599 cellular response to oxidative stress
Biological Process GO:0050665 hydrogen peroxide biosynthetic process
Biological Process GO:0032364 intracellular oxygen homeostasis
Biological Process GO:0008285 negative regulation of cell population proliferation
Biological Process GO:1902631 negative regulation of membrane hyperpolarization
Biological Process GO:0043524 negative regulation of neuron apoptotic process
Biological Process GO:1902176 negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
Biological Process GO:1904706 negative regulation of vascular associated smooth muscle cell proliferation

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] 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.

[4] 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.

[5] 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.

[6] 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.