![Superoxide dismutase [Mn], mitochondrial structure](/protein-images/P04179.jpeg)
P04179
SODM_HUMANSOD2
Superoxide dismutase [Mn], mitochondrial
Homo sapiensTaxon: 9606
3D-structureAcetylationAlternative splicingDirect protein sequencingManganeseMetal-bindingMitochondrionNitrationOxidoreductaseProteomics identificationReference proteomeTransit peptide+1
Sequence Length
222
amino acids
Molecular Weight
24.8 kDa
theoretical
Experimental Structures
48
PDB entries
Related Diseases
1
recorded
Function
Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems
Related Diseases
Microvascular complications of diabetes 6
Pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis.
Amino Acid Sequence
MLSRAVCGTSRQLAPVLGYLGSRQKHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVN NLNVTEEKYQEALAKGDVTAQIALQPALKFNGGGHINHSIFWTNLSPNGGGEPKGELLEA IKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERGHLQIAACPNQDPLQGTTGLIPLL GIDVWEHAYYLQYKNVRPDYLKAIWNVINWENVTERYMACKK
FASTA format · 222 amino acids · mass 24.8 kDa
Experimental Structures
48 PDB entries1AP51AP61EM11JA81LUV1LUW1MSD1N0J1N0N1PL41PM91QNM1SZX1VAR1XDC1XIL1ZSP1ZTE1ZUQ2ADP2ADQ2GDS2P4K2QKA2QKC3C3S3C3T5GXO5T305VF97KKS7KKU7KKW7KLB8SKS8VHW8VHY8VJ08VJ48VJ58VJ89BVY9BW29BWM9BWQ9BWR9NR09NSJ
Post-Translational Modifications
- •Nitrated under oxidative stress. Nitration coupled with oxidation inhibits the catalytic activity
- •Acetylation at Lys-122 decreases enzymatic activity. Deacetylated by SIRT3 upon exposure to ionizing radiations or after long fasting (By similarity)
- •Polyubiquitinated; leading to proteasomal degradation. Deubiquitinated by USP36 which increases protein stability