Q8HXP5 · SODM_HYLLA
- ProteinSuperoxide dismutase [Mn], mitochondrial
- GeneSOD2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids198 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic activity
- 2 superoxide + 2 H+ = H2O2 + O2
Cofactor
Note: Binds 1 Mn2+ ion per subunit.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial matrix | |
Molecular Function | manganese ion binding | |
Molecular Function | superoxide dismutase activity | |
Biological Process | cellular response to oxidative stress | |
Biological Process | regulation of transcription by RNA polymerase II | |
Biological Process | superoxide metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSuperoxide dismutase [Mn], mitochondrial
- EC number
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hylobatidae > Hylobates
Accessions
- Primary accessionQ8HXP5
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000159952 | 1-198 | Superoxide dismutase [Mn], mitochondrial | |||
Sequence: KHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQEALAKGDVTAQIALQPALKFNGGGHINHSIFWTNLSPNGGGEPKGELLEAIKRDFGSFDKFKEKLTATSVGVQGSGWGWLGFNKERGHLQIAACPNQDPLQGTTGLIPLLGIDVWEHAYYLQYKNVRPDYLKAIWNVINWENVTERYMACKK | ||||||
Modified residue | 34 | 3'-nitrotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 44 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 44 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 51 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 51 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 90 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 98 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 98 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 106 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 106 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 178 | N6-acetyllysine | ||||
Sequence: K |
Post-translational modification
Nitrated under oxidative stress. Nitration coupled with oxidation inhibits the catalytic activity.
Acetylation at Lys-98 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.
Keywords
- PTM
Interaction
Subunit
Homotetramer.
Structure
Sequence
- Sequence statusComplete
- Length198
- Mass (Da)22,234
- Last updated2003-11-21 v2
- ChecksumE266AFBBBDB34566