Q8HXP2 · SODM_MACMU
- ProteinSuperoxide dismutase [Mn], mitochondrial
- GeneSOD2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- 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 H+ + 2 superoxide = H2O2 + O2
Cofactor
Note: Binds 1 Mn2+ ion per subunit.
Features
Showing features for binding site.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial matrix | |
Cellular Component | mitochondrion | |
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 |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSuperoxide dismutase [Mn], mitochondrial
- EC number
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Cercopithecidae > Cercopithecinae > Macaca
Accessions
- Primary accessionQ8HXP2
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000159955 | 1-198 | Superoxide dismutase [Mn], mitochondrial | |||
Sequence: KHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQEALAKGDVTAQIALQPALKFNGGGHINHSIFWTNLSPNGGGEPKGELLEAIKRDFGSFEKFKEKLTAASVGVQGSGWGWLGFNKERGQLQIAACPNQDPLQGTTGLIPLLGIDVWEHAYYLQYKNVRPDYLKAIWNVINWENVTERYMACKK | ||||||
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
Proteomic databases
Interaction
Structure
Sequence
- Sequence statusComplete
- Length198
- Mass (Da)22,209
- Last updated2003-11-21 v2
- ChecksumFB4F6B063198E5CC
Sequence caution
Keywords
- Technical term