Q8HXP5 · SODM_HYLLA

Function

function

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

Catalytic activity

Cofactor

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Note: Binds 1 Mn2+ ion per subunit.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site26Mn2+ (UniProtKB | ChEBI)
Binding site74Mn2+ (UniProtKB | ChEBI)
Binding site159Mn2+ (UniProtKB | ChEBI)
Binding site163Mn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentmitochondrial matrix
Molecular Functionmanganese ion binding
Molecular Functionsuperoxide dismutase activity
Biological Processcellular response to oxidative stress
Biological Processregulation of transcription by RNA polymerase II
Biological Processsuperoxide metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Superoxide dismutase [Mn], mitochondrial
  • EC number

Gene names

    • Name
      SOD2

Organism names

Accessions

  • Primary accession
    Q8HXP5

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001599521-198Superoxide dismutase [Mn], mitochondrial
Modified residue343'-nitrotyrosine
Modified residue44N6-acetyllysine; alternate
Modified residue44N6-succinyllysine; alternate
Modified residue51N6-acetyllysine; alternate
Modified residue51N6-succinyllysine; alternate
Modified residue90N6-acetyllysine
Modified residue98N6-acetyllysine; alternate
Modified residue98N6-succinyllysine; alternate
Modified residue106N6-acetyllysine; alternate
Modified residue106N6-succinyllysine; alternate
Modified residue178N6-acetyllysine

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

Interaction

Subunit

Homotetramer.

Structure

Family & Domains

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    198
  • Mass (Da)
    22,234
  • Last updated
    2003-11-21 v2
  • Checksum
    E266AFBBBDB34566
KHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQEALAKGDVTAQIALQPALKFNGGGHINHSIFWTNLSPNGGGEPKGELLEAIKRDFGSFDKFKEKLTATSVGVQGSGWGWLGFNKERGHLQIAACPNQDPLQGTTGLIPLLGIDVWEHAYYLQYKNVRPDYLKAIWNVINWENVTERYMACKK

Sequence caution

The sequence BAC20355.1 differs from that shown. Reason: Erroneous initiation Extended N-terminus.

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB087276
EMBL· GenBank· DDBJ
BAC20355.1
EMBL· GenBank· DDBJ
mRNA Different initiation

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp