P04179 · SODM_HUMAN
- ProteinSuperoxide dismutase [Mn], mitochondrial
- GeneSOD2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids222 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group 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 > Hominidae > Homo
Accessions
- Primary accessionP04179
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Microvascular complications of diabetes 6 (MVCD6)
- Note
- DescriptionPathological 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.
- See alsoMIM:612634
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_019363 | 10 | in dbSNP:rs5746096 | |||
Sequence: S → I | ||||||
Natural variant | VAR_016183 | 16 | associated with a decreased susceptibility to diabetic nephropathy in Japanese and Chinese patients with type 2 diabetes; dbSNP:rs4880 | |||
Sequence: V → A | ||||||
Mutagenesis | 58 | Reduced enzyme activity. | ||||
Sequence: Y → A, H, N, V, or F | ||||||
Mutagenesis | 58 | Loss of nitration. Enhanced dityrosine formation on peroxynitrite treatment. | ||||
Sequence: Y → F | ||||||
Natural variant | VAR_019364 | 66 | in dbSNP:rs5746097 | |||
Sequence: E → V | ||||||
Natural variant | VAR_025898 | 76 | in dbSNP:rs4987023 | |||
Sequence: G → R | ||||||
Natural variant | VAR_007165 | 82 | in dbSNP:rs1141718 | |||
Sequence: I → T | ||||||
Natural variant | VAR_019365 | 156 | in dbSNP:rs5746129 | |||
Sequence: R → W |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 338 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
Protein family/group databases
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-24 | Mitochondrion | ||||
Sequence: MLSRAVCGTSRQLAPVLGYLGSRQ | ||||||
Chain | PRO_0000032869 | 25-222 | Superoxide dismutase [Mn], mitochondrial | |||
Sequence: KHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQEALAKGDVTAQIALQPALKFNGGGHINHSIFWTNLSPNGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERGHLQIAACPNQDPLQGTTGLIPLLGIDVWEHAYYLQYKNVRPDYLKAIWNVINWENVTERYMACKK | ||||||
Modified residue | 58 | 3'-nitrotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 68 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 68 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 75 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 75 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 114 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 122 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 122 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 130 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 130 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 202 | N6-acetyllysine | ||||
Sequence: K |
Post-translational modification
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.
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Induction
Expression is regulated by KRIT1.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homotetramer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P04179 | CEP70 Q8NHQ1 | 3 | EBI-716989, EBI-739624 | |
BINARY | P04179 | SOD2 P04179 | 2 | EBI-716989, EBI-716989 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence & Isoforms
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 4 isoforms produced by Alternative splicing.
P04179-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length222
- Mass (Da)24,750
- Last updated2017-12-20 v3
- ChecksumCA047D7900AE5905
P04179-2
- Name2
- Differences from canonical
- 75-113: Missing
P04179-3
- Name3
- Differences from canonical
- 115-174: Missing
P04179-4
- Name4
- Differences from canonical
- 1-46: Missing
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_053761 | 1-46 | in isoform 4 | |||
Sequence: Missing | ||||||
Sequence conflict | 14 | in Ref. 3 | ||||
Sequence: A → P | ||||||
Sequence conflict | 65 | in Ref. 5; CAA42066/CAA33228 | ||||
Sequence: T → N | ||||||
Sequence conflict | 66 | in Ref. 6 | ||||
Sequence: E → Q | ||||||
Alternative sequence | VSP_042558 | 75-113 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 112 | in Ref. 6 | ||||
Sequence: E → Q | ||||||
Alternative sequence | VSP_053762 | 115-174 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 123 | in Ref. 3; CAA30687 | ||||
Sequence: R → L | ||||||
Sequence conflict | 133 | in Ref. 6 | ||||
Sequence: E → Q | ||||||
Sequence conflict | 148-149 | in Ref. 6 | ||||
Sequence: Missing | ||||||
Sequence conflict | 155 | in Ref. 2; CAA68533 and 6 | ||||
Sequence: E → Q |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X59445 EMBL· GenBank· DDBJ | CAA42066.1 EMBL· GenBank· DDBJ | mRNA | ||
Y00472 EMBL· GenBank· DDBJ | CAA68533.1 EMBL· GenBank· DDBJ | mRNA | ||
Y00985 EMBL· GenBank· DDBJ | CAA68791.1 EMBL· GenBank· DDBJ | mRNA | ||
X07834 EMBL· GenBank· DDBJ | CAA30687.1 EMBL· GenBank· DDBJ | mRNA | ||
M36693 EMBL· GenBank· DDBJ | AAA36622.1 EMBL· GenBank· DDBJ | mRNA | ||
X15132 EMBL· GenBank· DDBJ | CAA33228.1 EMBL· GenBank· DDBJ | mRNA | ||
X14322 EMBL· GenBank· DDBJ | CAA32502.1 EMBL· GenBank· DDBJ | mRNA | ||
S77127 EMBL· GenBank· DDBJ | AAD14248.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
BT006967 EMBL· GenBank· DDBJ | AAP35613.1 EMBL· GenBank· DDBJ | mRNA | ||
AY267901 EMBL· GenBank· DDBJ | AAP03428.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK097395 EMBL· GenBank· DDBJ | BAG53464.1 EMBL· GenBank· DDBJ | mRNA | ||
AK296809 EMBL· GenBank· DDBJ | BAG59382.1 EMBL· GenBank· DDBJ | mRNA | ||
AK304766 EMBL· GenBank· DDBJ | BAG65521.1 EMBL· GenBank· DDBJ | mRNA | ||
AK313082 EMBL· GenBank· DDBJ | BAG35908.1 EMBL· GenBank· DDBJ | mRNA | ||
AL135914 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471051 EMBL· GenBank· DDBJ | EAW47630.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471051 EMBL· GenBank· DDBJ | EAW47631.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC012423 EMBL· GenBank· DDBJ | AAH12423.1 EMBL· GenBank· DDBJ | mRNA |