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Details on Person UniProt:P00441 SOD1

Class:IdReferenceGeneProduct:64824
_chainChangeLoginitiator methionine:1 added on Sat February 7 2015;chain:2-154 added on Sat February 7 2015;initiator methionine:1 for 64824 removed on Fri Nov 03 2023;initiator methionine: for 64824 added on Fri Nov 03 2023;initiator methionine: for 64824 removed on Fri Aug 15 2025;initiator methionine:1 for 64824 added on Fri Aug 15 2025
_displayNameUniProt:P00441 SOD1
_timestamp2026-02-20 22:16:17
chaininitiator methionine:1
chain:2-154
checksum25CA38DA8D564483
commentFUNCTION Destroys radicals which are normally produced within the cells and which are toxic to biological systems (PubMed:24140062). Catalyzes the oxidation of hydrogen sulfide (H2S) to sulfate, playing an important role in detoxifying H2S and limiting the accumulation of reactive sulfur species (RSS) such as persulfides and polysulfides (PubMed:36630448).CATALYTIC ACTIVITY 2 superoxide + 2 H(+) = H2O2 + O2CATALYTIC ACTIVITY hydrogen sulfide + 2 O2 = sulfate + H(+)COFACTOR Binds 1 copper ion per subunit.COFACTOR Binds 1 zinc ion per subunit.SUBUNIT Homodimer; non-disulfide-linked (By similarity). Homodimerization may take place via the ditryptophan cross-link at Trp-33. Heterodimer with SOD1 (PubMed:31292775). The heterodimer CCS:SOD1 interacts with SLC31A1; this heterotrimer is Cu(1+)-mediated and its maintenance is regulated through SOD1 activation (PubMed:31292775). Interacts with DAOA; the interaction is direct (PubMed:30037290).INTERACTION Predominantly cytoplasmic; the pathogenic variants ALS1 Arg-86 and Ala-94 gradually aggregates and accumulates in mitochondria.PTM Unlike wild-type protein, the pathogenic variants ALS1 Arg-38, Arg-47, Arg-86 and Ala-94 are polyubiquitinated by RNF19A leading to their proteasomal degradation. The pathogenic variants ALS1 Arg-86 and Ala-94 are ubiquitinated by MARCH5 leading to their proteasomal degradation.PTM The ditryptophan cross-link at Trp-33 is responsible for the non-disulfide-linked homodimerization. Such modification might only occur in extreme conditions and additional experimental evidence is required.PTM Palmitoylation helps nuclear targeting and decreases catalytic activity.PTM Succinylation, adjacent to copper catalytic site, probably inhibits activity. Desuccinylation by SIRT5 enhances activity.DISEASE The disease is caused by variants affecting the gene represented in this entry.DISEASE The disease is caused by variants affecting the gene represented in this entry.MISCELLANEOUS The protein (both wild-type and ALS1 variants) has a tendency to form fibrillar aggregates in the absence of the intramolecular disulfide bond or of bound zinc ions. These aggregates may have cytotoxic effects. Zinc binding promotes dimerization and stabilizes the native form.SIMILARITY Belongs to the Cu-Zn superoxide dismutase family.SEQUENCE CAUTION ALS genetic mutations dbONLINE INFORMATION Superoxide dismutase entry
descriptionrecommendedName: fullName evidence="81"Superoxide dismutase [Cu-Zn] ecNumber evidence="35"1.15.1.1 ecNumber evidence="81"1.8.-.- alternativeName: fullName evidence="80"Hydrogen sulfide oxidase alternativeName: Superoxide dismutase 1 shortName: hSod1
geneNameSOD1
identifierP00441
isSequenceChangedFALSE
keyword3D-structure
Acetylation
Amyotrophic lateral sclerosis
Antioxidant
Copper
Cytoplasm
Direct protein sequencing
Disease variant
Disulfide bond
Lipoprotein
Metal-binding
Neurodegeneration
Nucleus
Oxidoreductase
Palmitate
Phosphoprotein
Proteomics identification
Reference proteome
Ubl conjugation
Zinc
modified[InstanceEdit:9836292] Weiser, Joel, 2023-05-25
[InstanceEdit:9852000] Weiser, Joel, 2023-11-03
[InstanceEdit:9862192] Weiser, Joel, 2024-02-26
[InstanceEdit:9909836] Weiser, Joel, 2024-05-14
[InstanceEdit:9926675] Weiser, Joel, 2024-11-03
[InstanceEdit:9939033] Weiser, Joel, 2025-02-21
[InstanceEdit:9963647] Weiser, Joel, 2025-08-15
[InstanceEdit:9983091] Weiser, Joel, 2026-02-20
nameSOD1
referenceDatabase[ReferenceDatabase:2] UniProt
referenceGene[ReferenceDNASequence:8950613] ENSEMBL:ENSG00000142168 SOD1 [Homo sapiens]
secondaryIdentifierSODC_HUMAN
A6NHJ0
D3DSE4
Q16669
Q16711
Q16838
Q16839
Q16840
Q6NR85
sequenceLength154
species[Species:48887] Homo sapiens
(referenceEntity)[EntityWithAccessionedSequence:350697] SOD1 [cytosol] [Homo sapiens]
[EntityWithAccessionedSequence:350705] SOD1 [extracellular region] [Homo sapiens]
[EntityWithAccessionedSequence:3299726] 2xHC-SOD1 [cytosol] [Homo sapiens]
[EntityWithAccessionedSequence:3777082] SOD1 [mitochondrial intermembrane space] [Homo sapiens]
[EntityWithAccessionedSequence:3777108] 2xHC-SOD1 [mitochondrial intermembrane space] [Homo sapiens]
(referenceSequence)[IntraChainCrosslinkedResidue:3299696] Intra-chain Crosslink via L-cystine (cross-link) at 57 and 146
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