SOD1
entrez
6647
canonical
uniprot
P00441
canonical
ensembl
ENSG00000142168
resolver
ensp
ENSP00000270142
resolver
enst
ENST00000270142
resolver
genesymbol
HEL-S-44
resolver
genesymbol
SOD1
resolver
hgnc
HGNC:11179
resolver
uniprot
A6NHJ0
resolver
uniprot
D3DSE4
resolver
uniprot
Q16669
resolver
uniprot
Q16711
resolver
uniprot
Q16838
resolver
uniprot
Q16839
resolver
uniprot
Q16840
resolver
uniprot
Q6NR85
resolver
uniprot
V9HWC9
resolver
uniprot_entry
SODC_HUMAN
resolver
uniprot_entry
V9HWC9_HUMAN
resolver
uniprot_sec
A6NHJ0
resolver
uniprot_sec
D3DSE4
resolver
uniprot_sec
Q16669
resolver
uniprot_sec
Q16711
resolver
uniprot_sec
Q16838
resolver
uniprot_sec
Q16839
resolver
uniprot_sec
Q16840
resolver
uniprot_sec
Q6NR85
resolver
activity_regulation
ACTIVITY REGULATION: Activated by CCS/copper chaperone for superoxide dismutase; can also be activated independently of CCS. {ECO:0000269|PubMed:18948262}.
uniprot
proteins
amino_acid_sequence
MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERHVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
uniprot
proteins
disease_involvement
DISEASE: Amyotrophic lateral sclerosis 1 (ALS1) [MIM:105400]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases. {ECO:0000269|PubMed:10400992, ECO:0000269|PubMed:10430435, ECO:0000269|PubMed:10732812, ECO:0000269|PubMed:11369193, ECO:0000269|PubMed:11535232, ECO:0000269|PubMed:12145308, ECO:0000269|PubMed:12210393, ECO:0000269|PubMed:12402272, ECO:0000269|PubMed:12754496, ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:14506936, ECO:0000269|PubMed:15056757, ECO:0000269|PubMed:18301754, ECO:0000269|PubMed:18378676, ECO:0000269|PubMed:18552350, ECO:0000269|PubMed:19741096, ECO:0000269|PubMed:20460594, ECO:0000269|PubMed:21220647, ECO:0000269|PubMed:21247266, ECO:0000269|PubMed:24283821, ECO:0000269|PubMed:27604643, ECO:0000269|PubMed:31086828, ECO:0000269|PubMed:7496169, ECO:0000269|PubMed:7501156, ECO:0000269|PubMed:7647793, ECO:0000269|PubMed:7655468, ECO:0000269|PubMed:7655469, ECO:0000269|PubMed:7655471, ECO:0000269|PubMed:7700376, ECO:0000269|PubMed:7795609, ECO:0000269|PubMed:7836951, ECO:0000269|PubMed:7870076, ECO:0000269|PubMed:7881433, ECO:0000269|PubMed:7887412, ECO:0000269|PubMed:7951252, ECO:0000269|PubMed:7980516, ECO:0000269|PubMed:7997024, ECO:0000269|PubMed:8069312, ECO:0000269|PubMed:8179602, ECO:0000269|PubMed:8351519, ECO:0000269|PubMed:8446170, ECO:0000269|PubMed:8528216, ECO:0000269|PubMed:8682505, ECO:0000269|PubMed:8875253, ECO:0000269|PubMed:8907321, ECO:0000269|PubMed:8938700, ECO:0000269|PubMed:8990014, ECO:0000269|PubMed:9101297, ECO:0000269|PubMed:9131652, ECO:0000269|PubMed:9365366, ECO:0000269|PubMed:9455977, ECO:0000269|PubMed:9541385, ECO:0000269|PubMed:9696308, ECO:0000269|PubMed:9706719, ECO:0000269|Ref.86}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Spastic tetraplegia and axial hypotonia, progressive (STAHP) [MIM:618598]: An autosomal recessive, neurologic disorder characterized by loss of motor abilities in the first year of life, after which severe, progressive spastic tetraparesis develops. Affected individuals have severe axial hypotonia, hyperekplexia, hypertonia, and myokymia, reflecting upper motor neuron involvement. Cognitive development may be affected. {ECO:0000269|PubMed:31314961, ECO:0000269|PubMed:31332433}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
1.15.1.1
uniprot
proteins
ec_number
1.8.-.-
uniprot
proteins
function
FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems (PubMed:18948262, 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). {ECO:0000269|PubMed:18948262, ECO:0000269|PubMed:24140062, ECO:0000269|PubMed:36630448}.
uniprot
proteins
mass_dalton
15936
uniprot
proteins
mutagenesis
MUTAGEN 7; /note="C->S: No palmitoylation, reduced nuclear targeting. Enhances formation of fibrillar aggregates in the absence of bound zinc; when associated with S-58; S-112 and S-147."; /evidence="ECO:0000269|PubMed:17070542, ECO:0000269|PubMed:18552350, ECO:0000269|PubMed:22496122"; MUTAGEN 51..52; /note="FG->EE: Abolishes dimerization; when associated with Q-134."; /evidence="ECO:0000269|PubMed:10329151, ECO:0000269|PubMed:18552350"; MUTAGEN 58; /note="C->A: Exhibits very slow copper acquisition."; /evidence="ECO:0000269|PubMed:17070542, ECO:0000269|PubMed:18552350, ECO:0000269|PubMed:23625804"; MUTAGEN 58; /note="C->S: Enhances formation of fibrillar aggregates in the absence of bound zinc; when associated with S-7; S-112 and S-147."; /evidence="ECO:0000269|PubMed:17070542, ECO:0000269|PubMed:18552350, ECO:0000269|PubMed:23625804"; MUTAGEN 81; /note="H->A: Loss of zinc binding and enhanced tendency to form aggregates; when associated with A-84."; /evidence="ECO:0000269|PubMed:17888947, ECO:0000269|PubMed:18552350"; MUTAGEN 81; /note="H->S: Destabilization of dimer and loss of zinc binding; when associated with S-84."; /evidence="ECO:0000269|PubMed:17888947, ECO:0000269|PubMed:18552350"; MUTAGEN 84; /note="D->A: Loss of zinc binding and enhanced tendency to form aggregates; when associated with A-81."; /evidence="ECO:0000269|PubMed:17888947, ECO:0000269|PubMed:18552350"; MUTAGEN 84; /note="D->S: Destabilization of dimer and loss of zinc binding; when associated with S-81."; /evidence="ECO:0000269|PubMed:17888947, ECO:0000269|PubMed:18552350"; MUTAGEN 112; /note="C->S: Enhances formation of fibrillar aggregates in the absence of bound zinc; when associated with S-7; S-58 and S-147."; /evidence="ECO:0000269|PubMed:17070542, ECO:0000269|PubMed:18552350"; MUTAGEN 123; /note="K->A: Decreased succinylation."; /evidence="ECO:0000269|PubMed:24140062"; MUTAGEN 123; /note="K->E: Mimicks constitutive succinylation state; decreased activity."; /evidence="ECO:0000269|PubMed:24140062"; MUTAGEN 134; /note="E->Q: Abolishes dimerization; when associated with E-50 and E-51."; /evidence="ECO:0000269|PubMed:10329151"; MUTAGEN 147; /note="C->A: Exhibits very slow copper acquisition."; /evidence="ECO:0000269|PubMed:17070542, ECO:0000269|PubMed:18552350, ECO:0000269|PubMed:23625804"; MUTAGEN 147; /note="C->S: Enhances formation of fibrillar aggregates in the absence of bound zinc; when associated with S-7; S-58 and S-112."; /evidence="ECO:0000269|PubMed:17070542, ECO:0000269|PubMed:18552350, ECO:0000269|PubMed:23625804
uniprot
proteins
post_translational_modification
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. {ECO:0000269|PubMed:12145308, ECO:0000269|PubMed:19741096}.; 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. {ECO:0000269|PubMed:20600836}.; PTM: Palmitoylation helps nuclear targeting and decreases catalytic activity. {ECO:0000269|PubMed:22496122}.; PTM: Succinylation, adjacent to copper catalytic site, probably inhibits activity. Desuccinylation by SIRT5 enhances activity. {ECO:0000269|PubMed:24140062}.
uniprot
proteins
protein_family
Cu-Zn superoxide dismutase family
uniprot
proteins
pubmed
10329151
uniprot
proteins
pubmed
10400992
uniprot
proteins
pubmed
10430435
uniprot
proteins
pubmed
10732812
uniprot
proteins
pubmed
10830953
uniprot
proteins
pubmed
11369193
uniprot
proteins
pubmed
11535232
uniprot
proteins
pubmed
12145308
uniprot
proteins
pubmed
12210393
uniprot
proteins
pubmed
12402272
uniprot
proteins
pubmed
12754496
uniprot
proteins
pubmed
12911296
uniprot
proteins
pubmed
12963370
uniprot
proteins
pubmed
14506936
uniprot
proteins
pubmed
1463506
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15056757
uniprot
proteins
pubmed
15326189
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16291742
uniprot
proteins
pubmed
16406071
uniprot
proteins
pubmed
17070542
uniprot
proteins
pubmed
17548825
uniprot
proteins
pubmed
17888947
uniprot
proteins
pubmed
18301754
uniprot
proteins
pubmed
18378676
uniprot
proteins
pubmed
18552350
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18948262
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19741096
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20460594
uniprot
proteins
pubmed
20600836
uniprot
proteins
pubmed
20727846
uniprot
proteins
pubmed
21220647
uniprot
proteins
pubmed
21247266
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22496122
uniprot
proteins
pubmed
22905912
uniprot
proteins
pubmed
23625804
uniprot
proteins
pubmed
24140062
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24283821
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
27604643
uniprot
proteins
pubmed
2853161
uniprot
proteins
pubmed
30037290
uniprot
proteins
pubmed
31086828
uniprot
proteins
pubmed
31292775
uniprot
proteins
pubmed
31314961
uniprot
proteins
pubmed
31332433
uniprot
proteins
pubmed
3160582
uniprot
proteins
pubmed
36630448
uniprot
proteins
pubmed
3889846
uniprot
proteins
pubmed
6577438
uniprot
proteins
pubmed
6770891
uniprot
proteins
pubmed
7002610
uniprot
proteins
pubmed
7496169
uniprot
proteins
pubmed
7501156
uniprot
proteins
pubmed
7647793
uniprot
proteins
pubmed
7655468
uniprot
proteins
pubmed
7655469
uniprot
proteins
pubmed
7655471
uniprot
proteins
pubmed
7700376
uniprot
proteins
pubmed
7795609
uniprot
proteins
pubmed
7836951
uniprot
proteins
pubmed
7870076
uniprot
proteins
pubmed
7881433
uniprot
proteins
pubmed
7887412
uniprot
proteins
pubmed
7951252
uniprot
proteins
pubmed
7980516
uniprot
proteins
pubmed
7997024
uniprot
proteins
pubmed
8069312
uniprot
proteins
pubmed
8179602
uniprot
proteins
pubmed
8332197
uniprot
proteins
pubmed
8351519
uniprot
proteins
pubmed
8446170
uniprot
proteins
pubmed
8528216
uniprot
proteins
pubmed
8592323
uniprot
proteins
pubmed
8682505
uniprot
proteins
pubmed
8875253
uniprot
proteins
pubmed
8907321
uniprot
proteins
pubmed
8938700
uniprot
proteins
pubmed
8990014
uniprot
proteins
pubmed
9101297
uniprot
proteins
pubmed
9131652
uniprot
proteins
pubmed
9365366
uniprot
proteins
pubmed
9455977
uniprot
proteins
pubmed
9541385
uniprot
proteins
pubmed
9696308
uniprot
proteins
pubmed
9706719
uniprot
proteins
pubmed
9718300
uniprot
proteins
sequence_length
154
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19741096}. Nucleus {ECO:0000269|PubMed:22496122}. Note=Predominantly cytoplasmic; the pathogenic variants ALS1 Arg-86 and Ala-94 gradually aggregates and accumulates in mitochondria. {ECO:0000269|PubMed:19741096}.
uniprot
proteins