SOD1 information

SOD1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1AZV, 1BA9, 1DSW, 1FUN, 1HL4, 1HL5, 1KMG, 1L3N, 1MFM, 1N18, 1N19, 1OEZ, 1OZT, 1OZU, 1P1V, 1PTZ, 1PU0, 1RK7, 1SOS, 1SPD, 1UXL, 1UXM, 2AF2, 2C9S, 2C9U, 2C9V, 2GBT, 2GBU, 2GBV, 2LU5, 2MP3, 2NNX, 2R27, 2V0A, 2VR6, 2VR7, 2VR8, 2WKO, 2WYT, 2WYZ, 2WZ0, 2WZ5, 2WZ6, 2XJK, 2XJL, 2ZKW, 2ZKX, 2ZKY, 3CQP, 3CQQ, 3ECU, 3ECV, 3ECW, 3GQF, 3GTV, 3GZO, 3GZP, 3GZQ, 3H2P, 3H2Q, 3HFF, 3K91, 3KH3, 3KH4, 3LTV, 3QQD, 3RE0, 3T5W, 4A7G, 4A7Q, 4A7S, 4A7T, 4A7U, 4A7V, 4B3E, 4BCY, 4BCZ, 4BD4, 4FF9, 4MCM, 4MCN, 4NIN, 4NIP, 4OH2, 4XCR
Identifiers
Aliases	SOD1, ALS, ALS1, HEL-S-44, IPOA, SOD, hSod1, homodimer, superoxide dismutase 1, soluble, superoxide dismutase 1, STAHP
External IDs	OMIM: 147450 MGI: 98351 HomoloGene: 392 GeneCards: SOD1
Gene location (Human)
Chr.	Chromosome 21 (human)
End	31,668,931 bp
Gene location (Mouse)
Chr.	Chromosome 16 (mouse)
End	90,023,217 bp
RNA expression pattern
	Top expressed in
	pons; ; spinal ganglia; ; superior vestibular nucleus; ; right lobe of liver; ; Brodmann area 10; ; hypothalamus; ; frontal pole; ; dorsolateral prefrontal cortex; ; Brodmann area 9; ; renal medulla;
	Top expressed in
	otolith organ; ; utricle; ; Paneth cell; ; cumulus cell; ; fossa; ; facial motor nucleus; ; condyle; ; retinal pigment epithelium; ; semi-lunar valve; ; ascending aorta;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	metal ion binding; enzyme binding; oxidoreductase activity; superoxide dismutase activity; protein homodimerization activity; zinc ion binding; protein binding; copper ion binding; protein phosphatase 2B binding; chaperone binding; antioxidant activity; identical protein binding; superoxide dismutase copper chaperone activity;
Cellular component	cytoplasm; cytosol; mitochondrial intermembrane space; extracellular region; mitochondrion; neuron projection; dendrite cytoplasm; dense core granule; nucleus; myelin sheath; peroxisome; lysosome; extracellular exosome; extracellular matrix; plasma membrane; secretory granule; nucleoplasm; neuronal cell body; mitochondrial matrix; cytoplasmic vesicle; axon cytoplasm; extracellular space; protein-containing complex;
Biological process	negative regulation of neuron apoptotic process; muscle cell cellular homeostasis; response to copper ion; placenta development; response to amphetamine; positive regulation of catalytic activity; response to heat; response to organic substance; anterograde axonal transport; spermatogenesis; response to ethanol; neurofilament cytoskeleton organization; heart contraction; embryo implantation; locomotory behavior; thymus development; removal of superoxide radicals; regulation of GTPase activity; transmission of nerve impulse; response to antibiotic; myeloid cell homeostasis; response to oxidative stress; reactive oxygen species metabolic process; regulation of T cell differentiation in thymus; retina homeostasis; response to nutrient levels; hydrogen peroxide biosynthetic process; regulation of protein kinase activity; negative regulation of cholesterol biosynthetic process; cellular response to potassium ion; retrograde axonal transport; glutathione metabolic process; response to antipsychotic drug; negative regulation of apoptotic process; cellular response to cadmium ion; response to carbon monoxide; regulation of blood pressure; response to axon injury; relaxation of vascular associated smooth muscle; ovarian follicle development; cellular response to ATP; response to hydrogen peroxide; superoxide metabolic process; peripheral nervous system myelin maintenance; response to superoxide; positive regulation of cytokine production; regulation of multicellular organism growth; human ageing; platelet degranulation; sensory perception of sound; superoxide anion generation; auditory receptor cell stereocilium organization; regulation of mitochondrial membrane potential; positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; positive regulation of apoptotic process; positive regulation of superoxide anion generation; regulation of organ growth; cellular iron ion homeostasis; response to reactive oxygen species; cellular response to oxidative stress; interleukin-12-mediated signaling pathway; negative regulation of inflammatory response; positive regulation of phagocytosis;
	Sources:Amigo / QuickGO
Orthologs
	6647
	20655
	ENSG00000142168
	ENSMUSG00000022982
	P00441
	P08228
	NM_000454
	NM_011434
	NP_000445
	NP_035564
	Wikidata
View/Edit Human	View/Edit Mouse

Superoxide dismutase [Cu-Zn] also known as superoxide dismutase 1 or hSod1 is an enzyme that in humans is encoded by the SOD1 gene, located on chromosome 21. SOD1 is one of three human superoxide dismutases.^[5]^[6] It is implicated in apoptosis, familial amyotrophic lateral sclerosis and Parkinson's disease.^[6]^[7]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000142168 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000022982 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Milani P, Gagliardi S, Cova E, Cereda C (2011). "SOD1 Transcriptional and Posttranscriptional Regulation and Its Potential Implications in ALS". Neurology Research International. 2011: 458427. doi:10.1155/2011/458427. PMC 3096450. PMID 21603028.
^ ^a ^b Rosen DR, Siddique T, Patterson D, Figlewicz DA, Sapp P, Hentati A, et al. (March 1993). "Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis". Nature. 362 (6415): 59–62. Bibcode:1993Natur.362...59R. doi:10.1038/362059a0. PMID 8446170. S2CID 265436.
^ Trist BG, Hilton JB, Hare DJ, Crouch PJ, Double KL (April 2021). "Superoxide Dismutase 1 in Health and Disease: How a Frontline Antioxidant Becomes Neurotoxic". Angewandte Chemie. 60 (17): 9215–9246. doi:10.1002/anie.202000451. PMC 8247289. PMID 32144830.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000142168 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000022982 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid21603028-5] Milani P, Gagliardi S, Cova E, Cereda C (2011). "SOD1 Transcriptional and Posttranscriptional Regulation and Its Potential Implications in ALS". Neurology Research International. 2011: 458427. doi:10.1155/2011/458427. PMC 3096450. PMID 21603028.

[pmid8446170-6] Rosen DR, Siddique T, Patterson D, Figlewicz DA, Sapp P, Hentati A, et al. (March 1993). "Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis". Nature. 362 (6415): 59–62. Bibcode:1993Natur.362...59R. doi:10.1038/362059a0. PMID 8446170. S2CID 265436.

[7] Trist BG, Hilton JB, Hare DJ, Crouch PJ, Double KL (April 2021). "Superoxide Dismutase 1 in Health and Disease: How a Frontline Antioxidant Becomes Neurotoxic". Angewandte Chemie. 60 (17): 9215–9246. doi:10.1002/anie.202000451. PMC 8247289. PMID 32144830.

SOD1 information

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