SOD1 | ENSG00000142168 | NCBI 6647

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Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

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Other Information

This section provides additional information about the gene, including a description generated by an AI language model and details about associated proteins.

Description
Proteins

## Summary [SOD1](/details-gene/6647), or Superoxide Dismutase 1, is a well-characterized metalloenzyme that plays a critical role in cellular defense against oxidative stress. It functions as a homodimer, catalyzing the dismutation of superoxide radicals into molecular oxygen and hydrogen peroxide. This activity is fundamental to protecting cells from damage induced by reactive oxygen species (ROS). The gene is broadly expressed across a diverse array of cell types, but shows particularly high significance in cells with high metabolic activity or those forming environmental barriers, such as [ciliated epithelial cell](/details-cell/CL0000067) and various progenitor populations like the [hematopoietic stem cell](/details-cell/CL0000037). Clinically, mutations in the [SOD1](/details-gene/6647) gene are strongly associated with familial Amyotrophic Lateral Sclerosis (ALS), as noted in OMIM ([147450](https://omim.org/entry/147450)), where a toxic gain-of-function is implicated in motor neuron degeneration. ## Cellular Roles and Expression Landscape **Overall**, the expression profile of [SOD1](/details-gene/6647) highlights its essential role in cellular homeostasis across multiple lineages, with particular prominence in epithelial, progenitor, and secretory cells. The highest significance scores are observed in [ciliated epithelial cell](/details-cell/CL0000067) (CSI: 112.83) and [multi-ciliated epithelial cell](/details-cell/CL0005012) (CSI: 97.24), suggesting a vital function in protecting the respiratory and reproductive tracts from oxidative damage. Its importance is further underscored in highly proliferative and undifferentiated populations, including [hematopoietic stem cell](/details-cell/CL0000037) (CSI: 93.94), [megakaryocyte-erythroid progenitor cell](/details-cell/CL0000050) (CSI: 93.64), and [stem cell](/details-cell/CL0000034) (CSI: 81.82), where mitigating ROS-induced DNA damage is critical for maintaining genomic integrity and long-term viability. Specialized secretory cells, such as [pancreatic A cell](/details-cell/CL0000171) and [fallopian tube secretory epithelial cell](/details-cell/CL4030006), also show high [SOD1](/details-gene/6647) significance, consistent with the high metabolic demands of hormone and protein production. Conversely, [SOD1](/details-gene/6647) displays significantly lower importance in several mature, terminally differentiated cell types. Notably, it is an anti-marker for [alpha-beta T cell](/details-cell/CL0000789) (CSI: -60.65), suggesting that other antioxidant systems may be more dominant in this lymphocyte lineage. Its reduced significance in various endothelial cells, astrocytes ([mature astrocyte](/details-cell/CL0002627)), and specific neuronal subtypes ([serotonergic neuron](/details-cell/CL0000850)) indicates a specialized, rather than uniformly high, role within the circulatory and central nervous systems. This pattern suggests that while [SOD1](/details-gene/6647) provides a fundamental protective function, its relative importance varies substantially depending on the specific metabolic and signaling context of the cell. ## Pathways and Molecular Function The functional annotations for [SOD1](/details-gene/6647) confirm its primary role in antioxidant defense. The gene product is directly involved in the [Removal of superoxide radicals](/details-go/GO:0019430) and the broader [Reactive oxygen species metabolic process](/details-go/GO:0072593), as part of the Reactome pathway for [Detoxification of reactive oxygen species](/details-pathway/R-HSA-3299685). Its core molecular function is [Superoxide dismutase activity](/details-go/GO:0004784), which is dependent on both [Copper ion binding](/details-go/GO:0005507) and [Zinc ion binding](/details-go/GO:0008270). The enzyme is localized to multiple cellular compartments, including the [Cytosol](/details-go/GO:0005829), [Mitochondrion](/details-go/GO:0005739), and [Nucleus](/details-go/GO:0005634), and is also found in the [Extracellular exosome](/details-go/GO:0070062), allowing it to counteract oxidative stress in diverse subcellular environments. Beyond its canonical role, [SOD1](/details-gene/6647) is implicated in a wide range of cellular processes. It participates in the regulation of the [Apoptotic process](/details-go/GO:0006915), both positively and negatively, and plays a role in [Cellular responses to stress](/details-pathway/R-HSA-2262752). Its involvement in neuronal function is extensive, with annotations for [Anterograde axonal transport](/details-go/GO:0008089), [Retrograde axonal transport](/details-go/GO:0008090), and [Negative regulation of neuron apoptotic process](/details-go/GO:0043524). Furthermore, [SOD1](/details-gene/6647) is connected to the [Immune system](/details-pathway/R-HSA-168256) through pathways such as [Cytokine signaling in immune system](/details-pathway/R-HSA-1280215) and regulation of the [inflammatory response](/details-go/GO:0050728). This functional breadth aligns with its widespread, albeit context-dependent, expression and suggests it acts as a key node integrating cellular metabolism, stress response, and survival signaling. ## Research Directions The widespread expression of [SOD1](/details-gene/6647) coupled with its specific clinical relevance in ALS presents several avenues for future research. The data suggest its role is not merely housekeeping but is finely tuned to the needs of specific cell types. **Proposed Hypotheses:** 1. **Ciliary Protection:** Given its extremely high significance in [ciliated epithelial cell](/details-cell/CL0000067), [SOD1](/details-gene/6647) may be indispensable for protecting the motile cilia apparatus from oxidative damage. We hypothesize that localized [SOD1](/details-gene/6647) activity is critical for maintaining ciliary beat frequency and mucociliary clearance in the respiratory tract, and its dysfunction could contribute to chronic respiratory diseases. 2. **Stem Cell Quiescence and Longevity:** The high CSI values in [hematopoietic stem cell](/details-cell/CL0000037) and other progenitors suggest a crucial role in maintaining the integrity of these long-lived populations. We hypothesize that [SOD1](/details-gene/6647) is a key regulator of the cellular redox state that preserves stem cell quiescence and prevents premature exhaustion, with age-related declines in its function contributing to hematopoietic decline. 3. **Motor Neuron-Specific Vulnerability in ALS:** Although broadly expressed, the toxic gain-of-function from [SOD1](/details-gene/6647) mutations selectively affects motor neurons. We hypothesize that motor neurons possess a unique metabolic profile or a distinct protein-protein interaction network for [SOD1](/details-gene/6647) that makes them uniquely vulnerable to the conformational instability and aggregation of mutant [SOD1](/details-gene/6647) protein, a vulnerability not present in other high-expressing cells like keratinocytes. **Experimental Approach:** To test the hypothesis regarding its role in ciliary protection (Hypothesis 1), an effective approach would be to use an air-liquid interface (ALI) culture model of primary human bronchial epithelial cells, which differentiates to form a mucociliary layer. [SOD1](/details-gene/6647) expression could be specifically knocked down using lentiviral-delivered shRNA. The impact on ciliary function would be assessed by measuring cilia beat frequency (CBF) using high-speed video microscopy and quantifying mucociliary transport velocity via particle tracking. These experiments should be conducted under both basal conditions and following exposure to an oxidative stressor, such as cigarette smoke extract or H2O2, to determine if [SOD1](/details-gene/6647) is essential for maintaining ciliary resilience. **Therapeutic Potential:** The therapeutic potential of targeting [SOD1](/details-gene/6647) is most advanced in the context of ALS. Because the disease is caused by a toxic gain-of-function of the mutant protein [Link](https://doi.org/10.1093/hmg/4.7.1239), the primary therapeutic strategy is **inhibition** or reduction of [SOD1](/details-gene/6647) protein levels. This is the opposite of what might be expected for an antioxidant enzyme. Due to its ubiquitous expression, systemic inhibition of wild-type [SOD1](/details-gene/6647) would be deleterious. Therefore, strategies focus on specifically reducing the expression of the mutant allele or clearing the toxic protein aggregates. Antisense oligonucleotides (ASOs) that target [SOD1](/details-gene/6647) mRNA for degradation have shown significant promise in this area, representing a highly targeted therapeutic approach for patients with [SOD1](/details-gene/6647)-mediated familial ALS.

Disclaimer: This in-silico analysis is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

Superoxide dismutase 1

Genular Protein ID: 2065238907

Symbol: SODC_HUMAN

Name: Superoxide dismutase 1

UniProtKB Accession Codes:

P00441 A6NHJ0 D3DSE4 Q16669 Q16711 Q16838 Q16839 Q16840 Q6NR85

Database IDs:

Citations:

PubMed ID: 6577438

Title: Nucleotide sequence and expression of human chromosome 21-encoded superoxide dismutase mRNA.

PubMed ID: 6577438

DOI: 10.1073/pnas.80.18.5465

PubMed ID: 3160582

Title: Architecture and anatomy of the chromosomal locus in human chromosome 21 encoding the Cu/Zn superoxide dismutase.

PubMed ID: 3160582

DOI: 10.1002/j.1460-2075.1985.tb02320.x

PubMed ID: 3889846

Title: Human Cu/Zn superoxide dismutase cDNA: isolation of clones synthesising high levels of active or inactive enzyme from an expression library.

PubMed ID: 3889846

DOI: 10.1093/nar/13.6.2017

PubMed ID: 2853161

Title: Comparison of properties between human recombinant and placental copper-zinc SOD.

PubMed ID: 2853161

DOI: 10.1093/oxfordjournals.jbchem.a122562

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 10830953

Title: The DNA sequence of human chromosome 21.

PubMed ID: 10830953

DOI: 10.1038/35012518

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 6770891

Title: Some sulfhydryl properties and primary structure of human erythrocyte superoxide dismutase.

PubMed ID: 6770891

DOI: 10.1021/bi00552a005

PubMed ID: 7002610

Title: The complete amino acid sequence of human Cu/Zn superoxide dismutase.

PubMed ID: 7002610

DOI: 10.1016/0014-5793(80)81044-1

PubMed ID: 8528216

Title: Two novel mutations in the gene for copper zinc superoxide dismutase in UK families with amyotrophic lateral sclerosis.

PubMed ID: 8528216

DOI: 10.1093/hmg/4.7.1239

PubMed ID: 8682505

Title: Superoxide dismutase 1: identification of a novel mutation in a case of familial amyotrophic lateral sclerosis.

PubMed ID: 8682505

DOI: 10.1007/s004390050157

PubMed ID: 15326189

Title: The unusually stable quaternary structure of human Cu,Zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide status.

PubMed ID: 15326189

DOI: 10.1074/jbc.m406021200

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20600836

Title: A ditryptophan cross-link is responsible for the covalent dimerization of human superoxide dismutase 1 during its bicarbonate-dependent peroxidase activity.

PubMed ID: 20600836

DOI: 10.1016/j.freeradbiomed.2010.06.018

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 22496122

Title: Endothelial cell palmitoylproteomic identifies novel lipid-modified targets and potential substrates for protein acyl transferases.

PubMed ID: 22496122

DOI: 10.1161/circresaha.112.269514

PubMed ID: 22905912

Title: Resveratrol-induced changes of the human adipocyte secretion profile.

PubMed ID: 22905912

DOI: 10.1021/pr300539b

PubMed ID: 24140062

Title: SIRT5 desuccinylates and activates SOD1 to eliminate ROS.

PubMed ID: 24140062

DOI: 10.1016/j.bbrc.2013.10.033

PubMed ID: 23625804

Title: Mechanistic aspects of hSOD1 maturation from the solution structure of Cu(I) -loaded hCCS domain 1 and analysis of disulfide-free hSOD1 mutants.

PubMed ID: 23625804

DOI: 10.1002/cbic.201300042

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 30037290

Title: pLG72 induces superoxide radicals via interaction and aggregation with SOD1.

PubMed ID: 30037290

DOI: 10.1080/10715762.2018.1504293

PubMed ID: 31292775

Title: Copper-zinc superoxide dismutase (Sod1) activation terminates interaction between its copper chaperone (Ccs) and the cytosolic metal-binding domain of the copper importer Ctr1.

PubMed ID: 31292775

DOI: 10.1007/s10534-019-00206-3

PubMed ID: 31332433

Title: SOD1 deficiency: a novel syndrome distinct from amyotrophic lateral sclerosis.

PubMed ID: 31332433

DOI: 10.1093/brain/awz182

PubMed ID: 31314961

Title: Phenotype in an Infant with SOD1 Homozygous Truncating Mutation.

PubMed ID: 31314961

DOI: 10.1056/nejmc1905039

PubMed ID: 1463506

Title: Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase.

PubMed ID: 1463506

DOI: 10.1073/pnas.89.13.6109

PubMed ID: 9541385

Title: Subunit asymmetry in the three-dimensional structure of a human CuZnSOD mutant found in familial amyotrophic lateral sclerosis.

PubMed ID: 9541385

DOI: 10.1002/pro.5560070302

PubMed ID: 9718300

Title: Solution structure of reduced monomeric Q133M2 copper, zinc superoxide dismutase (SOD). Why is SOD a dimeric enzyme?

PubMed ID: 9718300

DOI: 10.1021/bi9803473

PubMed ID: 10329151

Title: The crystal structure of the monomeric human SOD mutant F50E/G51E/E133Q at atomic resolution. The enzyme mechanism revisited.

PubMed ID: 10329151

DOI: 10.1006/jmbi.1999.2681

PubMed ID: 12911296

Title: Solution structure of Apo Cu,Zn superoxide dismutase: role of metal ions in protein folding.

PubMed ID: 12911296

DOI: 10.1021/bi034324m

PubMed ID: 12963370

Title: ALS mutants of human superoxide dismutase form fibrous aggregates via framework destabilization.

PubMed ID: 12963370

DOI: 10.1016/s0022-2836(03)00889-1

PubMed ID: 12754496

Title: Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS.

PubMed ID: 12754496

DOI: 10.1038/nsb935

PubMed ID: 15056757

Title: Dimer destabilization in superoxide dismutase may result in disease-causing properties: structures of motor neuron disease mutants.

PubMed ID: 15056757

DOI: 10.1073/pnas.0305143101

PubMed ID: 16291742

Title: Human SOD1 before harboring the catalytic metal: solution structure of copper-depleted, disulfide-reduced form.

PubMed ID: 16291742

DOI: 10.1074/jbc.m506497200

PubMed ID: 16406071

Title: Variable metallation of human superoxide dismutase: atomic resolution crystal structures of Cu-Zn, Zn-Zn and as-isolated wild-type enzymes.

PubMed ID: 16406071

DOI: 10.1016/j.jmb.2005.11.081

PubMed ID: 17070542

Title: The coupling between disulphide status, metallation and dimer interface strength in Cu/Zn superoxide dismutase.

PubMed ID: 17070542

DOI: 10.1016/j.jmb.2006.09.048

PubMed ID: 17888947

Title: Structural characterization of zinc-deficient human superoxide dismutase and implications for ALS.

PubMed ID: 17888947

DOI: 10.1016/j.jmb.2007.07.043

PubMed ID: 17548825

Title: Molecular dynamics using atomic-resolution structure reveal structural fluctuations that may lead to polymerization of human Cu-Zn superoxide dismutase.

PubMed ID: 17548825

DOI: 10.1073/pnas.0703857104

PubMed ID: 18378676

Title: Structures of the G85R variant of SOD1 in familial amyotrophic lateral sclerosis.

PubMed ID: 18378676

DOI: 10.1074/jbc.m801522200

PubMed ID: 8592323

Title: Familial amyotrophic lateral sclerosis/motor neurone disease (FALS): a review of current developments.

PubMed ID: 8592323

DOI: 10.1136/jmg.32.11.841

PubMed ID: 20727846

Title: Structures of mouse SOD1 and human/mouse SOD1 chimeras.

PubMed ID: 20727846

DOI: 10.1016/j.abb.2010.08.014

PubMed ID: 8446170

Title: Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis.

PubMed ID: 8446170

DOI: 10.1038/362059a0

PubMed ID: 8332197

Title:

PubMed ID: 8332197

DOI: 10.1038/364362c0

PubMed ID: 8351519

Title: Amyotrophic lateral sclerosis and structural defects in Cu,Zn superoxide dismutase.

PubMed ID: 8351519

DOI: 10.1126/science.8351519

PubMed ID: 8179602

Title: A novel mutation in Cu/Zn superoxide dismutase gene in Japanese familial amyotrophic lateral sclerosis.

PubMed ID: 8179602

DOI: 10.1006/bbrc.1994.1506

PubMed ID: 7980516

Title: A new variant Cu/Zn superoxide dismutase (Val7-->Glu) deduced from lymphocyte mRNA sequences from Japanese patients with familial amyotrophic lateral sclerosis.

PubMed ID: 7980516

DOI: 10.1006/bbrc.1994.2497

PubMed ID: 8069312

Title: Identification of a novel SOD1 mutation in an apparently sporadic amyotrophic lateral sclerosis patient and the detection of Ile113Thr in three others.

PubMed ID: 8069312

DOI: 10.1093/hmg/3.4.649

PubMed ID: 7951252

Title: Identification of two novel mutations and a new polymorphism in the gene for Cu/Zn superoxide dismutase in patients with amyotrophic lateral sclerosis.

PubMed ID: 7951252

DOI: 10.1093/hmg/3.6.997

PubMed ID: 7881433

Title: Autosomal dominant amyotrophic lateral sclerosis: a novel mutation in the Cu/Zn superoxide dismutase-1 gene.

PubMed ID: 7881433

DOI: 10.1093/hmg/3.12.2261

PubMed ID: 7836951

Title: Familial amyotrophic lateral sclerosis (ALS) in Japan associated with H46R mutation in Cu/Zn superoxide dismutase gene: a possible new subtype of familial ALS.

PubMed ID: 7836951

DOI: 10.1016/0022-510x(94)90097-3

PubMed ID: 7997024

Title: 'Sporadic' motoneuron disease due to familial SOD1 mutation with low penetrance.

PubMed ID: 7997024

DOI: 10.1016/s0140-6736(94)92913-0

PubMed ID: 7870076

Title: Identification of a novel exon 4 SOD1 mutation in a sporadic amyotrophic lateral sclerosis patient.

PubMed ID: 7870076

DOI: 10.1006/mcpr.1994.1046

PubMed ID: 7887412

Title: Identification of new mutations in the Cu/Zn superoxide dismutase gene of patients with familial amyotrophic lateral sclerosis.

PubMed ID: 7887412

PubMed ID: 7795609

Title: A novel point mutation in the Cu/Zn superoxide dismutase gene in a patient with familial amyotrophic lateral sclerosis.

PubMed ID: 7795609

DOI: 10.1093/hmg/4.3.491

PubMed ID: 7655468

Title: An improved protocol for the analysis of SOD1 gene mutations, and a new mutation in exon 4.

PubMed ID: 7655468

DOI: 10.1093/hmg/4.6.1101

PubMed ID: 7655469

Title: The D90A mutation results in a polymorphism of Cu,Zn superoxide dismutase that is prevalent in northern Sweden and Finland.

PubMed ID: 7655469

DOI: 10.1093/hmg/4.6.1105

PubMed ID: 7655471

Title: Two novel SOD1 mutations in patients with familial amyotrophic lateral sclerosis.

PubMed ID: 7655471

DOI: 10.1093/hmg/4.6.1113

PubMed ID: 7700376

Title: A novel SOD mutant and ALS.

PubMed ID: 7700376

DOI: 10.1038/374504a0

PubMed ID: 7647793

Title: Amyotrophic lateral sclerosis associated with homozygosity for an Asp90Ala mutation in CuZn-superoxide dismutase.

PubMed ID: 7647793

DOI: 10.1038/ng0595-61

PubMed ID: 7501156

Title: Variable clinical symptoms in familial amyotrophic lateral sclerosis with a novel point mutation in the Cu/Zn superoxide dismutase gene.

PubMed ID: 7501156

DOI: 10.1212/wnl.45.11.2038

PubMed ID: 7496169

Title: Identification of three novel mutations in the gene for Cu/Zn superoxide dismutase in patients with familial amyotrophic lateral sclerosis.

PubMed ID: 7496169

DOI: 10.1016/0960-8966(95)00007-a

PubMed ID: 8875253

Title: Genetics of amyotrophic lateral sclerosis.

PubMed ID: 8875253

DOI: 10.1093/hmg/5.supplement_1.1465

PubMed ID: 8938700

Title: Three novel mutations and two variants in the gene for Cu/Zn superoxide dismutase in familial amyotrophic lateral sclerosis.

PubMed ID: 8938700

DOI: 10.1016/0960-8966(96)00353-7

PubMed ID: 8907321

Title: A novel two-base mutation in the Cu/Zn superoxide dismutase gene associated with familial amyotrophic lateral sclerosis in Japan.

PubMed ID: 8907321

DOI: 10.1016/0304-3940(96)12378-8

PubMed ID: 9365366

Title: Phenotypic heterogeneity in motor neuron disease patients with CuZn-superoxide dismutase mutations in Scandinavia.

PubMed ID: 9365366

DOI: 10.1093/brain/120.10.1723

PubMed ID: 24283821

Title: A novel mutation of SOD-1 (Gly 108 Val) in familial amyotrophic lateral sclerosis.

PubMed ID: 24283821

DOI: 10.1111/j.1468-1331.1997.tb00298.x

PubMed ID: 8990014

Title: A novel missense point mutation (S134N) of the Cu/Zn superoxide dismutase gene in a patient with familial motor neuron disease.

PubMed ID: 8990014

DOI: 10.1002/(sici)1098-1004(1997)9:1<69::aid-humu14>3.0.co;2-n

PubMed ID: 9101297

Title: Novel G16S (GGC-AGC) mutation in the SOD-1 gene in a patient with apparently sporadic young-onset amyotrophic lateral sclerosis.

PubMed ID: 9101297

DOI: 10.1002/(sici)1098-1004(1997)9:4<356::aid-humu9>3.0.co;2-3

PubMed ID: 9455977

Title: Familial ALS is associated with mutations in all exons of SOD1: a novel mutation in exon 3 (Gly72Ser).

PubMed ID: 9455977

DOI: 10.1016/s0022-510x(97)00181-0

PubMed ID: 10732812

Title: A missense mutation in the SOD1 gene in patients with amyotrophic lateral sclerosis from the Kii Peninsula and its vicinity, Japan.

PubMed ID: 10732812

DOI: 10.1007/s100480050016

PubMed ID: 9131652

Title: A novel SOD1 mutation in an Austrian family with amyotrophic lateral sclerosis.

PubMed ID: 9131652

DOI: 10.1016/s0960-8966(96)00419-1

PubMed ID: 9706719

Title: Identification of six novel SOD1 gene mutations in familial amyotrophic lateral sclerosis.

PubMed ID: 9706719

DOI: 10.1017/s0317167100034004

Title: A novel mutation Asp90Val in the SOD1 gene associated with Japanese familial ALS.

DOI: 10.1046/j.1468-1331.1998.540389.x

PubMed ID: 9696308

Title: Simple and defined method to detect the SOD-1 mutants from patients with familial amyotrophic lateral sclerosis by mass spectrometry.

PubMed ID: 9696308

DOI: 10.1016/s0165-0270(98)00012-0

PubMed ID: 10400992

Title: Variation in the biochemical/biophysical properties of mutant superoxide dismutase 1 enzymes and the rate of disease progression in familial amyotrophic lateral sclerosis kindreds.

PubMed ID: 10400992

DOI: 10.1093/hmg/8.8.1451

PubMed ID: 10430435

Title: A SOD1 gene mutation in a patient with slowly progressing familial ALS.

PubMed ID: 10430435

DOI: 10.1212/wnl.53.2.404

PubMed ID: 11535232

Title: A novel SOD1 gene mutation in familial ALS with low penetrance in females.

PubMed ID: 11535232

DOI: 10.1016/s0022-510x(01)00558-5

PubMed ID: 11369193

Title: Superoxide dismutase gene mutations in Italian patients with familial and sporadic amyotrophic lateral sclerosis: identification of three novel missense mutations.

PubMed ID: 11369193

DOI: 10.1016/s0960-8966(00)00215-7

PubMed ID: 12402272

Title: 'True' sporadic ALS associated with a novel SOD-1 mutation.

PubMed ID: 12402272

DOI: 10.1002/ana.10369

PubMed ID: 12145308

Title: Dorfin ubiquitylates mutant SOD1 and prevents mutant SOD1-mediated neurotoxicity.

PubMed ID: 12145308

DOI: 10.1074/jbc.m206559200

PubMed ID: 12210393

Title: Molecular analysis of the superoxide dismutase 1 gene in Spanish patients with sporadic or familial amyotrophic lateral sclerosis.

PubMed ID: 12210393

DOI: 10.1002/mus.10193

PubMed ID: 14506936

Title: Sixteen novel mutations in the Cu/Zn superoxide dismutase gene in amyotrophic lateral sclerosis: a decade of discoveries, defects and disputes.

PubMed ID: 14506936

DOI: 10.1080/14660820310011700

PubMed ID: 18552350

Title: Complete loss of post-translational modifications triggers fibrillar aggregation of SOD1 in the familial form of amyotrophic lateral sclerosis.

PubMed ID: 18552350

DOI: 10.1074/jbc.m802083200

PubMed ID: 18301754

Title: SOD1 and amyotrophic lateral sclerosis: mutations and oligomerization.

PubMed ID: 18301754

DOI: 10.1371/journal.pone.0001677

PubMed ID: 19741096

Title: Mitochondrial ubiquitin ligase MITOL ubiquitinates mutant SOD1 and attenuates mutant SOD1-induced reactive oxygen species generation.

PubMed ID: 19741096

DOI: 10.1091/mbc.e09-02-0112

PubMed ID: 20460594

Title: Four familial ALS pedigrees discordant for two SOD1 mutations: are all SOD1 mutations pathogenic?

PubMed ID: 20460594

DOI: 10.1136/jnnp.2009.192310

PubMed ID: 21247266

Title: A novel L67P SOD1 mutation in an Italian ALS patient.

PubMed ID: 21247266

DOI: 10.3109/17482968.2011.551939

PubMed ID: 21220647

Title: Large proportion of amyotrophic lateral sclerosis cases in Sardinia due to a single founder mutation of the TARDBP gene.

PubMed ID: 21220647

DOI: 10.1001/archneurol.2010.352

PubMed ID: 27604643

Title: Screening of SOD1, FUS and TARDBP genes in patients with amyotrophic lateral sclerosis in central-southern China.

PubMed ID: 27604643

DOI: 10.1038/srep32478

PubMed ID: 31086828

Title: Oligogenic basis of sporadic ALS: The example of SOD1 p.Ala90Val mutation.

PubMed ID: 31086828

DOI: 10.1212/nxg.0000000000000335

Sequence Information:

Length: 154
Mass: 15936
Checksum: 25CA38DA8D564483
Sequence:

MATKAVCVLK GDGPVQGIIN FEQKESNGPV KVWGSIKGLT EGLHGFHVHE FGDNTAGCTS 
AGPHFNPLSR KHGGPKDEER HVGDLGNVTA DKDGVADVSI EDSVISLSGD HCIIGRTLVV 
HEKADDLGKG GNEESTKTGN AGSRLACGVI GIAQ

	Overall overall
	Adrenal gland UBERON0002369
	Alzheimer disease MONDO0004975
	Ascending colon UBERON0001156
	Atherosclerosis MONDO0005311
	Axilla UBERON0009472
	Basal cell carcinoma MONDO0020804
	Bipolar I disorder MONDO0001866
	Blood UBERON0000178
	\|— Blood COVID-19 UBERON0000178_MONDO0100096
	\|— Blood Cytomegalovirus infection UBERON0000178_MONDO0005132
	\|— Blood Healthy UBERON0000178_PATO0000461
	Body of stomach UBERON0001161
	Bone marrow UBERON0002371
	\|— Bone marrow Healthy UBERON0002371_PATO0000461
	Brain UBERON0000955
	\|— Brain Healthy UBERON0000955_PATO0000461
	Breast UBERON0000310
	\|— Breast Healthy UBERON0000310_PATO0000461
	\|— Breast cancer MONDO0007254
	Bronchus UBERON0002185
	Caecum UBERON0001153
	\|— Caecum Healthy UBERON0001153_PATO0000461
	Caudate lobe of liver UBERON0001117
	Cerebellum UBERON0002037
	\|— Cerebellum Healthy UBERON0002037_PATO0000461
	Cerebral cortex UBERON0000956
	\|— Cerebral cortex Healthy UBERON0000956_PATO0000461
	Cerebrospinal fluid UBERON0001359
	Choroid plexus UBERON0001886
	Chronic kidney disease MONDO0005300
	Colon UBERON0001155
	\|— Colon Healthy UBERON0001155_PATO0000461
	\|— Colonic epithelium UBERON0000397
	\|— Colonic epithelium Healthy UBERON0000397_PATO0000461
	Colorectal cancer MONDO0005575
	Colorectum UBERON0012652
	Cortex of kidney UBERON0001225
	\|— Cortex of kidney Healthy UBERON0001225_PATO0000461
	COVID-19 MONDO0100096
	Crohn disease MONDO0005011
	Cytomegalovirus infection MONDO0005132
	Dementia MONDO0001627
	Dental pulp UBERON0001754
	Dorsolateral prefrontal cortex UBERON0009834
	\|— Dorsolateral prefrontal cortex Bipolar I disorder UBERON0009834_MONDO0001866
	\|— Dorsolateral prefrontal cortex Dementia UBERON0009834_MONDO0001627
	\|— Dorsolateral prefrontal cortex Healthy UBERON0009834_PATO0000461
	\|— Dorsolateral prefrontal cortex Schizophrenia UBERON0009834_MONDO0005090
	\|— Dorsolateral prefrontal cortex Vascular dementia UBERON0009834_MONDO0004648
	Duodenum UBERON0002114
	\|— Duodenum Healthy UBERON0002114_PATO0000461
	Fallopian tube UBERON0003889
	Fovea centralis UBERON0001786
	\|— Fovea centralis Healthy UBERON0001786_PATO0000461
	Frontal cortex UBERON0001870
	Glioblastoma MONDO0018177
	Healthy PATO0000461
	Heart left ventricle UBERON0002084
	\|— Heart left ventricle Healthy UBERON0002084_PATO0000461
	Heart right ventricle Healthy UBERON0002080_PATO0000461
	Hippocampal formation UBERON0002421
	\|— Hippocampal formation Healthy UBERON0002421_PATO0000461
	Hypothalamus UBERON0001898
	\|— Hypothalamus Healthy UBERON0001898_PATO0000461
	Ileal epithelium UBERON0008345
	Ileum UBERON0002116
	\|— Ileum Healthy UBERON0002116_PATO0000461
	\|— Ileum lamina propria UBERON8600035
	Interventricular septum UBERON0002094
	Islet of Langerhans UBERON0000006
	Isolated focal cortical dysplasia type II MONDO0011818
	Kidney UBERON0002113
	\|— Kidney Healthy UBERON0002113_PATO0000461
	Lamina propria of small intestine UBERON0001238
	Leukoencephalopathy, diffuse hereditary, with spheroids 1 MONDO0800027
	Liver UBERON0002107
	\|— Liver Breast cancer UBERON0002107_MONDO0007254
	\|— Liver Healthy UBERON0002107_PATO0000461
	Lung UBERON0002048
	\|— Lung Healthy UBERON0002048_PATO0000461
	\|— Lung Renal cell carcinoma UBERON0002048_MONDO0005086
	\|— Lung adenocarcinoma MONDO0005061
	\|— Lung parenchyma UBERON0008946
	Lymph node UBERON0000029
	\|— Lymph node Healthy UBERON0000029_PATO0000461
	\|— Lymph node Metastatic melanoma UBERON0000029_MONDO0005191
	Malignant ovarian serous tumor MONDO0024885
	Medial orbital frontal cortex UBERON0022352
	Mesenteric lymph node UBERON0002509
	\|— Mesenteric lymph node Healthy UBERON0002509_PATO0000461
	Metastatic melanoma MONDO0005191
	Midbrain UBERON0001891
	\|— Midbrain Healthy UBERON0001891_PATO0000461
	Nasopharynx UBERON0001728
	Neocortex UBERON0001950
	\|— Neocortex Healthy UBERON0001950_PATO0000461
	Neuroblastoma MONDO0005072
	Nonpapillary renal cell carcinoma MONDO0007763
	Occipital cortex UBERON0016540
	Ovary UBERON0000992
	\|— Ovary Healthy UBERON0000992_PATO0000461
	Pancreas UBERON0001264
	\|— Pancreas Healthy UBERON0001264_PATO0000461
	Parkinson disease MONDO0005180
	Peripheral region of retina UBERON0013682
	\|— Peripheral region of retina Healthy UBERON0013682_PATO0000461
	Placenta UBERON0001987
	\|— Placenta Healthy UBERON0001987_PATO0000461
	Pleural effusion UBERON0000175
	Pons UBERON0000988
	\|— Pons Healthy UBERON0000988_PATO0000461
	Prefrontal cortex UBERON0000451
	Primary motor cortex UBERON0001384
	Prostate gland UBERON0002367
	Rectum UBERON0001052
	Renal cell carcinoma MONDO0005086
	Renal medulla UBERON0000362
	\|— Renal medulla Healthy UBERON0000362_PATO0000461
	Respiratory airway UBERON0001005
	\|— Respiratory airway COVID-19 UBERON0001005_MONDO0100096
	Retina UBERON0000966
	\|— Retina Healthy UBERON0000966_PATO0000461
	Right atrium auricular region UBERON0006631
	Schizophrenia MONDO0005090
	Sigmoid colon UBERON0001159
	\|— Sigmoid colon Healthy UBERON0001159_PATO0000461
	Skin of body UBERON0002097
	\|— Skin of body Healthy UBERON0002097_PATO0000461
	Small cell lung carcinoma MONDO0008433
	Small intestine UBERON0002108
	\|— Small intestine Healthy UBERON0002108_PATO0000461
	Spleen UBERON0002106
	\|— Spleen Healthy UBERON0002106_PATO0000461
	Stomach UBERON0000945
	\|— Stomach Healthy UBERON0000945_PATO0000461
	Substantia nigra pars compacta UBERON0001965
	Telencephalon UBERON0001893
	\|— Telencephalon Healthy UBERON0001893_PATO0000461
	Thalamic complex UBERON0010225
	\|— Thalamic complex Healthy UBERON0010225_PATO0000461
	Thymus UBERON0002370
	\|— Thymus Healthy UBERON0002370_PATO0000461
	Transverse colon UBERON0001157
	UBERON0005290 UBERON0005290
	\|— UBERON0005290 Healthy UBERON0005290_PATO0000461
	UBERON8440012 UBERON8440012
	\|— UBERON8440012 Healthy UBERON8440012_PATO0000461
	Upper lobe of left lung UBERON0008952
	Vascular dementia MONDO0004648

Details for: SOD1

Cell Significance Landscape

Associated with

Significant Cells

Network Configuration

Legend:

Other Information

Nucleotide sequence and expression of human chromosome 21-encoded superoxide dismutase mRNA. PubMed ID: 6577438

Architecture and anatomy of the chromosomal locus in human chromosome 21 encoding the Cu/Zn superoxide dismutase. PubMed ID: 3160582

Human Cu/Zn superoxide dismutase cDNA: isolation of clones synthesising high levels of active or inactive enzyme from an expression library. PubMed ID: 3889846

Comparison of properties between human recombinant and placental copper-zinc SOD. PubMed ID: 2853161

Complete sequencing and characterization of 21,243 full-length human cDNAs. PubMed ID: 14702039

The DNA sequence of human chromosome 21. PubMed ID: 10830953

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Some sulfhydryl properties and primary structure of human erythrocyte superoxide dismutase. PubMed ID: 6770891

The complete amino acid sequence of human Cu/Zn superoxide dismutase. PubMed ID: 7002610

Two novel mutations in the gene for copper zinc superoxide dismutase in UK families with amyotrophic lateral sclerosis. PubMed ID: 8528216

Superoxide dismutase 1: identification of a novel mutation in a case of familial amyotrophic lateral sclerosis. PubMed ID: 8682505

The unusually stable quaternary structure of human Cu,Zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide status. PubMed ID: 15326189

A quantitative atlas of mitotic phosphorylation. PubMed ID: 18669648

Lysine acetylation targets protein complexes and co-regulates major cellular functions. PubMed ID: 19608861

A ditryptophan cross-link is responsible for the covalent dimerization of human superoxide dismutase 1 during its bicarbonate-dependent peroxidase activity. PubMed ID: 20600836

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PubMed ID: 20068231

Initial characterization of the human central proteome. PubMed ID: 21269460

Endothelial cell palmitoylproteomic identifies novel lipid-modified targets and potential substrates for protein acyl transferases. PubMed ID: 22496122

Resveratrol-induced changes of the human adipocyte secretion profile. PubMed ID: 22905912

SIRT5 desuccinylates and activates SOD1 to eliminate ROS. PubMed ID: 24140062

Mechanistic aspects of hSOD1 maturation from the solution structure of Cu(I) -loaded hCCS domain 1 and analysis of disulfide-free hSOD1 mutants. PubMed ID: 23625804

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

N-terminome analysis of the human mitochondrial proteome. PubMed ID: 25944712

pLG72 induces superoxide radicals via interaction and aggregation with SOD1. PubMed ID: 30037290

Copper-zinc superoxide dismutase (Sod1) activation terminates interaction between its copper chaperone (Ccs) and the cytosolic metal-binding domain of the copper importer Ctr1. PubMed ID: 31292775

SOD1 deficiency: a novel syndrome distinct from amyotrophic lateral sclerosis. PubMed ID: 31332433

Phenotype in an Infant with SOD1 Homozygous Truncating Mutation. PubMed ID: 31314961

Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase. PubMed ID: 1463506

Subunit asymmetry in the three-dimensional structure of a human CuZnSOD mutant found in familial amyotrophic lateral sclerosis. PubMed ID: 9541385

Solution structure of reduced monomeric Q133M2 copper, zinc superoxide dismutase (SOD). Why is SOD a dimeric enzyme? PubMed ID: 9718300

The crystal structure of the monomeric human SOD mutant F50E/G51E/E133Q at atomic resolution. The enzyme mechanism revisited. PubMed ID: 10329151

Solution structure of Apo Cu,Zn superoxide dismutase: role of metal ions in protein folding. PubMed ID: 12911296

ALS mutants of human superoxide dismutase form fibrous aggregates via framework destabilization. PubMed ID: 12963370

Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS. PubMed ID: 12754496

Dimer destabilization in superoxide dismutase may result in disease-causing properties: structures of motor neuron disease mutants. PubMed ID: 15056757

Human SOD1 before harboring the catalytic metal: solution structure of copper-depleted, disulfide-reduced form. PubMed ID: 16291742

Variable metallation of human superoxide dismutase: atomic resolution crystal structures of Cu-Zn, Zn-Zn and as-isolated wild-type enzymes. PubMed ID: 16406071

The coupling between disulphide status, metallation and dimer interface strength in Cu/Zn superoxide dismutase. PubMed ID: 17070542

Structural characterization of zinc-deficient human superoxide dismutase and implications for ALS. PubMed ID: 17888947

Molecular dynamics using atomic-resolution structure reveal structural fluctuations that may lead to polymerization of human Cu-Zn superoxide dismutase. PubMed ID: 17548825

Structures of the G85R variant of SOD1 in familial amyotrophic lateral sclerosis. PubMed ID: 18378676

Familial amyotrophic lateral sclerosis/motor neurone disease (FALS): a review of current developments. PubMed ID: 8592323

Structures of mouse SOD1 and human/mouse SOD1 chimeras. PubMed ID: 20727846

Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. PubMed ID: 8446170