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Entry version 244 (18 Sep 2019)
Sequence version 2 (23 Jan 2007)
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Protein

Superoxide dismutase [Cu-Zn]

Gene

SOD1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Destroys radicals which are normally produced within the cells and which are toxic to biological systems.

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.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi47Copper; catalytic2 Publications1
Metal bindingi49Copper; catalytic2 Publications1
Metal bindingi64Copper; catalytic2 Publications1
Metal bindingi64Zinc; via pros nitrogen1 Publication1
Metal bindingi72Zinc; via pros nitrogen1 Publication1
Metal bindingi81Zinc; via pros nitrogen1 Publication1
Metal bindingi84Zinc; structural1 Publication1
Metal bindingi121Copper; catalytic2 Publications1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAntioxidant, Oxidoreductase
LigandCopper, Metal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
MetaCyc:HS06899-MONOMER

BRENDA Comprehensive Enzyme Information System

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BRENDAi
1.15.1.1 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-114608 Platelet degranulation
R-HSA-3299685 Detoxification of Reactive Oxygen Species
R-HSA-8950505 Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation

SIGNOR Signaling Network Open Resource

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SIGNORi
P00441

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Superoxide dismutase [Cu-Zn] (EC:1.15.1.1)
Alternative name(s):
Superoxide dismutase 1
Short name:
hSod1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:SOD1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 21

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:11179 SOD1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
147450 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P00441

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Amyotrophic lateral sclerosis 1 (ALS1)46 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_0135185A → S in ALS1. 1
Natural variantiVAR_0071305A → T in ALS1. 1 PublicationCorresponds to variant dbSNP:rs121912444EnsemblClinVar.1
Natural variantiVAR_0071315A → V in ALS1; severe form; reduces structural stability and enzyme activity; increases tendency to form fibrillar aggregates. 3 PublicationsCorresponds to variant dbSNP:rs121912442EnsemblClinVar.1
Natural variantiVAR_0087177C → F in ALS1. 1 PublicationCorresponds to variant dbSNP:rs121912448EnsemblClinVar.1
Natural variantiVAR_0071328V → E in ALS1. 1 Publication1
Natural variantiVAR_0135199L → Q in ALS1. 1 Publication1
Natural variantiVAR_0135209L → V in ALS1. 1 Publication1
Natural variantiVAR_01352113G → R in ALS1. 1 PublicationCorresponds to variant dbSNP:rs121912456EnsemblClinVar.1
Natural variantiVAR_01352215V → G in ALS1. 1
Natural variantiVAR_00713315V → M in ALS1. 1 Publication1
Natural variantiVAR_00713417G → S in ALS1; sporadic young onset. 1 PublicationCorresponds to variant dbSNP:rs121912453EnsemblClinVar.1
Natural variantiVAR_04587621F → C in ALS1. 1 Publication1
Natural variantiVAR_01352322E → G in ALS1. 1
Natural variantiVAR_00713522E → K in ALS1. 1 PublicationCorresponds to variant dbSNP:rs121912450EnsemblClinVar.1
Natural variantiVAR_04587723Q → L in ALS1. 1 PublicationCorresponds to variant dbSNP:rs1169198442Ensembl.1
Natural variantiVAR_00713638G → R in ALS1; mild form; ubiquitinated by RNF19A. Ubiquitinated by MARCH5; leading to the degradation of mitochondrial SOD1. 4 PublicationsCorresponds to variant dbSNP:rs121912431EnsemblClinVar.1
Natural variantiVAR_01352439L → R in ALS1. 1
Natural variantiVAR_00713739L → V in ALS1. Corresponds to variant dbSNP:rs121912432EnsemblClinVar.1
Natural variantiVAR_00713942G → D in ALS1. Corresponds to variant dbSNP:rs121912434EnsemblClinVar.1
Natural variantiVAR_00713842G → S in ALS1. Corresponds to variant dbSNP:rs121912433EnsemblClinVar.1
Natural variantiVAR_00714044H → R in ALS1; reduces structural stability and enzyme activity; increases tendency to form fibrillar aggregates. 1 PublicationCorresponds to variant dbSNP:rs121912435EnsemblClinVar.1
Natural variantiVAR_01352546F → C in ALS1; slow progression. 1 PublicationCorresponds to variant dbSNP:rs121912457EnsemblClinVar.1
Natural variantiVAR_00714147H → R in ALS1; "benign" form; 80% of wild-type activity; ubiquitinated by RNF19A. 4 PublicationsCorresponds to variant dbSNP:rs121912443EnsemblClinVar.1
Natural variantiVAR_00714249H → Q in ALS1. 2 Publications1
Natural variantiVAR_04587849H → R in ALS1. 1 Publication1
Natural variantiVAR_01352650E → K in ALS1. 1
Natural variantiVAR_04587955T → R in ALS1; reduces tendency to form fibrillar aggregates. 2 PublicationsCorresponds to variant dbSNP:rs986277034Ensembl.1
Natural variantiVAR_01352766N → S in ALS1. 1
Natural variantiVAR_06556068L → P in ALS1. 1 Publication1
Natural variantiVAR_01352868L → R in ALS1. 1
Natural variantiVAR_00871873G → S in ALS1. 1 PublicationCorresponds to variant dbSNP:rs121912455EnsemblClinVar.1
Natural variantiVAR_01352977D → Y in ALS1. 1
Natural variantiVAR_01687481H → A in ALS1; sporadic form; interferes with zinc binding; requires 2 nucleotide substitutions. 1 Publication1
Natural variantiVAR_01353085L → F in ALS1. Corresponds to variant dbSNP:rs1315541036Ensembl.1
Natural variantiVAR_00714385L → V in ALS1. 1 PublicationCorresponds to variant dbSNP:rs121912452EnsemblClinVar.1
Natural variantiVAR_00714486G → R in ALS1; ubiquitinated by RNF19A; interferes with zinc-binding; ubiquitinated by MARCH5; leading to the degradation of mitochondrial SOD1. 6 PublicationsCorresponds to variant dbSNP:rs121912436EnsemblClinVar.1
Natural variantiVAR_01353187N → S in ALS1. 1 PublicationCorresponds to variant dbSNP:rs11556620EnsemblClinVar.1
Natural variantiVAR_04588088V → A in ALS1. 2 PublicationsCorresponds to variant dbSNP:rs1339283341Ensembl.1
Natural variantiVAR_04588190A → T in ALS1. 1 Publication1
Natural variantiVAR_01353290A → V in ALS1. Corresponds to variant dbSNP:rs1280042397Ensembl.1
Natural variantiVAR_00714591D → A in ALS1; does not seem to be linked with a decrease in activity. 3 PublicationsCorresponds to variant dbSNP:rs80265967EnsemblClinVar.1
Natural variantiVAR_01353391D → V in ALS1. 1
Natural variantiVAR_00714694G → A in ALS1; increases tendency to form fibrillar aggregates; ubiquitinated by RNF19A. 3 PublicationsCorresponds to variant dbSNP:rs121912438EnsemblClinVar.1
Natural variantiVAR_00714794G → C in ALS1. Corresponds to variant dbSNP:rs121912437EnsemblClinVar.1
Natural variantiVAR_00714894G → D in ALS1. 2 PublicationsCorresponds to variant dbSNP:rs121912438EnsemblClinVar.1
Natural variantiVAR_00714994G → R in ALS1; 30% of wild-type activity. 3 PublicationsCorresponds to variant dbSNP:rs121912437EnsemblClinVar.1
Natural variantiVAR_00871994G → V in ALS1. 1 Publication1
Natural variantiVAR_06519496A → G in ALS1. 1 Publication1
Natural variantiVAR_04588298V → M in ALS1; increases tendency to form fibrillar aggregates. 2 Publications1
Natural variantiVAR_007150101E → G in ALS1. Corresponds to variant dbSNP:rs121912439EnsemblClinVar.1
Natural variantiVAR_013534101E → K in ALS1. 1
Natural variantiVAR_007151102D → G in ALS1. 2 Publications1
Natural variantiVAR_007152102D → N in ALS1. 2 Publications1
Natural variantiVAR_008720105I → F in ALS1. 1 PublicationCorresponds to variant dbSNP:rs121912445EnsemblClinVar.1
Natural variantiVAR_013535106S → L in ALS1. Corresponds to variant dbSNP:rs1378590183Ensembl.1
Natural variantiVAR_007153107L → V in ALS1. Corresponds to variant dbSNP:rs121912440EnsemblClinVar.1
Natural variantiVAR_013536109G → V in ALS1. 1
Natural variantiVAR_077327112C → Y in ALS1. 1 Publication1
Natural variantiVAR_013537113I → M in ALS1. 1
Natural variantiVAR_007154113I → T in ALS1. 2 PublicationsCorresponds to variant dbSNP:rs74315452EnsemblClinVar.1
Natural variantiVAR_007155114I → T in ALS1; destabilizes dimeric protein structure and increases tendency to form fibrillar aggregates. 5 PublicationsCorresponds to variant dbSNP:rs121912441EnsemblClinVar.1
Natural variantiVAR_013538115G → A in ALS1. 1
Natural variantiVAR_007156116R → G in ALS1. 1 PublicationCorresponds to variant dbSNP:rs1301635320Ensembl.1
Natural variantiVAR_045883119V → L in ALS1. 1 PublicationCorresponds to variant dbSNP:rs1235629842EnsemblClinVar.1
Natural variantiVAR_008721119V → VFLQ in ALS1. 1
Natural variantiVAR_045884125D → G in ALS1. 1 Publication1
Natural variantiVAR_008722125D → V in ALS1. 1 Publication1
Natural variantiVAR_007157126D → H in ALS1. 1 Publication1
Natural variantiVAR_013539127L → S in ALS1. 1 Publication1
Natural variantiVAR_007158135S → N in ALS1; reduced metal binding; increases tendency to form fibrillar aggregates. 2 PublicationsCorresponds to variant dbSNP:rs121912451EnsemblClinVar.1
Natural variantiVAR_007159140N → K in ALS1. Corresponds to variant dbSNP:rs1804449Ensembl.1
Natural variantiVAR_007160145L → F in ALS1. 1 PublicationCorresponds to variant dbSNP:rs1482760341Ensembl.1
Natural variantiVAR_008724145L → S in ALS1. 1 PublicationCorresponds to variant dbSNP:rs121912446EnsemblClinVar.1
Natural variantiVAR_008725146A → T in ALS1. 1 PublicationCorresponds to variant dbSNP:rs121912447EnsemblClinVar.1
Natural variantiVAR_013540147C → R in ALS1. 1
Natural variantiVAR_045885148G → R in ALS1. 1 Publication1
Natural variantiVAR_007161149V → G in ALS1. Corresponds to variant dbSNP:rs1476760624Ensembl.1
Natural variantiVAR_007162149V → I in ALS1. 1 PublicationCorresponds to variant dbSNP:rs567511139Ensembl.1
Natural variantiVAR_007163150I → T in ALS1. 1 PublicationCorresponds to variant dbSNP:rs1424014997Ensembl.1
Natural variantiVAR_007164152I → T in ALS1. 1 PublicationCorresponds to variant dbSNP:rs121912449EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi7C → S: Enhances formation of fibrillar aggregates in the absence of bound zinc; when associated with S-58; S-112 and S-147. 3 Publications1
Mutagenesisi7C → S: No palmitoylation, reduced nuclear targeting. 3 Publications1
Mutagenesisi51 – 52FG → EE: Abolishes dimerization; when associated with Q-134. 2 Publications2
Mutagenesisi58C → A: Exhibits very slow copper acquisition. 3 Publications1
Mutagenesisi58C → S: Enhances formation of fibrillar aggregates in the absence of bound zinc; when associated with S-7; S-112 and S-147. 3 Publications1
Mutagenesisi81H → A: Loss of zinc binding and enhanced tendency to form aggregates; when associated with A-84. 2 Publications1
Mutagenesisi81H → S: Destabilization of dimer and loss of zinc binding; when associated with S-84. 2 Publications1
Mutagenesisi84D → A: Loss of zinc binding and enhanced tendency to form aggregates; when associated with A-81. 2 Publications1
Mutagenesisi84D → S: Destabilization of dimer and loss of zinc binding; when associated with S-81. 2 Publications1
Mutagenesisi112C → S: Enhances formation of fibrillar aggregates in the absence of bound zinc; when associated with S-7; S-58 and S-147. 2 Publications1
Mutagenesisi123K → A: Deacreased succinylation. 1 Publication1
Mutagenesisi123K → E: Mimicks constitutive succinylation state; decreased activity. 1 Publication1
Mutagenesisi134E → Q: Abolishes dimerization; when associated with E-50 and E-51. 1 Publication1
Mutagenesisi147C → A: Exhibits very slow copper acquisition. 3 Publications1
Mutagenesisi147C → S: Enhances formation of fibrillar aggregates in the absence of bound zinc; when associated with S-7; S-58 and S-112. 3 Publications1

Keywords - Diseasei

Amyotrophic lateral sclerosis, Disease mutation, Neurodegeneration

Organism-specific databases

DisGeNET

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DisGeNETi
6647

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
SOD1

MalaCards human disease database

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MalaCardsi
SOD1
MIMi105400 phenotype

Open Targets

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OpenTargetsi
ENSG00000142168

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
803 Amyotrophic lateral sclerosis

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA334

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2354

Drug and drug target database

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DrugBanki
DB01629 5-fluorouridine
DB14001 alpha-Tocopherol succinate
DB05025 Arimoclomol
DB09061 Cannabidiol
DB00958 Carboplatin
DB00515 Cisplatin
DB09130 Copper
DB06778 Cupric sulfate
DB14002 D-alpha-Tocopherol acetate
DB00988 Dopamine
DB01064 Isoprenaline
DB14009 Medical Cannabis
DB14011 Nabiximols
DB00526 Oxaliplatin
DB09221 Polaprezinc
DB03382 S-oxy-L-cysteine
DB00163 Vitamin E
DB01593 Zinc
DB14487 Zinc acetate
DB14533 Zinc chloride

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
SOD1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources2 Publications
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001640572 – 154Superoxide dismutase [Cu-Zn]Add BLAST153

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineCombined sources2 Publications1
Modified residuei4N6-succinyllysineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi7S-palmitoyl cysteine1 Publication1
Modified residuei10N6-succinyllysineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki331-(tryptophan-3-yl)-tryptophan (Trp-Trp) (interchain with W-33)1 Publication
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi58 ↔ 1474 Publications
Modified residuei92N6-succinyllysineBy similarity1
Modified residuei99PhosphoserineCombined sources1
Modified residuei103PhosphoserineCombined sources1
Modified residuei106PhosphoserineBy similarity1
Modified residuei108PhosphoserineBy similarity1
Modified residuei123N6-acetyllysine; alternateCombined sources1
Modified residuei123N6-succinyllysine; alternate1 Publication1
Modified residuei137N6-acetyllysine; alternateBy similarity1
Modified residuei137N6-succinyllysine; alternateBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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.2 Publications
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.1 Publication
Palmitoylation helps nuclear targeting and decreases catalytic activity.1 Publication
Succinylation, adjacent to copper catalytic site, probably inhibits activity. Desuccinylation by SIRT5 enhances activity.1 Publication

Keywords - PTMi

Acetylation, Disulfide bond, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P00441

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P00441

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
P00441

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P00441

PeptideAtlas

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PeptideAtlasi
P00441

PRoteomics IDEntifications database

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PRIDEi
P00441

ProteomicsDB human proteome resource

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ProteomicsDBi
12701
51250

Consortium for Top Down Proteomics

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TopDownProteomicsi
P00441

2D gel databases

DOSAC-COBS 2D-PAGE database

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DOSAC-COBS-2DPAGEi
P00441

USC-OGP 2-DE database

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OGPi
P00441

REPRODUCTION-2DPAGE

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REPRODUCTION-2DPAGEi
IPI00783680

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

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SWISS-2DPAGEi
P00441

University College Dublin 2-DE Proteome Database

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UCD-2DPAGEi
P00441

PTM databases

CarbonylDB database of protein carbonylation sites

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CarbonylDBi
P00441

GlyConnect protein glycosylation platform

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GlyConnecti
1778

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P00441

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P00441

SwissPalm database of S-palmitoylation events

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SwissPalmi
P00441

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000142168 Expressed in 236 organ(s), highest expression level in pons

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P00441 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P00441 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB008670
HPA001401

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer; non-disulfide linked. Homodimerization may take place via the ditryptophan cross-link at Trp-33. The pathogenic variants ALS1 Arg-38, Arg-47, Arg-86 and Ala-94 interact with RNF19A, whereas wild-type protein does not. The pathogenic variants ALS1 Arg-86 and Ala-94 interact with MARCH5, whereas wild-type protein does not.

10 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
112530, 341 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-2897 [Cu-Zn] Superoxide dismutase complex

Database of interacting proteins

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DIPi
DIP-44941N

Protein interaction database and analysis system

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IntActi
P00441, 246 interactors

Molecular INTeraction database

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MINTi
P00441

STRING: functional protein association networks

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STRINGi
9606.ENSP00000270142

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P00441

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1154
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P00441

Database of comparative protein structure models

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ModBasei
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Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P00441

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the Cu-Zn superoxide dismutase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0441 Eukaryota
COG2032 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000155551

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P00441

KEGG Orthology (KO)

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KOi
K04565

Identification of Orthologs from Complete Genome Data

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OMAi
HFNPHSK

Database of Orthologous Groups

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OrthoDBi
1574423at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P00441

TreeFam database of animal gene trees

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TreeFami
TF105131

Family and domain databases

Conserved Domains Database

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CDDi
cd00305 Cu-Zn_Superoxide_Dismutase, 1 hit

Database of protein disorder

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DisProti
DP00652

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.40.200, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR036423 SOD-like_Cu/Zn_dom_sf
IPR024134 SOD_Cu/Zn_/chaperone
IPR018152 SOD_Cu/Zn_BS
IPR001424 SOD_Cu_Zn_dom

The PANTHER Classification System

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PANTHERi
PTHR10003 PTHR10003, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00080 Sod_Cu, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00068 CUZNDISMTASE

Superfamily database of structural and functional annotation

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SUPFAMi
SSF49329 SSF49329, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00087 SOD_CU_ZN_1, 1 hit
PS00332 SOD_CU_ZN_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P00441-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MATKAVCVLK GDGPVQGIIN FEQKESNGPV KVWGSIKGLT EGLHGFHVHE
60 70 80 90 100
FGDNTAGCTS AGPHFNPLSR KHGGPKDEER HVGDLGNVTA DKDGVADVSI
110 120 130 140 150
EDSVISLSGD HCIIGRTLVV HEKADDLGKG GNEESTKTGN AGSRLACGVI

GIAQ
Length:154
Mass (Da):15,936
Last modified:January 23, 2007 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i25CA38DA8D564483
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H7BYH4H7BYH4_HUMAN
Superoxide dismutase [Cu-Zn]
SOD1
135Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti18I → S no nucleotide entry (PubMed:3889846).Curated1
Sequence conflicti99S → V no nucleotide entry (PubMed:3889846).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0135185A → S in ALS1. 1
Natural variantiVAR_0071305A → T in ALS1. 1 PublicationCorresponds to variant dbSNP:rs121912444EnsemblClinVar.1
Natural variantiVAR_0071315A → V in ALS1; severe form; reduces structural stability and enzyme activity; increases tendency to form fibrillar aggregates. 3 PublicationsCorresponds to variant dbSNP:rs121912442EnsemblClinVar.1
Natural variantiVAR_0087177C → F in ALS1. 1 PublicationCorresponds to variant dbSNP:rs121912448EnsemblClinVar.1
Natural variantiVAR_0071328V → E in ALS1. 1 Publication1
Natural variantiVAR_0135199L → Q in ALS1. 1 Publication1
Natural variantiVAR_0135209L → V in ALS1. 1 Publication1
Natural variantiVAR_01352113G → R in ALS1. 1 PublicationCorresponds to variant dbSNP:rs121912456EnsemblClinVar.1
Natural variantiVAR_01352215V → G in ALS1. 1
Natural variantiVAR_00713315V → M in ALS1. 1 Publication1
Natural variantiVAR_00713417G → S in ALS1; sporadic young onset. 1 PublicationCorresponds to variant dbSNP:rs121912453EnsemblClinVar.1
Natural variantiVAR_04587621F → C in ALS1. 1 Publication1
Natural variantiVAR_01352322E → G in ALS1. 1
Natural variantiVAR_00713522E → K in ALS1. 1 PublicationCorresponds to variant dbSNP:rs121912450EnsemblClinVar.1
Natural variantiVAR_04587723Q → L in ALS1. 1 PublicationCorresponds to variant dbSNP:rs1169198442Ensembl.1
Natural variantiVAR_00713638G → R in ALS1; mild form; ubiquitinated by RNF19A. Ubiquitinated by MARCH5; leading to the degradation of mitochondrial SOD1. 4 PublicationsCorresponds to variant dbSNP:rs121912431EnsemblClinVar.1
Natural variantiVAR_01352439L → R in ALS1. 1
Natural variantiVAR_00713739L → V in ALS1. Corresponds to variant dbSNP:rs121912432EnsemblClinVar.1
Natural variantiVAR_00713942G → D in ALS1. Corresponds to variant dbSNP:rs121912434EnsemblClinVar.1
Natural variantiVAR_00713842G → S in ALS1. Corresponds to variant dbSNP:rs121912433EnsemblClinVar.1
Natural variantiVAR_00714044H → R in ALS1; reduces structural stability and enzyme activity; increases tendency to form fibrillar aggregates. 1 PublicationCorresponds to variant dbSNP:rs121912435EnsemblClinVar.1
Natural variantiVAR_01352546F → C in ALS1; slow progression. 1 PublicationCorresponds to variant dbSNP:rs121912457EnsemblClinVar.1
Natural variantiVAR_00714147H → R in ALS1; "benign" form; 80% of wild-type activity; ubiquitinated by RNF19A. 4 PublicationsCorresponds to variant dbSNP:rs121912443EnsemblClinVar.1
Natural variantiVAR_00714249H → Q in ALS1. 2 Publications1
Natural variantiVAR_04587849H → R in ALS1. 1 Publication1
Natural variantiVAR_01352650E → K in ALS1. 1
Natural variantiVAR_04587955T → R in ALS1; reduces tendency to form fibrillar aggregates. 2 PublicationsCorresponds to variant dbSNP:rs986277034Ensembl.1
Natural variantiVAR_01352766N → S in ALS1. 1
Natural variantiVAR_06556068L → P in ALS1. 1 Publication1
Natural variantiVAR_01352868L → R in ALS1. 1
Natural variantiVAR_00871873G → S in ALS1. 1 PublicationCorresponds to variant dbSNP:rs121912455EnsemblClinVar.1
Natural variantiVAR_01352977D → Y in ALS1. 1
Natural variantiVAR_01687481H → A in ALS1; sporadic form; interferes with zinc binding; requires 2 nucleotide substitutions. 1 Publication1
Natural variantiVAR_01353085L → F in ALS1. Corresponds to variant dbSNP:rs1315541036Ensembl.1
Natural variantiVAR_00714385L → V in ALS1. 1 PublicationCorresponds to variant dbSNP:rs121912452EnsemblClinVar.1
Natural variantiVAR_00714486G → R in ALS1; ubiquitinated by RNF19A; interferes with zinc-binding; ubiquitinated by MARCH5; leading to the degradation of mitochondrial SOD1. 6 PublicationsCorresponds to variant dbSNP:rs121912436EnsemblClinVar.1
Natural variantiVAR_01353187N → S in ALS1. 1 PublicationCorresponds to variant dbSNP:rs11556620EnsemblClinVar.1
Natural variantiVAR_04588088V → A in ALS1. 2 PublicationsCorresponds to variant dbSNP:rs1339283341Ensembl.1
Natural variantiVAR_04588190A → T in ALS1. 1 Publication1
Natural variantiVAR_01353290A → V in ALS1. Corresponds to variant dbSNP:rs1280042397Ensembl.1
Natural variantiVAR_00714591D → A in ALS1; does not seem to be linked with a decrease in activity. 3 PublicationsCorresponds to variant dbSNP:rs80265967EnsemblClinVar.1
Natural variantiVAR_01353391D → V in ALS1. 1
Natural variantiVAR_00714694G → A in ALS1; increases tendency to form fibrillar aggregates; ubiquitinated by RNF19A. 3 PublicationsCorresponds to variant dbSNP:rs121912438EnsemblClinVar.1
Natural variantiVAR_00714794G → C in ALS1. Corresponds to variant dbSNP:rs121912437EnsemblClinVar.1
Natural variantiVAR_00714894G → D in ALS1. 2 PublicationsCorresponds to variant dbSNP:rs121912438EnsemblClinVar.1
Natural variantiVAR_00714994G → R in ALS1; 30% of wild-type activity. 3 PublicationsCorresponds to variant dbSNP:rs121912437EnsemblClinVar.1
Natural variantiVAR_00871994G → V in ALS1. 1 Publication1
Natural variantiVAR_06519496A → G in ALS1. 1 Publication1
Natural variantiVAR_04588298V → M in ALS1; increases tendency to form fibrillar aggregates. 2 Publications1
Natural variantiVAR_007150101E → G in ALS1. Corresponds to variant dbSNP:rs121912439EnsemblClinVar.1
Natural variantiVAR_013534101E → K in ALS1. 1
Natural variantiVAR_007151102D → G in ALS1. 2 Publications1
Natural variantiVAR_007152102D → N in ALS1. 2 Publications