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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-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

2 superoxide + 2 H+ = O2 + H2O2.

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

GO - Molecular functioni

  • chaperone binding Source: UniProtKB
  • copper ion binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: UniProtKB
  • protein phosphatase 2B binding Source: UniProtKB
  • Rac GTPase binding Source: UniProtKB
  • superoxide dismutase activity Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • activation of MAPK activity Source: UniProtKB
  • anterograde axonal transport Source: BHF-UCL
  • auditory receptor cell stereocilium organization Source: UniProtKB
  • cell aging Source: UniProtKB
  • cellular iron ion homeostasis Source: UniProtKB
  • cellular response to ATP Source: Ensembl
  • cellular response to cadmium ion Source: Ensembl
  • cellular response to potassium ion Source: Ensembl
  • embryo implantation Source: UniProtKB
  • glutathione metabolic process Source: UniProtKB
  • heart contraction Source: UniProtKB
  • hydrogen peroxide biosynthetic process Source: UniProtKB
  • locomotory behavior Source: UniProtKB
  • muscle cell cellular homeostasis Source: UniProtKB
  • myeloid cell homeostasis Source: UniProtKB
  • negative regulation of cholesterol biosynthetic process Source: UniProtKB
  • negative regulation of neuron apoptotic process Source: UniProtKB
  • neurofilament cytoskeleton organization Source: UniProtKB
  • ovarian follicle development Source: UniProtKB
  • peripheral nervous system myelin maintenance Source: UniProtKB
  • placenta development Source: UniProtKB
  • platelet degranulation Source: Reactome
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of catalytic activity Source: UniProtKB
  • positive regulation of cytokine production Source: UniProtKB
  • positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: BHF-UCL
  • positive regulation of superoxide anion generation Source: UniProtKB
  • reactive oxygen species metabolic process Source: UniProtKB
  • regulation of blood pressure Source: UniProtKB
  • regulation of GTPase activity Source: UniProtKB
  • regulation of mitochondrial membrane potential Source: UniProtKB
  • regulation of multicellular organism growth Source: UniProtKB
  • regulation of organ growth Source: UniProtKB
  • regulation of protein kinase activity Source: UniProtKB
  • regulation of T cell differentiation in thymus Source: UniProtKB
  • relaxation of vascular smooth muscle Source: UniProtKB
  • removal of superoxide radicals Source: UniProtKB
  • response to amphetamine Source: Ensembl
  • response to antibiotic Source: Ensembl
  • response to antipsychotic drug Source: Ensembl
  • response to axon injury Source: UniProtKB
  • response to carbon monoxide Source: Ensembl
  • response to copper ion Source: Ensembl
  • response to drug Source: UniProtKB
  • response to ethanol Source: UniProtKB
  • response to heat Source: UniProtKB
  • response to hydrogen peroxide Source: UniProtKB
  • response to nutrient levels Source: Ensembl
  • response to organic substance Source: UniProtKB
  • response to reactive oxygen species Source: Reactome
  • response to superoxide Source: UniProtKB
  • retina homeostasis Source: UniProtKB
  • retrograde axonal transport Source: BHF-UCL
  • sensory perception of sound Source: UniProtKB
  • spermatogenesis Source: UniProtKB
  • superoxide anion generation Source: Ensembl
  • superoxide metabolic process Source: UniProtKB
  • thymus development Source: UniProtKB
  • transmission of nerve impulse Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:HS06899-MONOMER.
ZFISH:HS06899-MONOMER.
BRENDAi1.15.1.1. 2681.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-3299685. Detoxification of Reactive Oxygen Species.

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Cu-Zn] (EC:1.15.1.1)
Alternative name(s):
Superoxide dismutase 1
Short name:
hSod1
Gene namesi
Name:SOD1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 21

Organism-specific databases

HGNCiHGNC:11179. SOD1.

Subcellular locationi

GO - Cellular componenti

  • axon cytoplasm Source: GOC
  • cytoplasm Source: UniProtKB
  • cytoplasmic vesicle Source: UniProtKB
  • cytosol Source: UniProtKB
  • dendrite cytoplasm Source: UniProtKB
  • dense core granule Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • lysosome Source: Ensembl
  • mitochondrial intermembrane space Source: Reactome
  • mitochondrial matrix Source: UniProtKB
  • mitochondrion Source: UniProtKB
  • myelin sheath Source: Ensembl
  • neuronal cell body Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • peroxisome Source: UniProtKB
  • protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

Pathology & Biotechi

Involvement in diseasei

Amyotrophic lateral sclerosis 1 (ALS1)35 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.
See also OMIM:105400
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0135185A → S in ALS1. 1
Natural variantiVAR_0071305A → T in ALS1. 1 PublicationCorresponds to variant rs121912444dbSNPEnsembl.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 rs121912442dbSNPEnsembl.1
Natural variantiVAR_0087177C → F in ALS1. 1 PublicationCorresponds to variant rs121912448dbSNPEnsembl.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 rs121912456dbSNPEnsembl.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 rs121912453dbSNPEnsembl.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 rs121912450dbSNPEnsembl.1
Natural variantiVAR_04587723Q → L in ALS1. 1 Publication1
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 rs121912431dbSNPEnsembl.1
Natural variantiVAR_01352439L → R in ALS1. 1
Natural variantiVAR_00713739L → V in ALS1. Corresponds to variant rs121912432dbSNPEnsembl.1
Natural variantiVAR_00713942G → D in ALS1. Corresponds to variant rs121912434dbSNPEnsembl.1
Natural variantiVAR_00713842G → S in ALS1. Corresponds to variant rs121912433dbSNPEnsembl.1
Natural variantiVAR_00714044H → R in ALS1; reduces structural stability and enzyme activity; increases tendency to form fibrillar aggregates. 1 PublicationCorresponds to variant rs121912435dbSNPEnsembl.1
Natural variantiVAR_01352546F → C in ALS1; slow progression. 1 PublicationCorresponds to variant rs121912457dbSNPEnsembl.1
Natural variantiVAR_00714147H → R in ALS1; "benign" form; 80% of wild-type activity; ubiquitinated by RNF19A. 4 PublicationsCorresponds to variant rs121912443dbSNPEnsembl.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 Publications1
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 rs121912455dbSNPEnsembl.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. 1
Natural variantiVAR_00714385L → V in ALS1. 1 PublicationCorresponds to variant rs121912452dbSNPEnsembl.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 rs121912436dbSNPEnsembl.1
Natural variantiVAR_01353187N → S in ALS1. Corresponds to variant rs11556620dbSNPEnsembl.1
Natural variantiVAR_04588088V → A in ALS1. 1 Publication1
Natural variantiVAR_04588190A → T in ALS1. 1 Publication1
Natural variantiVAR_01353290A → V in ALS1. 1
Natural variantiVAR_00714591D → A in ALS1; does not seem to be linked with a decrease in activity. 3 PublicationsCorresponds to variant rs80265967dbSNPEnsembl.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 rs121912438dbSNPEnsembl.1
Natural variantiVAR_00714794G → C in ALS1. Corresponds to variant rs121912437dbSNPEnsembl.1
Natural variantiVAR_00714894G → D in ALS1. 2 Publications1
Natural variantiVAR_00714994G → R in ALS1; 30% of wild-type activity. 3 PublicationsCorresponds to variant rs121912437dbSNPEnsembl.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 rs121912439dbSNPEnsembl.1
Natural variantiVAR_013534101E → K in ALS1. 1
Natural variantiVAR_007151102D → G in ALS1. 1 Publication1
Natural variantiVAR_007152102D → N in ALS1. 1 Publication1
Natural variantiVAR_008720105I → F in ALS1. 1 PublicationCorresponds to variant rs121912445dbSNPEnsembl.1
Natural variantiVAR_013535106S → L in ALS1. 1
Natural variantiVAR_007153107L → V in ALS1. Corresponds to variant rs121912440dbSNPEnsembl.1
Natural variantiVAR_013536109G → V in ALS1. 1
Natural variantiVAR_013537113I → M in ALS1. 1
Natural variantiVAR_007154113I → T in ALS1. 2 PublicationsCorresponds to variant rs74315452dbSNPEnsembl.1
Natural variantiVAR_007155114I → T in ALS1; destabilizes dimeric protein structure and increases tendency to form fibrillar aggregates. 5 PublicationsCorresponds to variant rs121912441dbSNPEnsembl.1
Natural variantiVAR_013538115G → A in ALS1. 1
Natural variantiVAR_007156116R → G in ALS1. 1 Publication1
Natural variantiVAR_045883119V → L in ALS1. 1 Publication1
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 rs121912451dbSNPEnsembl.1
Natural variantiVAR_007159140N → K in ALS1. 1
Natural variantiVAR_007160145L → F in ALS1. 1 Publication1
Natural variantiVAR_008724145L → S in ALS1. 1 PublicationCorresponds to variant rs121912446dbSNPEnsembl.1
Natural variantiVAR_008725146A → T in ALS1. 1 PublicationCorresponds to variant rs121912447dbSNPEnsembl.1
Natural variantiVAR_013540147C → R in ALS1. 1
Natural variantiVAR_045885148G → R in ALS1. 1 Publication1
Natural variantiVAR_007161149V → G in ALS1. 1
Natural variantiVAR_007162149V → I in ALS1. 1 PublicationCorresponds to variant rs567511139dbSNPEnsembl.1
Natural variantiVAR_007163150I → T in ALS1. 1 Publication1
Natural variantiVAR_007164152I → T in ALS1. 1 PublicationCorresponds to variant rs121912449dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

DisGeNETi6647.
MalaCardsiSOD1.
MIMi105400. phenotype.
OpenTargetsiENSG00000142168.
Orphaneti803. Amyotrophic lateral sclerosis.
PharmGKBiPA334.

Chemistry databases

ChEMBLiCHEMBL2354.
DrugBankiDB00958. Carboplatin.
DB00515. Cisplatin.
DB00526. Oxaliplatin.
DB00163. Vitamin E.

Polymorphism and mutation databases

BioMutaiSOD1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources2 Publications
ChainiPRO_00001640572 – 154Superoxide dismutase [Cu-Zn]Add BLAST153

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources2 Publications1
Modified residuei4N6-succinyllysineBy similarity1
Lipidationi7S-palmitoyl cysteine1 Publication1
Modified residuei10N6-succinyllysineBy similarity1
Cross-linki331-(tryptophan-3-yl)-tryptophan (Trp-Trp) (interchain with W-33)1 Publication
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

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

EPDiP00441.
PaxDbiP00441.
PeptideAtlasiP00441.
PRIDEiP00441.
TopDownProteomicsiP00441.

2D gel databases

DOSAC-COBS-2DPAGEP00441.
OGPiP00441.
REPRODUCTION-2DPAGEIPI00783680.
SWISS-2DPAGEP00441.
UCD-2DPAGEP00441.

PTM databases

iPTMnetiP00441.
PhosphoSitePlusiP00441.
SwissPalmiP00441.

Expressioni

Gene expression databases

BgeeiENSG00000142168.
CleanExiHS_SOD1.
ExpressionAtlasiP00441. baseline and differential.
GenevisibleiP00441. HS.

Organism-specific databases

HPAiCAB008670.
HPA001401.

Interactioni

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

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-990792,EBI-990792
ChgaP263395EBI-990792,EBI-990900From a different organism.
ChgbP160146EBI-990792,EBI-990820From a different organism.
DYNC2LI1Q8TCX13EBI-990792,EBI-8568003

GO - Molecular functioni

  • chaperone binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: UniProtKB
  • protein phosphatase 2B binding Source: UniProtKB
  • Rac GTPase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi112530. 162 interactors.
DIPiDIP-44941N.
IntActiP00441. 29 interactors.
MINTiMINT-204523.
STRINGi9606.ENSP00000270142.

Chemistry databases

BindingDBiP00441.

Structurei

Secondary structure

1154
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 10Combined sources8
Beta strandi12 – 14Combined sources3
Beta strandi16 – 25Combined sources10
Beta strandi26 – 28Combined sources3
Beta strandi30 – 38Combined sources9
Beta strandi41 – 50Combined sources10
Helixi54 – 56Combined sources3
Helixi58 – 61Combined sources4
Beta strandi63 – 65Combined sources3
Beta strandi67 – 69Combined sources3
Beta strandi74 – 76Combined sources3
Beta strandi77 – 79Combined sources3
Turni80 – 82Combined sources3
Beta strandi84 – 90Combined sources7
Helixi92 – 94Combined sources3
Beta strandi96 – 104Combined sources9
Beta strandi106 – 108Combined sources3
Helixi109 – 111Combined sources3
Beta strandi112 – 115Combined sources4
Beta strandi116 – 123Combined sources8
Beta strandi127 – 129Combined sources3
Beta strandi130 – 132Combined sources3
Helixi133 – 136Combined sources4
Turni138 – 140Combined sources3
Beta strandi143 – 149Combined sources7
Beta strandi151 – 153Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AZVX-ray1.90A/B2-154[»]
1BA9NMR-A2-154[»]
1DSWNMR-A2-154[»]
1FUNX-ray2.85A/B/C/D/E/F/G/H/I/J2-154[»]
1HL4X-ray1.82A/B/C/D2-154[»]
1HL5X-ray1.80A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/S2-154[»]
1KMGNMR-A2-154[»]
1L3NNMR-A/B2-154[»]
1MFMX-ray1.02A2-154[»]
1N18X-ray2.00A/B/C/D/E/F/G/H/I/J1-154[»]
1N19X-ray1.86A/B1-154[»]
1OEZX-ray2.15W/X/Y/Z2-154[»]
1OZTX-ray2.50G/H/I/J/K/L/M/N2-154[»]
1OZUX-ray1.30A/B2-154[»]
1P1VX-ray1.40A/B/C2-154[»]
1PTZX-ray1.80A/B2-154[»]
1PU0X-ray1.70A/B/C/D/E/F/G/H/I/J2-154[»]
1RK7NMR-A2-154[»]
1SOSX-ray2.50A/B/C/D/E/F/G/H/I/J2-154[»]
1SPDX-ray2.40A/B2-154[»]
1UXLX-ray1.60A/B/C/D/E/F/G/H/I/J2-154[»]
1UXMX-ray1.90A/B/C/D/E/F/G/H/I/J/K/L2-154[»]
2AF2NMR-A/B2-154[»]
2C9SX-ray1.24A/F2-154[»]
2C9UX-ray1.24A/F2-154[»]
2C9VX-ray1.07A/F2-154[»]
2GBTX-ray1.70A/B/C/D2-154[»]
2GBUX-ray2.00A/B/C/D2-154[»]
2GBVX-ray2.00A/B/C/D/E/F/G/H/I/J2-154[»]
2LU5NMR-A2-154[»]
2MP3NMR-A2-126[»]
2NNXX-ray2.30A/B/C/D2-154[»]
2R27X-ray2.00A/B1-154[»]
2V0AX-ray1.15A/F2-154[»]
2VR6X-ray1.30A/F2-154[»]
2VR7X-ray1.58A/F2-154[»]
2VR8X-ray1.36A/F2-154[»]
2WKOX-ray1.97A/F2-154[»]
2WYTX-ray1.00A/F2-154[»]
2WYZX-ray1.70A/F2-154[»]
2WZ0X-ray1.72A/F2-154[»]
2WZ5X-ray1.50A/F2-154[»]
2WZ6X-ray1.55A/F2-154[»]
2XJKX-ray1.45A2-154[»]
2XJLX-ray1.55A2-154[»]
2ZKWX-ray1.90A/B1-154[»]
2ZKXX-ray2.72A/B/C/D1-154[»]
2ZKYX-ray2.40A/B/C/D/E/F/G/H/I/J1-154[»]
3CQPX-ray1.95A/B/C/D2-154[»]
3CQQX-ray1.90A/B2-154[»]
3ECUX-ray1.90A/B/C/D2-154[»]
3ECVX-ray1.90A/B/C/D2-154[»]
3ECWX-ray2.15A/B/C/D2-154[»]
3GQFX-ray2.20A/B/C/D/E/F2-154[»]
3GTVX-ray2.20A/B/C/D/E/F/G/H/I/J/K/L2-81[»]
3GZOX-ray2.10A/B/C/D/E/F/G/H/I/J2-154[»]
3GZPX-ray3.10A/B/C/D2-154[»]
3GZQX-ray1.40A/B2-154[»]
3H2PX-ray1.55A/B2-154[»]
3H2QX-ray1.85A/B/C/D2-154[»]
3HFFX-ray2.20A2-154[»]
3K91X-ray1.75A/B2-154[»]
3KH3X-ray3.50A/B/C/D/E/F/G/H/I/J/K/L2-154[»]
3KH4X-ray3.50A/B/C/D/E/F2-154[»]
3LTVX-ray2.45A/B/C/D/E/F82-154[»]
3QQDX-ray1.65A/B2-154[»]
3RE0X-ray2.28A/B/C/D2-154[»]
3T5WX-ray1.80A/B/D/E/F/G/H/I/J/K/L/M2-154[»]
4A7GX-ray1.24A/F2-154[»]
4A7QX-ray1.22A/F2-154[»]
4A7SX-ray1.06A/F2-154[»]
4A7TX-ray1.45A/F2-154[»]
4A7UX-ray0.98A/F2-154[»]
4A7VX-ray1.00A/F2-154[»]
4B3EX-ray2.15A/B/C/D/E/F/G/H/I/J1-154[»]
4BCYX-ray1.27A2-154[»]
4BCZX-ray1.93A/B2-49[»]
A/B83-124[»]
A/B141-154[»]
4BD4X-ray2.78A/B/C/D/E/F/G/H/I2-49[»]
A/B/C/D/E/F/G/H/I83-124[»]
A/B/C/D/E/F/G/H/I141-154[»]
4FF9X-ray2.50A/B2-154[»]
4MCMX-ray2.20A/B/C/D/E/F/G/H/I/J/K/L2-154[»]
4MCNX-ray2.60A/B2-154[»]
4NINX-ray1.40A102-108[»]
4NIOX-ray1.30A148-154[»]
4NIPX-ray1.90A148-154[»]
4OH2X-ray2.38A/B/C/D/E/F/G/H/I/J2-154[»]
4SODmodel-A1-154[»]
4XCRX-ray3.60A/B2-154[»]
5DLIX-ray2.10A/B/C/D/E/F/G/H29-39[»]
DisProtiDP00652.
ProteinModelPortaliP00441.
SMRiP00441.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00441.

Family & Domainsi

Sequence similaritiesi

Belongs to the Cu-Zn superoxide dismutase family.Curated

Phylogenomic databases

eggNOGiKOG0441. Eukaryota.
COG2032. LUCA.
GeneTreeiENSGT00530000063226.
HOVERGENiHBG000062.
InParanoidiP00441.
KOiK04565.
OMAiVCVLKGT.
OrthoDBiEOG091G0OG2.
PhylomeDBiP00441.
TreeFamiTF105131.

Family and domain databases

CDDicd00305. Cu-Zn_Superoxide_Dismutase. 1 hit.
Gene3Di2.60.40.200. 1 hit.
InterProiIPR024134. SOD_Cu/Zn_/chaperone.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERiPTHR10003. PTHR10003. 1 hit.
PfamiPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSiPR00068. CUZNDISMTASE.
SUPFAMiSSF49329. SSF49329. 1 hit.
PROSITEiPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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
Checksum:i25CA38DA8D564483
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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 rs121912444dbSNPEnsembl.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 rs121912442dbSNPEnsembl.1
Natural variantiVAR_0087177C → F in ALS1. 1 PublicationCorresponds to variant rs121912448dbSNPEnsembl.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 rs121912456dbSNPEnsembl.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 rs121912453dbSNPEnsembl.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 rs121912450dbSNPEnsembl.1
Natural variantiVAR_04587723Q → L in ALS1. 1 Publication1
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 rs121912431dbSNPEnsembl.1
Natural variantiVAR_01352439L → R in ALS1. 1
Natural variantiVAR_00713739L → V in ALS1. Corresponds to variant rs121912432dbSNPEnsembl.1
Natural variantiVAR_00713942G → D in ALS1. Corresponds to variant rs121912434dbSNPEnsembl.1
Natural variantiVAR_00713842G → S in ALS1. Corresponds to variant rs121912433dbSNPEnsembl.1
Natural variantiVAR_00714044H → R in ALS1; reduces structural stability and enzyme activity; increases tendency to form fibrillar aggregates. 1 PublicationCorresponds to variant rs121912435dbSNPEnsembl.1
Natural variantiVAR_01352546F → C in ALS1; slow progression. 1 PublicationCorresponds to variant rs121912457dbSNPEnsembl.1
Natural variantiVAR_00714147H → R in ALS1; "benign" form; 80% of wild-type activity; ubiquitinated by RNF19A. 4 PublicationsCorresponds to variant rs121912443dbSNPEnsembl.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 Publications1
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 rs121912455dbSNPEnsembl.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. 1
Natural variantiVAR_00714385L → V in ALS1. 1 PublicationCorresponds to variant rs121912452dbSNPEnsembl.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 rs121912436dbSNPEnsembl.1
Natural variantiVAR_01353187N → S in ALS1. Corresponds to variant rs11556620dbSNPEnsembl.1
Natural variantiVAR_04588088V → A in ALS1. 1 Publication1
Natural variantiVAR_04588190A → T in ALS1. 1 Publication1
Natural variantiVAR_01353290A → V in ALS1. 1
Natural variantiVAR_00714591D → A in ALS1; does not seem to be linked with a decrease in activity. 3 PublicationsCorresponds to variant rs80265967dbSNPEnsembl.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 rs121912438dbSNPEnsembl.1
Natural variantiVAR_00714794G → C in ALS1. Corresponds to variant rs121912437dbSNPEnsembl.1
Natural variantiVAR_00714894G → D in ALS1. 2 Publications1
Natural variantiVAR_00714994G → R in ALS1; 30% of wild-type activity. 3 PublicationsCorresponds to variant rs121912437dbSNPEnsembl.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 rs121912439dbSNPEnsembl.1
Natural variantiVAR_013534101E → K in ALS1. 1
Natural variantiVAR_007151102D → G in ALS1. 1 Publication1
Natural variantiVAR_007152102D → N in ALS1. 1 Publication1
Natural variantiVAR_008720105I → F in ALS1. 1 PublicationCorresponds to variant rs121912445dbSNPEnsembl.1
Natural variantiVAR_013535106S → L in ALS1. 1
Natural variantiVAR_007153107L → V in ALS1. Corresponds to variant rs121912440dbSNPEnsembl.1
Natural variantiVAR_013536109G → V in ALS1. 1
Natural variantiVAR_013537113I → M in ALS1. 1
Natural variantiVAR_007154113I → T in ALS1. 2 PublicationsCorresponds to variant rs74315452dbSNPEnsembl.1
Natural variantiVAR_007155114I → T in ALS1; destabilizes dimeric protein structure and increases tendency to form fibrillar aggregates. 5 PublicationsCorresponds to variant rs121912441dbSNPEnsembl.1
Natural variantiVAR_013538115G → A in ALS1. 1
Natural variantiVAR_007156116R → G in ALS1. 1 Publication1
Natural variantiVAR_045883119V → L in ALS1. 1 Publication1
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_008723134Missing in ALS. 1 Publication1
Natural variantiVAR_007158135S → N in ALS1; reduced metal binding; increases tendency to form fibrillar aggregates. 2 PublicationsCorresponds to variant rs121912451dbSNPEnsembl.1
Natural variantiVAR_007159140N → K in ALS1. 1
Natural variantiVAR_007160145L → F in ALS1. 1 Publication1
Natural variantiVAR_008724145L → S in ALS1. 1 PublicationCorresponds to variant rs121912446dbSNPEnsembl.1
Natural variantiVAR_008725146A → T in ALS1. 1 PublicationCorresponds to variant rs121912447dbSNPEnsembl.1
Natural variantiVAR_013540147C → R in ALS1. 1
Natural variantiVAR_045885148G → R in ALS1. 1 Publication1
Natural variantiVAR_007161149V → G in ALS1. 1
Natural variantiVAR_007162149V → I in ALS1. 1 PublicationCorresponds to variant rs567511139dbSNPEnsembl.1
Natural variantiVAR_007163150I → T in ALS1. 1 Publication1
Natural variantiVAR_007164152I → T in ALS1. 1 PublicationCorresponds to variant rs121912449dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L44139
, L44135, L44136,