Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Superoxide dismutase [Cu-Zn]

Gene

Sod1

Organism
Mus musculus (Mouse)
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:
  • Cu cationBy similarityNote: Binds 1 copper ion per subunit.By similarity
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi47Copper; catalyticBy similarity1
Metal bindingi49Copper; catalyticBy similarity1
Metal bindingi64Copper; catalyticBy similarity1
Metal bindingi64Zinc; via pros nitrogen1 Publication1
Metal bindingi72Zinc; via pros nitrogen1 Publication1
Metal bindingi81Zinc; via pros nitrogen1 Publication1
Metal bindingi84Zinc; structural1 Publication1
Metal bindingi121Copper; catalyticBy similarity1

GO - Molecular functioni

GO - Biological processi

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

Keywords - Molecular functioni

Antioxidant, Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-114608. Platelet degranulation.
R-MMU-3299685. Detoxification of Reactive Oxygen Species.

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Cu-Zn] (EC:1.15.1.1)
Gene namesi
Name:Sod1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:98351. Sod1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

40% reduction in hepatic GPX1 activity.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001640622 – 154Superoxide dismutase [Cu-Zn]Add BLAST153

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei4N6-succinyllysineCombined sources1
Lipidationi7S-palmitoyl cysteineBy similarity1
Modified residuei10N6-succinyllysineCombined sources1
Disulfide bondi58 ↔ 147By similarity
Modified residuei92N6-succinyllysineCombined sources1
Modified residuei99PhosphoserineBy similarity1
Modified residuei106PhosphoserineBy similarity1
Modified residuei108PhosphoserineCombined sources1
Modified residuei123N6-acetyllysine; alternateCombined sources1
Modified residuei123N6-succinyllysine; alternateCombined sources1
Modified residuei137N6-acetyllysine; alternateCombined sources1
Modified residuei137N6-succinyllysine; alternateCombined sources1

Post-translational modificationi

Palmitoylation helps nuclear targeting and decreases catalytic activity.By similarity
Succinylation, adjacent to copper catalytic site, probably inhibits activity. Desuccinylation by SIRT5 enhances activity.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

EPDiP08228.
MaxQBiP08228.
PaxDbiP08228.
PeptideAtlasiP08228.
PRIDEiP08228.

2D gel databases

DOSAC-COBS-2DPAGEP08228.
REPRODUCTION-2DPAGEIPI00130589.
P08228.
SWISS-2DPAGEP08228.
UCD-2DPAGEP08228.

PTM databases

iPTMnetiP08228.
PhosphoSitePlusiP08228.
SwissPalmiP08228.

Expressioni

Gene expression databases

BgeeiENSMUSG00000022982.
CleanExiMM_SOD1.
GenevisibleiP08228. MM.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Rac1P630014EBI-1635090,EBI-413646

GO - Molecular functioni

Protein-protein interaction databases

BioGridi203387. 30 interactors.
DIPiDIP-48691N.
IntActiP08228. 32 interactors.
MINTiMINT-1869618.
STRINGi10090.ENSMUSP00000023707.

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 strandi30 – 38Combined sources9
Beta strandi41 – 50Combined sources10
Turni55 – 58Combined sources4
Helixi59 – 61Combined sources3
Beta strandi77 – 79Combined sources3
Beta strandi84 – 90Combined sources7
Beta strandi96 – 109Combined sources14
Beta strandi116 – 123Combined sources8
Beta strandi130 – 132Combined sources3
Helixi133 – 138Combined sources6
Beta strandi143 – 149Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3GTTX-ray2.40A/B/C/D/E/F2-154[»]
3GTVX-ray2.20A/B/C/D/E/F/G/H/I/J/K/L82-154[»]
3LTVX-ray2.45A/B/C/D/E/F2-81[»]
ProteinModelPortaliP08228.
SMRiP08228.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08228.

Family & Domainsi

Sequence similaritiesi

Belongs to the Cu-Zn superoxide dismutase family.Curated

Phylogenomic databases

eggNOGiKOG0441. Eukaryota.
COG2032. LUCA.
GeneTreeiENSGT00530000063226.
HOGENOMiHOG000263447.
HOVERGENiHBG000062.
InParanoidiP08228.
KOiK04565.
OMAiVCVLKGT.
OrthoDBiEOG091G0OG2.
PhylomeDBiP08228.
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.

P08228-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAMKAVCVLK GDGPVQGTIH FEQKASGEPV VLSGQITGLT EGQHGFHVHQ
60 70 80 90 100
YGDNTQGCTS AGPHFNPHSK KHGGPADEER HVGDLGNVTA GKDGVANVSI
110 120 130 140 150
EDRVISLSGE HSIIGRTMVV HEKQDDLGKG GNEESTKTGN AGSRLACGVI

GIAQ
Length:154
Mass (Da):15,943
Last modified:January 23, 2007 - v2
Checksum:iCAE548C66043BAC4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti102D → H in AAA40121 (PubMed:2022332).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06683 mRNA. Translation: CAA29880.1.
M60798
, M60794, M60795, M60796, M60797 Genomic DNA. Translation: AAA40121.1.
M35725 mRNA. Translation: AAA37518.1.
AK020624 mRNA. Translation: BAB32154.1.
AK077284 mRNA. Translation: BAC36730.1.
BC002066 mRNA. Translation: AAH02066.1.
BC048874 mRNA. Translation: AAH48874.1.
BC086886 mRNA. Translation: AAH86886.1.
CCDSiCCDS37395.1.
PIRiJQ0915.
RefSeqiNP_035564.1. NM_011434.1.
UniGeneiMm.276325.
Mm.466779.

Genome annotation databases

EnsembliENSMUST00000023707; ENSMUSP00000023707; ENSMUSG00000022982.
GeneIDi20655.
KEGGimmu:20655.
UCSCiuc007zvz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06683 mRNA. Translation: CAA29880.1.
M60798
, M60794, M60795, M60796, M60797 Genomic DNA. Translation: AAA40121.1.
M35725 mRNA. Translation: AAA37518.1.
AK020624 mRNA. Translation: BAB32154.1.
AK077284 mRNA. Translation: BAC36730.1.
BC002066 mRNA. Translation: AAH02066.1.
BC048874 mRNA. Translation: AAH48874.1.
BC086886 mRNA. Translation: AAH86886.1.
CCDSiCCDS37395.1.
PIRiJQ0915.
RefSeqiNP_035564.1. NM_011434.1.
UniGeneiMm.276325.
Mm.466779.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3GTTX-ray2.40A/B/C/D/E/F2-154[»]
3GTVX-ray2.20A/B/C/D/E/F/G/H/I/J/K/L82-154[»]
3LTVX-ray2.45A/B/C/D/E/F2-81[»]
ProteinModelPortaliP08228.
SMRiP08228.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203387. 30 interactors.
DIPiDIP-48691N.
IntActiP08228. 32 interactors.
MINTiMINT-1869618.
STRINGi10090.ENSMUSP00000023707.

PTM databases

iPTMnetiP08228.
PhosphoSitePlusiP08228.
SwissPalmiP08228.

2D gel databases

DOSAC-COBS-2DPAGEP08228.
REPRODUCTION-2DPAGEIPI00130589.
P08228.
SWISS-2DPAGEP08228.
UCD-2DPAGEP08228.

Proteomic databases

EPDiP08228.
MaxQBiP08228.
PaxDbiP08228.
PeptideAtlasiP08228.
PRIDEiP08228.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023707; ENSMUSP00000023707; ENSMUSG00000022982.
GeneIDi20655.
KEGGimmu:20655.
UCSCiuc007zvz.1. mouse.

Organism-specific databases

CTDi6647.
MGIiMGI:98351. Sod1.

Phylogenomic databases

eggNOGiKOG0441. Eukaryota.
COG2032. LUCA.
GeneTreeiENSGT00530000063226.
HOGENOMiHOG000263447.
HOVERGENiHBG000062.
InParanoidiP08228.
KOiK04565.
OMAiVCVLKGT.
OrthoDBiEOG091G0OG2.
PhylomeDBiP08228.
TreeFamiTF105131.

Enzyme and pathway databases

ReactomeiR-MMU-114608. Platelet degranulation.
R-MMU-3299685. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

ChiTaRSiSod1. mouse.
EvolutionaryTraceiP08228.
PROiP08228.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000022982.
CleanExiMM_SOD1.
GenevisibleiP08228. MM.

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]
ProtoNetiSearch...

Entry informationi

Entry nameiSODC_MOUSE
AccessioniPrimary (citable) accession number: P08228
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 189 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.