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Protein

Superoxide dismutase [Cu-Zn]

Gene

Sod1

Organism
Mus musculus (Mouse)
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.

<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:
  • 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
<p>This subsection of the ‘Function’ 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; 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

<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

Reactome - a knowledgebase of biological pathways and processes

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

<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)
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 16

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:98351 Sod1

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, 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 describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

40% reduction in hepatic GPX1 activity.1 Publication

<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 sources
<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_00001640622 – 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 sources1
Modified residuei4N6-succinyllysineCombined sources1
<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 cysteineBy similarity1
Modified residuei10N6-succinyllysineCombined sources1
<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 ↔ 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

<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

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

Encyclopedia of Proteome Dynamics

More...
EPDi
P08228

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P08228

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

More...
PaxDbi
P08228

PeptideAtlas

More...
PeptideAtlasi
P08228

PRoteomics IDEntifications database

More...
PRIDEi
P08228

2D gel databases

DOSAC-COBS 2D-PAGE database

More...
DOSAC-COBS-2DPAGEi
P08228

REPRODUCTION-2DPAGE

More...
REPRODUCTION-2DPAGEi
IPI00130589
P08228

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

More...
SWISS-2DPAGEi
P08228

University College Dublin 2-DE Proteome Database

More...
UCD-2DPAGEi
P08228

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P08228

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

More...
PhosphoSitePlusi
P08228

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P08228

<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

More...
Bgeei
ENSMUSG00000022982 Expressed in 306 organ(s), highest expression level in cumulus cell

CleanEx database of gene expression profiles

More...
CleanExi
MM_SOD1

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P08228 MM

<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.1 Publication

<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)

More...
BioGridi
203387, 29 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-2898 [Cu-Zn] Superoxide dismutase complex

Database of interacting proteins

More...
DIPi
DIP-48691N

Protein interaction database and analysis system

More...
IntActi
P08228, 53 interactors

Molecular INTeraction database

More...
MINTi
P08228

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000023707

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P08228

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

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SMRi
P08228

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P08228

<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

More...
eggNOGi
KOG0441 Eukaryota
COG2032 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000155551

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000263447

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG000062

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P08228

KEGG Orthology (KO)

More...
KOi
K04565

Identification of Orthologs from Complete Genome Data

More...
OMAi
MAMKAVC

Database of Orthologous Groups

More...
OrthoDBi
EOG091G0OG2

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P08228

TreeFam database of animal gene trees

More...
TreeFami
TF105131

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00305 Cu-Zn_Superoxide_Dismutase, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.200, 1 hit

Integrated resource of protein families, domains and functional sites

More...
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

More...
PANTHERi
PTHR10003 PTHR10003, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00080 Sod_Cu, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00068 CUZNDISMTASE

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49329 SSF49329, 1 hit

PROSITE; a protein domain and family database

More...
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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<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.

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
<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:iCAE548C66043BAC4
GO

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 conflicti102D → H in AAA40121 (PubMed:2022332).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS37395.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JQ0915

NCBI Reference Sequences

More...
RefSeqi
NP_035564.1, NM_011434.1

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Mm.276325
Mm.466779

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000023707; ENSMUSP00000023707; ENSMUSG00000022982

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
20655

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:20655

UCSC genome browser

More...
UCSCi
uc007zvz.1 mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
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, 29 interactors
ComplexPortaliCPX-2898 [Cu-Zn] Superoxide dismutase complex
DIPiDIP-48691N
IntActiP08228, 53 interactors
MINTiP08228
STRINGi10090.ENSMUSP00000023707

PTM databases

iPTMnetiP08228
PhosphoSitePlusiP08228
SwissPalmiP08228

2D gel databases

DOSAC-COBS-2DPAGEiP08228
REPRODUCTION-2DPAGEiIPI00130589
P08228
SWISS-2DPAGEiP08228
UCD-2DPAGEiP08228

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

Comparative Toxicogenomics Database

More...
CTDi
6647
MGIiMGI:98351 Sod1

Phylogenomic databases

eggNOGiKOG0441 Eukaryota
COG2032 LUCA
GeneTreeiENSGT00940000155551
HOGENOMiHOG000263447
HOVERGENiHBG000062
InParanoidiP08228
KOiK04565
OMAiMAMKAVC
OrthoDBiEOG091G0OG2
PhylomeDBiP08228
TreeFamiTF105131

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
Sod1 mouse
EvolutionaryTraceiP08228

Protein Ontology

More...
PROi
PR:P08228

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000022982 Expressed in 306 organ(s), highest expression level in cumulus cell
CleanExiMM_SOD1
GenevisibleiP08228 MM

Family and domain databases

CDDicd00305 Cu-Zn_Superoxide_Dismutase, 1 hit
Gene3Di2.60.40.200, 1 hit
InterProiView 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
PANTHERiPTHR10003 PTHR10003, 1 hit
PfamiView protein in Pfam
PF00080 Sod_Cu, 1 hit
PRINTSiPR00068 CUZNDISMTASE
SUPFAMiSSF49329 SSF49329, 1 hit
PROSITEiView protein in PROSITE
PS00087 SOD_CU_ZN_1, 1 hit
PS00332 SOD_CU_ZN_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSODC_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P08228
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: December 5, 2018
This is version 204 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

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