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Protein

Superoxide dismutase [Cu-Zn]

Gene

SOD1

Organism
Macaca mulatta (Rhesus macaque)
Status
Reviewed-Annotation score: -Experimental evidence at transcript 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; structuralBy similarity1
Metal bindingi72Zinc; structuralBy similarity1
Metal bindingi81Zinc; structuralBy similarity1
Metal bindingi84Zinc; structuralBy similarity1
Metal bindingi121Copper; catalyticBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAntioxidant, Oxidoreductase
LigandCopper, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Cu-Zn] (EC:1.15.1.1)
Gene namesi
Name:SOD1
OrganismiMacaca mulatta (Rhesus macaque)
Taxonomic identifieri9544 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca
Proteomesi
  • UP000006718 Componenti: Chromosome 3

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001640612 – 154Superoxide dismutase [Cu-Zn]Add BLAST153

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei4N6-succinyllysineBy similarity1
Lipidationi7S-palmitoyl cysteineBy similarity1
Modified residuei10N6-succinyllysineBy similarity1
Disulfide bondi58 ↔ 147By similarity
Modified residuei92N6-succinyllysineBy similarity1
Modified residuei99PhosphoserineBy similarity1
Modified residuei103PhosphoserineBy similarity1
Modified residuei106PhosphoserineBy similarity1
Modified residuei108PhosphoserineBy similarity1
Modified residuei123N6-acetyllysine; alternateBy similarity1
Modified residuei123N6-succinyllysine; alternateBy similarity1
Modified residuei137N6-acetyllysine; alternateBy similarity1
Modified residuei137N6-succinyllysine; alternateBy similarity1

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

PRIDEiQ8HXQ0

Expressioni

Gene expression databases

BgeeiENSMMUG00000001711
ExpressionAtlasiQ8HXQ0 baseline

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9544.ENSMMUP00000002283

Structurei

3D structure databases

ProteinModelPortaliQ8HXQ0
SMRiQ8HXQ0
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Cu-Zn superoxide dismutase family.Curated

Phylogenomic databases

eggNOGiKOG0441 Eukaryota
COG2032 LUCA
GeneTreeiENSGT00530000063226
HOGENOMiHOG000263447
HOVERGENiHBG000062
InParanoidiQ8HXQ0
KOiK04565
OMAiIHTFGDN
OrthoDBiEOG091G0OG2
TreeFamiTF105131

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

Sequencei

Sequence statusi: Complete.

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

Q8HXQ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAMKAVCVLK GDSPVQGTIN FEQKESNGPV KVWGSITGLT EGLHGFHVHQ
60 70 80 90 100
FGDNTQGCTS AGPHFNPLSR QHGGPKDEER HVGDLGNVTA GKDGVAKVSF
110 120 130 140 150
EDSVISLSGD HSIIGRTLVV HEKADDLGKG GNEESKKTGN AGGRLACGVI

GIAQ
Length:154
Mass (Da):15,983
Last modified:January 23, 2007 - v3
Checksum:i7B77BC2ED8CDDC2F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB087271 mRNA Translation: BAC20350.1
RefSeqiNP_001027976.1, NM_001032804.1
UniGeneiMmu.882

Genome annotation databases

EnsembliENSMMUT00000002415; ENSMMUP00000002283; ENSMMUG00000001711
GeneIDi574096
KEGGimcc:574096

Similar proteinsi

Entry informationi

Entry nameiSODC_MACMU
AccessioniPrimary (citable) accession number: Q8HXQ0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 21, 2003
Last sequence update: January 23, 2007
Last modified: April 25, 2018
This is version 116 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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