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Protein

Superoxide dismutase [Cu-Zn]

Gene

SOD1

Organism
Macaca mulatta (Rhesus macaque)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase

Keywords - Ligandi

Copper, 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

GO - Cellular componenti

Complete GO annotation...

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. differential.

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9544.ENSMMUP00000002283.

Structurei

3D structure databases

ProteinModelPortaliQ8HXQ0.
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.
OMAiKVWGSIT.
OrthoDBiEOG091G0OG2.
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.

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.

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliQ8HXQ0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9544.ENSMMUP00000002283.

Proteomic databases

PRIDEiQ8HXQ0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMMUT00000002415; ENSMMUP00000002283; ENSMMUG00000001711.
GeneIDi574096.
KEGGimcc:574096.

Organism-specific databases

CTDi6647.

Phylogenomic databases

eggNOGiKOG0441. Eukaryota.
COG2032. LUCA.
GeneTreeiENSGT00530000063226.
HOGENOMiHOG000263447.
HOVERGENiHBG000062.
InParanoidiQ8HXQ0.
KOiK04565.
OMAiKVWGSIT.
OrthoDBiEOG091G0OG2.
TreeFamiTF105131.

Gene expression databases

BgeeiENSMMUG00000001711.
ExpressionAtlasiQ8HXQ0. differential.

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_MACMU
AccessioniPrimary (citable) accession number: Q8HXQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 21, 2003
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 108 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.