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Protein

Superoxide dismutase [Cu-Zn]

Gene

SOD1

Organism
Pan troglodytes (Chimpanzee)
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
OrganismiPan troglodytes (Chimpanzee)
Taxonomic identifieri9598 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePan
Proteomesi
  • UP000002277 Componenti: Unplaced

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_00001640632 – 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

PaxDbiP60052.

Expressioni

Gene expression databases

BgeeiENSPTRG00000013847.

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9598.ENSPTRP00000023837.

Structurei

3D structure databases

ProteinModelPortaliP60052.
SMRiP60052.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Cu-Zn superoxide dismutase family.Curated

Phylogenomic databases

eggNOGiKOG0441. Eukaryota.
COG2032. LUCA.
GeneTreeiENSGT00530000063226.
HOGENOMiHOG000263447.
HOVERGENiHBG000062.
InParanoidiP60052.
KOiK04565.
OMAiVCVLKGT.
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.

P60052-1 [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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB087266 mRNA. Translation: BAC20345.1.
RefSeqiNP_001009025.1. NM_001009025.1.
UniGeneiPtr.428.

Genome annotation databases

EnsembliENSPTRT00000025826; ENSPTRP00000023837; ENSPTRG00000013847.
GeneIDi449637.
KEGGiptr:449637.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB087266 mRNA. Translation: BAC20345.1.
RefSeqiNP_001009025.1. NM_001009025.1.
UniGeneiPtr.428.

3D structure databases

ProteinModelPortaliP60052.
SMRiP60052.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9598.ENSPTRP00000023837.

Proteomic databases

PaxDbiP60052.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSPTRT00000025826; ENSPTRP00000023837; ENSPTRG00000013847.
GeneIDi449637.
KEGGiptr:449637.

Organism-specific databases

CTDi6647.

Phylogenomic databases

eggNOGiKOG0441. Eukaryota.
COG2032. LUCA.
GeneTreeiENSGT00530000063226.
HOGENOMiHOG000263447.
HOVERGENiHBG000062.
InParanoidiP60052.
KOiK04565.
OMAiVCVLKGT.
OrthoDBiEOG091G0OG2.
TreeFamiTF105131.

Gene expression databases

BgeeiENSPTRG00000013847.

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_PANTR
AccessioniPrimary (citable) accession number: P60052
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 21, 2003
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 109 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

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.