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P60052 (SODC_PANTR) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Superoxide dismutase [Cu-Zn]

EC=1.15.1.1
Gene names
Name:SOD1
OrganismPan troglodytes (Chimpanzee) [Reference proteome]
Taxonomic identifier9598 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePan

Protein attributes

Sequence length154 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Destroys radicals which are normally produced within the cells and which are toxic to biological systems.

Catalytic activity

2 superoxide + 2 H+ = O2 + H2O2.

Cofactor

Binds 1 copper ion per subunit By similarity.

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Post-translational modification

Palmitoylation helps nuclear targeting and decreases catalytic activity By similarity.

Succinylation, adjacent to copper catalytic site probably inhibit activity. Desuccinylated by SIRT5, enhancing activity By similarity.

Sequence similarities

Belongs to the Cu-Zn superoxide dismutase family.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   LigandCopper
Metal-binding
Zinc
   Molecular functionAntioxidant
Oxidoreductase
   PTMAcetylation
Disulfide bond
Lipoprotein
Palmitate
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of MAPK activity

Inferred from sequence or structural similarity. Source: UniProtKB

anterograde axon cargo transport

Inferred from electronic annotation. Source: Ensembl

apoptotic DNA fragmentation

Inferred from sequence or structural similarity. Source: UniProtKB

auditory receptor cell stereocilium organization

Inferred from sequence or structural similarity. Source: UniProtKB

cell aging

Inferred from sequence or structural similarity. Source: UniProtKB

cellular iron ion homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

double-strand break repair

Inferred from sequence or structural similarity. Source: UniProtKB

embryo implantation

Inferred from sequence or structural similarity. Source: UniProtKB

glutathione metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

heart contraction

Inferred from sequence or structural similarity. Source: UniProtKB

hydrogen peroxide biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

locomotory behavior

Inferred from sequence or structural similarity. Source: UniProtKB

muscle cell cellular homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

myeloid cell homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cholesterol biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of neuron apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

neurofilament cytoskeleton organization

Inferred from sequence or structural similarity. Source: UniProtKB

ovarian follicle development

Inferred from sequence or structural similarity. Source: UniProtKB

peripheral nervous system myelin maintenance

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of catalytic activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cytokine production

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of intrinsic apoptotic signaling pathway in response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

positive regulation of superoxide anion generation

Inferred from electronic annotation. Source: Ensembl

reactive oxygen species metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of Rac GTPase activity

Inferred from electronic annotation. Source: Ensembl

regulation of blood pressure

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of mitochondrial membrane potential

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of multicellular organism growth

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of protein kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

relaxation of vascular smooth muscle

Inferred from sequence or structural similarity. Source: UniProtKB

removal of superoxide radicals

Inferred from sequence or structural similarity. Source: UniProtKB

response to axon injury

Inferred from sequence or structural similarity. Source: UniProtKB

response to drug

Inferred from sequence or structural similarity. Source: UniProtKB

response to ethanol

Inferred from sequence or structural similarity. Source: UniProtKB

response to heat

Inferred from sequence or structural similarity. Source: UniProtKB

response to hydrogen peroxide

Inferred from sequence or structural similarity. Source: UniProtKB

response to organic substance

Inferred from sequence or structural similarity. Source: UniProtKB

response to superoxide

Inferred from sequence or structural similarity. Source: UniProtKB

retina homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

retrograde axon cargo transport

Inferred from electronic annotation. Source: Ensembl

sensory perception of sound

Inferred from sequence or structural similarity. Source: UniProtKB

spermatogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

superoxide anion generation

Inferred from electronic annotation. Source: Ensembl

superoxide metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

transmission of nerve impulse

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasmic vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

dendrite cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular matrix

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular space

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrion

Inferred from sequence or structural similarity. Source: UniProtKB

neuronal cell body

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: Ensembl

protein complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionchaperone binding

Inferred from sequence or structural similarity. Source: UniProtKB

copper ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein phosphatase 2B binding

Inferred from sequence or structural similarity. Source: UniProtKB

superoxide dismutase activity

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 154153Superoxide dismutase [Cu-Zn]
PRO_0000164063

Sites

Metal binding471Copper; catalytic By similarity
Metal binding491Copper; catalytic By similarity
Metal binding641Copper; catalytic By similarity
Metal binding641Zinc; structural By similarity
Metal binding721Zinc; structural By similarity
Metal binding811Zinc; structural By similarity
Metal binding841Zinc; structural By similarity
Metal binding1211Copper; catalytic By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue41N6-succinyllysine By similarity
Modified residue101N6-succinyllysine By similarity
Modified residue921N6-succinyllysine By similarity
Modified residue991Phosphoserine By similarity
Modified residue1231N6-acetyllysine; alternate By similarity
Modified residue1231N6-succinyllysine; alternate By similarity
Modified residue1371N6-acetyllysine; alternate By similarity
Modified residue1371N6-succinyllysine; alternate By similarity
Lipidation71S-palmitoyl cysteine By similarity
Disulfide bond58 ↔ 147 By similarity

Sequences

Sequence LengthMass (Da)Tools
P60052 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 25CA38DA8D564483

FASTA15415,936
        10         20         30         40         50         60 
MATKAVCVLK GDGPVQGIIN FEQKESNGPV KVWGSIKGLT EGLHGFHVHE FGDNTAGCTS 

        70         80         90        100        110        120 
AGPHFNPLSR KHGGPKDEER HVGDLGNVTA DKDGVADVSI EDSVISLSGD HCIIGRTLVV 

       130        140        150 
HEKADDLGKG GNEESTKTGN AGSRLACGVI GIAQ 

« Hide

References

[1]"Structure, molecular evolution, and gene expression of primate superoxide dismutases."
Fukuhara R., Tezuka T., Kageyama T.
Gene 296:99-109(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB087266 mRNA. Translation: BAC20345.1.
RefSeqNP_001009025.1. NM_001009025.1.
UniGenePtr.428.

3D structure databases

ProteinModelPortalP60052.
SMRP60052. Positions 2-154.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9598.ENSPTRP00000056696.

Chemistry

BindingDBP60052.

Proteomic databases

PRIDEP60052.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSPTRT00000025826; ENSPTRP00000023837; ENSPTRG00000013847.
GeneID449637.
KEGGptr:449637.

Organism-specific databases

CTD6647.

Phylogenomic databases

eggNOGCOG2032.
GeneTreeENSGT00530000063226.
HOGENOMHOG000263447.
HOVERGENHBG000062.
KOK04565.
OMAEIEVKLH.
OrthoDBEOG776SR4.
TreeFamTF105131.

Family and domain databases

Gene3D2.60.40.200. 1 hit.
InterProIPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PfamPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSPR00068. CUZNDISMTASE.
SUPFAMSSF49329. SSF49329. 1 hit.
PROSITEPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20832742.

Entry information

Entry nameSODC_PANTR
AccessionPrimary (citable) accession number: P60052
Entry history
Integrated into UniProtKB/Swiss-Prot: November 21, 2003
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families