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Protein

Superoxide dismutase [Mn], mitochondrial

Gene

SOD2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.1 Publication

Catalytic activityi

2 superoxide + 2 H+ = O2 + H2O2.

Cofactori

Mn2+Note: Binds 1 Mn2+ ion per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi50Manganese1
Metal bindingi98Manganese1
Metal bindingi183Manganese1
Metal bindingi187Manganese1

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • manganese ion binding Source: UniProtKB
  • superoxide dismutase activity Source: UniProtKB

GO - Biological processi

  • acetylcholine-mediated vasodilation involved in regulation of systemic arterial blood pressure Source: BHF-UCL
  • age-dependent response to reactive oxygen species Source: UniProtKB
  • cellular response to oxidative stress Source: Reactome
  • interleukin-12-mediated signaling pathway Source: Reactome
  • negative regulation of cell proliferation Source: BHF-UCL
  • negative regulation of neuron apoptotic process Source: BHF-UCL
  • negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: BHF-UCL
  • negative regulation of vascular smooth muscle cell proliferation Source: BHF-UCL
  • oxygen homeostasis Source: BHF-UCL
  • positive regulation of cell migration Source: BHF-UCL
  • positive regulation of vascular associated smooth muscle cell apoptotic process Source: BHF-UCL
  • positive regulation of vascular smooth muscle cell differentiation involved in phenotypic switching Source: BHF-UCL
  • protein homotetramerization Source: UniProtKB
  • regulation of blood pressure Source: BHF-UCL
  • regulation of transcription by RNA polymerase II Source: UniProtKB
  • release of cytochrome c from mitochondria Source: BHF-UCL
  • removal of superoxide radicals Source: BHF-UCL
  • response to superoxide Source: BHF-UCL
  • superoxide metabolic process Source: UniProtKB

Keywordsi

Molecular functionOxidoreductase
LigandManganese, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS03515-MONOMER
BRENDAi1.15.1.1 2681
ReactomeiR-HSA-2151201 Transcriptional activation of mitochondrial biogenesis
R-HSA-3299685 Detoxification of Reactive Oxygen Species
R-HSA-8862803 Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models
R-HSA-8950505 Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation
SIGNORiP04179

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Mn], mitochondrial (EC:1.15.1.1)
Gene namesi
Name:SOD2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

EuPathDBiHostDB:ENSG00000112096.16
HGNCiHGNC:11180 SOD2
MIMi147460 gene
neXtProtiNX_P04179

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

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Microvascular complications of diabetes 6 (MVCD6)2 Publications
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionPathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis.
See also OMIM:612634

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi58Y → A, H, N, V or F: Reduced enzyme activity. 1 Publication1
Mutagenesisi58Y → F: Loss of nitration. Enhanced dityrosine formation on peroxynitrite treatment. 1 Publication1

Organism-specific databases

DisGeNETi6648
MalaCardsiSOD2
MIMi612634 phenotype
OpenTargetsiENSG00000112096
PharmGKBiPA36017

Protein family/group databases

Allergomei784 Hom s MnSOD

Chemistry databases

DrugBankiDB04436 3-Fluorotyrosine
DB03297 Benzylsulfinic Acid

Polymorphism and mutation databases

BioMutaiSOD2
DMDMi134665

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 24Mitochondrion4 PublicationsAdd BLAST24
ChainiPRO_000003286925 – 222Superoxide dismutase [Mn], mitochondrialAdd BLAST198

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei58Nitrated tyrosine2 Publications1
Modified residuei68N6-acetyllysine; alternateCombined sources1
Modified residuei68N6-succinyllysine; alternateBy similarity1
Modified residuei75N6-acetyllysine; alternateBy similarity1
Modified residuei75N6-succinyllysine; alternateBy similarity1
Modified residuei114N6-acetyllysineBy similarity1
Modified residuei122N6-acetyllysine; alternateBy similarity1
Modified residuei122N6-succinyllysine; alternateBy similarity1
Modified residuei130N6-acetyllysine; alternateCombined sources1
Modified residuei130N6-succinyllysine; alternateBy similarity1
Modified residuei202N6-acetyllysineBy similarity1

Post-translational modificationi

Nitrated under oxidative stress. Nitration coupled with oxidation inhibits the catalytic activity.2 Publications
Acetylation at Lys-122 decreases enzymatic activity. Deacetylated by SIRT3 upon exposure to ionizing radiations or after long fasting (By similarity).By similarity
Polyubiquitinated; leading to proteasomal degradation. Deubiquitinated by USP36 which increases protein stability.1 Publication

Keywords - PTMi

Acetylation, Nitration, Ubl conjugation

Proteomic databases

EPDiP04179
MaxQBiP04179
PaxDbiP04179
PeptideAtlasiP04179
PRIDEiP04179
TopDownProteomicsiP04179-1 [P04179-1]
P04179-2 [P04179-2]

2D gel databases

DOSAC-COBS-2DPAGEP04179
OGPiP04179
SWISS-2DPAGEP04179
UCD-2DPAGEP04179

PTM databases

iPTMnetiP04179
PhosphoSitePlusiP04179
SwissPalmiP04179

Expressioni

Inductioni

Expression is regulated by KRIT1.1 Publication

Gene expression databases

BgeeiENSG00000112096
CleanExiHS_SOD2
ExpressionAtlasiP04179 baseline and differential
GenevisibleiP04179 HS

Organism-specific databases

HPAiCAB002013
HPA001814

Interactioni

Subunit structurei

Homotetramer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-716989,EBI-716989

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi112531, 40 interactors
IntActiP04179, 21 interactors
MINTiP04179
STRINGi9606.ENSP00000356022

Structurei

Secondary structure

1222
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni35 – 41Combined sources7
Helixi44 – 52Combined sources9
Helixi54 – 74Combined sources21
Helixi78 – 83Combined sources6
Helixi85 – 103Combined sources19
Helixi115 – 125Combined sources11
Helixi128 – 140Combined sources13
Beta strandi144 – 153Combined sources10
Turni154 – 157Combined sources4
Beta strandi158 – 165Combined sources8
Helixi170 – 174Combined sources5
Beta strandi177 – 183Combined sources7
Helixi186 – 188Combined sources3
Helixi190 – 193Combined sources4
Helixi197 – 204Combined sources8
Helixi205 – 207Combined sources3
Helixi210 – 219Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AP5X-ray2.20A/B25-222[»]
1AP6X-ray1.90A/B25-222[»]
1EM1X-ray2.13A/B25-222[»]
1JA8X-ray2.12A/B25-222[»]
1LUVX-ray1.85A/B25-222[»]
1LUWX-ray2.30A/B25-222[»]
1MSDX-ray3.20A/B25-222[»]
1N0JX-ray2.20A/B25-222[»]
1N0NX-ray1.82A/B25-222[»]
1PL4X-ray1.47A/B/C/D25-222[»]
1PM9X-ray1.70A/B25-222[»]
1QNMX-ray2.30A/B25-222[»]
1SZXX-ray1.95A/B25-222[»]
1VARX-ray2.50A/B25-222[»]
1XDCX-ray1.85A/B25-222[»]
1XILX-ray1.53A/B25-222[»]
1ZSPX-ray1.90A/B25-222[»]
1ZTEX-ray1.85A/B/C/D25-222[»]
1ZUQX-ray2.00A/B25-222[»]
2ADPX-ray2.40A25-222[»]
2ADQX-ray2.40B25-222[»]
2GDSX-ray2.30A/B/C/D25-222[»]
2P4KX-ray1.48A/B/C/D25-222[»]
2QKAX-ray2.20A/C25-220[»]
2QKCX-ray2.30A/C25-220[»]
3C3SX-ray2.50A/B25-222[»]
3C3TX-ray2.20A/B25-222[»]
5GXOX-ray2.30A/B25-222[»]
5T30X-ray1.77A/B24-222[»]
5VF9X-ray1.82A/B24-222[»]
ProteinModelPortaliP04179
SMRiP04179
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04179

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0876 Eukaryota
COG0605 LUCA
GeneTreeiENSGT00390000011877
HOGENOMiHOG000013583
HOVERGENiHBG004451
InParanoidiP04179
KOiK04564
PhylomeDBiP04179
TreeFamiTF105132

Family and domain databases

Gene3Di1.10.287.990, 1 hit
2.40.500.20, 1 hit
InterProiView protein in InterPro
IPR001189 Mn/Fe_SOD
IPR019833 Mn/Fe_SOD_BS
IPR019832 Mn/Fe_SOD_C
IPR019831 Mn/Fe_SOD_N
IPR036324 Mn/Fe_SOD_N_sf
IPR036314 SOD_C_sf
PfamiView protein in Pfam
PF02777 Sod_Fe_C, 1 hit
PF00081 Sod_Fe_N, 1 hit
PIRSFiPIRSF000349 SODismutase, 1 hit
PRINTSiPR01703 MNSODISMTASE
SUPFAMiSSF46609 SSF46609, 1 hit
SSF54719 SSF54719, 1 hit
PROSITEiView protein in PROSITE
PS00088 SOD_MN, 1 hit

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P04179-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLSRAVCGTS RQLAPVLGYL GSRQKHSLPD LPYDYGALEP HINAQIMQLH
60 70 80 90 100
HSKHHAAYVN NLNVTEEKYQ EALAKGDVTA QIALQPALKF NGGGHINHSI
110 120 130 140 150
FWTNLSPNGG GEPKGELLEA IKRDFGSFDK FKEKLTAASV GVQGSGWGWL
160 170 180 190 200
GFNKERGHLQ IAACPNQDPL QGTTGLIPLL GIDVWEHAYY LQYKNVRPDY
210 220
LKAIWNVINW ENVTERYMAC KK
Length:222
Mass (Da):24,750
Last modified:December 20, 2017 - v3
Checksum:iCA047D7900AE5905
GO
Isoform 2 (identifier: P04179-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     75-113: Missing.

Note: No experimental confirmation available.
Show »
Length:183
Mass (Da):20,724
Checksum:i513D204966621B88
GO
Isoform 3 (identifier: P04179-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     115-174: Missing.

Note: No experimental confirmation available.
Show »
Length:162
Mass (Da):18,262
Checksum:i54271EA009B62959
GO
Isoform 4 (identifier: P04179-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-46: Missing.

Note: No experimental confirmation available.
Show »
Length:176
Mass (Da):19,730
Checksum:i5AB24FB15A80A1AF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti14A → P (PubMed:3399391).Curated1
Sequence conflicti65T → N in CAA42066 (PubMed:1699607).Curated1
Sequence conflicti65T → N in CAA33228 (PubMed:1699607).Curated1
Sequence conflicti66E → Q (PubMed:1988135).Curated1
Sequence conflicti112E → Q (PubMed:1988135).Curated1
Sequence conflicti123R → L in CAA30687 (PubMed:3399391).Curated1
Sequence conflicti133E → Q (PubMed:1988135).Curated1
Sequence conflicti148 – 149Missing (PubMed:1988135).Curated2
Sequence conflicti155E → Q in CAA68533 (PubMed:3684581).Curated1
Sequence conflicti155E → Q (PubMed:1988135).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01936310S → I1 PublicationCorresponds to variant dbSNP:rs5746096Ensembl.1
Natural variantiVAR_01618316V → A Frequent polymorphism; associated with a decreased susceptibility to diabetic nephropathy in Japanese and Chinese patients with type 2 diabetes. 2 PublicationsCorresponds to variant dbSNP:rs4880EnsemblClinVar.1
Natural variantiVAR_01936466E → V1 PublicationCorresponds to variant dbSNP:rs5746097Ensembl.1
Natural variantiVAR_02589876G → R. Corresponds to variant dbSNP:rs4987023Ensembl.1
Natural variantiVAR_00716582I → T1 PublicationCorresponds to variant dbSNP:rs1141718Ensembl.1
Natural variantiVAR_019365156R → W1 PublicationCorresponds to variant dbSNP:rs5746129Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0537611 – 46Missing in isoform 4. 1 PublicationAdd BLAST46
Alternative sequenceiVSP_04255875 – 113Missing in isoform 2. 1 PublicationAdd BLAST39
Alternative sequenceiVSP_053762115 – 174Missing in isoform 3. 1 PublicationAdd BLAST60

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59445 mRNA Translation: CAA42066.1
Y00472 mRNA Translation: CAA68533.1
Y00985 mRNA Translation: CAA68791.1
X07834 mRNA Translation: CAA30687.1
M36693 mRNA Translation: AAA36622.1
X15132 mRNA Translation: CAA33228.1
X14322 mRNA Translation: CAA32502.1
S77127 Genomic DNA Translation: AAD14248.1 Sequence problems.
BT006967 mRNA Translation: AAP35613.1
AY267901 Genomic DNA Translation: AAP03428.1
AK097395 mRNA Translation: BAG53464.1
AK296809 mRNA Translation: BAG59382.1
AK304766 mRNA Translation: BAG65521.1
AK313082 mRNA Translation: BAG35908.1
AL135914 Genomic DNA No translation available.
CH471051 Genomic DNA Translation: EAW47630.1
CH471051 Genomic DNA Translation: EAW47631.1
BC012423 mRNA Translation: AAH12423.1
CCDSiCCDS34564.1 [P04179-2]
CCDS5265.1 [P04179-1]
CCDS83141.1 [P04179-4]
CCDS83143.1 [P04179-3]
PIRiS13162 DSHUN
RefSeqiNP_000627.2, NM_000636.3 [P04179-1]
NP_001019636.1, NM_001024465.2 [P04179-1]
NP_001019637.1, NM_001024466.2 [P04179-2]
NP_001309743.1, NM_001322814.1 [P04179-2]
NP_001309744.1, NM_001322815.1 [P04179-3]
NP_001309746.1, NM_001322817.1 [P04179-4]
NP_001309748.1, NM_001322819.1 [P04179-4]
NP_001309749.1, NM_001322820.1 [P04179-4]
UniGeneiHs.487046

Genome annotation databases

EnsembliENST00000337404; ENSP00000337127; ENSG00000112096 [P04179-2]
ENST00000367054; ENSP00000356021; ENSG00000112096 [P04179-2]
ENST00000367055; ENSP00000356022; ENSG00000112096 [P04179-1]
ENST00000444946; ENSP00000404804; ENSG00000112096 [P04179-3]
ENST00000538183; ENSP00000446252; ENSG00000112096 [P04179-1]
ENST00000546087; ENSP00000442920; ENSG00000112096 [P04179-4]
GeneIDi6648
KEGGihsa:6648
UCSCiuc003qsf.6 human [P04179-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiSODM_HUMAN
AccessioniPrimary (citable) accession number: P04179
Secondary accession number(s): B2R7R1
, B3KUK2, B4DL20, B4E3K9, E1P5A9, P78434, Q16792, Q5TCM1, Q96EE6, Q9P2Z3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: December 20, 2017
Last modified: May 23, 2018
This is version 221 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

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