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Protein

Superoxide dismutase [Mn], mitochondrial

Gene

SOD2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi50 – 501Manganese
Metal bindingi98 – 981Manganese
Metal bindingi183 – 1831Manganese
Metal bindingi187 – 1871Manganese

GO - Molecular functioni

  1. DNA binding Source: Ensembl
  2. identical protein binding Source: IntAct
  3. manganese ion binding Source: UniProtKB
  4. oxygen binding Source: Ensembl
  5. superoxide dismutase activity Source: UniProtKB

GO - Biological processi

  1. age-dependent response to reactive oxygen species Source: UniProtKB
  2. cellular response to ethanol Source: Ensembl
  3. detection of oxygen Source: Ensembl
  4. erythrophore differentiation Source: Ensembl
  5. glutathione metabolic process Source: Ensembl
  6. heart development Source: Ensembl
  7. hemopoiesis Source: Ensembl
  8. hydrogen peroxide biosynthetic process Source: Ensembl
  9. intrinsic apoptotic signaling pathway in response to DNA damage Source: Ensembl
  10. intrinsic apoptotic signaling pathway in response to oxidative stress Source: Ensembl
  11. iron ion homeostasis Source: Ensembl
  12. liver development Source: Ensembl
  13. locomotory behavior Source: Ensembl
  14. negative regulation of cell proliferation Source: BHF-UCL
  15. negative regulation of fat cell differentiation Source: Ensembl
  16. negative regulation of fibroblast proliferation Source: Ensembl
  17. negative regulation of neuron apoptotic process Source: BHF-UCL
  18. negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: BHF-UCL
  19. neuron development Source: Ensembl
  20. oxygen homeostasis Source: BHF-UCL
  21. positive regulation of nitric oxide biosynthetic process Source: Ensembl
  22. post-embryonic development Source: Ensembl
  23. protein homotetramerization Source: UniProtKB
  24. regulation of blood pressure Source: BHF-UCL
  25. regulation of catalytic activity Source: Ensembl
  26. regulation of mitochondrial membrane potential Source: Ensembl
  27. regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  28. release of cytochrome c from mitochondria Source: BHF-UCL
  29. removal of superoxide radicals Source: BHF-UCL
  30. respiratory electron transport chain Source: Ensembl
  31. response to activity Source: Ensembl
  32. response to axon injury Source: Ensembl
  33. response to cadmium ion Source: Ensembl
  34. response to cold Source: Ensembl
  35. response to drug Source: Ensembl
  36. response to electrical stimulus Source: Ensembl
  37. response to gamma radiation Source: Ensembl
  38. response to hydrogen peroxide Source: Ensembl
  39. response to hyperoxia Source: Ensembl
  40. response to hypoxia Source: Ensembl
  41. response to immobilization stress Source: Ensembl
  42. response to isolation stress Source: Ensembl
  43. response to L-ascorbic acid Source: Ensembl
  44. response to lipopolysaccharide Source: Ensembl
  45. response to magnetism Source: Ensembl
  46. response to manganese ion Source: Ensembl
  47. response to reactive oxygen species Source: Reactome
  48. response to selenium ion Source: Ensembl
  49. response to silicon dioxide Source: Ensembl
  50. response to superoxide Source: BHF-UCL
  51. response to zinc ion Source: Ensembl
  52. superoxide anion generation Source: Ensembl
  53. superoxide metabolic process Source: UniProtKB
  54. vasodilation by acetylcholine involved in regulation of systemic arterial blood pressure Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi1.15.1.1. 2681.
ReactomeiREACT_264249. Detoxification of Reactive Oxygen Species.

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
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:11180. SOD2.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProtKB
  2. mitochondrial inner membrane Source: Ensembl
  3. mitochondrial matrix Source: BHF-UCL
  4. mitochondrial nucleoid Source: Ensembl
  5. mitochondrion Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Microvascular complications of diabetes 6 (MVCD6)

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi58 – 581Y → A, H, N, V or F: Reduced enzyme activity. 1 Publication
Mutagenesisi58 – 581Y → F: Loss of nitration. Enhanced dityrosine formation on peroxynitrite treatment. 1 Publication

Organism-specific databases

MIMi612634. phenotype.
PharmGKBiPA36017.

Protein family/group databases

Allergomei784. Hom s MnSOD.

Polymorphism and mutation databases

BioMutaiSOD2.
DMDMi134665.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2424Mitochondrion4 PublicationsAdd
BLAST
Chaini25 – 222198Superoxide dismutase [Mn], mitochondrialPRO_0000032869Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei58 – 581Nitrated tyrosine2 Publications
Modified residuei68 – 681N6-acetyllysine; alternate1 Publication
Modified residuei68 – 681N6-succinyllysine; alternateBy similarity
Modified residuei75 – 751N6-acetyllysine; alternateBy similarity
Modified residuei75 – 751N6-succinyllysine; alternateBy similarity
Modified residuei114 – 1141N6-acetyllysineBy similarity
Modified residuei122 – 1221N6-acetyllysine; alternateBy similarity
Modified residuei122 – 1221N6-succinyllysine; alternateBy similarity
Modified residuei130 – 1301N6-acetyllysine; alternate1 Publication
Modified residuei130 – 1301N6-succinyllysine; alternateBy similarity
Modified residuei202 – 2021N6-acetyllysineBy similarity

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

Keywords - PTMi

Acetylation, Nitration

Proteomic databases

MaxQBiP04179.
PaxDbiP04179.
PRIDEiP04179.

2D gel databases

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

PTM databases

PhosphoSiteiP04179.

Expressioni

Inductioni

Expression is regulated by KRIT1.1 Publication

Gene expression databases

BgeeiP04179.
CleanExiHS_SOD2.
ExpressionAtlasiP04179. baseline and differential.
GenevestigatoriP04179.

Organism-specific databases

HPAiCAB002013.
HPA001814.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Binary interactionsi

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

Protein-protein interaction databases

BioGridi112531. 19 interactions.
IntActiP04179. 20 interactions.
MINTiMINT-5002369.
STRINGi9606.ENSP00000337127.

Structurei

Secondary structure

1
222
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni35 – 417Combined sources
Helixi44 – 529Combined sources
Helixi54 – 7421Combined sources
Helixi78 – 836Combined sources
Helixi85 – 10319Combined sources
Helixi115 – 12511Combined sources
Helixi128 – 14013Combined sources
Beta strandi144 – 15310Combined sources
Turni154 – 1574Combined sources
Beta strandi158 – 1658Combined sources
Helixi170 – 1745Combined sources
Beta strandi177 – 1837Combined sources
Helixi186 – 1883Combined sources
Helixi190 – 1934Combined sources
Helixi197 – 2048Combined sources
Helixi205 – 2073Combined sources
Helixi210 – 21910Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP04179.
SMRiP04179. Positions 25-222.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04179.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0605.
GeneTreeiENSGT00390000011877.
HOGENOMiHOG000013583.
HOVERGENiHBG004451.
InParanoidiP04179.
KOiK04564.
OrthoDBiEOG7FV3R5.
PhylomeDBiP04179.
TreeFamiTF105132.

Family and domain databases

InterProiIPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]
PANTHERiPTHR11404. PTHR11404. 1 hit.
PfamiPF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000349. SODismutase. 1 hit.
PRINTSiPR01703. MNSODISMTASE.
SUPFAMiSSF46609. SSF46609. 1 hit.
SSF54719. SSF54719. 1 hit.
PROSITEiPS00088. SOD_MN. 1 hit.
[Graphical view]

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 RQLAPALGYL 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):24,722
Last modified:April 1, 1990 - v2
Checksum:i648435C080E6E47B
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):20,696
Checksum:i1C427B935D71B90F
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):18,234
Checksum:i4256776626017959
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141A → P (PubMed:3399391).Curated
Sequence conflicti65 – 651T → N in CAA42066 (PubMed:1699607).Curated
Sequence conflicti65 – 651T → N in CAA33228 (PubMed:1699607).Curated
Sequence conflicti66 – 661E → Q (PubMed:1988135).Curated
Sequence conflicti112 – 1121E → Q (PubMed:1988135).Curated
Sequence conflicti123 – 1231R → L in CAA30687 (PubMed:3399391).Curated
Sequence conflicti133 – 1331E → Q (PubMed:1988135).Curated
Sequence conflicti148 – 1492Missing (PubMed:1988135).Curated
Sequence conflicti155 – 1551E → Q in CAA68533 (PubMed:3684581).Curated
Sequence conflicti155 – 1551E → Q (PubMed:1988135).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti10 – 101S → I.1 Publication
Corresponds to variant rs5746096 [ dbSNP | Ensembl ].
VAR_019363
Natural varianti16 – 161A → V Very frequent polymorphism; associated with susceptibility to diabetic nephropathy in Japanese patients with type 2 diabetes. 8 Publications
Corresponds to variant rs4880 [ dbSNP | Ensembl ].
VAR_016183
Natural varianti66 – 661E → V.1 Publication
Corresponds to variant rs5746097 [ dbSNP | Ensembl ].
VAR_019364
Natural varianti76 – 761G → R.
Corresponds to variant rs4987023 [ dbSNP | Ensembl ].
VAR_025898
Natural varianti82 – 821I → T.1 Publication
Corresponds to variant rs1141718 [ dbSNP | Ensembl ].
VAR_007165
Natural varianti156 – 1561R → W.1 Publication
Corresponds to variant rs5746129 [ dbSNP | Ensembl ].
VAR_019365

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4646Missing in isoform 4. 1 PublicationVSP_053761Add
BLAST
Alternative sequencei75 – 11339Missing in isoform 2. 1 PublicationVSP_042558Add
BLAST
Alternative sequencei115 – 17460Missing in isoform 3. 1 PublicationVSP_053762Add
BLAST

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. Translation: CAI21845.1.
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]
PIRiS13162. DSHUN.
RefSeqiNP_000627.2. NM_000636.2.
NP_001019636.1. NM_001024465.1.
NP_001019637.1. NM_001024466.1.
UniGeneiHs.487046.

Genome annotation databases

EnsembliENST00000546087; ENSP00000442920; ENSG00000112096. [P04179-4]
GeneIDi6648.
KEGGihsa:6648.
UCSCiuc003qsg.3. human. [P04179-1]
uc003qsh.3. human. [P04179-2]
uc011efu.1. human.

Polymorphism and mutation databases

BioMutaiSOD2.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Superoxide dismutase entry

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. Translation: CAI21845.1.
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]
PIRiS13162. DSHUN.
RefSeqiNP_000627.2. NM_000636.2.
NP_001019636.1. NM_001024465.1.
NP_001019637.1. NM_001024466.1.
UniGeneiHs.487046.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP04179.
SMRiP04179. Positions 25-222.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112531. 19 interactions.
IntActiP04179. 20 interactions.
MINTiMINT-5002369.
STRINGi9606.ENSP00000337127.

Protein family/group databases

Allergomei784. Hom s MnSOD.

PTM databases

PhosphoSiteiP04179.

Polymorphism and mutation databases

BioMutaiSOD2.
DMDMi134665.

2D gel databases

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

Proteomic databases

MaxQBiP04179.
PaxDbiP04179.
PRIDEiP04179.

Protocols and materials databases

DNASUi6648.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000546087; ENSP00000442920; ENSG00000112096. [P04179-4]
GeneIDi6648.
KEGGihsa:6648.
UCSCiuc003qsg.3. human. [P04179-1]
uc003qsh.3. human. [P04179-2]
uc011efu.1. human.

Organism-specific databases

CTDi6648.
GeneCardsiGC06M160102.
HGNCiHGNC:11180. SOD2.
HPAiCAB002013.
HPA001814.
MIMi147460. gene.
612634. phenotype.
neXtProtiNX_P04179.
PharmGKBiPA36017.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0605.
GeneTreeiENSGT00390000011877.
HOGENOMiHOG000013583.
HOVERGENiHBG004451.
InParanoidiP04179.
KOiK04564.
OrthoDBiEOG7FV3R5.
PhylomeDBiP04179.
TreeFamiTF105132.

Enzyme and pathway databases

BRENDAi1.15.1.1. 2681.
ReactomeiREACT_264249. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

ChiTaRSiSOD2. human.
EvolutionaryTraceiP04179.
GeneWikiiSOD2.
GenomeRNAii6648.
NextBioi25907.
PROiP04179.
SOURCEiSearch...

Gene expression databases

BgeeiP04179.
CleanExiHS_SOD2.
ExpressionAtlasiP04179. baseline and differential.
GenevestigatoriP04179.

Family and domain databases

InterProiIPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]
PANTHERiPTHR11404. PTHR11404. 1 hit.
PfamiPF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000349. SODismutase. 1 hit.
PRINTSiPR01703. MNSODISMTASE.
SUPFAMiSSF46609. SSF46609. 1 hit.
SSF54719. SSF54719. 1 hit.
PROSITEiPS00088. SOD_MN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Synthesis and processing of the precursor for human mangano-superoxide dismutase."
    Wispe J.R., Clark J.C., Burhans M.S., Kropp K.E., Korfhagen T.R., Whitsett J.A.
    Biochim. Biophys. Acta 994:30-36(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Isolation of cDNAs encoding human manganese superoxide dismutase."
    Heckl K.
    Nucleic Acids Res. 16:6224-6224(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-16.
  4. "Isolation and characterization of complementary DNAs encoding human manganese-containing superoxide dismutase."
    Ho Y.-S., Crapo J.D.
    FEBS Lett. 229:256-260(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  5. "Manganese superoxide dismutase: nucleotide and deduced amino acid sequence of a cDNA encoding a new human transcript."
    Church S.L.
    Biochim. Biophys. Acta 1087:250-252(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  6. "Complementary DNA encoding human colon cancer manganese superoxide dismutase and the expression of its gene in human cells."
    St Clair D.K., Holland J.C.
    Cancer Res. 51:939-943(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Colon.
  7. "Molecular structure and organization of the human manganese superoxide dismutase gene."
    Wan X.S., Devalaraja M.N., St Clair D.K.
    DNA Cell Biol. 13:1127-1136(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  8. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT VAL-16.
  9. NIEHS SNPs program
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ILE-10; VAL-16; VAL-66 AND TRP-156.
  10. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4), VARIANT VAL-16.
    Tissue: Hippocampus, Testis, Tongue and Uterus.
  11. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-16.
  12. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-16.
  13. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT VAL-16.
    Tissue: Lung.
  14. "The primary structure of human liver manganese superoxide dismutase."
    Barra D., Schinina M.E., Simmaco M., Bannister J.V., Bannister W.H., Rotilio G., Bossa F.
    J. Biol. Chem. 259:12595-12601(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 25-222.
  15. "The human myocardial two-dimensional gel protein database: update 1994."
    Corbett J.M., Wheeler C.H., Baker C.S., Yacoub M.H., Dunn M.J.
    Electrophoresis 15:1459-1465(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 25-39.
    Tissue: Heart.
  16. "The major protein expression profile and two-dimensional protein database of human heart."
    Kovalyov L.I., Shishkin S.S., Efimochkin A.S., Kovalyova M.A., Ershova E.S., Egorov T.A., Musalyamov A.K.
    Electrophoresis 16:1160-1169(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 25-39.
    Tissue: Heart.
  17. "Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2."
    Rasmussen R.K., Ji H., Eddes J.S., Moritz R.L., Reid G.E., Simpson R.J., Dorow D.S.
    Electrophoresis 18:588-598(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 25-39.
    Tissue: Mammary carcinoma.
  18. "Tyrosine modifications and inactivation of active site manganese superoxide dismutase mutant (Y34F) by peroxynitrite."
    MacMillan-Crow L.A., Thompson J.A.
    Arch. Biochem. Biophys. 366:82-88(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NITRATION AT TYR-58, FUNCTION, MUTAGENESIS OF TYR-58.
  19. "Detection of sequence-specific tyrosine nitration of manganese SOD and SERCA in cardiovascular disease and aging."
    Xu S., Ying J., Jiang B., Guo W., Adachi T., Sharov V., Lazar H., Menzoian J., Knyushko T.V., Bigelow D., Schoeneich C., Cohen R.A.
    Am. J. Physiol. 290:H2220-H2227(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NITRATION AT TYR-58.
  20. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-68 AND LYS-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "KRIT1 regulates the homeostasis of intracellular reactive oxygen species."
    Goitre L., Balzac F., Degani S., Degan P., Marchi S., Pinton P., Retta S.F.
    PLoS ONE 5:E11786-E11786(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  24. "The structure of human mitochondrial manganese superoxide dismutase reveals a novel tetrameric interface of two 4-helix bundles."
    Borgstahl G.E.O., Parge H.E., Hickey M.J., Beyer W.F. Jr., Hallewell R.A., Tainer J.A.
    Cell 71:107-118(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
  25. "Human mitochondrial manganese superoxide dismutase polymorphic variant Ile58Thr reduces activity by destabilizing the tetrameric interface."
    Borgstahl G.E.O., Parge H.E., Hickey M.J., Johnson M.J., Boissinot M., Hallewell R.A., Lepock J.R., Cabelli D.E., Tainer J.A.
    Biochemistry 35:4287-4297(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF VARIANT THR-82.
  26. "Probing the active site of human manganese superoxide dismutase: the role of glutamine 143."
    Hsieh Y., Guan Y., Tu C., Bratt P.J., Angerhofer A., Lepock J.R., Hickey M.J., Tainer J.A., Nick H.S., Silverman D.N.
    Biochemistry 37:4731-4739(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT ASN-167.
  27. "Crystal structure of Y34F mutant human mitochondrial manganese superoxide dismutase and the functional role of tyrosine 34."
    Guan Y., Hickey M.J., Borgstahl G.E.O., Hallewell R.A., Lepock J.R., O'Connor D., Hsieh Y., Nick H.S., Silverman D.N., Tainer J.A.
    Biochemistry 37:4722-4730(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT TYR-58.
  28. "Multiple replacements of glutamine 143 in human manganese superoxide dismutase: effects on structure, stability, and catalysis."
    Leveque V.J.-P., Stroupe M.E., Lepock J.R., Cabelli D.E., Tainer J.A., Nick H.S., Silverman D.N.
    Biochemistry 39:7131-7137(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS) OF MUTANT ALA-167.
  29. "Kinetic analysis of product inhibition in human manganese superoxide dismutase."
    Hearn A.S., Stroupe M.E., Cabelli D.E., Lepock J.R., Tainer J.A., Nick H.S., Silverman D.N.
    Biochemistry 40:12051-12058(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF MUTANT ALA-185.
  30. "Contribution of human manganese superoxide dismutase tyrosine 34 to structure and catalysis."
    Perry J.J., Hearn A.S., Cabelli D.E., Nick H.S., Tainer J.A., Silverman D.N.
    Biochemistry 48:3417-3424(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF MUTANTS ALA/ASN/HIS/VAL-58 IN COMPLEX WITH MANGANESE IONS, SUBUNIT.
  31. "The polymorphism of manganese superoxide dismutase is associated with diabetic nephropathy in Japanese type 2 diabetic patients."
    Nomiyama T., Tanaka Y., Piao L., Nagasaka K., Sakai K., Ogihara T., Nakajima K., Watada H., Kawamori R.
    J. Hum. Genet. 48:138-141(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT VAL-16, ASSOCIATION WITH DIABETIC NEPHROPATHY SUSCEPTIBILITY.

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 historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: April 1, 1990
Last modified: April 29, 2015
This is version 189 of the entry and version 2 of the sequence. [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

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.