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P04179

- SODM_HUMAN

UniProt

P04179 - SODM_HUMAN

Protein

Superoxide dismutase [Mn], mitochondrial

Gene

SOD2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 182 (01 Oct 2014)
      Sequence version 2 (01 Apr 1990)
      Previous versions | rss
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    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

    Binds 1 manganese 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 drug Source: Ensembl
    35. response to electrical stimulus Source: Ensembl
    36. response to gamma radiation Source: Ensembl
    37. response to hydrogen peroxide Source: Ensembl
    38. response to hyperoxia Source: Ensembl
    39. response to hypoxia Source: Ensembl
    40. response to L-ascorbic acid Source: Ensembl
    41. response to lipopolysaccharide Source: Ensembl
    42. response to manganese ion Source: Ensembl
    43. response to selenium ion Source: Ensembl
    44. response to silicon dioxide Source: Ensembl
    45. response to superoxide Source: BHF-UCL
    46. response to zinc ion Source: Ensembl
    47. superoxide anion generation Source: Ensembl
    48. superoxide metabolic process Source: UniProtKB
    49. vasodilation by acetylcholine involved in regulation of systemic arterial blood pressure Source: BHF-UCL

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_172715. 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: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:11180. SOD2.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Microvascular complications of diabetes 6 (MVCD6) [MIM:612634]: Pathological 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.
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

    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.

    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

    ArrayExpressiP04179.
    BgeeiP04179.
    CleanExiHS_SOD2.
    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. 19 interactions.
    MINTiMINT-5002369.
    STRINGi9606.ENSP00000337127.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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. Align

    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

    MLSRAVCGTS RQLAPALGYL GSRQKHSLPD LPYDYGALEP HINAQIMQLH    50
    HSKHHAAYVN NLNVTEEKYQ EALAKGDVTA QIALQPALKF NGGGHINHSI 100
    FWTNLSPNGG GEPKGELLEA IKRDFGSFDK FKEKLTAASV GVQGSGWGWL 150
    GFNKERGHLQ IAACPNQDPL QGTTGLIPLL GIDVWEHAYY LQYKNVRPDY 200
    LKAIWNVINW ENVTERYMAC KK 222
    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.
    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:
    EMBL
    GenBank
    DDBJ
    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

    EnsembliENST00000337404; ENSP00000337127; ENSG00000112096.
    ENST00000367054; ENSP00000356021; ENSG00000112096.
    ENST00000367055; ENSP00000356022; ENSG00000112096.
    ENST00000444946; ENSP00000404804; ENSG00000112096.
    ENST00000538183; ENSP00000446252; ENSG00000112096.
    ENST00000546087; ENSP00000442920; ENSG00000112096. [P04179-4]
    GeneIDi6648.
    KEGGihsa:6648.
    UCSCiuc003qsg.3. human. [P04179-1]
    uc003qsh.3. human. [P04179-2]

    Polymorphism databases

    DMDMi134665.

    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS34564.1. [P04179-2 ]
    CCDS5265.1. [P04179-1 ]
    PIRi S13162. DSHUN.
    RefSeqi NP_000627.2. NM_000636.2.
    NP_001019636.1. NM_001024465.1.
    NP_001019637.1. NM_001024466.1.
    UniGenei Hs.487046.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AP5 X-ray 2.20 A/B 25-222 [» ]
    1AP6 X-ray 1.90 A/B 25-222 [» ]
    1EM1 X-ray 2.13 A/B 25-222 [» ]
    1JA8 X-ray 2.12 A/B 25-222 [» ]
    1LUV X-ray 1.85 A/B 25-222 [» ]
    1LUW X-ray 2.30 A/B 25-222 [» ]
    1MSD X-ray 3.20 A/B 25-222 [» ]
    1N0J X-ray 2.20 A/B 25-222 [» ]
    1N0N X-ray 1.82 A/B 25-222 [» ]
    1PL4 X-ray 1.47 A/B/C/D 25-222 [» ]
    1PM9 X-ray 1.70 A/B 25-222 [» ]
    1QNM X-ray 2.30 A/B 25-222 [» ]
    1SZX X-ray 1.95 A/B 25-222 [» ]
    1VAR X-ray 2.50 A/B 25-222 [» ]
    1XDC X-ray 1.85 A/B 25-222 [» ]
    1XIL X-ray 1.53 A/B 25-222 [» ]
    1ZSP X-ray 1.90 A/B 25-222 [» ]
    1ZTE X-ray 1.85 A/B/C/D 25-222 [» ]
    1ZUQ X-ray 2.00 A/B 25-222 [» ]
    2ADP X-ray 2.40 A 25-222 [» ]
    2ADQ X-ray 2.40 B 25-222 [» ]
    2GDS X-ray 2.30 A/B/C/D 25-222 [» ]
    2P4K X-ray 1.48 A/B/C/D 25-222 [» ]
    2QKA X-ray 2.20 A/C 25-220 [» ]
    2QKC X-ray 2.30 A/C 25-220 [» ]
    3C3S X-ray 2.50 A/B 25-222 [» ]
    3C3T X-ray 2.20 A/B 25-222 [» ]
    ProteinModelPortali P04179.
    SMRi P04179. Positions 25-222.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112531. 19 interactions.
    IntActi P04179. 19 interactions.
    MINTi MINT-5002369.
    STRINGi 9606.ENSP00000337127.

    Protein family/group databases

    Allergomei 784. Hom s MnSOD.

    PTM databases

    PhosphoSitei P04179.

    Polymorphism databases

    DMDMi 134665.

    2D gel databases

    DOSAC-COBS-2DPAGE P04179.
    OGPi P04179.
    SWISS-2DPAGE P04179.
    UCD-2DPAGE P04179.

    Proteomic databases

    MaxQBi P04179.
    PaxDbi P04179.
    PRIDEi P04179.

    Protocols and materials databases

    DNASUi 6648.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000337404 ; ENSP00000337127 ; ENSG00000112096 .
    ENST00000367054 ; ENSP00000356021 ; ENSG00000112096 .
    ENST00000367055 ; ENSP00000356022 ; ENSG00000112096 .
    ENST00000444946 ; ENSP00000404804 ; ENSG00000112096 .
    ENST00000538183 ; ENSP00000446252 ; ENSG00000112096 .
    ENST00000546087 ; ENSP00000442920 ; ENSG00000112096 . [P04179-4 ]
    GeneIDi 6648.
    KEGGi hsa:6648.
    UCSCi uc003qsg.3. human. [P04179-1 ]
    uc003qsh.3. human. [P04179-2 ]

    Organism-specific databases

    CTDi 6648.
    GeneCardsi GC06M160102.
    HGNCi HGNC:11180. SOD2.
    HPAi CAB002013.
    HPA001814.
    MIMi 147460. gene.
    612634. phenotype.
    neXtProti NX_P04179.
    PharmGKBi PA36017.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0605.
    HOGENOMi HOG000013583.
    HOVERGENi HBG004451.
    InParanoidi P04179.
    KOi K04564.
    OrthoDBi EOG7FV3R5.
    PhylomeDBi P04179.
    TreeFami TF105132.

    Enzyme and pathway databases

    Reactomei REACT_172715. Detoxification of Reactive Oxygen Species.

    Miscellaneous databases

    ChiTaRSi SOD2. human.
    EvolutionaryTracei P04179.
    GeneWikii SOD2.
    GenomeRNAii 6648.
    NextBioi 25907.
    PROi P04179.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P04179.
    Bgeei P04179.
    CleanExi HS_SOD2.
    Genevestigatori P04179.

    Family and domain databases

    InterProi IPR001189. Mn/Fe_SOD.
    IPR019833. Mn/Fe_SOD_BS.
    IPR019832. Mn/Fe_SOD_C.
    IPR019831. Mn/Fe_SOD_N.
    [Graphical view ]
    PANTHERi PTHR11404. PTHR11404. 1 hit.
    Pfami PF02777. Sod_Fe_C. 1 hit.
    PF00081. Sod_Fe_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000349. SODismutase. 1 hit.
    PRINTSi PR01703. MNSODISMTASE.
    SUPFAMi SSF46609. SSF46609. 1 hit.
    SSF54719. SSF54719. 1 hit.
    PROSITEi PS00088. SOD_MN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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).
    24. "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.
    25. "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.
    26. "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.
    27. "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.
    28. "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.
    29. "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.
    30. "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: October 1, 2014
    This is version 182 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