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P04179 (SODM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 178. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Superoxide dismutase [Mn], mitochondrial

EC=1.15.1.1
Gene names
Name:SOD2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length222 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. Ref.18

Catalytic activity

2 superoxide + 2 H+ = O2 + H2O2.

Cofactor

Binds 1 manganese ion per subunit.

Subunit structure

Homotetramer. Ref.29

Subcellular location

Mitochondrion matrix.

Induction

Expression is regulated by KRIT1. Ref.21

Post-translational modification

Nitrated under oxidative stress. Nitration coupled with oxidation inhibits the catalytic activity.

Acetylation at Lys-122 decreases enzymatic activity. Deacetylated by SIRT3 upon exposure to ionizing radiations or after long fasting By similarity.

Involvement in disease

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.

Sequence similarities

Belongs to the iron/manganese superoxide dismutase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransit peptide
   LigandManganese
Metal-binding
   Molecular functionOxidoreductase
   PTMAcetylation
Nitration
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processage-dependent response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

age-dependent response to reactive oxygen species

Inferred from mutant phenotype PubMed 14980699. Source: UniProtKB

cellular response to ethanol

Inferred from electronic annotation. Source: Ensembl

detection of oxygen

Inferred from electronic annotation. Source: Ensembl

erythrophore differentiation

Inferred from electronic annotation. Source: Ensembl

glutathione metabolic process

Inferred from electronic annotation. Source: Ensembl

heart development

Inferred from electronic annotation. Source: Ensembl

hemopoiesis

Inferred from electronic annotation. Source: Ensembl

hydrogen peroxide biosynthetic process

Inferred from electronic annotation. Source: Ensembl

intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from electronic annotation. Source: Ensembl

intrinsic apoptotic signaling pathway in response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

iron ion homeostasis

Inferred from electronic annotation. Source: Ensembl

liver development

Inferred from electronic annotation. Source: Ensembl

locomotory behavior

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from mutant phenotype PubMed 16179351. Source: BHF-UCL

negative regulation of fat cell differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of fibroblast proliferation

Inferred from electronic annotation. Source: Ensembl

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

Inferred from mutant phenotype PubMed 12551919. Source: BHF-UCL

negative regulation of neuron apoptotic process

Inferred from genetic interaction PubMed 17251466. Source: BHF-UCL

neuron development

Inferred from electronic annotation. Source: Ensembl

oxygen homeostasis

Inferred from mutant phenotype PubMed 16179351. Source: BHF-UCL

positive regulation of nitric oxide biosynthetic process

Inferred from electronic annotation. Source: Ensembl

post-embryonic development

Inferred from electronic annotation. Source: Ensembl

protein homooligomerization

Inferred from electronic annotation. Source: Ensembl

protein homotetramerization

Inferred from physical interaction Ref.29. Source: UniProtKB

regulation of blood pressure

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of catalytic activity

Inferred from electronic annotation. Source: Ensembl

regulation of mitochondrial membrane potential

Inferred from electronic annotation. Source: Ensembl

regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 9393747. Source: UniProtKB

release of cytochrome c from mitochondria

Inferred from electronic annotation. Source: Ensembl

removal of superoxide radicals

Inferred from electronic annotation. Source: Ensembl

respiratory electron transport chain

Inferred from electronic annotation. Source: Ensembl

response to L-ascorbic acid

Inferred from electronic annotation. Source: Ensembl

response to activity

Inferred from electronic annotation. Source: Ensembl

response to axon injury

Inferred from electronic annotation. Source: Ensembl

response to cadmium ion

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to electrical stimulus

Inferred from electronic annotation. Source: Ensembl

response to gamma radiation

Inferred from electronic annotation. Source: Ensembl

response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

response to hyperoxia

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to manganese ion

Inferred from electronic annotation. Source: Ensembl

response to selenium ion

Inferred from electronic annotation. Source: Ensembl

response to silicon dioxide

Inferred from electronic annotation. Source: Ensembl

response to superoxide

Inferred from mutant phenotype PubMed 16179351. Source: BHF-UCL

response to zinc ion

Inferred from electronic annotation. Source: Ensembl

superoxide anion generation

Inferred from electronic annotation. Source: Ensembl

superoxide metabolic process

Inferred from electronic annotation. Source: InterPro

vasodilation by acetylcholine involved in regulation of systemic arterial blood pressure

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentmitochondrial inner membrane

Inferred from electronic annotation. Source: Ensembl

mitochondrial matrix

Traceable author statement PubMed 10511315. Source: BHF-UCL

mitochondrial nucleoid

Inferred from electronic annotation. Source: Ensembl

mitochondrion

Inferred from direct assay PubMed 12551919. Source: BHF-UCL

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: Ensembl

identical protein binding

Inferred from physical interaction PubMed 19822147PubMed 21988832. Source: IntAct

manganese ion binding

Inferred from direct assay Ref.29. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: InterPro

oxygen binding

Inferred from electronic annotation. Source: Ensembl

superoxide dismutase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-716989,EBI-716989

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P04179-1)

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.
Isoform 2 (identifier: P04179-2)

The sequence of this isoform differs from the canonical sequence as follows:
     75-113: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P04179-3)

The sequence of this isoform differs from the canonical sequence as follows:
     115-174: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: P04179-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-46: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2424Mitochondrion Ref.14 Ref.15 Ref.16 Ref.17
Chain25 – 222198Superoxide dismutase [Mn], mitochondrial
PRO_0000032869

Sites

Metal binding501Manganese
Metal binding981Manganese
Metal binding1831Manganese
Metal binding1871Manganese

Amino acid modifications

Modified residue581Nitrated tyrosine Ref.19
Modified residue681N6-acetyllysine; alternate Ref.20
Modified residue681N6-succinyllysine; alternate By similarity
Modified residue751N6-acetyllysine; alternate By similarity
Modified residue751N6-succinyllysine; alternate By similarity
Modified residue1141N6-acetyllysine By similarity
Modified residue1221N6-acetyllysine; alternate By similarity
Modified residue1221N6-succinyllysine; alternate By similarity
Modified residue1301N6-acetyllysine; alternate Ref.20
Modified residue1301N6-succinyllysine; alternate By similarity
Modified residue2021N6-acetyllysine By similarity

Natural variations

Alternative sequence1 – 4646Missing in isoform 4.
VSP_053761
Alternative sequence75 – 11339Missing in isoform 2.
VSP_042558
Alternative sequence115 – 17460Missing in isoform 3.
VSP_053762
Natural variant101S → I. Ref.9
Corresponds to variant rs5746096 [ dbSNP | Ensembl ].
VAR_019363
Natural variant161A → V Very frequent polymorphism; associated with susceptibility to diabetic nephropathy in Japanese patients with type 2 diabetes. Ref.3 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.30
Corresponds to variant rs4880 [ dbSNP | Ensembl ].
VAR_016183
Natural variant661E → V. Ref.9
Corresponds to variant rs5746097 [ dbSNP | Ensembl ].
VAR_019364
Natural variant761G → R.
Corresponds to variant rs4987023 [ dbSNP | Ensembl ].
VAR_025898
Natural variant821I → T. Ref.24
Corresponds to variant rs1141718 [ dbSNP | Ensembl ].
VAR_007165
Natural variant1561R → W. Ref.9
Corresponds to variant rs5746129 [ dbSNP | Ensembl ].
VAR_019365

Experimental info

Mutagenesis581Y → A, H, N, V or F: Reduced enzyme activity. Ref.18
Mutagenesis581Y → F: Loss of nitration. Enhanced dityrosine formation on peroxynitrite treatment. Ref.18
Sequence conflict141A → P Ref.3
Sequence conflict651T → N in CAA42066. Ref.5
Sequence conflict651T → N in CAA33228. Ref.5
Sequence conflict661E → Q Ref.6
Sequence conflict1121E → Q Ref.6
Sequence conflict1231R → L in CAA30687. Ref.3
Sequence conflict1331E → Q Ref.6
Sequence conflict148 – 1492Missing Ref.6
Sequence conflict1551E → Q in CAA68533. Ref.2
Sequence conflict1551E → Q Ref.6

Secondary structure

................................ 222
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 1, 1990. Version 2.
Checksum: 648435C080E6E47B

FASTA22224,722
        10         20         30         40         50         60 
MLSRAVCGTS RQLAPALGYL GSRQKHSLPD LPYDYGALEP HINAQIMQLH HSKHHAAYVN 

        70         80         90        100        110        120 
NLNVTEEKYQ EALAKGDVTA QIALQPALKF NGGGHINHSI FWTNLSPNGG GEPKGELLEA 

       130        140        150        160        170        180 
IKRDFGSFDK FKEKLTAASV GVQGSGWGWL GFNKERGHLQ IAACPNQDPL QGTTGLIPLL 

       190        200        210        220 
GIDVWEHAYY LQYKNVRPDY LKAIWNVINW ENVTERYMAC KK 

« Hide

Isoform 2 [UniParc].

Checksum: 1C427B935D71B90F
Show »

FASTA18320,696
Isoform 3 [UniParc].

Checksum: 4256776626017959
Show »

FASTA16218,234
Isoform 4 [UniParc].

Checksum: 5AB24FB15A80A1AF
Show »

FASTA17619,730

References

« Hide 'large scale' references
[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]"Human Mn superoxide dismutase cDNA sequence."
Beck Y., Oren R., Amit B., Levanon A., Gorecki M., Hartman J.R.
Nucleic Acids Res. 15:9076-9076(1987) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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, 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

NIEHS-SNPs
SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Superoxide dismutase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRDSHUN. S13162.
RefSeqNP_000627.2. NM_000636.2.
NP_001019636.1. NM_001024465.1.
NP_001019637.1. NM_001024466.1.
UniGeneHs.487046.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP04179.
SMRP04179. Positions 25-222.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112531. 19 interactions.
IntActP04179. 19 interactions.
MINTMINT-5002369.
STRING9606.ENSP00000337127.

Protein family/group databases

Allergome784. Hom s MnSOD.

PTM databases

PhosphoSiteP04179.

Polymorphism databases

DMDM134665.

2D gel databases

DOSAC-COBS-2DPAGEP04179.
OGPP04179.
SWISS-2DPAGEP04179.
UCD-2DPAGEP04179.

Proteomic databases

PaxDbP04179.
PRIDEP04179.

Protocols and materials databases

DNASU6648.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000337404; ENSP00000337127; ENSG00000112096.
ENST00000367054; ENSP00000356021; ENSG00000112096.
ENST00000367055; ENSP00000356022; ENSG00000112096.
ENST00000444946; ENSP00000404804; ENSG00000112096.
ENST00000538183; ENSP00000446252; ENSG00000112096.
ENST00000546087; ENSP00000442920; ENSG00000112096.
GeneID6648.
KEGGhsa:6648.
UCSCuc003qsg.3. human. [P04179-1]
uc003qsh.3. human. [P04179-2]

Organism-specific databases

CTD6648.
GeneCardsGC06M160102.
HGNCHGNC:11180. SOD2.
HPACAB002013.
HPA001814.
MIM147460. gene.
612634. phenotype.
neXtProtNX_P04179.
PharmGKBPA36017.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0605.
HOGENOMHOG000013583.
HOVERGENHBG004451.
InParanoidP04179.
KOK04564.
OrthoDBEOG7FV3R5.
PhylomeDBP04179.
TreeFamTF105132.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.

Gene expression databases

ArrayExpressP04179.
BgeeP04179.
CleanExHS_SOD2.
GenevestigatorP04179.

Family and domain databases

InterProIPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]
PANTHERPTHR11404. PTHR11404. 1 hit.
PfamPF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]
PIRSFPIRSF000349. SODismutase. 1 hit.
PRINTSPR01703. MNSODISMTASE.
SUPFAMSSF46609. SSF46609. 1 hit.
SSF54719. SSF54719. 1 hit.
PROSITEPS00088. SOD_MN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSOD2. human.
EvolutionaryTraceP04179.
GeneWikiSOD2.
GenomeRNAi6648.
NextBio25907.
PROP04179.
SOURCESearch...

Entry information

Entry nameSODM_HUMAN
AccessionPrimary (citable) accession number: P04179
Secondary accession number(s): B2R7R1 expand/collapse secondary AC list , B3KUK2, B4DL20, B4E3K9, E1P5A9, P78434, Q16792, Q5TCM1, Q96EE6, Q9P2Z3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: April 1, 1990
Last modified: April 16, 2014
This is version 178 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM