P04179 (SODM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Superoxide dismutase [Mn], mitochondrial
EC=1.15.1.1

Gene names

Name:

SOD2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	222 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Involvement in disease	Genetic variation in SOD2 is associated with susceptibility to microvascular complications of diabetes type 6 (MVCD6) [MIM:612634]. These are 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.
Sequence similarities	Belongs to the iron/manganese superoxide dismutase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Ligand	Manganese Metal-binding
Molecular function	Oxidoreductase
PTM	Acetylation Nitration
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	age-dependent response to reactive oxygen species Inferred from mutant phenotype. Source: UniProtKB negative regulation of neuron apoptosis Inferred from genetic interaction. Source: BHF-UCL oxygen homeostasis Inferred from mutant phenotype. Source: BHF-UCL protein homotetramerization Inferred from physical interaction Ref.29. Source: UniProtKB regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype. Source: UniProtKB release of cytochrome c from mitochondria Inferred from sequence or structural similarity. Source: BHF-UCL removal of superoxide radicals Inferred from mutant phenotype. Source: BHF-UCL vasodilation by acetylcholine involved in regulation of systemic arterial blood pressure Inferred from sequence or structural similarity. Source: BHF-UCL
Molecular function	manganese ion binding Inferred from direct assay Ref.29. Source: UniProtKB superoxide dismutase activity Inferred from direct assay Ref.29. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 24

24

Mitochondrion Ref.14 Ref.15 Ref.16 Ref.17

Chain

25 – 222

198

Superoxide dismutase [Mn], mitochondrial

PRO_0000032869

Sites

Metal binding

50

1

Manganese

Metal binding

98

1

Manganese

Metal binding

183

1

Manganese

Metal binding

187

1

Manganese

Amino acid modifications

Modified residue

58

1

Nitrated tyrosine Ref.19

Modified residue

68

1

N6-acetyllysine Ref.20

Modified residue

130

1

N6-acetyllysine Ref.20

Natural variations

Natural variant

10

1

S → I. Ref.9
Corresponds to variant rs5746096 [ dbSNP | Ensembl ].

VAR_019363

Natural variant

16

1

A → 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 variant

66

1

E → V. Ref.9
Corresponds to variant rs5746097 [ dbSNP | Ensembl ].

VAR_019364

Natural variant

76

1

G → R.
Corresponds to variant rs4987023 [ dbSNP | Ensembl ].

VAR_025898

Natural variant

82

1

I → T. Ref.24
Corresponds to variant rs1141718 [ dbSNP | Ensembl ].

VAR_007165

Natural variant

156

1

R → W. Ref.9
Corresponds to variant rs5746129 [ dbSNP | Ensembl ].

VAR_019365

Experimental info

Mutagenesis

58

1

Y → A, H, N, V or F: Reduced enzyme activity. Ref.18

Mutagenesis

58

1

Y → F: Loss of nitration. Enhanced dityrosine formation on peroxynitrite treatment. Ref.18

Sequence conflict

14

1

A → P Ref.3

Sequence conflict

65

1

T → N in CAA42066. Ref.5

Sequence conflict

65

1

T → N in CAA33228. Ref.5

Sequence conflict

66

1

E → Q Ref.6

Sequence conflict

112

1

E → Q Ref.6

Sequence conflict

123

1

R → L in CAA30687. Ref.3

Sequence conflict

133

1

E → Q Ref.6

Sequence conflict

148 – 149

2

Missing Ref.6

Sequence conflict

155

1

E → Q in CAA68533. Ref.2

Sequence conflict

155

1

E → Q Ref.6

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

222

Helix Strand Turn

Details...

Turn

35 – 41

7

Helix

44 – 52

9

Helix

54 – 74

21

Helix

78 – 83

6

Helix

85 – 103

19

Helix

115 – 125

11

Helix

128 – 140

13

Beta strand

144 – 153

10

Turn

154 – 157

4

Beta strand

158 – 165

8

Helix

170 – 174

5

Beta strand

177 – 183

7

Helix

186 – 188

3

Helix

190 – 193

4

Helix

197 – 204

8

Helix

205 – 207

3

Helix

210 – 219

10

Sequences

	Sequence		Length	Mass (Da)
	P04179 [UniParc]. Last modified April 1, 1990. Version 2. Checksum: 648435C080E6E47B	FASTA	222	24,722
	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

References

	« Hide 'large scale' referencesShow '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: 2462451] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 3684581] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Isolation of cDNAs encoding human manganese superoxide dismutase." Heckl K. Nucleic Acids Res. 16:6224-6224(1988) [PubMed: 3399391] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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: 2831093] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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: 1699607] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 1988135] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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: 7702755] [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], 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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-16. Tissue: Hippocampus.
[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: 14574404] [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. , 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], 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: 6386798] [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: 7895732] [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: 7498159] [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: 9150946] [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: 10334867] [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: 16399855] [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., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-68 AND LYS-130, MASS SPECTROMETRY.
[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: 20668652] [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: 21269460] [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: 1394426] [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: 8605177] [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: 9537988] [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: 9537987] [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: 10852710] [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: 11580280] [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: 19265433] [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: 12624725] [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.
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.

IPI

IPI00022314.

PIR

DSHUN. S13162.

RefSeq

NP_000627.2. NM_000636.2.
NP_001019636.1. NM_001024465.1.

UniGene

Hs.487046.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P04179.

SMR

P04179. Positions 25-222.

ModBase

Search...

Protein-protein interaction databases

IntAct

P04179. 21 interactions.

MINT

MINT-5002369.

STRING

P04179.

Protein family/group databases

Allergome

784. Hom s MnSOD.

PTM databases

PhosphoSite

P04179.

Polymorphism databases

DMDM

134665.

2D gel databases

SWISS-2DPAGE

P04179.

DOSAC-COBS-2DPAGE

P04179.

OGP

P04179.

PMMA-2DPAGE

P04179.

Siena-2DPAGE

P04179.

UCD-2DPAGE

P04179.

Proteomic databases

PRIDE

P04179.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000337404; ENSP00000337127; ENSG00000112096.
ENST00000367055; ENSP00000356022; ENSG00000112096.

GeneID

6648.

KEGG

hsa:6648.

Organism-specific databases

CTD

6648.

GeneCards

GC06M160102.

HGNC

HGNC:11180. SOD2.

HPA

CAB002013.
HPA001814.

MIM

147460. gene.
612634. phenotype.

neXtProt

NX_P04179.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG18046.

HOGENOM

HBG507761.

HOVERGEN

HBG004451.

InParanoid

P04179.

OrthoDB

EOG4R503R.

PhylomeDB

P04179.

Enzyme and pathway databases

Pathway_Interaction_DB

foxopathway. FoxO family signaling.

Gene expression databases

ArrayExpress

P04179.

Bgee

P04179.

CleanEx

HS_SOD2.

Genevestigator

P04179.

GermOnline

ENSG00000112096. Homo sapiens.

Family and domain databases

InterPro

IPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]

KO

K04564.

PANTHER

PTHR11404. SODismutase. 1 hit.

Pfam

PF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]

PIRSF

PIRSF000349. SODismutase. 1 hit.

PRINTS

PR01703. MNSODISMTASE.

SUPFAM

SSF46609. SODismutase. 1 hit.
SSF54719. SODismutase. 1 hit.

PROSITE

PS00088. SOD_MN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

25907.

SOURCE

Search...

Entry information

Entry name

SODM_HUMAN

Accession

Primary (citable) accession number: P04179
Secondary accession number(s): B2R7R1 , E1P5A9, P78434, Q16792, Q5TCM1, Q96EE6, Q9P2Z3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 1987
Last sequence update:	April 1, 1990
Last modified:	January 25, 2012
This is version 156 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.