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UniProtKB/Swiss-Prot entry P08228


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SODC_MOUSE
Primary accession number P08228
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1988
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 110)
Name and origin of the protein
Protein name Superoxide dismutase [Cu-Zn]
Synonym EC 1.15.1.1
Gene name
Name: Sod1
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=SWR/J;
TISSUE=Liver;
DOI=10.1093/nar/16.6.2728; PubMed=3362683 [NCBI, ExPASy, EBI, Israel, Japan]
Bewley G.C.;
"cDNA and deduced amino acid sequence of murine Cu-Zn superoxide dismutase.";
Nucleic Acids Res. 16:2728-2728(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0378-1119(91)90126-V; PubMed=2022332 [NCBI, ExPASy, EBI, Israel, Japan]
Benedetto M.T., Anzai Y., Gordon J.W.;
"Isolation and analysis of the mouse genomic sequence encoding Cu(2+)-Zn2+ superoxide dismutase.";
Gene 99:191-195(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Ovary, Urinary bladder, and Uterus;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Liver, Mammary gland, and Retina;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 4-23.
DOI=10.1083/jcb.111.3.1217; PubMed=2391363 [NCBI, ExPASy, EBI, Israel, Japan]
Pluthero F.G., Shreeve M., Eskinazi D., van der Gaag H., Huang K.S., Hulmes J.D., Blum M., Axelrad A.A.;
"Purification of an inhibitor of erythroid progenitor cell cycling and antagonist to interleukin 3 from mouse marrow cell supernatants and its identification as cytosolic superoxide dismutase.";
J. Cell Biol. 111:1217-1223(1990).
[6]
PROTEIN SEQUENCE OF 11-24 AND 104-116, AND MASS SPECTROMETRY.
STRAIN=OF1;
TISSUE=Hippocampus;
Lubec G., Klug S., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-71, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1016/j.molcel.2006.06.026; PubMed=16916647 [NCBI, ExPASy, EBI, Israel, Japan]
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.";
Mol. Cell 23:607-618(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X06683; CAA29880.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M60798; AAA40121.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M60794; AAA40121.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M60795; AAA40121.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M60796; AAA40121.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M60797; AAA40121.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M35725; AAA37518.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK020624; BAB32154.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK077284; BAC36730.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002066; AAH02066.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC048874; AAH48874.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC086886; AAH86886.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00130589; -.
PIR JQ0915; JQ0915.
RefSeq NP_035564.1; -.
UniGene Mm.276325
3D structure databases
HSSP P00441; 1HL5. [HSSP ENTRY / PDB]
SMR P08228; 2-154.
ModBase P08228.
PTM databases
PhosphoSite P08228; -.
Enzyme and pathway databases
BRENDA 1.15.1.1; 244.
2D gel databases
SWISS-2DPAGE P08228; -.
DOSAC-COBS-2DPAGE P08228; -.
REPRODUCTION-2DPAGE P08228; -.
Organism-specific databases
MGI MGI:98351; Sod1.
Gene expression databases
Bgee P08228; -.
CleanEx MM_SOD1; -.
GermOnline ENSMUSG00000047905; Mus musculus.
Ontologies
GO
GO:0043025; Cellular component: cell soma (inferred from sequence or structural similarity from UniProtKB).
GO:0031410; Cellular component: cytoplasmic vesicle (inferred from sequence or structural similarity from UniProtKB).
GO:0005829; Cellular component: cytosol (inferred from sequence or structural similarity from UniProtKB).
GO:0032839; Cellular component: dendrite cytoplasm (inferred from sequence or structural similarity from UniProtKB).
GO:0031012; Cellular component: extracellular matrix (inferred from sequence or structural similarity from UniProtKB).
GO:0005615; Cellular component: extracellular space (inferred from sequence or structural similarity from UniProtKB).
GO:0005739; Cellular component: mitochondrion (inferred from sequence or structural similarity from UniProtKB).
GO:0005634; Cellular component: nucleus (inferred from sequence or structural similarity from UniProtKB).
GO:0043234; Cellular component: protein complex (inferred from sequence or structural similarity from UniProtKB).
GO:0016209; Molecular function: antioxidant activity (inferred from electronic annotation from UniProtKB-KW).
GO:0051087; Molecular function: chaperone binding (inferred from sequence or structural similarity from UniProtKB).
GO:0005507; Molecular function: copper ion binding (inferred from sequence or structural similarity from UniProtKB).
GO:0030346; Molecular function: protein phosphatase 2B binding (inferred from sequence or structural similarity from UniProtKB).
GO:0004784; Molecular function: superoxide dismutase activity (inferred from direct assay from MGI).
GO:0008270; Molecular function: zinc ion binding (inferred from sequence or structural similarity from UniProtKB).
GO:0000187; Biological process: activation of MAPK activity (inferred from direct assay from MGI).
GO:0060088; Biological process: auditory receptor cell stereocilium organization (inferred from mutant phenotype from MGI).
GO:0007569; Biological process: cell aging (inferred from sequence or structural similarity from UniProtKB).
GO:0006879; Biological process: cellular iron ion homeostasis (inferred from mutant phenotype from MGI).
GO:0006309; Biological process: DNA fragmentation involved in apoptosis (inferred from direct assay from MGI).
GO:0006302; Biological process: double-strand break repair (inferred from mutant phenotype from MGI).
GO:0007566; Biological process: embryo implantation (inferred from mutant phenotype from MGI).
GO:0006749; Biological process: glutathione metabolic process (inferred from mutant phenotype from MGI).
GO:0060047; Biological process: heart contraction (inferred from mutant phenotype from MGI).
GO:0050665; Biological process: hydrogen peroxide biosynthetic process (inferred from mutant phenotype from MGI).
GO:0007626; Biological process: locomotory behavior (inferred from mutant phenotype from MGI).
GO:0046716; Biological process: muscle maintenance (inferred from mutant phenotype from MGI).
GO:0032287; Biological process: myelin maintenance in the peripheral nervous system (inferred from mutant phenotype from MGI).
GO:0002262; Biological process: myeloid cell homeostasis (inferred from genetic interaction from MGI).
GO:0045541; Biological process: negative regulation of cholesterol biosynthetic process (inferred from sequence or structural similarity from UniProtKB).
GO:0043524; Biological process: negative regulation of neuron apoptosis (inferred from mutant phenotype from MGI).
GO:0060052; Biological process: neurofilament cytoskeleton organization (inferred from genetic interaction from MGI).
GO:0001541; Biological process: ovarian follicle development (inferred from mutant phenotype from MGI).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0001819; Biological process: positive regulation of cytokine production (inferred from sequence or structural similarity from UniProtKB).
GO:0008217; Biological process: regulation of blood pressure (inferred from mutant phenotype from MGI).
GO:0051881; Biological process: regulation of mitochondrial membrane potential (inferred from sequence or structural similarity from UniProtKB).
GO:0040014; Biological process: regulation of multicellular organism growth (inferred from mutant phenotype from MGI).
GO:0060087; Biological process: relaxation of vascular smooth muscle (inferred from mutant phenotype from MGI).
GO:0019430; Biological process: removal of superoxide radicals (inferred from mutant phenotype from MGI).
GO:0048678; Biological process: response to axon injury (inferred from mutant phenotype from MGI).
GO:0042493; Biological process: response to drug (inferred from mutant phenotype from MGI).
GO:0045471; Biological process: response to ethanol (inferred from mutant phenotype from MGI).
GO:0009408; Biological process: response to heat (inferred from mutant phenotype from MGI).
GO:0042542; Biological process: response to hydrogen peroxide (inferred from mutant phenotype from MGI).
GO:0000303; Biological process: response to superoxide (inferred from mutant phenotype from MGI).
GO:0001895; Biological process: retina homeostasis (inferred from mutant phenotype from MGI).
GO:0007605; Biological process: sensory perception of sound (inferred from mutant phenotype from MGI).
GO:0007283; Biological process: spermatogenesis (inferred from mutant phenotype from MGI).
GO:0042554; Biological process: superoxide anion generation (inferred from direct assay from MGI).
QuickGo view.
Family and domain databases
InterPro IPR018152; SOD_Cu/Zn_BS.
IPR001424; SOD_Cu_Zn.
Graphical view of domain structure.
Gene3D G3DSA:2.60.40.200; SOD_Cu_Zn; 1.
PANTHER PTHR10003; SOD_Cu_Zn; 1.
Pfam PF00080; Sod_Cu; 1.
Pfam graphical view of domain structure.
PRINTS PR00068; CUZNDISMTASE.
ProDom PD000469; SOD_CU_ZN; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00087; SOD_CU_ZN_1; 1.
PS00332; SOD_CU_ZN_2; 1.
Proteomic databases
PRIDE P08228; -.
Genome annotation databases
Ensembl ENSMUSG00000022982; Mus musculus. [Contig view]
GeneID 20655; -.
KEGG mmu:20655; -.
NMPDR fig|10090.3.peg.1866; -.
Phylogenomic databases
HOGENOM P08228; -.
HOVERGEN P08228; -.
OMA P08228; GPHFNPN.
Other
NextBio 299081; -.
SOURCE Sod1; Mus musculus.
ProtoNet P08228.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Antioxidant; Copper; Cytoplasm; Direct protein sequencing; Disulfide bond; Metal-binding; Oxidoreductase; Phosphoprotein; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   154  153     Superoxide dismutase [Cu-Zn]. PRO_0000164062
METAL   47    47        Copper; catalytic (By similarity). 
METAL   49    49        Copper; catalytic (By similarity). 
METAL   64    64        Copper; catalytic (By similarity). 
METAL   64    64        Zinc; structural (By similarity). 
METAL   72    72        Zinc; structural (By similarity). 
METAL   81    81        Zinc; structural (By similarity). 
METAL   84    84        Zinc; structural (By similarity). 
METAL   121   121        Copper; catalytic (By similarity). 
MOD_RES   71    71        N6-acetyllysine. 
MOD_RES   99    99        Phosphoserine (By similarity). 
DISULFID   58   147        By similarity. 
CONFLICT   102   102        D -> H (in Ref. 2; AAA40121). 
Sequence information
Length: 154 AA [This is the length of the unprocessed precursor] Molecular weight: 15943 Da [This is the MW of the unprocessed precursor] CRC64: CAE548C66043BAC4 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAMKAVCVLK GDGPVQGTIH FEQKASGEPV VLSGQITGLT EGQHGFHVHQ YGDNTQGCTS 

        70         80         90        100        110        120 
AGPHFNPHSK KHGGPADEER HVGDLGNVTA GKDGVANVSI EDRVISLSGE HSIIGRTMVV 

       130        140        150 
HEKQDDLGKG GNEESTKTGN AGSRLACGVI GIAQ 

P08228 in FASTA format

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