UniProt Accession

 SODC_MOUSE; P08228 

Genbank Protein ID

 X06683; M60798; M60794; M60795; M60796; M60797; M35725; AK020624; AK077284; BC002066; BC048874; BC086886 

Genbank Nucleotide ID

 CAA29880.1; AAA40121.1; AAA40121.1; AAA40121.1; AAA40121.1; AAA40121.1; AAA37518.1; BAB32154.1; BAC36730.1; AAH02066.1; AAH48874.1; AAH86886.1 

Protein Name

 Superoxide dismutase [Cu-Zn] 

Protein Synonyms/Alias

  

Gene Name

 Sod1 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
4	****MAMKAVCVLKG	acetylation	[1, 2]
4	****MAMKAVCVLKG	succinylation	[2]
10	MKAVCVLKGDGPVQG	acetylation	[1, 2, 3]
10	MKAVCVLKGDGPVQG	succinylation	[2]
10	MKAVCVLKGDGPVQG	ubiquitination	[4]
71	HFNPHSKKHGGPADE	acetylation	[1, 2, 5]
71	HFNPHSKKHGGPADE	ubiquitination	[4]
92	LGNVTAGKDGVANVS	acetylation	[2]
92	LGNVTAGKDGVANVS	succinylation	[2]
92	LGNVTAGKDGVANVS	ubiquitination	[4]
123	RTMVVHEKQDDLGKG	acetylation	[1, 2, 3, 6, 7, 8, 9]
123	RTMVVHEKQDDLGKG	succinylation	[2]
123	RTMVVHEKQDDLGKG	ubiquitination	[4]
129	EKQDDLGKGGNEEST	acetylation	[7]
137	GGNEESTKTGNAGSR	acetylation	[1, 2, 3, 6, 7, 8, 9]
137	GGNEESTKTGNAGSR	succinylation	[2]
137	GGNEESTKTGNAGSR	ubiquitination	[4]

Reference

 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [3] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]
 [4] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [5] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [6] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [7] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [8] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [9] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654] 

Functional Description

 Destroys radicals which are normally produced within the cells and which are toxic to biological systems. 

Sequence Annotation

 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; via pros nitrogen.
 METAL 72 72 Zinc; via pros nitrogen.
 METAL 81 81 Zinc; via pros nitrogen.
 METAL 84 84 Zinc; structural.
 METAL 121 121 Copper; catalytic (By similarity).
 MOD_RES 2 2 N-acetylalanine (By similarity).
 MOD_RES 71 71 N6-acetyllysine.
 MOD_RES 99 99 Phosphoserine (By similarity).
 MOD_RES 123 123 N6-acetyllysine (By similarity).
 DISULFID 58 147 By similarity.  

Keyword

 3D-structure; Acetylation; Antioxidant; Complete proteome; Copper; Cytoplasm; Direct protein sequencing; Disulfide bond; Metal-binding; Oxidoreductase; Phosphoprotein; Reference proteome; Zinc. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 154 AA 

Protein Sequence

Gene Ontology

 GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
 GO:0005829; C:cytosol; ISS:UniProtKB.
 GO:0032839; C:dendrite cytoplasm; ISS:UniProtKB.
 GO:0031012; C:extracellular matrix; ISS:UniProtKB.
 GO:0005615; C:extracellular space; ISS:UniProtKB.
 GO:0005739; C:mitochondrion; ISS:UniProtKB.
 GO:0043025; C:neuronal cell body; ISS:UniProtKB.
 GO:0005634; C:nucleus; ISS:UniProtKB.
 GO:0005777; C:peroxisome; IEA:Compara.
 GO:0005886; C:plasma membrane; IEA:Compara.
 GO:0043234; C:protein complex; ISS:UniProtKB.
 GO:0051087; F:chaperone binding; ISS:UniProtKB.
 GO:0005507; F:copper ion binding; ISS:UniProtKB.
 GO:0030346; F:protein phosphatase 2B binding; ISS:UniProtKB.
 GO:0004784; F:superoxide dismutase activity; IDA:MGI.
 GO:0008270; F:zinc ion binding; ISS:UniProtKB.
 GO:0000187; P:activation of MAPK activity; IDA:MGI.
 GO:0007568; P:aging; IMP:MGI.
 GO:0008089; P:anterograde axon cargo transport; IMP:BHF-UCL.
 GO:0060088; P:auditory receptor cell stereocilium organization; IMP:MGI.
 GO:0007569; P:cell aging; IEA:Compara.
 GO:0006879; P:cellular iron ion homeostasis; IMP:MGI.
 GO:0007566; P:embryo implantation; IMP:MGI.
 GO:0006749; P:glutathione metabolic process; IMP:MGI.
 GO:0060047; P:heart contraction; IMP:MGI.
 GO:0050665; P:hydrogen peroxide biosynthetic process; IMP:MGI.
 GO:0007626; P:locomotory behavior; IMP:MGI.
 GO:0046716; P:muscle cell homeostasis; IMP:MGI.
 GO:0002262; P:myeloid cell homeostasis; IMP:MGI.
 GO:0045541; P:negative regulation of cholesterol biosynthetic process; ISS:UniProtKB.
 GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
 GO:0060052; P:neurofilament cytoskeleton organization; IMP:MGI.
 GO:0001541; P:ovarian follicle development; IMP:MGI.
 GO:0032287; P:peripheral nervous system myelin maintenance; IMP:MGI.
 GO:0001819; P:positive regulation of cytokine production; ISS:UniProtKB.
 GO:0008217; P:regulation of blood pressure; IMP:MGI.
 GO:0051881; P:regulation of mitochondrial membrane potential; ISS:UniProtKB.
 GO:0040014; P:regulation of multicellular organism growth; IMP:MGI.
 GO:0060087; P:relaxation of vascular smooth muscle; IMP:MGI.
 GO:0019430; P:removal of superoxide radicals; IMP:MGI.
 GO:0001975; P:response to amphetamine; IEA:Compara.
 GO:0048678; P:response to axon injury; IMP:MGI.
 GO:0046688; P:response to copper ion; IEA:Compara.
 GO:0042493; P:response to drug; IMP:MGI.
 GO:0045471; P:response to ethanol; IMP:MGI.
 GO:0009408; P:response to heat; IMP:MGI.
 GO:0042542; P:response to hydrogen peroxide; IMP:MGI.
 GO:0031667; P:response to nutrient levels; IEA:Compara.
 GO:0001895; P:retina homeostasis; IMP:MGI.
 GO:0008090; P:retrograde axon cargo transport; IMP:BHF-UCL.
 GO:0007605; P:sensory perception of sound; IMP:MGI.
 GO:0007283; P:spermatogenesis; IMP:MGI.
 GO:0042554; P:superoxide anion generation; IDA:MGI. 

Interpro

 IPR024134; SOD_Cu/Zn_/chaperones.
 IPR018152; SOD_Cu/Zn_BS.
 IPR001424; SOD_Cu_Zn_dom. 

Pfam

 PF00080; Sod_Cu 

SMART

  

PROSITE

 PS00087; SOD_CU_ZN_1
 PS00332; SOD_CU_ZN_2 

PRINTS

 PR00068; CUZNDISMTASE.