UniProt Accession

 SODM_MOUSE; P09671; Q64670; Q8VEM5 

Genbank Protein ID

 X04972; Z18857; L35528; L35525; L35526; L35527; S78846; S78832; S78842; S78844; AK002428; AK002534; AK012354; BC010548; BC018173 

Genbank Nucleotide ID

 CAA28645.1; CAA79308.1; AAB60902.1; AAB60902.1; AAB60902.1; AAB60902.1; AAB34899.1; AAB34899.1; AAB34899.1; AAB34899.1; BAB22095.1; BAB22170.1; BAB28183.1; AAH10548.1; AAH18173.1 

Protein Name

 Superoxide dismutase [Mn], mitochondrial 

Protein Synonyms/Alias

  

Gene Name

 Sod2 

Gene Synonyms/Alias

 Sod-2 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
25	GAAGSRHKHSLPDLP	acetylation	[1]
53	IMQLHHSKHHAAYVN	acetylation	[1]
68	NLNATEEKYHEALAK	acetylation	[1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11]
68	NLNATEEKYHEALAK	succinylation	[10]
68	NLNATEEKYHEALAK	ubiquitination	[12]
75	KYHEALAKGDVTTQV	acetylation	[1, 7, 10, 11]
75	KYHEALAKGDVTTQV	succinylation	[10]
75	KYHEALAKGDVTTQV	ubiquitination	[12]
89	VALQPALKFNGGGHI	acetylation	[11, 13]
108	FWTNLSPKGGGEPKG	acetylation	[7, 11]
114	PKGGGEPKGELLEAI	acetylation	[1, 3, 5, 7, 10, 11]
114	PKGGGEPKGELLEAI	succinylation	[10]
114	PKGGGEPKGELLEAI	ubiquitination	[12]
122	GELLEAIKRDFGSFE	acetylation	[1, 3, 7, 10, 11, 14]
122	GELLEAIKRDFGSFE	succinylation	[10]
130	RDFGSFEKFKEKLTA	acetylation	[1, 3, 4, 5, 7, 8, 9, 10, 11]
130	RDFGSFEKFKEKLTA	succinylation	[10]
130	RDFGSFEKFKEKLTA	ubiquitination	[12]
132	FGSFEKFKEKLTAVS	acetylation	[1, 3, 7]
134	SFEKFKEKLTAVSVG	acetylation	[3]
154	WGWLGFNKEQGRLQI	acetylation	[1, 3]
202	NVRPDYLKAIWNVIN	acetylation	[1, 3, 13]
221	TERYTACKK******	acetylation	[7, 11]

Reference

 [1] 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]
 [2] 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]
 [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] Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice.
 Fritz KS, Galligan JJ, Hirschey MD, Verdin E, Petersen DR.
 J Proteome Res. 2012 Mar 2;11(3):1633-43. [PMID: 22309199]
 [5] 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]
 [6] 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]
 [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] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [9] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
 Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
 Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599]
 [10] 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]
 [11] 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]
 [12] 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]
 [13] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [14] Sirt3-mediated deacetylation of evolutionarily conserved lysine 122 regulates MnSOD activity in response to stress.
 Tao R, Coleman MC, Pennington JD, Ozden O, Park SH, Jiang H, Kim HS, Flynn CR, Hill S, Hayes McDonald W, Olivier AK, Spitz DR, Gius D.
 Mol Cell. 2010 Dec 22;40(6):893-904. [PMID: 21172655] 

Functional Description

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

Sequence Annotation

 METAL 50 50 Manganese (By similarity).
 METAL 98 98 Manganese (By similarity).
 METAL 183 183 Manganese (By similarity).
 METAL 187 187 Manganese (By similarity).
 MOD_RES 58 58 Nitrated tyrosine (By similarity).
 MOD_RES 68 68 N6-acetyllysine.
 MOD_RES 130 130 N6-acetyllysine (By similarity).  

Keyword

 Acetylation; Complete proteome; Direct protein sequencing; Manganese; Metal-binding; Mitochondrion; Nitration; Oxidoreductase; Reference proteome; Transit peptide. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 222 AA 

Protein Sequence

Gene Ontology

 GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
 GO:0042645; C:mitochondrial nucleoid; IEA:Compara.
 GO:0003677; F:DNA binding; IEA:Compara.
 GO:0030145; F:manganese ion binding; ISS:UniProtKB.
 GO:0019825; F:oxygen binding; IEA:Compara.
 GO:0004784; F:superoxide dismutase activity; ISS:UniProtKB.
 GO:0001315; P:age-dependent response to reactive oxygen species; ISS:UniProtKB.
 GO:0071361; P:cellular response to ethanol; IEA:Compara.
 GO:0003032; P:detection of oxygen; IMP:MGI.
 GO:0048773; P:erythrophore differentiation; IMP:MGI.
 GO:0006749; P:glutathione metabolic process; IMP:MGI.
 GO:0007507; P:heart development; IMP:MGI.
 GO:0030097; P:hemopoiesis; IMP:MGI.
 GO:0050665; P:hydrogen peroxide biosynthetic process; IEA:Compara.
 GO:0055072; P:iron ion homeostasis; IMP:MGI.
 GO:0001889; P:liver development; IMP:MGI.
 GO:0007626; P:locomotory behavior; IMP:MGI.
 GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
 GO:0045599; P:negative regulation of fat cell differentiation; IMP:MGI.
 GO:0048147; P:negative regulation of fibroblast proliferation; IDA:MGI.
 GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Compara.
 GO:0048666; P:neuron development; IMP:MGI.
 GO:0032364; P:oxygen homeostasis; IEA:Compara.
 GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IMP:MGI.
 GO:0009791; P:post-embryonic development; IMP:MGI.
 GO:0051289; P:protein homotetramerization; IEA:Compara.
 GO:0050790; P:regulation of catalytic activity; IMP:MGI.
 GO:0051881; P:regulation of mitochondrial membrane potential; IMP:MGI.
 GO:0006357; P:regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
 GO:0001836; P:release of cytochrome c from mitochondria; IMP:MGI.
 GO:0019430; P:removal of superoxide radicals; IMP:MGI.
 GO:0022904; P:respiratory electron transport chain; IMP:MGI.
 GO:0014823; P:response to activity; IMP:MGI.
 GO:0048678; P:response to axon injury; IMP:MGI.
 GO:0046686; P:response to cadmium ion; IEA:Compara.
 GO:0042493; P:response to drug; IEA:Compara.
 GO:0051602; P:response to electrical stimulus; IEA:Compara.
 GO:0010332; P:response to gamma radiation; IGI:MGI.
 GO:0042542; P:response to hydrogen peroxide; IMP:MGI.
 GO:0055093; P:response to hyperoxia; IMP:MGI.
 GO:0001666; P:response to hypoxia; IEA:Compara.
 GO:0033591; P:response to L-ascorbic acid; IEA:Compara.
 GO:0032496; P:response to lipopolysaccharide; IEA:Compara.
 GO:0010042; P:response to manganese ion; IEA:Compara.
 GO:0010269; P:response to selenium ion; IEA:Compara.
 GO:0034021; P:response to silicon dioxide; IEA:Compara.
 GO:0010043; P:response to zinc ion; IEA:Compara.
 GO:0042554; P:superoxide anion generation; IMP:MGI.
 GO:0003069; P:vasodilation by acetylcholine involved in regulation of systemic arterial blood pressure; IMP:MGI. 

Interpro

 IPR001189; Mn/Fe_SOD.
 IPR019833; Mn/Fe_SOD_BS.
 IPR019832; Mn/Fe_SOD_C.
 IPR019831; Mn/Fe_SOD_N. 

Pfam

 PF02777; Sod_Fe_C
 PF00081; Sod_Fe_N 

SMART

  

PROSITE

 PS00088; SOD_MN 

PRINTS

 PR01703; MNSODISMTASE.