MOUSE:SODM

Species (Taxon ID)	Mus musculus (Mouse). (10090)
Gene Name(s)	Sod2 (synonyms: Sod-2)
Protein Name(s)	Superoxide dismutase [Mn], mitochondrial
External Links
UniProt	P09671
EMBL	X04972 Z18857 L35528 L35525 L35526 L35527 S78846 S78832 S78842 S78844 AK002428 AK002534 AK012354 BC010548 BC018173
CCDS	CCDS28399.1
PIR	I57023
RefSeq	NP_038699.2
UniGene	Mm.290876
ProteinModelPortal	P09671
SMR	P09671
BioGrid	203388
IntAct	P09671
MINT	MINT-1861884
PhosphoSite	P09671
REPRODUCTION-2DPAGE	IPI00109109 P09671
SWISS-2DPAGE	P09671
MaxQB	P09671
PaxDb	P09671
PRIDE	P09671
Ensembl	ENSMUST00000007012
GeneID	20656
KEGG	mmu:20656
UCSC	uc008alv.1
CTD	6648
MGI	MGI:98352
eggNOG	COG0605
HOGENOM	HOG000013583
HOVERGEN	HBG004451
InParanoid	P09671
KO	K04564
OMA	VNWDDVE
OrthoDB	EOG7FV3R5
PhylomeDB	P09671
TreeFam	TF105132
Reactome	REACT_189141
ChiTaRS	Sod2
NextBio	299085
PRO	PR:P09671
Proteomes	UP000000589
Bgee	P09671
CleanEx	MM_SOD2
ExpressionAtlas	P09671
Genevestigator	P09671
GO	GO:0070062 GO:0005743 GO:0042645 GO:0005739 GO:0003677 GO:0030145 GO:0019825 GO:0004784 GO:0001306 GO:0001315 GO:0008637 GO:0071361 GO:0003032 GO:0048773 GO:0006749 GO:0007507 GO:0030097 GO:0050665 GO:0008630 GO:0008631 GO:0055072 GO:0001889 GO:0007626 GO:0007005 GO:0045599 GO:0048147 GO:0043524 GO:1902176 GO:0048666 GO:0032364 GO:0045429 GO:0009791 GO:0051289 GO:0008217 GO:0050790 GO:0051881 GO:0006357 GO:0001836 GO:0019430 GO:0022904 GO:0014823 GO:0048678 GO:0046686 GO:0009409 GO:0042493 GO:0051602 GO:0010332 GO:0042542 GO:0055093 GO:0001666 GO:0035902 GO:0035900 GO:0033591 GO:0032496 GO:0071000 GO:0010042 GO:0006979 GO:0000302 GO:0010269 GO:0034021 GO:0000303 GO:0010043 GO:0042554 GO:0006801 GO:0042311 GO:0003069
InterPro	IPR001189 IPR019833 IPR019832 IPR019831
PANTHER	PTHR11404
Pfam	PF02777 PF00081
PIRSF	PIRSF000349
PRINTS	PR01703
SUPFAM	SSF46609 SSF54719
PROSITE	PS00088

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0016491	oxidoreductase activity	PMID:15205258^[1]	ECO:0000315			F		Figure 4 shows a Western blot that demonstrates the importance of Sod2 to the oxidation state of proteins in erythrocytes. In the progenitor stage and in both the cytosol and membranes of erythrocytes, the Sod2 -/- mutants have significantly more oxidation (here shown as darker bands, since the blot detected carbonyls resulting from reactive oxygen species activity). That Sod2 has direct oxidoreductase activity is further reinforced by the proteomics analysis in Table 2. Other proteins that might have significant oxidoreductase activity, such as Cytochrome C oxidase subunit Va, are not differentially expressed. Since the absence of Sod2 does not affect expression of these other oxidoreductases, the difference in oxidation states in the mutant is likely due to a lack of activity by Sod2 in this function, rather than as a transcription factor for other oxidoreductases.	complete CACAO 4909
	GO:1903944	negative regulation of hepatocyte apoptotic process	24710718:24710718	ECO:0000315			P		Figure 4b supports the knowledge that there is more apoptosis in cells deficient of Cav1 than there is in wild type cells	complete CACAO 11708
enables	GO:0016491	oxidoreductase activity	PMID:15205258^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0043209	myelin sheath	PMID:17634366^[2]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000128)	Seeded From UniProt	complete
enables	GO:0030145	manganese ion binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P04179	F		Seeded From UniProt	complete
involved_in	GO:0006801	superoxide metabolic process	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P04179	P		Seeded From UniProt	complete
involved_in	GO:0006357	regulation of transcription by RNA polymerase II	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P04179	P		Seeded From UniProt	complete
enables	GO:0004784	superoxide dismutase activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P04179	F		Seeded From UniProt	complete
involved_in	GO:0001315	age-dependent response to reactive oxygen species	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P04179	P		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	PMID:21873635^[3]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000150074 UniProtKB:O81235	F		Seeded From UniProt	complete
enables	GO:0030145	manganese ion binding	PMID:21873635^[3]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000150074 PomBase:SPAC1486.01 RGD:3732 UniProtKB:P04179 UniProtKB:Q92450	F		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:21873635^[3]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:98352 PANTHER:PTN000150076 PomBase:SPAC1486.01 RGD:3732 SGD:S000001050 UniProtKB:O81235 UniProtKB:P04179 UniProtKB:P09233 WB:WBGene00004932	C		Seeded From UniProt	complete
enables	GO:0004784	superoxide dismutase activity	PMID:21873635^[3]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:98352 PANTHER:PTN000150074 PomBase:SPAC1486.01 RGD:3732 SGD:S000001050 UniProtKB:A0A1D8PQH5 UniProtKB:O81235 UniProtKB:P04179 UniProtKB:P09233 UniProtKB:P9WGE7 WB:WBGene00004931 WB:WBGene00004932	F		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:1905932	positive regulation of vascular smooth muscle cell differentiation involved in phenotypic switching	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P04179	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:1905461	positive regulation of vascular associated smooth muscle cell apoptotic process	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P04179	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:1904706	negative regulation of vascular smooth muscle cell proliferation	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P04179	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:1902176	negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P04179	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0055093	response to hyperoxia	PMID:11796207^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857344	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0055072	iron ion homeostasis	PMID:15205258^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857344	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0051881	regulation of mitochondrial membrane potential	PMID:17367743^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:2177602,MGI:MGI:2447406	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0051289	protein homotetramerization	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P04179	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0051260	protein homooligomerization	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:3732	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0050790	regulation of catalytic activity	PMID:9927656^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857344	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0050665	hydrogen peroxide biosynthetic process	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:3732	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0048773	erythrophore differentiation	PMID:15205258^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857344	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0048678	response to axon injury	PMID:16677818^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:2447406,MGI:MGI:2679331	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0048666	neuron development	PMID:8790408^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857480	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0048147	negative regulation of fibroblast proliferation	PMID:18218638^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0045599	negative regulation of fat cell differentiation	PMID:16219542^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0045429	positive regulation of nitric oxide biosynthetic process	PMID:15637112^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857480	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0043524	negative regulation of neuron apoptotic process	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P04179	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0043066	negative regulation of apoptotic process	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:3732	P		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P04179	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:3732	F		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0042743	hydrogen peroxide metabolic process	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:3732	P		Seeded From UniProt	complete
part_of	GO:0042645	mitochondrial nucleoid	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:3732	C		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0042554	superoxide anion generation	PMID:16677818^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:2447406,MGI:MGI:2679331	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0042554	superoxide anion generation	PMID:15781740^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857480	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0042554	superoxide anion generation	PMID:10212301^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857344	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0042542	response to hydrogen peroxide	PMID:15642323^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857480	P	has_participant:(EMAPA:32871)	Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0042493	response to drug	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:3732	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0042311	vasodilation	PMID:15637112^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857480	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0032364	oxygen homeostasis	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P04179	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0031667	response to nutrient levels	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:3732	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0030335	positive regulation of cell migration	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P04179	P		Seeded From UniProt	complete
enables	GO:0030145	manganese ion binding	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P04179	F		Seeded From UniProt	complete
enables	GO:0030145	manganese ion binding	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:3732	F		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0030097	hemopoiesis	PMID:8790408^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857480	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0030097	hemopoiesis	PMID:16219542^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0022904	respiratory electron transport chain	PMID:19478076^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857344	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0022904	respiratory electron transport chain	PMID:11226230^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857344	P		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:3732	F		Seeded From UniProt	complete
enables	GO:0019825	oxygen binding	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:3732	F		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0019430	removal of superoxide radicals	PMID:16873728^[17]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857129 MGI:MGI:1857480	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0019430	removal of superoxide radicals	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P04179	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0019430	removal of superoxide radicals	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:3732	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0014823	response to activity	PMID:15781740^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857480	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0010332	response to gamma radiation	PMID:15182862^[18]	ECO:0000316	genetic interaction evidence used in manual assertion	MGI:MGI:104887 MGI:MGI:98352	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0009791	post-embryonic development	PMID:8790408^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857480	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0009791	post-embryonic development	PMID:7493016^[19]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857344	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0008637	apoptotic mitochondrial changes	PMID:11226230^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857344	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0008631	intrinsic apoptotic signaling pathway in response to oxidative stress	PMID:15642323^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857480	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0008630	intrinsic apoptotic signaling pathway in response to DNA damage	PMID:15642323^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857480	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0008285	negative regulation of cell population proliferation	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P04179	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0008217	regulation of blood pressure	PMID:17023572^[20]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857344	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0007626	locomotory behavior	PMID:8790408^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857480	P		Seeded From UniProt	complete
NOT\|acts_upstream_of_or_within	GO:0007605	sensory perception of sound	PMID:16843623^[21]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857344	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0007507	heart development	PMID:7493016^[19]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857344	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0007005	mitochondrion organization	PMID:8790408^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857480	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0007005	mitochondrion organization	PMID:15205258^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857344	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0007005	mitochondrion organization	PMID:11527927^[22]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857344	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0006979	response to oxidative stress	PMID:19478076^[15]	ECO:0000316	genetic interaction evidence used in manual assertion	MGI:MGI:107207	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0006979	response to oxidative stress	PMID:17322295^[23]	ECO:0000316	genetic interaction evidence used in manual assertion	MGI:MGI:109169	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0006979	response to oxidative stress	PMID:15182862^[18]	ECO:0000316	genetic interaction evidence used in manual assertion	MGI:MGI:104887 MGI:MGI:98352	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0006979	response to oxidative stress	PMID:19478076^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857344	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0006979	response to oxidative stress	PMID:15182862^[18]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857344	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0006801	superoxide metabolic process	PMID:15637112^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857480	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0006801	superoxide metabolic process	PMID:12176043^[24]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:2176435,MGI:MGI:2447406	P	occurs_in:(EMAPA:16846)	Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0006801	superoxide metabolic process	PMID:10049502^[25]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857344	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0006801	superoxide metabolic process	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P04179	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0006749	glutathione metabolic process	PMID:10049502^[25]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857344	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0006357	regulation of transcription by RNA polymerase II	PMID:17670746^[26]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0006357	regulation of transcription by RNA polymerase II	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P04179	P		Seeded From UniProt	complete
part_of	GO:0005759	mitochondrial matrix	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P04179	C		Seeded From UniProt	complete
part_of	GO:0005743	mitochondrial inner membrane	PMID:12865426^[27]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:18614015^[28]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:14651853^[29]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(EMAPA:16846)\|part_of:(EMAPA:16894)\|part_of:(EMAPA:17373)\|part_of:(EMAPA:16105)	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:24191052^[30]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:22474353^[31]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:17923681^[32]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:17597094^[33]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:16103131^[34]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:12931191^[35]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000182)	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:11583975^[36]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(EMAPA:16846) part_of:(CL:0000182)	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P04179	C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:3732	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:3732	C		Seeded From UniProt	complete
enables	GO:0004784	superoxide dismutase activity	PMID:23195678^[37]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:2447406,MGI:MGI:2665300	F	occurs_in:(EMAPA:17373)	Seeded From UniProt	complete
enables	GO:0004784	superoxide dismutase activity	PMID:15182862^[18]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857344	F	occurs_in:(EMAPA:16894)\|occurs_in:(EMAPA:16105)\|occurs_in:(EMAPA:16846)	Seeded From UniProt	complete
enables	GO:0004784	superoxide dismutase activity	PMID:12176043^[24]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:2176435,MGI:MGI:2447406	F	occurs_in:(EMAPA:16846)	Seeded From UniProt	complete
enables	GO:0004784	superoxide dismutase activity	PMID:9651187^[38]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004784	superoxide dismutase activity	PMID:7333654^[39]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004784	superoxide dismutase activity	PMID:18218638^[9]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004784	superoxide dismutase activity	PMID:12646716^[40]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004784	superoxide dismutase activity	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P04179	F		Seeded From UniProt	complete
enables	GO:0004784	superoxide dismutase activity	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:3732	F		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:3732	F		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0003069	acetylcholine-mediated vasodilation involved in regulation of systemic arterial blood pressure	PMID:16873728^[17]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857129 MGI:MGI:1857480	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0003032	detection of oxygen	PMID:11156968^[41]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857344	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0001889	liver development	PMID:17367743^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:2177602,MGI:MGI:2447406	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0001836	release of cytochrome c from mitochondria	PMID:15642323^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857480	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0001836	release of cytochrome c from mitochondria	PMID:10212301^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857344	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0001315	age-dependent response to reactive oxygen species	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P04179	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0001306	age-dependent response to oxidative stress	PMID:11226230^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857344	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0000303	response to superoxide	PMID:15642323^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857480	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0000303	response to superoxide	PMID:11156968^[41]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857344	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0000303	response to superoxide	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P04179	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0000302	response to reactive oxygen species	PMID:9927656^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857344	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0000302	response to reactive oxygen species	PMID:9462746^[42]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857344	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0000302	response to reactive oxygen species	PMID:17145560^[43]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857344	P	occurs_in:(EMAPA:35578) occurs_in:(CL:0000515)	Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0000302	response to reactive oxygen species	PMID:16219542^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0000302	response to reactive oxygen species	PMID:15205258^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:1857344	P		Seeded From UniProt	complete
involved_in	GO:0071361	cellular response to ethanol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07895 ensembl:ENSRNOP00000025794	P		Seeded From UniProt	complete
involved_in	GO:0071000	response to magnetism	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07895 ensembl:ENSRNOP00000025794	P		Seeded From UniProt	complete
involved_in	GO:0051602	response to electrical stimulus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07895 ensembl:ENSRNOP00000025794	P		Seeded From UniProt	complete
involved_in	GO:0051260	protein homooligomerization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07895 ensembl:ENSRNOP00000025794	P		Seeded From UniProt	complete
involved_in	GO:0050665	hydrogen peroxide biosynthetic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07895 ensembl:ENSRNOP00000025794	P		Seeded From UniProt	complete
involved_in	GO:0046686	response to cadmium ion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07895 ensembl:ENSRNOP00000025794	P		Seeded From UniProt	complete
involved_in	GO:0043066	negative regulation of apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07895 ensembl:ENSRNOP00000025794	P		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07895 ensembl:ENSRNOP00000025794	F		Seeded From UniProt	complete
involved_in	GO:0042743	hydrogen peroxide metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07895 ensembl:ENSRNOP00000025794	P		Seeded From UniProt	complete
part_of	GO:0042645	mitochondrial nucleoid	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07895 ensembl:ENSRNOP00000025794	C		Seeded From UniProt	complete
involved_in	GO:0042542	response to hydrogen peroxide	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07895 ensembl:ENSRNOP00000025794	P		Seeded From UniProt	complete
involved_in	GO:0042493	response to drug	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07895 ensembl:ENSRNOP00000025794	P		Seeded From UniProt	complete
involved_in	GO:0035902	response to immobilization stress	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07895 ensembl:ENSRNOP00000025794	P		Seeded From UniProt	complete
involved_in	GO:0035900	response to isolation stress	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07895 ensembl:ENSRNOP00000025794	P		Seeded From UniProt	complete
involved_in	GO:0034021	response to silicon dioxide	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07895 ensembl:ENSRNOP00000025794	P		Seeded From UniProt	complete
involved_in	GO:0033591	response to L-ascorbic acid	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07895 ensembl:ENSRNOP00000025794	P		Seeded From UniProt	complete
involved_in	GO:0032496	response to lipopolysaccharide	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07895 ensembl:ENSRNOP00000025794	P		Seeded From UniProt	complete
involved_in	GO:0031667	response to nutrient levels	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07895 ensembl:ENSRNOP00000025794	P		Seeded From UniProt	complete
enables	GO:0030145	manganese ion binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07895 ensembl:ENSRNOP00000025794	F		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07895 ensembl:ENSRNOP00000025794	F		Seeded From UniProt	complete
enables	GO:0019825	oxygen binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07895 ensembl:ENSRNOP00000025794	F		Seeded From UniProt	complete
involved_in	GO:0019430	removal of superoxide radicals	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07895 ensembl:ENSRNOP00000025794	P		Seeded From UniProt	complete
involved_in	GO:0014823	response to activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07895 ensembl:ENSRNOP00000025794	P		Seeded From UniProt	complete
involved_in	GO:0010269	response to selenium ion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07895 ensembl:ENSRNOP00000025794	P		Seeded From UniProt	complete
involved_in	GO:0010043	response to zinc ion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07895 ensembl:ENSRNOP00000025794	P		Seeded From UniProt	complete
involved_in	GO:0010042	response to manganese ion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07895 ensembl:ENSRNOP00000025794	P		Seeded From UniProt	complete
involved_in	GO:0009409	response to cold	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07895 ensembl:ENSRNOP00000025794	P		Seeded From UniProt	complete
involved_in	GO:0009314	response to radiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07895 ensembl:ENSRNOP00000025794	P		Seeded From UniProt	complete
involved_in	GO:0007568	aging	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07895 ensembl:ENSRNOP00000025794	P		Seeded From UniProt	complete
involved_in	GO:0006979	response to oxidative stress	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07895 ensembl:ENSRNOP00000025794	P		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07895 ensembl:ENSRNOP00000025794	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07895 ensembl:ENSRNOP00000025794	C		Seeded From UniProt	complete
enables	GO:0004784	superoxide dismutase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07895 ensembl:ENSRNOP00000025794	F		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07895 ensembl:ENSRNOP00000025794	F		Seeded From UniProt	complete
involved_in	GO:0001666	response to hypoxia	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P07895 ensembl:ENSRNOP00000025794	P		Seeded From UniProt	complete
enables	GO:0004784	superoxide dismutase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001189 InterPro:IPR019831 InterPro:IPR019832 InterPro:IPR019833	F		Seeded From UniProt	complete
involved_in	GO:0006801	superoxide metabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001189 InterPro:IPR019831 InterPro:IPR019832 InterPro:IPR019833	P		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001189 InterPro:IPR019831 InterPro:IPR019832 InterPro:IPR019833	F		Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001189 InterPro:IPR019831 InterPro:IPR019832 InterPro:IPR019833	P		Seeded From UniProt	complete
enables	GO:0004784	superoxide dismutase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:1.15.1.1	F		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0496	C		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
enables	GO:0016491	oxidoreductase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0560	F		Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0560	P		Seeded From UniProt	complete
part_of	GO:0005759	mitochondrial matrix	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0170	C		Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 Friedman, JS et al. (2004) SOD2-deficiency anemia: protein oxidation and altered protein expression reveal targets of damage, stress response, and antioxidant responsiveness. Blood 104 2565-73 PubMed GONUTS page
↑ Werner, HB et al. (2007) Proteolipid protein is required for transport of sirtuin 2 into CNS myelin. J. Neurosci. 27 7717-30 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Asikainen, TM et al. (2002) Increased sensitivity of homozygous Sod2 mutant mice to oxygen toxicity. Free Radic. Biol. Med. 32 175-86 PubMed GONUTS page
↑ ^5.0 ^5.1 Lenart, J et al. (2007) Deficiency of manganese superoxide dismutase in hepatocytes disrupts zonated gene expression in mouse liver. Arch. Biochem. Biophys. 462 238-44 PubMed GONUTS page
↑ ^6.0 ^6.1 Melov, S et al. (1999) Mitochondrial disease in superoxide dismutase 2 mutant mice. Proc. Natl. Acad. Sci. U.S.A. 96 846-51 PubMed GONUTS page
↑ ^7.0 ^7.1 Misawa, H et al. (2006) Conditional knockout of Mn superoxide dismutase in postnatal motor neurons reveals resistance to mitochondrial generated superoxide radicals. Neurobiol. Dis. 23 169-77 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 ^8.3 ^8.4 Lebovitz, RM et al. (1996) Neurodegeneration, myocardial injury, and perinatal death in mitochondrial superoxide dismutase-deficient mice. Proc. Natl. Acad. Sci. U.S.A. 93 9782-7 PubMed GONUTS page
↑ ^9.0 ^9.1 Bogunovic, B et al. (2008) An unexpected functional link between lysosomal thiol reductase and mitochondrial manganese superoxide dismutase. J. Biol. Chem. 283 8855-62 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 Lechpammer, S et al. (2005) Adipocyte differentiation in Sod2(-/-) and Sod2(+/+) murine bone marrow stromal cells is associated with low antioxidant pools. Exp. Hematol. 33 1201-8 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 Yan, C et al. (2005) Increased superoxide leads to decreased flow-induced dilation in resistance arteries of Mn-SOD-deficient mice. Am. J. Physiol. Heart Circ. Physiol. 288 H2225-31 PubMed GONUTS page
↑ ^12.0 ^12.1 Kinugawa, S et al. (2005) Limited exercise capacity in heterozygous manganese superoxide dismutase gene-knockout mice: roles of superoxide anion and nitric oxide. Circulation 111 1480-6 PubMed GONUTS page
↑ ^13.0 ^13.1 Fujimura, M et al. (1999) Manganese superoxide dismutase mediates the early release of mitochondrial cytochrome C and subsequent DNA fragmentation after permanent focal cerebral ischemia in mice. J. Neurosci. 19 3414-22 PubMed GONUTS page
↑ ^14.0 ^14.1 ^14.2 ^14.3 ^14.4 Reddy, VN et al. (2004) Effects of variation in superoxide dismutases (SOD) on oxidative stress and apoptosis in lens epithelium. Exp. Eye Res. 79 859-68 PubMed GONUTS page
↑ ^15.0 ^15.1 ^15.2 Lapointe, J et al. (2009) Reversal of the mitochondrial phenotype and slow development of oxidative biomarkers of aging in long-lived Mclk1+/- mice. J. Biol. Chem. 284 20364-74 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 Kokoszka, JE et al. (2001) Increased mitochondrial oxidative stress in the Sod2 (+/-) mouse results in the age-related decline of mitochondrial function culminating in increased apoptosis. Proc. Natl. Acad. Sci. U.S.A. 98 2278-83 PubMed GONUTS page
↑ ^17.0 ^17.1 Ohashi, M et al. (2006) MnSOD deficiency increases endothelial dysfunction in ApoE-deficient mice. Arterioscler. Thromb. Vasc. Biol. 26 2331-6 PubMed GONUTS page
↑ ^18.0 ^18.1 ^18.2 ^18.3 Van Remmen, H et al. (2004) Multiple deficiencies in antioxidant enzymes in mice result in a compound increase in sensitivity to oxidative stress. Free Radic. Biol. Med. 36 1625-34 PubMed GONUTS page
↑ ^19.0 ^19.1 Li, Y et al. (1995) Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase. Nat. Genet. 11 376-81 PubMed GONUTS page
↑ Rodriguez-Iturbe, B et al. (2007) Association of mitochondrial SOD deficiency with salt-sensitive hypertension and accelerated renal senescence. J. Appl. Physiol. 102 255-60 PubMed GONUTS page
↑ Le, T & Keithley, EM (2007) Effects of antioxidants on the aging inner ear. Hear. Res. 226 194-202 PubMed GONUTS page
↑ Sandbach, JM et al. (2001) Ocular pathology in mitochondrial superoxide dismutase (Sod2)-deficient mice. Invest. Ophthalmol. Vis. Sci. 42 2173-8 PubMed GONUTS page
↑ Oktay, Y et al. (2007) Hypoxia-inducible factor 2alpha regulates expression of the mitochondrial aconitase chaperone protein frataxin. J. Biol. Chem. 282 11750-6 PubMed GONUTS page
↑ ^24.0 ^24.1 Ikegami, T et al. (2002) Model mice for tissue-specific deletion of the manganese superoxide dismutase (MnSOD) gene. Biochem. Biophys. Res. Commun. 296 729-36 PubMed GONUTS page
↑ ^25.0 ^25.1 Van Remmen, H et al. (1999) Characterization of the antioxidant status of the heterozygous manganese superoxide dismutase knockout mouse. Arch. Biochem. Biophys. 363 91-7 PubMed GONUTS page
↑ Yao, D et al. (2007) High glucose increases angiopoietin-2 transcription in microvascular endothelial cells through methylglyoxal modification of mSin3A. J. Biol. Chem. 282 31038-45 PubMed GONUTS page
↑ Da Cruz, S et al. (2003) Proteomic analysis of the mouse liver mitochondrial inner membrane. J. Biol. Chem. 278 41566-71 PubMed GONUTS page
↑ Pagliarini, DJ et al. (2008) A mitochondrial protein compendium elucidates complex I disease biology. Cell 134 112-23 PubMed GONUTS page
↑ Mootha, VK et al. (2003) Integrated analysis of protein composition, tissue diversity, and gene regulation in mouse mitochondria. Cell 115 629-40 PubMed GONUTS page
↑ Mashimo, M et al. (2013) ADP-ribosyl-acceptor hydrolase 3 regulates poly (ADP-ribose) degradation and cell death during oxidative stress. Proc. Natl. Acad. Sci. U.S.A. 110 18964-9 PubMed GONUTS page
↑ Ke, BX et al. (2012) Tissue-specific splicing of an Ndufs6 gene-trap insertion generates a mitochondrial complex I deficiency-specific cardiomyopathy. Proc. Natl. Acad. Sci. U.S.A. 109 6165-70 PubMed GONUTS page
↑ Lombard, DB et al. (2007) Mammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation. Mol. Cell. Biol. 27 8807-14 PubMed GONUTS page
↑ Martelli, A et al. (2007) Frataxin is essential for extramitochondrial Fe-S cluster proteins in mammalian tissues. Hum. Mol. Genet. 16 2651-8 PubMed GONUTS page
↑ Diaz, F et al. (2005) Mice lacking COX10 in skeletal muscle recapitulate the phenotype of progressive mitochondrial myopathies associated with cytochrome c oxidase deficiency. Hum. Mol. Genet. 14 2737-48 PubMed GONUTS page
↑ Danial, NN et al. (2003) BAD and glucokinase reside in a mitochondrial complex that integrates glycolysis and apoptosis. Nature 424 952-6 PubMed GONUTS page
↑ Baumgart, E et al. (2001) Mitochondrial alterations caused by defective peroxisomal biogenesis in a mouse model for Zellweger syndrome (PEX5 knockout mouse). Am. J. Pathol. 159 1477-94 PubMed GONUTS page
↑ Parajuli, N & MacMillan-Crow, LA (2013) Role of reduced manganese superoxide dismutase in ischemia-reperfusion injury: a possible trigger for autophagy and mitochondrial biogenesis? Am. J. Physiol. Renal Physiol. 304 F257-67 PubMed GONUTS page
↑ Tsan, MF et al. (1998) Susceptibility of heterozygous MnSOD gene-knockout mice to oxygen toxicity. Am. J. Respir. Cell Mol. Biol. 19 114-20 PubMed GONUTS page
↑ Szymura, JM et al. (1981) Mouse mitochondrial superoxide dismutase locus is on chromosome 17. Immunogenetics 14 231-40 PubMed GONUTS page
↑ Khan, JY & Black, SM (2003) Developmental changes in murine brain antioxidant enzymes. Pediatr. Res. 54 77-82 PubMed GONUTS page
↑ ^41.0 ^41.1 Copin, JC et al. (2001) Prolonged hypoxia during cell development protects mature manganese superoxide dismutase-deficient astrocytes from damage by oxidative stress. FASEB J. 15 525-34 PubMed GONUTS page
↑ Melov, S et al. (1998) A novel neurological phenotype in mice lacking mitochondrial manganese superoxide dismutase. Nat. Genet. 18 159-63 PubMed GONUTS page
↑ Vasilaki, A et al. (2006) Genetic modification of the manganese superoxide dismutase/glutathione peroxidase 1 pathway influences intracellular ROS generation in quiescent, but not contracting, skeletal muscle cells. Free Radic. Biol. Med. 41 1719-25 PubMed GONUTS page

[PMID:15205258-1] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 Friedman, JS et al. (2004) SOD2-deficiency anemia: protein oxidation and altered protein expression reveal targets of damage, stress response, and antioxidant responsiveness. Blood 104 2565-73 PubMed GONUTS page

[PMID:17634366-2] Werner, HB et al. (2007) Proteolipid protein is required for transport of sirtuin 2 into CNS myelin. J. Neurosci. 27 7717-30 PubMed GONUTS page

[PMID:21873635-3] 3.0 ^3.1 ^3.2 ^3.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:11796207-4] Asikainen, TM et al. (2002) Increased sensitivity of homozygous Sod2 mutant mice to oxygen toxicity. Free Radic. Biol. Med. 32 175-86 PubMed GONUTS page

[PMID:17367743-5] 5.0 ^5.1 Lenart, J et al. (2007) Deficiency of manganese superoxide dismutase in hepatocytes disrupts zonated gene expression in mouse liver. Arch. Biochem. Biophys. 462 238-44 PubMed GONUTS page

[PMID:9927656-6] 6.0 ^6.1 Melov, S et al. (1999) Mitochondrial disease in superoxide dismutase 2 mutant mice. Proc. Natl. Acad. Sci. U.S.A. 96 846-51 PubMed GONUTS page

[PMID:16677818-7] 7.0 ^7.1 Misawa, H et al. (2006) Conditional knockout of Mn superoxide dismutase in postnatal motor neurons reveals resistance to mitochondrial generated superoxide radicals. Neurobiol. Dis. 23 169-77 PubMed GONUTS page

[PMID:8790408-8] 8.0 ^8.1 ^8.2 ^8.3 ^8.4 Lebovitz, RM et al. (1996) Neurodegeneration, myocardial injury, and perinatal death in mitochondrial superoxide dismutase-deficient mice. Proc. Natl. Acad. Sci. U.S.A. 93 9782-7 PubMed GONUTS page

[PMID:18218638-9] 9.0 ^9.1 Bogunovic, B et al. (2008) An unexpected functional link between lysosomal thiol reductase and mitochondrial manganese superoxide dismutase. J. Biol. Chem. 283 8855-62 PubMed GONUTS page

[PMID:16219542-10] 10.0 ^10.1 ^10.2 Lechpammer, S et al. (2005) Adipocyte differentiation in Sod2(-/-) and Sod2(+/+) murine bone marrow stromal cells is associated with low antioxidant pools. Exp. Hematol. 33 1201-8 PubMed GONUTS page

[PMID:15637112-11] 11.0 ^11.1 ^11.2 Yan, C et al. (2005) Increased superoxide leads to decreased flow-induced dilation in resistance arteries of Mn-SOD-deficient mice. Am. J. Physiol. Heart Circ. Physiol. 288 H2225-31 PubMed GONUTS page

[PMID:15781740-12] 12.0 ^12.1 Kinugawa, S et al. (2005) Limited exercise capacity in heterozygous manganese superoxide dismutase gene-knockout mice: roles of superoxide anion and nitric oxide. Circulation 111 1480-6 PubMed GONUTS page

[PMID:10212301-13] 13.0 ^13.1 Fujimura, M et al. (1999) Manganese superoxide dismutase mediates the early release of mitochondrial cytochrome C and subsequent DNA fragmentation after permanent focal cerebral ischemia in mice. J. Neurosci. 19 3414-22 PubMed GONUTS page

[PMID:15642323-14] 14.0 ^14.1 ^14.2 ^14.3 ^14.4 Reddy, VN et al. (2004) Effects of variation in superoxide dismutases (SOD) on oxidative stress and apoptosis in lens epithelium. Exp. Eye Res. 79 859-68 PubMed GONUTS page

[PMID:19478076-15] 15.0 ^15.1 ^15.2 Lapointe, J et al. (2009) Reversal of the mitochondrial phenotype and slow development of oxidative biomarkers of aging in long-lived Mclk1+/- mice. J. Biol. Chem. 284 20364-74 PubMed GONUTS page

[PMID:11226230-16] 16.0 ^16.1 ^16.2 Kokoszka, JE et al. (2001) Increased mitochondrial oxidative stress in the Sod2 (+/-) mouse results in the age-related decline of mitochondrial function culminating in increased apoptosis. Proc. Natl. Acad. Sci. U.S.A. 98 2278-83 PubMed GONUTS page

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MOUSE:SODM

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