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MGI:Sod1

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Species (Taxon ID) Mus musculus (house mouse) (taxon:10090)
Gene Name(s) Sod1 ( synonyms: Cu(2+)-Zn2+ superoxide dismutase, Cu/Zn-SOD, CuZnSOD, Ipo-1, Ipo1, Sod-1, SODC )
Protein Name(s) superoxide dismutase 1, soluble,
External Links
MGI MGI:98351

Annotations

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0000187

activation of MAPK activity

MGI:MGI:2387280
PMID:12223545[1]

IDA: Inferred from Direct Assay

P

From MGI

GO:0000302

response to reactive oxygen species

MGI:MGI:3699763
PMID:17059387[2]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857873

P

From MGI

GO:0000303

response to superoxide

MGI:MGI:1201750
PMID:9516486[3]

IMP: Inferred from Mutant Phenotype

MGI:MGI:3526701

P

From MGI

GO:0000303

response to superoxide

MGI:MGI:1314762
PMID:9788901[4]

IMP: Inferred from Mutant Phenotype

MGI:MGI:3526701

P

From MGI

GO:0000303

response to superoxide

MGI:MGI:3611643
PMID:16357131[5]

IMP: Inferred from Mutant Phenotype

MGI:MGI:2680903

P

From MGI

GO:0000303

response to superoxide

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P00441

P

From MGI

GO:0001541

ovarian follicle development

MGI:MGI:1889068
PMID:9724058[6]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857873

P

From MGI

GO:0001819

positive regulation of cytokine production

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P00441

P

From MGI

GO:0001895

retina homeostasis

MGI:MGI:3654862
PMID:16844785[7]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857873

P

From MGI

GO:0002262

myeloid cell homeostasis

MGI:MGI:2149223
PMID:11493445[8]

IGI: Inferred from Genetic Interaction

MGI:MGI:95480

P

From MGI

GO:0002262

myeloid cell homeostasis

MGI:MGI:2149223
PMID:11493445[8]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857872

P

From MGI

GO:0004784

superoxide dismutase activity

MGI:MGI:1201750
PMID:9516486[3]

IMP: Inferred from Mutant Phenotype

MGI:MGI:3526701

F

From MGI

GO:0004784

superoxide dismutase activity

MGI:MGI:1314762
PMID:9788901[4]

IMP: Inferred from Mutant Phenotype

MGI:MGI:3526701

F

From MGI

GO:0004784

superoxide dismutase activity

MGI:MGI:1342989
PMID:10436316[9]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857872

F

From MGI

GO:0004784

superoxide dismutase activity

MGI:MGI:1351737
PMID:10471451[10]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857872

F

From MGI

GO:0004784

superoxide dismutase activity

MGI:MGI:1353351
PMID:10679476[11]

IMP: Inferred from Mutant Phenotype

MGI:MGI:2387861

F

From MGI

GO:0004784

superoxide dismutase activity

MGI:MGI:2136726
PMID:11404260[12]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857872

F

From MGI

GO:0004784

superoxide dismutase activity

MGI:MGI:2152694
PMID:11557311[13]

TAS: Traceable Author Statement

F

From MGI

GO:0004784

superoxide dismutase activity

MGI:MGI:2387280
PMID:12223545[1]

TAS: Traceable Author Statement

F

From MGI

GO:0004784

superoxide dismutase activity

MGI:MGI:2655950
PMID:12646716[14]

IDA: Inferred from Direct Assay

F

From MGI

GO:0004784

superoxide dismutase activity

MGI:MGI:2682495
PMID:14679182[15]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857873

F

From MGI

GO:0004784

superoxide dismutase activity

MGI:MGI:3522379
PMID:15317809[16]

IDA: Inferred from Direct Assay

F

From MGI

GO:0004784

superoxide dismutase activity

MGI:MGI:3608389
PMID:12968068[17]

IDA: Inferred from Direct Assay

F

From MGI

GO:0004784

superoxide dismutase activity

MGI:MGI:3624710
PMID:16716900[18]

IMP: Inferred from Mutant Phenotype

MGI:MGI:2680903

F

From MGI

GO:0004784

superoxide dismutase activity

MGI:MGI:3625573
PMID:12433839[19]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857873

F

From MGI

GO:0004784

superoxide dismutase activity

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P07632

F

From MGI

GO:0004784

superoxide dismutase activity

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P00441

F

From MGI

GO:0004784

superoxide dismutase activity

MGI:MGI:54701
PMID:291939[20]

IDA: Inferred from Direct Assay

F

From MGI

GO:0004784

superoxide dismutase activity

MGI:MGI:54917
PMID:7444718[21]

IDA: Inferred from Direct Assay

F

From MGI

GO:0004784

superoxide dismutase activity

MGI:MGI:80951
PMID:8673102[22]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857872

F

From MGI

GO:0005507

copper ion binding

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P07632

F

From MGI

GO:0005507

copper ion binding

MGI:MGI:4459044

PANTHER:PTN000000113

F

From MGI

GO:0005507

copper ion binding

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P00441

F

From MGI

GO:0005515

protein binding

MGI:MGI:77968
PMID:2960971[23]

IPI: Inferred from Physical Interaction

UniProtKB:P00441

F

From MGI

GO:0005615

extracellular space

MGI:MGI:3574179
PMID:15634772[24]

IDA: Inferred from Direct Assay

C

From MGI

GO:0005615

extracellular space

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P00441

C

From MGI

GO:0005622

intracellular

MGI:MGI:4837328
PMID:20510358[25]

IMP: Inferred from Mutant Phenotype

C

From MGI

GO:0005634

nucleus

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P07632

C

From MGI

GO:0005634

nucleus

MGI:MGI:4459044

PANTHER:PTN000000161

C

From MGI

GO:0005634

nucleus

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P00441

C

From MGI

GO:0005737

cytoplasm

MGI:MGI:2152694
PMID:11557311[13]

TAS: Traceable Author Statement

C

From MGI

GO:0005737

cytoplasm

MGI:MGI:2154458

ISO: Inferred from Sequence Orthology

UniProtKB:P00441

C

From MGI

GO:0005737

cytoplasm

MGI:MGI:3822232
PMID:18809582[26]

ISO: Inferred from Sequence Orthology

UniProtKB:P00441

C

From MGI

GO:0005737

cytoplasm

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P07632

C

From MGI

GO:0005739

mitochondrion

MGI:MGI:2682130
PMID:14651853[27]

IDA: Inferred from Direct Assay

C

From MGI

GO:0005739

mitochondrion

MGI:MGI:3852644
PMID:18614015[28]

IDA: Inferred from Direct Assay

C

From MGI

GO:0005739

mitochondrion

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P07632

C

From MGI

GO:0005739

mitochondrion

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P00441

C

From MGI

GO:0005777

peroxisome

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P07632

C

From MGI

GO:0005777

peroxisome

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P00441

C

From MGI

GO:0005829

cytosol

MGI:MGI:4459044

PANTHER:PTN000000161

C

From MGI

GO:0005829

cytosol

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P00441

C

From MGI

GO:0006302

double-strand break repair

MGI:MGI:3691744
PMID:15642323[29]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857873

P

From MGI

GO:0006309

apoptotic DNA fragmentation

MGI:MGI:2387280
PMID:12223545[1]

IDA: Inferred from Direct Assay

P

From MGI

GO:0006749

glutathione metabolic process

MGI:MGI:3640408
PMID:16377630[30]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857872

P

From MGI

GO:0006801

superoxide metabolic process

MGI:MGI:2136726
PMID:11404260[12]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857872

P

From MGI

GO:0006801

superoxide metabolic process

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P07632

P

From MGI

GO:0006879

cellular iron ion homeostasis

MGI:MGI:3640408
PMID:16377630[30]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857872

P

From MGI

GO:0006979

response to oxidative stress

MGI:MGI:2387280
PMID:12223545[1]

IDA: Inferred from Direct Assay

P

From MGI

GO:0006979

response to oxidative stress

MGI:MGI:3624710
PMID:16716900[18]

IMP: Inferred from Mutant Phenotype

MGI:MGI:2680903

P

From MGI

GO:0006979

response to oxidative stress

MGI:MGI:3699763
PMID:17059387[2]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857873

P

From MGI

GO:0006979

response to oxidative stress

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P07632

P

From MGI

GO:0007283

spermatogenesis

MGI:MGI:3688805
PMID:16036348[31]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857873

P

From MGI

GO:0007566

embryo implantation

MGI:MGI:1201750
PMID:9516486[3]

IMP: Inferred from Mutant Phenotype

MGI:MGI:3526701

P

From MGI

GO:0007568

aging

MGI:MGI:3640408
PMID:16377630[30]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857872

P

From MGI

GO:0007569

cell aging

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P00441

P

From MGI

GO:0007605

sensory perception of sound

MGI:MGI:1342989
PMID:10436316[9]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857872

P

From MGI

GO:0007605

sensory perception of sound

MGI:MGI:3607480
PMID:16055286[32]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857873

P

From MGI

GO:0007605

sensory perception of sound

MGI:MGI:3700629
PMID:10464373[33]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857872

P

From MGI

GO:0007605

sensory perception of sound

MGI:MGI:3700629
PMID:10464373[33]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857872

P

From MGI

GO:0007626

locomotory behavior

MGI:MGI:1344528
PMID:10433959[34]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857872

P

From MGI

GO:0008089

anterograde axon cargo transport

MGI:MGI:4837328
PMID:20510358[25]

IMP: Inferred from Mutant Phenotype

P

From MGI

GO:0008090

retrograde axon cargo transport

MGI:MGI:4837328
PMID:20510358[25]

IMP: Inferred from Mutant Phenotype

P

From MGI

GO:0008217

regulation of blood pressure

MGI:MGI:3625573
PMID:12433839[19]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857873

P

From MGI

GO:0008270

zinc ion binding

MGI:MGI:4459044

PANTHER:PTN000000113

F

From MGI

GO:0008270

zinc ion binding

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P00441

F

From MGI

GO:0009408

response to heat

MGI:MGI:3688941
PMID:16942767[35]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857873

P

From MGI

GO:0010033

response to organic substance

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P00441

P

From MGI

GO:0016209

antioxidant activity

MGI:MGI:1354194

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0049

F

From MGI

GO:0016491

oxidoreductase activity

MGI:MGI:1354194

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0560

F

From MGI

GO:0019226

transmission of nerve impulse

MGI:MGI:1344528
PMID:10433959[34]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857872

P

From MGI

GO:0019430

removal of superoxide radicals

MGI:MGI:1201750
PMID:9516486[3]

IMP: Inferred from Mutant Phenotype

MGI:MGI:3526701

P

From MGI

GO:0019430

removal of superoxide radicals

MGI:MGI:1314762
PMID:9788901[4]

IMP: Inferred from Mutant Phenotype

MGI:MGI:3526701

P

From MGI

GO:0019430

removal of superoxide radicals

MGI:MGI:1342989
PMID:10436316[9]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857872

P

From MGI

GO:0019430

removal of superoxide radicals

MGI:MGI:1351737
PMID:10471451[10]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857872

P

From MGI

GO:0019430

removal of superoxide radicals

MGI:MGI:1353351
PMID:10679476[11]

IMP: Inferred from Mutant Phenotype

MGI:MGI:2387861

P

From MGI

GO:0019430

removal of superoxide radicals

MGI:MGI:2149223
PMID:11493445[8]

IGI: Inferred from Genetic Interaction

MGI:MGI:95480

P

From MGI

GO:0019430

removal of superoxide radicals

MGI:MGI:2149223
PMID:11493445[8]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857872

P

From MGI

GO:0019430

removal of superoxide radicals

MGI:MGI:2152694
PMID:11557311[13]

TAS: Traceable Author Statement

P

From MGI

GO:0019430

removal of superoxide radicals

MGI:MGI:3625573
PMID:12433839[19]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857873

P

From MGI

GO:0019430

removal of superoxide radicals

MGI:MGI:3710732
PMID:17448893[36]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857873

P

From MGI

GO:0019430

removal of superoxide radicals

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P07632

P

From MGI

GO:0019430

removal of superoxide radicals

MGI:MGI:80951
PMID:8673102[22]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857872

P

From MGI

GO:0030346

protein phosphatase 2B binding

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P00441

F

From MGI

GO:0031012

extracellular matrix

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P00441

C

From MGI

GO:0031410

cytoplasmic vesicle

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P00441

C

From MGI

GO:0031667

response to nutrient levels

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P07632

P

From MGI

GO:0032287

peripheral nervous system myelin maintenance

MGI:MGI:1344528
PMID:10433959[34]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857872

P

From MGI

GO:0032839

dendrite cytoplasm

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P00441

C

From MGI

GO:0040014

regulation of multicellular organism growth

MGI:MGI:3640408
PMID:16377630[30]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857872

P

From MGI

GO:0042493

response to drug

MGI:MGI:3692725
PMID:16831125[37]

IMP: Inferred from Mutant Phenotype

MGI:MGI:3526701

P

From MGI

GO:0042542

response to hydrogen peroxide

MGI:MGI:3691744
PMID:15642323[29]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857873

P

From MGI

GO:0042554

superoxide anion generation

MGI:MGI:3522379
PMID:15317809[16]

IDA: Inferred from Direct Assay

P

From MGI

GO:0043025

neuronal cell body

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P07632

C

From MGI

GO:0043025

neuronal cell body

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P00441

C

From MGI

GO:0043066

negative regulation of apoptotic process

MGI:MGI:3688805
PMID:16036348[31]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857873

P

From MGI

GO:0043066

negative regulation of apoptotic process

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P07632

P

From MGI

GO:0043085

positive regulation of catalytic activity

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P07632

P

From MGI

GO:0043085

positive regulation of catalytic activity

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P00441

P

From MGI

GO:0043234

protein complex

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P00441

C

From MGI

GO:0043524

negative regulation of neuron apoptotic process

MGI:MGI:3700629
PMID:10464373[33]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857872

P

From MGI

GO:0045471

response to ethanol

MGI:MGI:3710732
PMID:17448893[36]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857873

P

From MGI

GO:0045541

negative regulation of cholesterol biosynthetic process

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P00441

P

From MGI

GO:0045859

regulation of protein kinase activity

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P00441

P

From MGI

GO:0046688

response to copper ion

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P07632

P

From MGI

GO:0046716

muscle cell homeostasis

MGI:MGI:3624710
PMID:16716900[18]

IMP: Inferred from Mutant Phenotype

MGI:MGI:2680903

P

From MGI

GO:0046872

metal ion binding

MGI:MGI:1354194

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0479

F

From MGI

GO:0046872

metal ion binding

MGI:MGI:2152098

IEA: Inferred from Electronic Annotation

InterPro:IPR001424

F

From MGI

GO:0048678

response to axon injury

MGI:MGI:80951
PMID:8673102[22]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857872

P

From MGI

GO:0050665

hydrogen peroxide biosynthetic process

MGI:MGI:2682495
PMID:14679182[15]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857873

P

From MGI

GO:0050665

hydrogen peroxide biosynthetic process

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P07632

P

From MGI

GO:0050665

hydrogen peroxide biosynthetic process

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P00441

P

From MGI

GO:0051087

chaperone binding

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P00441

F

From MGI

GO:0051881

regulation of mitochondrial membrane potential

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P00441

P

From MGI

GO:0055114

oxidation-reduction process

MGI:MGI:1201750
PMID:9516486[3]

IMP: Inferred from Mutant Phenotype

MGI:MGI:3526701

P

From MGI

GO:0055114

oxidation-reduction process

MGI:MGI:1314762
PMID:9788901[4]

IMP: Inferred from Mutant Phenotype

MGI:MGI:3526701

P

From MGI

GO:0055114

oxidation-reduction process

MGI:MGI:1342989
PMID:10436316[9]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857872

P

From MGI

GO:0055114

oxidation-reduction process

MGI:MGI:1351737
PMID:10471451[10]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857872

P

From MGI

GO:0055114

oxidation-reduction process

MGI:MGI:1353351
PMID:10679476[11]

IMP: Inferred from Mutant Phenotype

MGI:MGI:2387861

P

From MGI

GO:0055114

oxidation-reduction process

MGI:MGI:2136726
PMID:11404260[12]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857872

P

From MGI

GO:0055114

oxidation-reduction process

MGI:MGI:2152694
PMID:11557311[13]

TAS: Traceable Author Statement

P

From MGI

GO:0055114

oxidation-reduction process

MGI:MGI:2387280
PMID:12223545[1]

TAS: Traceable Author Statement

P

From MGI

GO:0055114

oxidation-reduction process

MGI:MGI:2655950
PMID:12646716[14]

IDA: Inferred from Direct Assay

P

From MGI

GO:0055114

oxidation-reduction process

MGI:MGI:2682495
PMID:14679182[15]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857873

P

From MGI

GO:0055114

oxidation-reduction process

MGI:MGI:3522379
PMID:15317809[16]

IDA: Inferred from Direct Assay

P

From MGI

GO:0055114

oxidation-reduction process

MGI:MGI:3608389
PMID:12968068[17]

IDA: Inferred from Direct Assay

P

From MGI

GO:0055114

oxidation-reduction process

MGI:MGI:3624710
PMID:16716900[18]

IMP: Inferred from Mutant Phenotype

MGI:MGI:2680903

P

From MGI

GO:0055114

oxidation-reduction process

MGI:MGI:3625573
PMID:12433839[19]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857873

P

From MGI

GO:0055114

oxidation-reduction process

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P07632

P

From MGI

GO:0055114

oxidation-reduction process

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P00441

P

From MGI

GO:0055114

oxidation-reduction process

MGI:MGI:54701
PMID:291939[20]

IDA: Inferred from Direct Assay

P

From MGI

GO:0055114

oxidation-reduction process

MGI:MGI:54917
PMID:7444718[21]

IDA: Inferred from Direct Assay

P

From MGI

GO:0055114

oxidation-reduction process

MGI:MGI:80951
PMID:8673102[22]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857872

P

From MGI

GO:0060047

heart contraction

MGI:MGI:1353351
PMID:10679476[11]

IMP: Inferred from Mutant Phenotype

MGI:MGI:2387861

P

From MGI

GO:0060047

heart contraction

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P00441

P

From MGI

GO:0060052

neurofilament cytoskeleton organization

MGI:MGI:1934092
PMID:11343650[38]

IGI: Inferred from Genetic Interaction

MGI:MGI:97313

P

From MGI

GO:0060052

neurofilament cytoskeleton organization

MGI:MGI:1934092
PMID:11343650[38]

IMP: Inferred from Mutant Phenotype

MGI:MGI:3574016

P

From MGI

GO:0060087

relaxation of vascular smooth muscle

MGI:MGI:2682495
PMID:14679182[15]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857873

P

From MGI

GO:0060087

relaxation of vascular smooth muscle

MGI:MGI:3625573
PMID:12433839[19]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857873

P

From MGI

GO:0060088

auditory receptor cell stereocilium organization

MGI:MGI:1344578
PMID:10466888[39]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857872

P

From MGI

GO:0060088

auditory receptor cell stereocilium organization

MGI:MGI:3700629
PMID:10464373[33]

IMP: Inferred from Mutant Phenotype

MGI:MGI:1857872

P

From MGI


Notes

References

See Help:References for how to manage references in GONUTS.
  1. 1.0 1.1 1.2 1.3 1.4 Noshita, N et al. (2002) Copper/zinc superoxide dismutase attenuates neuronal cell death by preventing extracellular signal-regulated kinase activation after transient focal cerebral ischemia in mice. J. Neurosci. 22 7923-30 PubMed GONUTS page
  2. 2.0 2.1 Iuchi, Y et al. (2007) Elevated oxidative stress in erythrocytes due to a SOD1 deficiency causes anaemia and triggers autoantibody production. Biochem. J. 402 219-27 PubMed GONUTS page
  3. 3.0 3.1 3.2 3.3 3.4 Ho, YS et al. (1998) Reduced fertility in female mice lacking copper-zinc superoxide dismutase. J. Biol. Chem. 273 7765-9 PubMed GONUTS page
  4. 4.0 4.1 4.2 4.3 Ho, YS et al. (1998) The nature of antioxidant defense mechanisms: a lesson from transgenic studies. Environ. Health Perspect. 106 Suppl 5 1219-28 PubMed GONUTS page
  5. Busuttil, RA et al. (2005) Organ-specific increase in mutation accumulation and apoptosis rate in CuZn-superoxide dismutase-deficient mice. Cancer Res. 65 11271-5 PubMed GONUTS page
  6. Matzuk, MM et al. (1998) Ovarian function in superoxide dismutase 1 and 2 knockout mice. Endocrinology 139 4008-11 PubMed GONUTS page
  7. Imamura, Y et al. (2006) Drusen, choroidal neovascularization, and retinal pigment epithelium dysfunction in SOD1-deficient mice: a model of age-related macular degeneration. Proc. Natl. Acad. Sci. U.S.A. 103 11282-7 PubMed GONUTS page
  8. 8.0 8.1 8.2 8.3 Hadjur, S et al. (2001) Defective hematopoiesis and hepatic steatosis in mice with combined deficiencies of the genes encoding Fancc and Cu/Zn superoxide dismutase. Blood 98 1003-11 PubMed GONUTS page
  9. 9.0 9.1 9.2 9.3 Ohlemiller, KK et al. () Targeted deletion of the cytosolic Cu/Zn-superoxide dismutase gene (Sod1) increases susceptibility to noise-induced hearing loss. Audiol. Neurootol. 4 237-46 PubMed GONUTS page
  10. 10.0 10.1 10.2 Kawase, M et al. (1999) Exacerbation of delayed cell injury after transient global ischemia in mutant mice with CuZn superoxide dismutase deficiency. Stroke 30 1962-8 PubMed GONUTS page
  11. 11.0 11.1 11.2 11.3 Yoshida, T et al. (2000) Targeted disruption of the mouse Sod I gene makes the hearts vulnerable to ischemic reperfusion injury. Circ. Res. 86 264-9 PubMed GONUTS page
  12. 12.0 12.1 12.2 Levy, MA et al. (2001) Cellular response of antioxidant metalloproteins in Cu/Zn SOD transgenic mice exposed to hyperoxia. Am. J. Physiol. Lung Cell Mol. Physiol. 281 L172-82 PubMed GONUTS page
  13. 13.0 13.1 13.2 13.3 Behndig, A et al. (2001) In vitro photochemical cataract in mice lacking copper-zinc superoxide dismutase. Free Radic. Biol. Med. 31 738-44 PubMed GONUTS page
  14. 14.0 14.1 Khan, JY & Black, SM (2003) Developmental changes in murine brain antioxidant enzymes. Pediatr. Res. 54 77-82 PubMed GONUTS page
  15. 15.0 15.1 15.2 15.3 Morikawa, K et al. (2003) Pivotal role of Cu,Zn-superoxide dismutase in endothelium-dependent hyperpolarization. J. Clin. Invest. 112 1871-9 PubMed GONUTS page
  16. 16.0 16.1 16.2 Muller, FL et al. (2004) Complex III releases superoxide to both sides of the inner mitochondrial membrane. J. Biol. Chem. 279 49064-73 PubMed GONUTS page
  17. 17.0 17.1 Prohaska, JR et al. (2003) Copper, zinc-superoxide dismutase protein but not mRNA is lower in copper-deficient mice and mice lacking the copper chaperone for superoxide dismutase. Exp. Biol. Med. (Maywood) 228 959-66 PubMed GONUTS page
  18. 18.0 18.1 18.2 18.3 Muller, FL et al. (2006) Absence of CuZn superoxide dismutase leads to elevated oxidative stress and acceleration of age-dependent skeletal muscle atrophy. Free Radic. Biol. Med. 40 1993-2004 PubMed GONUTS page
  19. 19.0 19.1 19.2 19.3 19.4 Didion, SP et al. (2002) Increased superoxide and vascular dysfunction in CuZnSOD-deficient mice. Circ. Res. 91 938-44 PubMed GONUTS page
  20. 20.0 20.1 Francke, U & Taggart, RT (1979) Assignment of the gene for cytoplasmic superoxide dismutase (Sod-1) to a region of chromosome 16 and of Hprt to a region of the X chromosome in the mouse. Proc. Natl. Acad. Sci. U.S.A. 76 5230-3 PubMed GONUTS page
  21. 21.0 21.1 Schäfer, R et al. (1980) Assignment of the gene for cytoplasmic glutamate-oxaloacetate transaminase to mouse chromosome 19 using chinese hamster x mouse somatic cell hybrids. Somatic Cell Genet. 6 709-17 PubMed GONUTS page
  22. 22.0 22.1 22.2 22.3 Reaume, AG et al. (1996) Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury. Nat. Genet. 13 43-7 PubMed GONUTS page
  23. Epstein, CJ et al. (1987) Transgenic mice with increased Cu/Zn-superoxide dismutase activity: animal model of dosage effects in Down syndrome. Proc. Natl. Acad. Sci. U.S.A. 84 8044-8 PubMed GONUTS page
  24. Turner, BJ et al. (2005) Impaired extracellular secretion of mutant superoxide dismutase 1 associates with neurotoxicity in familial amyotrophic lateral sclerosis. J. Neurosci. 25 108-17 PubMed GONUTS page
  25. 25.0 25.1 25.2 Shi, P et al. (2010) Effects of ALS-related SOD1 mutants on dynein- and KIF5-mediated retrograde and anterograde axonal transport. Biochim. Biophys. Acta 1802 707-16 PubMed GONUTS page
  26. Maggi, LB Jr et al. (2008) Nucleophosmin serves as a rate-limiting nuclear export chaperone for the Mammalian ribosome. Mol. Cell. Biol. 28 7050-65 PubMed GONUTS page
  27. 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
  28. Pagliarini, DJ et al. (2008) A mitochondrial protein compendium elucidates complex I disease biology. Cell 134 112-23 PubMed GONUTS page
  29. 29.0 29.1 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
  30. 30.0 30.1 30.2 30.3 Sentman, ML et al. (2006) Phenotypes of mice lacking extracellular superoxide dismutase and copper- and zinc-containing superoxide dismutase. J. Biol. Chem. 281 6904-9 PubMed GONUTS page
  31. 31.0 31.1 Ishii, T et al. (2005) Accelerated impairment of spermatogenic cells in SOD1-knockout mice under heat stress. Free Radic. Res. 39 697-705 PubMed GONUTS page
  32. Keithley, EM et al. (2005) Cu/Zn superoxide dismutase and age-related hearing loss. Hear. Res. 209 76-85 PubMed GONUTS page
  33. 33.0 33.1 33.2 33.3 McFadden, SL et al. (1999) Cu/Zn SOD deficiency potentiates hearing loss and cochlear pathology in aged 129,CD-1 mice. J. Comp. Neurol. 413 101-12 PubMed GONUTS page
  34. 34.0 34.1 34.2 Flood, DG et al. (1999) Hindlimb motor neurons require Cu/Zn superoxide dismutase for maintenance of neuromuscular junctions. Am. J. Pathol. 155 663-72 PubMed GONUTS page
  35. Schmidt-Ott, KM et al. (2006) c-kit delineates a distinct domain of progenitors in the developing kidney. Dev. Biol. 299 238-49 PubMed GONUTS page
  36. 36.0 36.1 Kessova, IG & Cederbaum, AI (2007) Mitochondrial alterations in livers of Sod1-/- mice fed alcohol. Free Radic. Biol. Med. 42 1470-80 PubMed GONUTS page
  37. Lei, XG et al. (2006) Mice deficient in Cu,Zn-superoxide dismutase are resistant to acetaminophen toxicity. Biochem. J. 399 455-61 PubMed GONUTS page
  38. 38.0 38.1 Nguyen, MD et al. (2001) Deregulation of Cdk5 in a mouse model of ALS: toxicity alleviated by perikaryal neurofilament inclusions. Neuron 30 135-47 PubMed GONUTS page
  39. McFadden, SL et al. () Age-related cochlear hair cell loss is enhanced in mice lacking copper/zinc superoxide dismutase. Neurobiol. Aging 20 1-8 PubMed GONUTS page
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