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Protein Page:
SOD1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
SOD1 Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Homodimer; non-disulfide linked. Homodimerization may take place via the ditryptophan cross-link at Trp-33. The pathogenic variants ALS1 Arg-38, Arg-47, Arg-86 and Ala-94 interact with RNF19A, whereas wild-type protein does not. The pathogenic variants ALS1 Arg-86 and Ala-94 interact with MARCH5, whereas wild-type protein does not. Belongs to the Cu-Zn superoxide dismutase family. Note: This description may include information from UniProtKB.
Protein type: Mitochondrial; Nuclear receptor co-regulator; EC 1.15.1.1; Apoptosis; Oxidoreductase
Chromosomal Location of Human Ortholog: 21q22.11
Cellular Component: cell soma; cytoplasm; cytoplasmic vesicle; cytosol; dendrite cytoplasm; extracellular matrix; extracellular region; extracellular space; lysosome; mitochondrial intermembrane space; mitochondrial matrix; mitochondrion; myelin sheath; nucleoplasm; nucleus; peroxisome; plasma membrane; protein complex
Molecular Function: chaperone binding; copper ion binding; identical protein binding; protein binding; protein homodimerization activity; protein phosphatase 2B binding; Rac GTPase binding; superoxide dismutase activity; zinc ion binding
Biological Process: activation of MAPK activity; anterograde axon cargo transport; auditory receptor cell stereocilium organization and biogenesis; cell aging; cellular iron ion homeostasis; embryo implantation; glutathione metabolic process; heart contraction; hydrogen peroxide biosynthetic process; locomotory behavior; muscle maintenance; myelin maintenance in the peripheral nervous system; myeloid cell homeostasis; negative regulation of cholesterol biosynthetic process; negative regulation of neuron apoptosis; neurofilament cytoskeleton organization and biogenesis; ovarian follicle development; placenta development; platelet degranulation; positive regulation of apoptosis; positive regulation of catalytic activity; positive regulation of cytokine production; positive regulation of superoxide release; regulation of blood pressure; regulation of GTPase activity; regulation of mitochondrial membrane potential; regulation of multicellular organism growth; regulation of organ growth; regulation of protein kinase activity; regulation of T cell differentiation in the thymus; relaxation of vascular smooth muscle; removal of superoxide radicals; response to amphetamine; response to antibiotic; response to axon injury; response to copper ion; response to drug; response to ethanol; response to heat; response to hydrogen peroxide; response to nutrient levels; response to organic substance; response to reactive oxygen species; response to superoxide; retinal homeostasis; retrograde axon cargo transport; sensory perception of sound; spermatogenesis; superoxide metabolic process; superoxide release; thymus development; transmission of nerve impulse
Disease: Amyotrophic Lateral Sclerosis 1
Reference #:  P00441 (UniProtKB)
Alt. Names/Synonyms: ALS; ALS1; Cu/Zn superoxide dismutase; homodimer; indophenoloxidase A; IPOA; SOD; SOD, soluble; SOD1; SODC; superoxide dismutase; superoxide dismutase 1, soluble; Superoxide dismutase [Cu-Zn]; superoxide dismutase, cystolic
Gene Symbols: SOD1
Molecular weight: 15,936 Da
Basal Isoelectric point: 5.7  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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SOD1

Protein Structure Not Found.
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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 2 T3‑p _____MAtKAVCVLk
0 1 K4 ____MAtKAVCVLkG
0 3 K10‑ub tKAVCVLkGDGPVQG
0 1 K10‑sc tKAVCVLkGDGPVQG
0 3 K10‑ac tKAVCVLkGDGPVQG
0 2 I18 GDGPVQGIINFEQkE
0 1 K24‑ac GIINFEQkEsNGPVk
0 1 K24‑ub GIINFEQkEsNGPVk
0 1 S26‑p INFEQkEsNGPVkVW
0 1 K31‑ub kEsNGPVkVWGsIKG
0 8 S35‑p GPVkVWGsIKGLTEG
0 2 T59‑p GDNTAGCtsAGPHFN
0 1 S60‑p DNTAGCtsAGPHFNP
0 1 S69‑p GPHFNPLsRkHGGPk
1 1 K71‑ac HFNPLsRkHGGPkDE
0 2 K71 HFNPLsRKHGGPkDE
1 0 K76‑sm sRkHGGPkDEERHVG
0 1 K76‑sc sRkHGGPkDEERHVG
0 2 K76‑ub sRkHGGPkDEERHVG
0 4 T89‑p VGDLGNVtADKDGVA
0 2 K92 LGNVtADKDGVADVs
0 2 K92 LGNVtADKDGVADVs
0 1 K92 LGNVtADKDGVADVs
0 25 S99‑p KDGVADVsIEDsVIs
0 3 S103‑p ADVsIEDsVIsLsGD
0 9 S106‑p sIEDsVIsLsGDHCI
0 15 S108‑p EDsVIsLsGDHCIIG
0 1 C112 IsLsGDHCIIGRTLV
0 9 K123‑ac RTLVVHEkADDLGKG
0 2 K123‑ub RTLVVHEkADDLGKG
0 1 K123‑sc RTLVVHEkADDLGKG
0 1 K129 EkADDLGKGGNEEST
0 1 K129 EkADDLGKGGNEEST
0 13 K137‑ub GGNEESTkTGNAGSR
0 1 K137 GGNEESTKTGNAGSR
0 4 K137 GGNEESTKTGNAGSR
  mouse

 
M3 _____MAMKAVCVLk
K4 ____MAMKAVCVLkG
K10‑ub MKAVCVLkGDGPVQG
K10 MKAVCVLKGDGPVQG
K10‑ac MKAVCVLkGDGPVQG
T18‑p GDGPVQGtIHFEQKA
K24 GtIHFEQKASGEPVV
K24 GtIHFEQKASGEPVV
S26 IHFEQKASGEPVVLS
V31 KASGEPVVLSGQITG
Q35 EPVVLSGQITGLTEG
T59 GDNTQGCTSAGPHFN
S60 DNTQGCTSAGPHFNP
S69 GPHFNPHSKkHGGPA
K71‑ac HFNPHSKkHGGPADE
K71‑ub HFNPHSKkHGGPADE
A76 SKkHGGPADEERHVG
A76 SKkHGGPADEERHVG
A76 SKkHGGPADEERHVG
T89‑p VGDLGNVtAGkDGVA
K92‑ac LGNVtAGkDGVANVs
K92‑ub LGNVtAGkDGVANVs
K92‑sc LGNVtAGkDGVANVs
S99‑p kDGVANVsIEDRVIs
R103 ANVsIEDRVIsLsGE
S106‑p sIEDRVIsLsGEHsI
S108‑p EDRVIsLsGEHsIIG
S112‑p IsLsGEHsIIGRTMV
K123‑ac RTMVVHEkQDDLGkG
K123‑ub RTMVVHEkQDDLGkG
K123‑sc RTMVVHEkQDDLGkG
K129 EkQDDLGKGGNEEST
K129‑sc EkQDDLGkGGNEEST
K137‑ub GGNEESTkTGNAGSR
K137‑sc GGNEESTkTGNAGSR
K137‑ac GGNEESTkTGNAGSR
  rat

 
M3 _____MAMkAVCVLk
K4‑ac ____MAMkAVCVLkG
K10 MkAVCVLKGDGPVQG
K10 MkAVCVLKGDGPVQG
K10‑ac MkAVCVLkGDGPVQG
V18 GDGPVQGVIHFEQKA
K24 GVIHFEQKASGEPVV
K24 GVIHFEQKASGEPVV
S26 IHFEQKASGEPVVVS
V31 KASGEPVVVSGQITG
Q35 EPVVVSGQITGLTEG
T59 GDNTQGCTTAGPHFN
T60 DNTQGCTTAGPHFNP
S69 GPHFNPHSKKHGGPA
K71 HFNPHSKKHGGPADE
K71 HFNPHSKKHGGPADE
A76 SKKHGGPADEERHVG
A76 SKKHGGPADEERHVG
A76 SKKHGGPADEERHVG
A89 VGDLGNVAAGkDGVA
K92‑ac LGNVAAGkDGVANVs
K92 LGNVAAGKDGVANVs
K92 LGNVAAGKDGVANVs
S99‑p kDGVANVsIEDRVIs
R103 ANVsIEDRVIsLsGE
S106‑p sIEDRVIsLsGEHSI
S108‑p EDRVIsLsGEHSIIG
S112 IsLsGEHSIIGRTMV
K123‑ac RTMVVHEkQDDLGkG
K123 RTMVVHEKQDDLGkG
K123 RTMVVHEKQDDLGkG
K129‑ac EkQDDLGkGGNEEST
K129 EkQDDLGKGGNEEST
K137 GGNEESTKTGNAGSR
K137 GGNEESTKTGNAGSR
K137‑ac GGNEESTkTGNAGSR
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