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Protein Page:
SOD2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
SOD2 Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. Genetic variation in SOD2 is associated with susceptibility to microvascular complications of diabetes type 6 (MVCD6). These are pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new- onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis. Belongs to the iron/manganese superoxide dismutase family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Oxidoreductase; Mitochondrial; EC 1.15.1.1
Cellular Component: mitochondrion; mitochondrial matrix; mitochondrial inner membrane
Molecular Function: identical protein binding; DNA binding; manganese ion binding; superoxide dismutase activity; oxygen binding
Biological Process: oxygen homeostasis; positive regulation of nitric oxide biosynthetic process; removal of superoxide radicals; heart development; response to lipopolysaccharide; locomotory behavior; response to L-ascorbic acid; post-embryonic development; protein homotetramerization; negative regulation of cell proliferation; response to selenium ion; glutathione metabolic process; acetylcholine vasodilation involved in regulation of systemic arterial blood pressure; regulation of mitochondrial membrane potential; regulation of catalytic activity; regulation of blood pressure; response to gamma radiation; hemopoiesis; negative regulation of neuron apoptosis; response to axon injury; response to electrical stimulus; response to drug; erythrophore differentiation; response to superoxide; release of cytochrome c from mitochondria; superoxide metabolic process; liver development; negative regulation of fat cell differentiation; response to manganese ion; regulation of transcription from RNA polymerase II promoter; iron ion homeostasis; response to silicon dioxide; response to hyperoxia; response to cadmium ion; DNA damage response, signal transduction resulting in induction of apoptosis; response to hydrogen peroxide; detection of oxygen; response to zinc ion; negative regulation of fibroblast proliferation; age-dependent response to reactive oxygen species; response to hypoxia; neuron development; response to activity; superoxide release; induction of apoptosis by oxidative stress; hydrogen peroxide biosynthetic process
Reference #:  P04179 (UniProtKB)
Alt. Names/Synonyms: indophenoloxidase B; IPOB; manganese-containing superoxide dismutase; mangano-superoxide dismutase; Mn superoxide dismutase; MNSOD; MVCD6; SOD2; SODM; superoxide dismutase 2, mitochondrial; Superoxide dismutase [Mn], mitochondrial
Gene Symbols: SOD2
Molecular weight: 24,722 Da
Basal Isoelectric point: 8.35  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

SOD2

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


 SS 

SS: 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.


 MS 

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


       human

 
0 1 K53 IMQLHHSKHHAAyVN
0 3 Y58-p HSKHHAAyVNNLNVT
1 14 K68-ac NLNVTEEkYQEALAK
0 1 K68 NLNVTEEKYQEALAK
0 2 K68-sc NLNVTEEkYQEALAK
0 1 K75 kYQEALAKGDVTAQI
0 1 K75 kYQEALAKGDVTAQI
0 2 K75 kYQEALAKGDVTAQI
0 1 K89 IALQPALKFNGGGHI
2 0 S106-p SIFWTNLsPNGGGEP
0 9 N108 FWTNLsPNGGGEPKG
0 11 K114 PNGGGEPKGELLEAI
0 1 K114 PNGGGEPKGELLEAI
0 1 K114 PNGGGEPKGELLEAI
1 71 K122-ac GELLEAIkRDFGSFD
0 2 K122-sc GELLEAIkRDFGSFD
1 10 K130-ac RDFGSFDkFkEKLTA
0 2 K130-ub RDFGSFDkFkEKLTA
0 2 K130-sc RDFGSFDkFkEKLTA
0 8 K132-ac FGSFDkFkEKLTAAS
0 1 K132 FGSFDkFKEKLTAAS
0 1 K134 SFDkFkEKLTAASVG
0 1 K154 WGWLGFNKERGHLQI
0 2 K202 NVRPDYLKAIWNVIN
1 19 K221-ac TERYMACkK______
0 13 K222 ERYMACkK_______
  mouse

 
K53-ac IMQLHHSkHHAAYVN
Y58 HSkHHAAYVNNLNAT
K68-ac NLNATEEkYHEALAk
K68-ub NLNATEEkYHEALAk
K68-sc NLNATEEkYHEALAk
K75-ac kYHEALAkGDVTTQV
K75-ub kYHEALAkGDVTTQV
K75-sc kYHEALAkGDVTTQV
K89-ac VALQPALkFNGGGHI
S106 TIFWTNLSPkGGGEP
K108-ac FWTNLSPkGGGEPkG
K114-ac PkGGGEPkGELLEAI
K114-ub PkGGGEPkGELLEAI
K114-sc PkGGGEPkGELLEAI
K122-ac GELLEAIkRDFGSFE
K122-sc GELLEAIkRDFGSFE
K130-ac RDFGSFEkFkEkLTA
K130-ub RDFGSFEkFkEkLTA
K130-sc RDFGSFEkFkEkLTA
K132-ac FGSFEkFkEkLTAVS
K132-sc FGSFEkFkEkLTAVS
K134-ac SFEkFkEkLTAVSVG
K154-ac WGWLGFNkEQGRLQI
K202-ac NVRPDYLkAIWNVIN
K221-ac TERYTACkk______
K222-ac ERYTACkk_______
  rat

 
K53 IMQLHHSKHHATYVN
Y58 HSKHHATYVNNLNVT
K68 NLNVTEEKYHEALAK
K68 NLNVTEEKYHEALAK
K68 NLNVTEEKYHEALAK
K75 KYHEALAKGDVTTQV
K75 KYHEALAKGDVTTQV
K75 KYHEALAKGDVTTQV
K89 VALQPALKFNGGGHI
S106-p SIFWTNLsPKGGGEP
K108 FWTNLsPKGGGEPKG
K114 PKGGGEPKGELLEAI
K114 PKGGGEPKGELLEAI
K114 PKGGGEPKGELLEAI
K122-ac GELLEAIkRDFGSFE
K122 GELLEAIKRDFGSFE
K130-ac RDFGSFEkFKEKLTA
K130 RDFGSFEKFKEKLTA
K130 RDFGSFEKFKEKLTA
K132 FGSFEkFKEKLTAVS
K132 FGSFEkFKEKLTAVS
K134 SFEkFKEKLTAVSVG
K154 WGWLGFNKEQGRLQI
K202 NVRPDYLKAIWNVIN
K221 SQRYIVCKK______
K222 QRYIVCKK_______
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