Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
SOD2 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

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: EC 1.15.1.1; Oxidoreductase; Mitochondrial
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; locomotory behavior; response to lipopolysaccharide; response to L-ascorbic acid; protein homotetramerization; post-embryonic development; negative regulation of cell proliferation; response to selenium ion; glutathione metabolic process; regulation of mitochondrial membrane potential; acetylcholine vasodilation involved in regulation of systemic arterial blood pressure; regulation of catalytic activity; regulation of blood pressure; response to gamma radiation; hemopoiesis; response to axon injury; negative regulation of neuron apoptosis; response to electrical stimulus; response to drug; erythrophore differentiation; release of cytochrome c from mitochondria; response to superoxide; superoxide metabolic process; negative regulation of fat cell differentiation; liver development; regulation of transcription from RNA polymerase II promoter; response to manganese ion; response to silicon dioxide; iron ion homeostasis; response to hyperoxia; response to cadmium ion; response to hydrogen peroxide; DNA damage response, signal transduction resulting in induction of apoptosis; negative regulation of fibroblast proliferation; age-dependent response to reactive oxygen species; detection of oxygen; response to zinc ion; 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.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho3D  |  DISEASE  |  Source  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene


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 3 Y58-p HSKHHAAyVNNLNVT
1 13 K68-a NLNVTEEkYQEALAK
0 1 K68 NLNVTEEKYQEALAK
0 1 K75 kYQEALAKGDVTAQI
2 0 S106-p SIFWTNLsPNGGGEP
0 9 N108 FWTNLsPNGGGEPKG
0 10 K114 PNGGGEPKGELLEAI
0 1 K114 PNGGGEPKGELLEAI
1 70 K122-a GELLEAIkRDFGSFD
1 9 K130-a RDFGSFDkFkEKLTA
0 2 K130-u RDFGSFDkFkEKLTA
0 8 K132-a FGSFDkFkEKLTAAS
0 1 K134 SFDkFkEKLTAASVG
0 1 K154 WGWLGFNKERGHLQI
0 1 K202 NVRPDYLKAIWNVIN
1 19 K221-a TERYMACkK______
0 13 K222 ERYMACkK_______
  mouse

 
Y58 HSKHHAAYVNNLNAT
K68-a NLNATEEkYHEALAk
K68-u NLNATEEkYHEALAk
K75-u kYHEALAkGDVTTQV
S106 TIFWTNLSPkGGGEP
K108-a FWTNLSPkGGGEPkG
K114-a PkGGGEPkGELLEAI
K114-u PkGGGEPkGELLEAI
K122-a GELLEAIkRDFGSFE
K130-a RDFGSFEkFkEkLTA
K130-u RDFGSFEkFkEkLTA
K132-a FGSFEkFkEkLTAVS
K134-a SFEkFkEkLTAVSVG
K154-a WGWLGFNkEQGRLQI
K202-a NVRPDYLkAIWNVIN
K221-a TERYTACkk______
K222-a ERYTACkk_______
  rat

 
Y58 HSKHHATYVNNLNVT
K68 NLNVTEEKYHEALAK
K68 NLNVTEEKYHEALAK
K75 KYHEALAKGDVTTQV
S106-p SIFWTNLsPKGGGEP
K108 FWTNLsPKGGGEPKG
K114 PKGGGEPKGELLEAI
K114 PKGGGEPKGELLEAI
K122-a GELLEAIkRDFGSFE
K130-a RDFGSFEkFKEKLTA
K130 RDFGSFEKFKEKLTA
K132 FGSFEkFKEKLTAVS
K134 SFEkFKEKLTAVSVG
K154 WGWLGFNKEQGRLQI
K202 NVRPDYLKAIWNVIN
K221 SQRYIVCKK______
K222 QRYIVCKK_______
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.