SOD2

Functionⁱ

Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.

1 Publication

Catalytic activityⁱ

2
H⁺
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+ 2
superoxide
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
=
H₂O₂
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
O₂
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
7 Publications
Manual assertion based on experiment inⁱ
- Ref.18
  "Tyrosine modifications and inactivation of active site manganese superoxide dismutase mutant (Y34F) by peroxynitrite."
  MacMillan-Crow L.A., Thompson J.A.
  Arch. Biochem. Biophys. 366:82-88(1999) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, NITRATION AT TYR-58, MUTAGENESIS OF TYR-58.
- Ref.27
  "Human mitochondrial manganese superoxide dismutase polymorphic variant Ile58Thr reduces activity by destabilizing the tetrameric interface."
  Borgstahl G.E.O., Parge H.E., Hickey M.J., Johnson M.J., Boissinot M., Hallewell R.A., Lepock J.R., Cabelli D.E., Tainer J.A.
  Biochemistry 35:4287-4297(1996) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)OF 25-222 AND OF VARIANT THR-82, CATALYTIC ACTIVITY.
- Ref.28
  "Probing the active site of human manganese superoxide dismutase: the role of glutamine 143."
  Hsieh Y., Guan Y., Tu C., Bratt P.J., Angerhofer A., Lepock J.R., Hickey M.J., Tainer J.A., Nick H.S., Silverman D.N.
  Biochemistry 37:4731-4739(1998) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 25-222 AND OF MUTANT ASN-167 IN COMPLEX WITH MANGANESE, CATALYTIC ACTIVITY.
- Ref.29
  "Crystal structure of Y34F mutant human mitochondrial manganese superoxide dismutase and the functional role of tyrosine 34."
  Guan Y., Hickey M.J., Borgstahl G.E.O., Hallewell R.A., Lepock J.R., O'Connor D., Hsieh Y., Nick H.S., Silverman D.N., Tainer J.A.
  Biochemistry 37:4722-4730(1998) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 25-222 AND OF MUTANT TYR-58 IN COMPLEX WITH MANGANESE, CATALYTIC ACTIVITY.
- Ref.30
  "Multiple replacements of glutamine 143 in human manganese superoxide dismutase: effects on structure, stability, and catalysis."
  Leveque V.J.-P., Stroupe M.E., Lepock J.R., Cabelli D.E., Tainer J.A., Nick H.S., Silverman D.N.
  Biochemistry 39:7131-7137(2000) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS) OF 25-222 AND OF MUTANT ALA-167 IN COMPLEX WITH MANGANESE, CATALYTIC ACTIVITY.
- Ref.31
  "Kinetic analysis of product inhibition in human manganese superoxide dismutase."
  Hearn A.S., Stroupe M.E., Cabelli D.E., Lepock J.R., Tainer J.A., Nick H.S., Silverman D.N.
  Biochemistry 40:12051-12058(2001) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 25-222 AND MUTANT ALA-185 IN COMPLEX WITH MANGANESE, CATALYTIC ACTIVITY.
- Ref.32
  "Contribution of human manganese superoxide dismutase tyrosine 34 to structure and catalysis."
  Perry J.J., Hearn A.S., Cabelli D.E., Nick H.S., Tainer J.A., Silverman D.N.
  Biochemistry 48:3417-3424(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 25-222 AND OF MUTANTS ALA/ASN/HIS/VAL-58 IN COMPLEX WITH MANGANESE, CATALYTIC ACTIVITY, SUBUNIT.
EC:
1.15.1.1
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
- Search reactions for this EC number in Rhea.
7 Publications
Manual assertion based on experiment inⁱ
- Ref.18
  "Tyrosine modifications and inactivation of active site manganese superoxide dismutase mutant (Y34F) by peroxynitrite."
  MacMillan-Crow L.A., Thompson J.A.
  Arch. Biochem. Biophys. 366:82-88(1999) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, NITRATION AT TYR-58, MUTAGENESIS OF TYR-58.
- Ref.27
  "Human mitochondrial manganese superoxide dismutase polymorphic variant Ile58Thr reduces activity by destabilizing the tetrameric interface."
  Borgstahl G.E.O., Parge H.E., Hickey M.J., Johnson M.J., Boissinot M., Hallewell R.A., Lepock J.R., Cabelli D.E., Tainer J.A.
  Biochemistry 35:4287-4297(1996) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)OF 25-222 AND OF VARIANT THR-82, CATALYTIC ACTIVITY.
- Ref.28
  "Probing the active site of human manganese superoxide dismutase: the role of glutamine 143."
  Hsieh Y., Guan Y., Tu C., Bratt P.J., Angerhofer A., Lepock J.R., Hickey M.J., Tainer J.A., Nick H.S., Silverman D.N.
  Biochemistry 37:4731-4739(1998) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 25-222 AND OF MUTANT ASN-167 IN COMPLEX WITH MANGANESE, CATALYTIC ACTIVITY.
- Ref.29
  "Crystal structure of Y34F mutant human mitochondrial manganese superoxide dismutase and the functional role of tyrosine 34."
  Guan Y., Hickey M.J., Borgstahl G.E.O., Hallewell R.A., Lepock J.R., O'Connor D., Hsieh Y., Nick H.S., Silverman D.N., Tainer J.A.
  Biochemistry 37:4722-4730(1998) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 25-222 AND OF MUTANT TYR-58 IN COMPLEX WITH MANGANESE, CATALYTIC ACTIVITY.
- Ref.30
  "Multiple replacements of glutamine 143 in human manganese superoxide dismutase: effects on structure, stability, and catalysis."
  Leveque V.J.-P., Stroupe M.E., Lepock J.R., Cabelli D.E., Tainer J.A., Nick H.S., Silverman D.N.
  Biochemistry 39:7131-7137(2000) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS) OF 25-222 AND OF MUTANT ALA-167 IN COMPLEX WITH MANGANESE, CATALYTIC ACTIVITY.
- Ref.31
  "Kinetic analysis of product inhibition in human manganese superoxide dismutase."
  Hearn A.S., Stroupe M.E., Cabelli D.E., Lepock J.R., Tainer J.A., Nick H.S., Silverman D.N.
  Biochemistry 40:12051-12058(2001) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 25-222 AND MUTANT ALA-185 IN COMPLEX WITH MANGANESE, CATALYTIC ACTIVITY.
- Ref.32
  "Contribution of human manganese superoxide dismutase tyrosine 34 to structure and catalysis."
  Perry J.J., Hearn A.S., Cabelli D.E., Nick H.S., Tainer J.A., Silverman D.N.
  Biochemistry 48:3417-3424(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 25-222 AND OF MUTANTS ALA/ASN/HIS/VAL-58 IN COMPLEX WITH MANGANESE, CATALYTIC ACTIVITY, SUBUNIT.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
2
H⁺
+
2
superoxide
zoom
=
H₂O₂
+
O₂

Cofactorⁱ

Mn²⁺6 PublicationsNote: Binds 1 Mn²⁺ ion per subunit.6 Publications

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	50	Manganese; via tele nitrogenCombined sources6 PublicationsImported	1
Metal bindingⁱ	98	Manganese; via tele nitrogenCombined sources6 PublicationsImported	1
Metal bindingⁱ	183	ManganeseCombined sources6 PublicationsImported	1
Metal bindingⁱ	187	Manganese; via tele nitrogenCombined sources6 PublicationsImported	1

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Oxidoreductase
Ligand	Manganese, Metal-binding

Enzyme and pathway databases

BRENDAⁱ	1.15.1.1, 2681
PathwayCommonsⁱ	P04179
Reactomeⁱ	R-HSA-2151201, Transcriptional activation of mitochondrial biogenesis R-HSA-3299685, Detoxification of Reactive Oxygen Species R-HSA-8862803, Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models R-HSA-8950505, Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation R-HSA-9615017, FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes
SABIO-RKⁱ	P04179
SignaLinkⁱ	P04179
SIGNORⁱ	P04179

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Superoxide dismutase [Mn], mitochondrial (EC:1.15.1.17 Publications)
Gene namesⁱ	Name:SOD2
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 6

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:11180, SOD2
MIMⁱ	147460, gene
neXtProtⁱ	NX_P04179
VEuPathDBⁱ	HostDB:ENSG00000112096

Keywords - Cellular componentⁱ

Mitochondrion

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Microvascular complications of diabetes 6 (MVCD6)2 Publications

Disease susceptibility is associated with variants affecting the gene represented in this entry.

Disease descriptionPathological 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.

Related information in OMIM

Mutagenesis

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Mutagenesisⁱ	58	Y → A, H, N, V or F: Reduced enzyme activity. 1 Publication		1
Mutagenesisⁱ	58	Y → F: Loss of nitration. Enhanced dityrosine formation on peroxynitrite treatment. 1 Publication		1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	6648
MalaCards human disease database More...MalaCardsⁱ	SOD2
MIMⁱ	612634, phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000112096
PharmGKBⁱ	PA36017

Miscellaneous databases

Pharosⁱ	P04179, Tbio

Pharosⁱ

P04179, Tbio

Protein family/group databases

Allergomeⁱ	784, Hom s MnSOD

Allergomeⁱ

784, Hom s MnSOD

Chemistry databases

ChEMBLⁱ	CHEMBL4105776
Drug and drug target database More...DrugBankⁱ	DB04436, 3-Fluoro-L-tyrosine DB09096, Benzoyl peroxide DB03297, Benzylsulfonic acid DB06796, Mangafodipir DB09221, Polaprezinc DB11590, Thimerosal
DrugCentral More...DrugCentralⁱ	P04179

Genetic variation databases

BioMutaⁱ	SOD2
DMDMⁱ	134665

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Transit peptideⁱ	1 – 24	Mitochondrion4 PublicationsAdd BLAST		24
ChainⁱPRO_0000032869	25 – 222	Superoxide dismutase [Mn], mitochondrialAdd BLAST		198

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	58	3'-nitrotyrosine2 Publications	1
Modified residueⁱ	68	N6-acetyllysine; alternateCombined sources	1
Modified residueⁱ	68	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	75	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	75	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	114	N6-acetyllysineBy similarity	1
Modified residueⁱ	122	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	122	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	130	N6-acetyllysine; alternateCombined sources	1
Modified residueⁱ	130	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	202	N6-acetyllysineBy similarity	1

Post-translational modificationⁱ

Acetylation at Lys-122 decreases enzymatic activity. Deacetylated by SIRT3 upon exposure to ionizing radiations or after long fasting (By similarity).By similarity

Polyubiquitinated; leading to proteasomal degradation. Deubiquitinated by USP36 which increases protein stability.1 Publication

Keywords - PTMⁱ

Acetylation, Nitration, Ubl conjugation

Proteomic databases

EPDⁱ	P04179
jPOSTⁱ	P04179
MassIVEⁱ	P04179
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P04179
PaxDbⁱ	P04179
PeptideAtlas More...PeptideAtlasⁱ	P04179
PRIDEⁱ	P04179
ProteomicsDBⁱ	3715 51669 [P04179-1] 51670 [P04179-2] 5907
TopDownProteomicsⁱ	P04179-1 [P04179-1] P04179-2 [P04179-2]

2D gel databases

DOSAC-COBS 2D-PAGE database More...DOSAC-COBS-2DPAGEⁱ	P04179
USC-OGP 2-DE database More...OGPⁱ	P04179
SWISS-2DPAGEⁱ	P04179
UCD-2DPAGEⁱ	P04179

PTM databases

GlyGenⁱ	P04179, 1 site, 1 O-linked glycan (1 site)
iPTMnetⁱ	P04179
PhosphoSitePlusⁱ	P04179
SwissPalmⁱ	P04179

Expressionⁱ

Inductionⁱ

Expression is regulated by KRIT1.1 Publication

Gene expression databases

Bgeeⁱ	ENSG00000112096, Expressed in gastrocnemius and 240 other tissues
ExpressionAtlasⁱ	P04179, baseline and differential
Genevisibleⁱ	P04179, HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	ENSG00000112096, Group enriched (bone marrow, skeletal muscle)

HPAⁱ

ENSG00000112096, Group enriched (bone marrow, skeletal muscle)

Interactionⁱ

Subunit structureⁱ

Homotetramer.

1 Publication

Binary interactionsⁱ

Hide details

P04179

With	#Exp.	IntAct
CEP70 [Q8NHQ1]	3	EBI-716989,EBI-739624
itself	2	EBI-716989,EBI-716989

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGRIDⁱ	112531, 77 interactors
IntActⁱ	P04179, 28 interactors
Molecular INTeraction database More...MINTⁱ	P04179
STRINGⁱ	9606.ENSP00000446252

Miscellaneous databases

RNActⁱ	P04179, protein

RNActⁱ

P04179, protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Turnⁱ	35 – 41	Combined sources	7
Helixⁱ	44 – 52	Combined sources	9
Helixⁱ	54 – 74	Combined sources	21
Helixⁱ	78 – 83	Combined sources	6
Helixⁱ	85 – 103	Combined sources	19
Helixⁱ	115 – 125	Combined sources	11
Helixⁱ	128 – 140	Combined sources	13
Beta strandⁱ	144 – 153	Combined sources	10
Turnⁱ	154 – 157	Combined sources	4
Beta strandⁱ	158 – 165	Combined sources	8
Helixⁱ	170 – 174	Combined sources	5
Beta strandⁱ	177 – 183	Combined sources	7
Helixⁱ	186 – 188	Combined sources	3
Helixⁱ	190 – 193	Combined sources	4
Helixⁱ	197 – 204	Combined sources	8
Helixⁱ	205 – 207	Combined sources	3
Helixⁱ	210 – 219	Combined sources	10

Show more details

3D structure databases

AlphaFoldDBⁱ	P04179
SMRⁱ	P04179
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P04179

EvolutionaryTraceⁱ

P04179

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the iron/manganese superoxide dismutase family.Curated

Keywords - Domainⁱ

Transit peptide

Phylogenomic databases

eggNOGⁱ	KOG0876, Eukaryota
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000011877
HOGENOMⁱ	CLU_031625_2_0_1
InParanoidⁱ	P04179
OMAⁱ	KWGSFDK
Database of Orthologous Groups More...OrthoDBⁱ	1353361at2759
PhylomeDBⁱ	P04179
TreeFamⁱ	TF105132

Family and domain databases

Gene3Dⁱ	1.10.287.990, 1 hit 3.55.40.20, 1 hit
InterProⁱ	View protein in InterPro IPR001189, Mn/Fe_SOD IPR019833, Mn/Fe_SOD_BS IPR019832, Mn/Fe_SOD_C IPR019831, Mn/Fe_SOD_N IPR036324, Mn/Fe_SOD_N_sf IPR036314, SOD_C_sf
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF02777, Sod_Fe_C, 1 hit PF00081, Sod_Fe_N, 1 hit
PIRSFⁱ	PIRSF000349, SODismutase, 1 hit
PRINTSⁱ	PR01703, MNSODISMTASE
SUPFAMⁱ	SSF46609, SSF46609, 1 hit SSF54719, SSF54719, 1 hit
PROSITEⁱ	View protein in PROSITE PS00088, SOD_MN, 1 hit

Sequences (4+)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 4 described isoforms and 6 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: P04179-1) [UniParc]FASTA Add to basket

This isoform has been chosen as the canonicalⁱ sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLSRAVCGTS RQLAPVLGYL GSRQKHSLPD LPYDYGALEP HINAQIMQLH 
        60         70         80         90        100
HSKHHAAYVN NLNVTEEKYQ EALAKGDVTA QIALQPALKF NGGGHINHSI 
       110        120        130        140        150
FWTNLSPNGG GEPKGELLEA IKRDFGSFDK FKEKLTAASV GVQGSGWGWL 
       160        170        180        190        200
GFNKERGHLQ IAACPNQDPL QGTTGLIPLL GIDVWEHAYY LQYKNVRPDY 
       210        220 
LKAIWNVINW ENVTERYMAC KK

Length:222

Mass (Da):24,750

Last modified:December 20, 2017 - v3

Checksum:ⁱCA047D7900AE5905

GO

Isoform 2 (identifier: P04179-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
75-113: Missing.

« Hide

        10         20         30         40         50
MLSRAVCGTS RQLAPVLGYL GSRQKHSLPD LPYDYGALEP HINAQIMQLH 
        60         70         80         90        100
HSKHHAAYVN NLNVTEEKYQ EALAKGELLE AIKRDFGSFD KFKEKLTAAS 
       110        120        130        140        150
VGVQGSGWGW LGFNKERGHL QIAACPNQDP LQGTTGLIPL LGIDVWEHAY 
       160        170        180 
YLQYKNVRPD YLKAIWNVIN WENVTERYMA CKK

Show »

Length:183

Mass (Da):20,724

Checksum:ⁱ513D204966621B88

GO

Isoform 3 (identifier: P04179-3) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
115-174: Missing.

« Hide

        10         20         30         40         50
MLSRAVCGTS RQLAPVLGYL GSRQKHSLPD LPYDYGALEP HINAQIMQLH 
        60         70         80         90        100
HSKHHAAYVN NLNVTEEKYQ EALAKGDVTA QIALQPALKF NGGGHINHSI 
       110        120        130        140        150
FWTNLSPNGG GEPKGLIPLL GIDVWEHAYY LQYKNVRPDY LKAIWNVINW 
       160 
ENVTERYMAC KK

Show »

Length:162

Mass (Da):18,262

Checksum:ⁱ54271EA009B62959

GO

Isoform 4 (identifier: P04179-4) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-46: Missing.

« Hide

        10         20         30         40         50
MQLHHSKHHA AYVNNLNVTE EKYQEALAKG DVTAQIALQP ALKFNGGGHI 
        60         70         80         90        100
NHSIFWTNLS PNGGGEPKGE LLEAIKRDFG SFDKFKEKLT AASVGVQGSG 
       110        120        130        140        150
WGWLGFNKER GHLQIAACPN QDPLQGTTGL IPLLGIDVWE HAYYLQYKNV 
       160        170 
RPDYLKAIWN VINWENVTER YMACKK

Show »

Length:176

Mass (Da):19,730

Checksum:ⁱ5AB24FB15A80A1AF

GO

Computationally mapped potential isoform sequencesⁱ

There are 6 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

F5GYZ5	F5GYZ5_HUMAN	Superoxide dismutase Superoxide dismutase, EC 1.15.1.1	SOD2	190	Annotation score:
F5H4R2	F5H4R2_HUMAN	Superoxide dismutase Superoxide dismutase, EC 1.15.1.1	SOD2	183	Annotation score:
F5H3C5	F5H3C5_HUMAN	Superoxide dismutase Superoxide dismutase, EC 1.15.1.1	SOD2	111	Annotation score:
G8JLJ2	G8JLJ2_HUMAN	Superoxide dismutase Superoxide dismutase, EC 1.15.1.1	SOD2	61	Annotation score:
G5E9P6	G5E9P6_HUMAN	Superoxide dismutase [Mn], mitochon... Superoxide dismutase [Mn], mitochondrial	SOD2 hCG_34035	140	Annotation score:
F5GXZ9	F5GXZ9_HUMAN	Superoxide dismutase [Mn], mitochon... Superoxide dismutase [Mn], mitochondrial	SOD2	141	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	14	A → P (PubMed:3399391).Curated	1
Sequence conflictⁱ	65	T → N in CAA42066 (PubMed:1699607).Curated	1
Sequence conflictⁱ	65	T → N in CAA33228 (PubMed:1699607).Curated	1
Sequence conflictⁱ	66	E → Q (PubMed:1988135).Curated	1
Sequence conflictⁱ	112	E → Q (PubMed:1988135).Curated	1
Sequence conflictⁱ	123	R → L in CAA30687 (PubMed:3399391).Curated	1
Sequence conflictⁱ	133	E → Q (PubMed:1988135).Curated	1
Sequence conflictⁱ	148 – 149	Missing (PubMed:1988135).Curated	2
Sequence conflictⁱ	155	E → Q in CAA68533 (PubMed:3684581).Curated	1
Sequence conflictⁱ	155	E → Q (PubMed:1988135).Curated	1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_019363	10	S → I1 PublicationCorresponds to variant dbSNP:rs5746096Ensembl.	1
Natural variantⁱVAR_016183	16	V → A Associated with a decreased susceptibility to diabetic nephropathy in Japanese and Chinese patients with type 2 diabetes. 2 PublicationsCorresponds to variant dbSNP:rs4880EnsemblClinVar.	1
Natural variantⁱVAR_019364	66	E → V1 PublicationCorresponds to variant dbSNP:rs5746097Ensembl.	1
Natural variantⁱVAR_025898	76	G → R. Corresponds to variant dbSNP:rs4987023Ensembl.	1
Natural variantⁱVAR_007165	82	I → T1 PublicationCorresponds to variant dbSNP:rs1141718Ensembl.	1
Natural variantⁱVAR_019365	156	R → W1 PublicationCorresponds to variant dbSNP:rs5746129Ensembl.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Length
Alternative sequenceⁱVSP_053761	1 – 46	Missing in isoform 4. 1 PublicationAdd BLAST	46
Alternative sequenceⁱVSP_042558	75 – 113	Missing in isoform 2. 1 PublicationAdd BLAST	39
Alternative sequenceⁱVSP_053762	115 – 174	Missing in isoform 3. 1 PublicationAdd BLAST	60

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X59445 mRNA Translation: CAA42066.1 Y00472 mRNA Translation: CAA68533.1 Y00985 mRNA Translation: CAA68791.1 X07834 mRNA Translation: CAA30687.1 M36693 mRNA Translation: AAA36622.1 X15132 mRNA Translation: CAA33228.1 X14322 mRNA Translation: CAA32502.1 S77127 Genomic DNA Translation: AAD14248.1 Sequence problems. BT006967 mRNA Translation: AAP35613.1 AY267901 Genomic DNA Translation: AAP03428.1 AK097395 mRNA Translation: BAG53464.1 AK296809 mRNA Translation: BAG59382.1 AK304766 mRNA Translation: BAG65521.1 AK313082 mRNA Translation: BAG35908.1 AL135914 Genomic DNA No translation available. CH471051 Genomic DNA Translation: EAW47630.1 CH471051 Genomic DNA Translation: EAW47631.1 BC012423 mRNA Translation: AAH12423.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS34564.1 [P04179-2] CCDS5265.1 [P04179-1] CCDS83141.1 [P04179-4] CCDS83143.1 [P04179-3]
PIRⁱ	S13162, DSHUN
NCBI Reference Sequences More...RefSeqⁱ	NP_000627.2, NM_000636.3 [P04179-1] NP_001019636.1, NM_001024465.2 [P04179-1] NP_001019637.1, NM_001024466.2 [P04179-2] NP_001309743.1, NM_001322814.1 [P04179-2] NP_001309744.1, NM_001322815.1 [P04179-3] NP_001309746.1, NM_001322817.1 [P04179-4] NP_001309748.1, NM_001322819.1 [P04179-4] NP_001309749.1, NM_001322820.1 [P04179-4]

Genome annotation databases

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P04179	Superoxide dismutase		HUMAN		222	UniRef100_P04179
Superoxide dismutase [Mn], mitochondrial (Fragment)		HUMAN		76
P04179-4	Superoxide dismutase [Mn], mitochondrial		PANTR		198	UniRef100_Q8HXP7
Superoxide dismutase		PONAB		245
Superoxide dismutase		AILME		198
Superoxide dismutase (Fragment)		HUMAN		111
Superoxide dismutase (Fragment)		PONAB		111
+4

Protein	Similar proteins		Species	Score	Length	Source
P04179	Superoxide dismutase [Mn], mitochondrial		MACNE		222	UniRef90_P04179
Superoxide dismutase [Mn], mitochondrial		PONPY		222
Superoxide dismutase [Mn], mitochondrial		MACFA		222
Superoxide dismutase [Mn], mitochondrial		PANTR		198
Superoxide dismutase [Mn], mitochondrial		CALJA		198
+59
P04179-2	Superoxide dismutase		AOTNA		185	UniRef90_P04179-2
Superoxide dismutase		CEBIM		183
Superoxide dismutase		CALJA		183
Superoxide dismutase		PONAB		183
Superoxide dismutase (Fragment)		HUMAN		61
+11
P04179-3	Superoxide dismutase		AOTNA		164	UniRef90_P04179-3
Superoxide dismutase		PROSS		162
Superoxide dismutase		HORSE		162
Superoxide dismutase		CEBIM		162
Superoxide dismutase		CANLF		162
+24

Protein	Similar proteins		Species	Score	Length	Source
P04179	Superoxide dismutase [Mn], mitochondrial		MOUSE		222	UniRef50_P09671
Superoxide dismutase [Mn], mitochondrial		RAT		222
Superoxide dismutase [Mn], mitochondrial		PONPY		222
Superoxide dismutase [Mn], mitochondrial		MACFA		222
Superoxide dismutase [Mn], mitochondrial		MACNE		222
+429
P04179-2	Superoxide dismutase		AOTNA		185	UniRef50_P04179-2
Superoxide dismutase		PONAB		183
Superoxide dismutase (Fragment)		HUMAN		61
Superoxide dismutase (Fragment)		PANTR		61
Superoxide dismutase		CEBIM		183
+39
P04179-3	Superoxide dismutase [Mn] (Fragment)		MYCKA		163	UniRef50_P04179-3
Superoxide dismutase [Mn] (Fragment)		MYCMR		138
Superoxide dismutase [Mn] (Fragment)		MYCSC		163
Superoxide dismutase		AOTNA		164
Superoxide dismutase		CALJA		162
+98

Cross-referencesⁱ

Web resourcesⁱ

NIEHS-SNPs

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Superoxide dismutase entry

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X59445 mRNA Translation: CAA42066.1 Y00472 mRNA Translation: CAA68533.1 Y00985 mRNA Translation: CAA68791.1 X07834 mRNA Translation: CAA30687.1 M36693 mRNA Translation: AAA36622.1 X15132 mRNA Translation: CAA33228.1 X14322 mRNA Translation: CAA32502.1 S77127 Genomic DNA Translation: AAD14248.1 Sequence problems. BT006967 mRNA Translation: AAP35613.1 AY267901 Genomic DNA Translation: AAP03428.1 AK097395 mRNA Translation: BAG53464.1 AK296809 mRNA Translation: BAG59382.1 AK304766 mRNA Translation: BAG65521.1 AK313082 mRNA Translation: BAG35908.1 AL135914 Genomic DNA No translation available. CH471051 Genomic DNA Translation: EAW47630.1 CH471051 Genomic DNA Translation: EAW47631.1 BC012423 mRNA Translation: AAH12423.1
CCDSⁱ	CCDS34564.1 [P04179-2] CCDS5265.1 [P04179-1] CCDS83141.1 [P04179-4] CCDS83143.1 [P04179-3]
PIRⁱ	S13162, DSHUN
RefSeqⁱ	NP_000627.2, NM_000636.3 [P04179-1] NP_001019636.1, NM_001024465.2 [P04179-1] NP_001019637.1, NM_001024466.2 [P04179-2] NP_001309743.1, NM_001322814.1 [P04179-2] NP_001309744.1, NM_001322815.1 [P04179-3] NP_001309746.1, NM_001322817.1 [P04179-4] NP_001309748.1, NM_001322819.1 [P04179-4] NP_001309749.1, NM_001322820.1 [P04179-4]

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1AP5	X-ray	2.20	A/B	25-222	[»]
	1AP6	X-ray	1.90	A/B	25-222	[»]
	1EM1	X-ray	2.13	A/B	25-222	[»]
	1JA8	X-ray	2.12	A/B	25-222	[»]
	1LUV	X-ray	1.85	A/B	25-222	[»]
	1LUW	X-ray	2.30	A/B	25-222	[»]
	1MSD	X-ray	3.20	A/B	25-222	[»]
	1N0J	X-ray	2.20	A/B	25-222	[»]
	1N0N	X-ray	1.82	A/B	25-222	[»]
	1PL4	X-ray	1.47	A/B/C/D	25-222	[»]
	1PM9	X-ray	1.70	A/B	25-222	[»]
	1QNM	X-ray	2.30	A/B	25-222	[»]
	1SZX	X-ray	1.95	A/B	25-222	[»]
	1VAR	X-ray	2.50	A/B	25-222	[»]
	1XDC	X-ray	1.85	A/B	25-222	[»]
	1XIL	X-ray	1.53	A/B	25-222	[»]
	1ZSP	X-ray	1.90	A/B	25-222	[»]
	1ZTE	X-ray	1.85	A/B/C/D	25-222	[»]
	1ZUQ	X-ray	2.00	A/B	25-222	[»]
	2ADP	X-ray	2.40	A	25-222	[»]
	2ADQ	X-ray	2.40	B	25-222	[»]
	2GDS	X-ray	2.30	A/B/C/D	25-222	[»]
	2P4K	X-ray	1.48	A/B/C/D	25-222	[»]
	2QKA	X-ray	2.20	A/C	25-220	[»]
	2QKC	X-ray	2.30	A/C	25-220	[»]
	3C3S	X-ray	2.50	A/B	25-222	[»]
	3C3T	X-ray	2.20	A/B	25-222	[»]
	5GXO	X-ray	2.30	A/B	25-222	[»]
	5T30	X-ray	1.77	A/B	24-222	[»]
	5VF9	X-ray	1.82	A/B	24-222	[»]
	7KKS	neutron diffraction	2.20	A/B	24-222	[»]
	7KKU	X-ray	2.02	A/B	24-222	[»]
	7KKW	neutron diffraction	2.30	A/B	24-222	[»]
	7KLB	X-ray	2.16	A/B	24-222	[»]
AlphaFoldDBⁱ	P04179
SMRⁱ	P04179
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	112531, 77 interactors
IntActⁱ	P04179, 28 interactors
MINTⁱ	P04179
STRINGⁱ	9606.ENSP00000446252

Chemistry databases

ChEMBLⁱ	CHEMBL4105776
DrugBankⁱ	DB04436, 3-Fluoro-L-tyrosine DB09096, Benzoyl peroxide DB03297, Benzylsulfonic acid DB06796, Mangafodipir DB09221, Polaprezinc DB11590, Thimerosal
DrugCentralⁱ	P04179

Protein family/group databases

Allergomeⁱ	784, Hom s MnSOD

Allergomeⁱ

784, Hom s MnSOD

PTM databases

GlyGenⁱ	P04179, 1 site, 1 O-linked glycan (1 site)
iPTMnetⁱ	P04179
PhosphoSitePlusⁱ	P04179
SwissPalmⁱ	P04179

Genetic variation databases

BioMutaⁱ	SOD2
DMDMⁱ	134665

2D gel databases

DOSAC-COBS-2DPAGEⁱ	P04179
OGPⁱ	P04179
SWISS-2DPAGEⁱ	P04179
UCD-2DPAGEⁱ	P04179

Proteomic databases

EPDⁱ	P04179
jPOSTⁱ	P04179
MassIVEⁱ	P04179
MaxQBⁱ	P04179
PaxDbⁱ	P04179
PeptideAtlasⁱ	P04179
PRIDEⁱ	P04179
ProteomicsDBⁱ	3715 51669 [P04179-1] 51670 [P04179-2] 5907
TopDownProteomicsⁱ	P04179-1 [P04179-1] P04179-2 [P04179-2]

Protocols and materials databases

Antibodypediaⁱ	785, 1074 antibodies from 47 providers
The DNASU plasmid repository More...DNASUⁱ	6648

Genome annotation databases

Ensemblⁱ	ENST00000337404.8; ENSP00000337127.4; ENSG00000112096.19 [P04179-2] ENST00000367054.6; ENSP00000356021.2; ENSG00000112096.19 [P04179-2] ENST00000367055.8; ENSP00000356022.4; ENSG00000112096.19 ENST00000444946.6; ENSP00000404804.2; ENSG00000112096.19 [P04179-3] ENST00000538183.7; ENSP00000446252.1; ENSG00000112096.19 ENST00000546087.5; ENSP00000442920.1; ENSG00000112096.19 [P04179-4]
GeneIDⁱ	6648
KEGGⁱ	hsa:6648
MANE-Selectⁱ	ENST00000538183.7; ENSP00000446252.1; NM_000636.4; NP_000627.2
UCSCⁱ	uc003qsf.6, human [P04179-1]

Organism-specific databases

CTDⁱ	6648
DisGeNETⁱ	6648
GeneCardsⁱ	SOD2
HGNCⁱ	HGNC:11180, SOD2
HPAⁱ	ENSG00000112096, Group enriched (bone marrow, skeletal muscle)
MalaCardsⁱ	SOD2
MIMⁱ	147460, gene 612634, phenotype
neXtProtⁱ	NX_P04179
OpenTargetsⁱ	ENSG00000112096
PharmGKBⁱ	PA36017
VEuPathDBⁱ	HostDB:ENSG00000112096
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG0876, Eukaryota
GeneTreeⁱ	ENSGT00390000011877
HOGENOMⁱ	CLU_031625_2_0_1
InParanoidⁱ	P04179
OMAⁱ	KWGSFDK
OrthoDBⁱ	1353361at2759
PhylomeDBⁱ	P04179
TreeFamⁱ	TF105132

Enzyme and pathway databases

BRENDAⁱ	1.15.1.1, 2681
PathwayCommonsⁱ	P04179
Reactomeⁱ	R-HSA-2151201, Transcriptional activation of mitochondrial biogenesis R-HSA-3299685, Detoxification of Reactive Oxygen Species R-HSA-8862803, Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models R-HSA-8950505, Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation R-HSA-9615017, FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes
SABIO-RKⁱ	P04179
SignaLinkⁱ	P04179
SIGNORⁱ	P04179

Miscellaneous databases

BioGRID-ORCSⁱ	6648, 522 hits in 1077 CRISPR screens
ChiTaRSⁱ	SOD2, human
EvolutionaryTraceⁱ	P04179
GeneWikiⁱ	SOD2
GenomeRNAiⁱ	6648
Pharosⁱ	P04179, Tbio
Protein Ontology More...PROⁱ	PR:P04179
RNActⁱ	P04179, protein
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000112096, Expressed in gastrocnemius and 240 other tissues
ExpressionAtlasⁱ	P04179, baseline and differential
Genevisibleⁱ	P04179, HS

Family and domain databases

Gene3Dⁱ	1.10.287.990, 1 hit 3.55.40.20, 1 hit
InterProⁱ	View protein in InterPro IPR001189, Mn/Fe_SOD IPR019833, Mn/Fe_SOD_BS IPR019832, Mn/Fe_SOD_C IPR019831, Mn/Fe_SOD_N IPR036324, Mn/Fe_SOD_N_sf IPR036314, SOD_C_sf
Pfamⁱ	View protein in Pfam PF02777, Sod_Fe_C, 1 hit PF00081, Sod_Fe_N, 1 hit
PIRSFⁱ	PIRSF000349, SODismutase, 1 hit
PRINTSⁱ	PR01703, MNSODISMTASE
SUPFAMⁱ	SSF46609, SSF46609, 1 hit SSF54719, SSF54719, 1 hit
PROSITEⁱ	View protein in PROSITE PS00088, SOD_MN, 1 hit
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	SODM_HUMAN
Accessionⁱ	P04179Primary (citable) accession number: P04179 Secondary accession number(s): B2R7R1 Q9P2Z3
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	March 20, 1987
	Last sequence update:	December 20, 2017
	Last modified:	May 25, 2022
	This is version 248 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Direct protein sequencing, Reference proteome

Documents

Human chromosome 6
Human chromosome 6: entries, gene names and cross-references to MIM
Human entries with genetic variants
List of human entries with genetic variants
Human variants curated from literature reports
Index of human variants curated from literature reports
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families

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UniProtKB - P04179 (SODM_HUMAN)

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Superoxide dismutase [Mn], mitochondrial

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Mitochondrion

Extracellular region or secreted

Mitochondrion

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Miscellaneous databases

Protein family/group databases

Chemistry databases

Genetic variation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

2D gel databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

P04179

GO - Molecular functioni

Protein-protein interaction databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

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Chemistry databases

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Genetic variation databases

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Miscellaneous databases

Gene expression databases

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Functionⁱ

Catalytic activityⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ