[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=2462451 [NCBI, ExPASy, EBI, Israel, Japan] Wispe J.R., Clark J.C., Burhans M.S., Kropp K.E., Korfhagen T.R., Whitsett J.A.; "Synthesis and processing of the precursor for human mangano-superoxide dismutase."; Biochim. Biophys. Acta 994:30-36(1989).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1093/nar/15.21.9076; PubMed=3684581 [NCBI, ExPASy, EBI, Israel, Japan] Beck Y., Oren R., Amit B., Levanon A., Gorecki M., Hartman J.R.; "Human Mn superoxide dismutase cDNA sequence."; Nucleic Acids Res. 15:9076-9076(1987).
[3]	NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-16. DOI=10.1093/nar/16.13.6224; PubMed=3399391 [NCBI, ExPASy, EBI, Israel, Japan] Heckl K.; "Isolation of cDNAs encoding human manganese superoxide dismutase."; Nucleic Acids Res. 16:6224-6224(1988).
[4]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; DOI=10.1016/0014-5793(88)81136-0; PubMed=2831093 [NCBI, ExPASy, EBI, Israel, Japan] Ho Y.-S., Crapo J.D.; "Isolation and characterization of complementary DNAs encoding human manganese-containing superoxide dismutase."; FEBS Lett. 229:256-260(1988).
[5]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0167-4781(90)90213-L; PubMed=1699607 [NCBI, ExPASy, EBI, Israel, Japan] Church S.L.; "Manganese superoxide dismutase: nucleotide and deduced amino acid sequence of a cDNA encoding a new human transcript."; Biochim. Biophys. Acta 1087:250-252(1990).
[6]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Colon; PubMed=1988135 [NCBI, ExPASy, EBI, Israel, Japan] St Clair D.K., Holland J.C.; "Complementary DNA encoding human colon cancer manganese superoxide dismutase and the expression of its gene in human cells."; Cancer Res. 51:939-943(1991).
[7]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1089/dna.1994.13.1127; PubMed=7702755 [NCBI, ExPASy, EBI, Israel, Japan] Wan X.S., Devalaraja M.N., St Clair D.K.; "Molecular structure and organization of the human manganese superoxide dismutase gene."; DNA Cell Biol. 13:1127-1136(1994).
[8]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-16. Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.; "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[9]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-10; VAL-16; VAL-66 AND TRP-156. NIEHS SNPs program; Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
[10]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-16. DOI=10.1038/nature02055; PubMed=14574404 [NCBI, ExPASy, EBI, Israel, Japan] Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; "The DNA sequence and analysis of human chromosome 6."; Nature 425:805-811(2003).
[11]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-16. TISSUE=Lung; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[12]	PROTEIN SEQUENCE OF 25-222. PubMed=6386798 [NCBI, ExPASy, EBI, Israel, Japan] Barra D., Schinina M.E., Simmaco M., Bannister J.V., Bannister W.H., Rotilio G., Bossa F.; "The primary structure of human liver manganese superoxide dismutase."; J. Biol. Chem. 259:12595-12601(1984).
[13]	PROTEIN SEQUENCE OF 25-39. TISSUE=Heart; DOI=10.1002/elps.11501501209; PubMed=7895732 [NCBI, ExPASy, EBI, Israel, Japan] Corbett J.M., Wheeler C.H., Baker C.S., Yacoub M.H., Dunn M.J.; "The human myocardial two-dimensional gel protein database: update 1994."; Electrophoresis 15:1459-1465(1994).
[14]	PROTEIN SEQUENCE OF 25-39. TISSUE=Heart; DOI=10.1002/elps.11501601192; PubMed=7498159 [NCBI, ExPASy, EBI, Israel, Japan] Kovalyov L.I., Shishkin S.S., Efimochkin A.S., Kovalyova M.A., Ershova E.S., Egorov T.A., Musalyamov A.K.; "The major protein expression profile and two-dimensional protein database of human heart."; Electrophoresis 16:1160-1169(1995).
[15]	PROTEIN SEQUENCE OF 25-39. TISSUE=Mammary carcinoma; DOI=10.1002/elps.1150180342; PubMed=9150946 [NCBI, ExPASy, EBI, Israel, Japan] Rasmussen R.K., Ji H., Eddes J.S., Moritz R.L., Reid G.E., Simpson R.J., Dorow D.S.; "Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2."; Electrophoresis 18:588-598(1997).
[16]	NITRATION, FUNCTION, AND MUTAGENESIS OF TYR-58. DOI=10.1006/abbi.1999.1202; PubMed=10334867 [NCBI, ExPASy, EBI, Israel, Japan] MacMillan-Crow L.A., Thompson J.A.; "Tyrosine modifications and inactivation of active site manganese superoxide dismutase mutant (Y34F) by peroxynitrite."; Arch. Biochem. Biophys. 366:82-88(1999).
[17]	NITRATION AT TYR-58. DOI=10.1152/ajpheart.01293.2005; PubMed=16399855 [NCBI, ExPASy, EBI, Israel, Japan] Xu S., Ying J., Jiang B., Guo W., Adachi T., Sharov V., Lazar H., Menzoian J., Knyushko T.V., Bigelow D., Schoeneich C., Cohen R.A.; "Detection of sequence-specific tyrosine nitration of manganese SOD and SERCA in cardiovascular disease and aging."; Am. J. Physiol. 290:H2220-H2227(2006).
[18]	IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. Colinge J., Superti-Furga G., Bennett K.L.; Submitted (OCT-2008) to UniProtKB.
[19]	X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). DOI=10.1016/0092-8674(92)90270-M; PubMed=1394426 [NCBI, ExPASy, EBI, Israel, Japan] Borgstahl G.E.O., Parge H.E., Hickey M.J., Beyer W.F. Jr., Hallewell R.A., Tainer J.A.; "The structure of human mitochondrial manganese superoxide dismutase reveals a novel tetrameric interface of two 4-helix bundles."; Cell 71:107-118(1992).
[20]	X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF VARIANT THR-82. DOI=10.1021/bi951892w; PubMed=8605177 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Human mitochondrial manganese superoxide dismutase polymorphic variant Ile58Thr reduces activity by destabilizing the tetrameric interface."; Biochemistry 35:4287-4297(1996).
[21]	X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT ASN-167. DOI=10.1021/bi972395d; PubMed=9537988 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Probing the active site of human manganese superoxide dismutase: the role of glutamine 143."; Biochemistry 37:4731-4739(1998).
[22]	X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT TYR-58. DOI=10.1021/bi972394l; PubMed=9537987 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Crystal structure of Y34F mutant human mitochondrial manganese superoxide dismutase and the functional role of tyrosine 34."; Biochemistry 37:4722-4730(1998).
[23]	X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS) OF MUTANT ALA-167. DOI=10.1021/bi9929958; PubMed=10852710 [NCBI, ExPASy, EBI, Israel, Japan] Leveque V.J.-P., Stroupe M.E., Lepock J.R., Cabelli D.E., Tainer J.A., Nick H.S., Silverman D.N.; "Multiple replacements of glutamine 143 in human manganese superoxide dismutase: effects on structure, stability, and catalysis."; Biochemistry 39:7131-7137(2000).
[24]	X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF MUTANT ALA-185. DOI=10.1021/bi011047f; PubMed=11580280 [NCBI, ExPASy, EBI, Israel, Japan] Hearn A.S., Stroupe M.E., Cabelli D.E., Lepock J.R., Tainer J.A., Nick H.S., Silverman D.N.; "Kinetic analysis of product inhibition in human manganese superoxide dismutase."; Biochemistry 40:12051-12058(2001).
[25]	VARIANT VAL-16, AND ASSOCIATION WITH DIABETIC NEPHROPATHY SUSCEPTIBILITY. DOI=10.1007/s100380300021; PubMed=12624725 [NCBI, ExPASy, EBI, Israel, Japan] Nomiyama T., Tanaka Y., Piao L., Nagasaka K., Sakai K., Ogihara T., Nakajima K., Watada H., Kawamori R.; "The polymorphism of manganese superoxide dismutase is associated with diabetic nephropathy in Japanese type 2 diabetic patients."; J. Hum. Genet. 48:138-141(2003).

Comments

FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
CATALYTIC ACTIVITY: 2 superoxide + 2 H⁺ = O₂ + H₂O₂.
COFACTOR: Binds 1 manganese ion per subunit.
SUBUNIT: Homotetramer.
INTERACTION:
O14965:AURKA; NbExp=1; IntAct=EBI-716989, EBI-448680;
SUBCELLULAR LOCATION: Mitochondrion matrix.
PTM: Nitrated under oxidative stress. Nitration coupled with oxidation inhibits the catalytic activity.
DISEASE: Genetic variation in SOD2 is associated with susceptibility to diabetic nephropathy [MIM:612634]; also called susceptibility to microvascular complications of diabetes type 6 (MVCD6). Diabetic nephropathy is a kidney disease and resultant kidney function impairment due to the long standing effects of diabetes on the microvasculature (glomerulus) of the kidney. Features include increased urine protein and declining kidney function.
SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/sod2/";.
WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and polymorphism database; URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=SOD2";.
WEB RESOURCE: Name=Wikipedia; Note=Superoxide dismutase entry; URL="http://en.wikipedia.org/wiki/Superoxide_dismutase";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X59445; CAA42066.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Y00472; CAA68533.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Y00985; CAA68791.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X07834; CAA30687.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M36693; AAA36622.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X15132; CAA33228.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X14322; CAA32502.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S77127; AAD14248.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BT006967; AAP35613.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY267901; AAP03428.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL135914; CAI21845.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC012423; AAH12423.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00022314; -.

PIR

S13162; DSHUN.

RefSeq

NP_000627.2; -.
NP_001019636.1; -.

UniGene

Hs.487046

3D structure databases

PDB

1AP5; X-ray; 2.20 A; A/B=25-222.	[ExPASy / RCSB / EBI]
1AP6; X-ray; 1.90 A; A/B=25-222.	[ExPASy / RCSB / EBI]
1EM1; X-ray; 2.13 A; A/B=25-222.	[ExPASy / RCSB / EBI]
1JA8; X-ray; 2.12 A; A/B=25-222.	[ExPASy / RCSB / EBI]
1LUV; X-ray; 1.85 A; A/B=25-222.	[ExPASy / RCSB / EBI]
1LUW; X-ray; 2.30 A; A/B=25-222.	[ExPASy / RCSB / EBI]
1MSD; X-ray; 3.20 A; A/B=25-222.	[ExPASy / RCSB / EBI]
1N0J; X-ray; 2.20 A; A/B=25-222.	[ExPASy / RCSB / EBI]
1N0N; X-ray; 1.82 A; A/B=25-222.	[ExPASy / RCSB / EBI]
1PL4; X-ray; 1.47 A; A/B/C/D=25-222.	[ExPASy / RCSB / EBI]
1PM9; X-ray; 1.70 A; A/B=25-222.	[ExPASy / RCSB / EBI]
1QNM; X-ray; 2.30 A; A/B=25-222.	[ExPASy / RCSB / EBI]
1SZX; X-ray; 1.95 A; A/B=25-222.	[ExPASy / RCSB / EBI]
1VAR; X-ray; 2.50 A; A/B=25-222.	[ExPASy / RCSB / EBI]
1XDC; X-ray; 1.85 A; A/B=25-222.	[ExPASy / RCSB / EBI]
1XIL; X-ray; 1.53 A; A/B=25-222.	[ExPASy / RCSB / EBI]
1ZSP; X-ray; 1.90 A; A/B=25-222.	[ExPASy / RCSB / EBI]
1ZTE; X-ray; 1.85 A; A/B/C/D=25-222.	[ExPASy / RCSB / EBI]
1ZUQ; X-ray; 2.00 A; A/B=25-222.	[ExPASy / RCSB / EBI]
2ADP; X-ray; 2.40 A; A=25-222.	[ExPASy / RCSB / EBI]
2ADQ; X-ray; 2.40 A; B=25-222.	[ExPASy / RCSB / EBI]
2GDS; X-ray; 2.30 A; A/B/C/D=25-222.	[ExPASy / RCSB / EBI]
2P4K; X-ray; 1.48 A; A/B/C/D=25-222.	[ExPASy / RCSB / EBI]
2QKA; X-ray; 2.20 A; A/C=25-220.	[ExPASy / RCSB / EBI]
2QKC; X-ray; 2.30 A; A/C=25-220.	[ExPASy / RCSB / EBI]
3C3S; X-ray; 2.50 A; A/B=25-222.	[ExPASy / RCSB / EBI]
3C3T; X-ray; 2.20 A; A/B=25-222.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1AP5; -.
1AP6; -.
1EM1; -.
1JA8; -.
1LUV; -.
1LUW; -.
1MSD; -.
1N0J; -.
1N0N; -.
1PL4; -.
1PM9; -.
1QNM; -.
1SZX; -.
1VAR; -.
1XDC; -.
1XIL; -.
1ZSP; -.
1ZTE; -.
1ZUQ; -.
2ADP; -.
2ADQ; -.
2GDS; -.
2P4K; -.
2QKA; -.
2QKC; -.
3C3S; -.
3C3T; -.

ModBase

P04179.

Protein-protein interaction databases

IntAct

P04179; 20.

PTM databases

PhosphoSite

P04179; -.

Enzyme and pathway databases

BRENDA

1.15.1.1; 247.

Pathway_Interaction_DB

foxopathway; FoxO family signaling.

2D gel databases

P04179; -.

P04179; -.

P04179; -.

P04179; -.

P04179; -.

P04179; -.

Organism-specific databases

GC06M160020; -.

HGNC:11180; SOD2.

CAB002013; -.
HPA001814; -.

MIM

147460; gene. [NCBI / EBI]
612634; phenotype. [NCBI / EBI]

PharmGKB

PA36017; -.

Gene expression databases

P04179; -.

P04179; -.

HS_SOD2; -.

ENSG00000112096; Homo sapiens.

Ontologies

GO:0005759;	Cellular component: mitochondrial matrix (traceable author statement from UniProtKB).
GO:0030145;	Molecular function: manganese ion binding (traceable author statement from UniProtKB).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004784;	Molecular function: superoxide dismutase activity (inferred from direct assay from UniProtKB).
GO:0001315;	Biological process: age-dependent response to reactive oxygen species (inferred from mutant phenotype from UniProtKB).
GO:0043524;	Biological process: negative regulation of neuron apoptosis (inferred from genetic interaction from UniProtKB).
GO:0032364;	Biological process: oxygen homeostasis (inferred from mutant phenotype from UniProtKB).
GO:0006357;	Biological process: regulation of transcription from RNA polymerase II promoter (inferred from mutant phenotype from UniProtKB).
GO:0001836;	Biological process: release of cytochrome c from mitochondria (inferred from sequence or structural similarity from UniProtKB).
GO:0019430;	Biological process: removal of superoxide radicals (inferred from mutant phenotype from UniProtKB).
GO:0000303;	Biological process: response to superoxide (inferred from mutant phenotype from UniProtKB).
GO:0003069;	Biological process: vasodilation by acetylcholine involved in regulation of systemic arterial blood pressure (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR001189; Mn/Fe_SOD.
IPR019833; Mn/Fe_SOD_BS.
IPR019832; Mn/Fe_SOD_C.
IPR019831; Mn/Fe_SOD_N.
Graphical view of domain structure.

PANTHER

PTHR11404; SODismutase; 1.

Pfam

PF02777; Sod_Fe_C; 1.
PF00081; Sod_Fe_N; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000349; SODismutase; 1.

PRINTS

PR01703; MNSODISMTASE.

ProDom

PD000475; SODismutase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00088; SOD_MN; 1.

Proteomic databases

PRIDE

P04179; -.

Genome annotation databases

Ensembl

ENSG00000112096; Homo sapiens. [Contig view]

GeneID

6648; -.

KEGG

hsa:6648; -.

Phylogenomic databases

HOGENOM

P04179; -.

HOVERGEN

P04179; -.

Other

25907; -.

SOD2; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acetylation; Direct protein sequencing; Manganese; Metal-binding; Mitochondrion; Nitration; Oxidoreductase; Polymorphism; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 24`	`24`	`Mitochondrion.`
`CHAIN`	`25 222`	`198`	`Superoxide dismutase [Mn], mitochondrial.`	`PRO_0000032869`
`METAL`	`50 50`		`Manganese.`
`METAL`	`98 98`		`Manganese.`
`METAL`	`183 183`		`Manganese.`
`METAL`	`187 187`		`Manganese.`
`MOD_RES`	`58 58`		`Nitrated tyrosine.`
`MOD_RES`	`68 68`		`N6-acetyllysine (By similarity).`
`VARIANT`	`10 10`	`1`	`S -> I (in dbSNP:rs5746096 [NCBI]).`	`VAR_019363`
`VARIANT`	`16 16`	`1`	`A -> V (very frequent polymorphism; associated with susceptibility to diabetic nephropathy in Japanese patients with type 2 diabetes; dbSNP:rs4880 [NCBI]).`	`VAR_016183`
`VARIANT`	`66 66`	`1`	`E -> V (in dbSNP:rs5746097 [NCBI]).`	`VAR_019364 [3D]`
`VARIANT`	`76 76`	`1`	`G -> R (in dbSNP:rs4987023 [NCBI]).`	`VAR_025898 [3D]`
`VARIANT`	`82 82`	`1`	`I -> T (in dbSNP:rs1141718 [NCBI]).`	`VAR_007165 [3D]`
`VARIANT`	`156 156`	`1`	`R -> W (in dbSNP:rs5746129 [NCBI]).`	`VAR_019365 [3D]`
`MUTAGEN`	`58 58`		`Y->F: Loss of nitration. Enhanced dityrosine formation on peroxynitrite treatment.`
`CONFLICT`	`14 14`		`A -> P (in Ref. 3).`
`CONFLICT`	`65 65`		`T -> N (in Ref. 5; CAA42066/CAA33228).`
`CONFLICT`	`66 66`		`E -> Q (in Ref. 6).`
`CONFLICT`	`112 112`		`E -> Q (in Ref. 6).`
`CONFLICT`	`123 123`		`R -> L (in Ref. 3; CAA30687).`
`CONFLICT`	`133 133`		`E -> Q (in Ref. 6).`
`CONFLICT`	`148 149`		`Missing (in Ref. 6).`
`CONFLICT`	`155 155`		`E -> Q (in Ref. 2 and 6).`
`TURN`	`35 41`	`7`
`HELIX`	`44 52`	`9`
`HELIX`	`54 74`	`21`
`HELIX`	`78 83`	`6`
`HELIX`	`85 103`	`19`
`HELIX`	`115 125`	`11`
`HELIX`	`128 140`	`13`
`STRAND`	`144 153`	`10`
`TURN`	`154 157`	`4`
`STRAND`	`158 165`	`8`
`HELIX`	`170 174`	`5`
`STRAND`	`177 183`	`7`
`HELIX`	`186 188`	`3`
`HELIX`	`190 193`	`4`
`HELIX`	`197 204`	`8`
`HELIX`	`205 207`	`3`
`HELIX`	`210 219`	`10`

Sequence information

Length: 222 AA [This is the length of the unprocessed precursor]

Molecular weight: 24722 Da [This is the MW of the unprocessed precursor]

CRC64: 648435C080E6E47B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLSRAVCGTS RQLAPALGYL GSRQKHSLPD LPYDYGALEP HINAQIMQLH HSKHHAAYVN 

        70         80         90        100        110        120 
NLNVTEEKYQ EALAKGDVTA QIALQPALKF NGGGHINHSI FWTNLSPNGG GEPKGELLEA 

       130        140        150        160        170        180 
IKRDFGSFDK FKEKLTAASV GVQGSGWGWL GFNKERGHLQ IAACPNQDPL QGTTGLIPLL 

       190        200        210        220 
GIDVWEHAYY LQYKNVRPDY LKAIWNVINW ENVTERYMAC KK

P04179 in FASTA format

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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools