Superoxide dismutase [Mn], mitochondrial precursor

Hide | Top

Names and origin

Protein names

Recommended name:
Superoxide dismutase [Mn], mitochondrial
EC=1.15.1.1

Gene names

Name:

SOD2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Hide | Top

Protein attributes

Sequence length	222 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

Hide | Top

General annotation (Comments)

Function	Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Ref.18
Catalytic activity	2 superoxide + 2 H⁺ = O₂ + H₂O₂.
Cofactor	Binds 1 manganese ion per subunit.
Subunit structure	Homotetramer. Ref.28
Subcellular location	Mitochondrion matrix.
Post-translational modification	Nitrated under oxidative stress. Nitration coupled with oxidation inhibits the catalytic activity.
Involvement in 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.
Sequence similarities	Belongs to the iron/manganese superoxide dismutase family.

Hide | Top

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Ligand	Manganese Metal-binding
Molecular function	Oxidoreductase
PTM	Acetylation Nitration
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	age-dependent response to reactive oxygen species Inferred from mutant phenotype. Source: UniProtKB negative regulation of neuron apoptosis Inferred from genetic interaction. Source: UniProtKB oxygen homeostasis Inferred from mutant phenotype. Source: UniProtKB protein homotetramerization Ref.28 Inferred from physical interaction. Source: UniProtKB regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype. Source: UniProtKB release of cytochrome c from mitochondria Inferred from sequence or structural similarity. Source: UniProtKB removal of superoxide radicals Inferred from mutant phenotype. Source: UniProtKB vasodilation by acetylcholine involved in regulation of systemic arterial blood pressure Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	mitochondrial matrix Traceable author statement. Source: UniProtKB
Molecular function	manganese ion binding Ref.28 Inferred from direct assay. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct superoxide dismutase activity Ref.28 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Hide | Top

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AURKA	O14965	1	EBI-716989,EBI-448680

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 24

24

Mitochondrion Ref.14 Ref.15 Ref.16 Ref.17

Chain

25 – 222

198

Superoxide dismutase [Mn], mitochondrial

PRO_0000032869

Sites

Metal binding

50

1

Manganese

Metal binding

98

1

Manganese

Metal binding

183

1

Manganese

Metal binding

187

1

Manganese

Amino acid modifications

Modified residue

58

1

Nitrated tyrosine Ref.19

Modified residue

68

1

N6-acetyllysine Ref.21

Modified residue

130

1

N6-acetyllysine Ref.21

Natural variations

Natural variant

10

1

S → I: dbSNP rs5746096. Ref.9

VAR_019363

Natural variant

16

1

A → V Very frequent polymorphism; associated with susceptibility to diabetic nephropathy in Japanese patients with type 2 diabetes. dbSNP rs4880. Ref.9 Ref.3 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.29

VAR_016183

Natural variant

66

1

E → V: dbSNP rs5746097. Ref.9

VAR_019364

Natural variant

76

1

G → R: dbSNP rs4987023.

VAR_025898

Natural variant

82

1

I → T: dbSNP rs1141718. Ref.23

VAR_007165

Natural variant

156

1

R → W: dbSNP rs5746129. Ref.9

VAR_019365

Experimental info

Mutagenesis

58

1

Y → A, H, N, V or F: Reduced enzyme activity. Ref.18

Mutagenesis

58

1

Y → F: Loss of nitration. Enhanced dityrosine formation on peroxynitrite treatment. Ref.18

Sequence conflict

14

1

A → P Ref.3

Sequence conflict

65

1

T → N in CAA42066. Ref.5

Sequence conflict

65

1

T → N in CAA33228. Ref.5

Sequence conflict

66

1

E → Q Ref.6

Sequence conflict

112

1

E → Q Ref.6

Sequence conflict

123

1

R → L in CAA30687. Ref.3

Sequence conflict

133

1

E → Q Ref.6

Sequence conflict

148 – 149

2

Missing Ref.6

Sequence conflict

155

1

E → Q Ref.2

Sequence conflict

155

1

E → Q Ref.6

Secondary structure

1

.

222

Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P04179-1 [UniParc].

Last modified April 1, 1990. Version 2.
Checksum: 648435C080E6E47B
Show »

FASTA

222

24,722

        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

« Hide

Hide | Top

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Synthesis and processing of the precursor for human mangano-superoxide dismutase." Wispe J.R., Clark J.C., Burhans M.S., Kropp K.E., Korfhagen T.R., Whitsett J.A. Biochim. Biophys. Acta 994:30-36(1989) [PubMed: 2462451] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Human Mn superoxide dismutase cDNA sequence." Beck Y., Oren R., Amit B., Levanon A., Gorecki M., Hartman J.R. Nucleic Acids Res. 15:9076-9076(1987) [PubMed: 3684581] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Isolation of cDNAs encoding human manganese superoxide dismutase." Heckl K. Nucleic Acids Res. 16:6224-6224(1988) [PubMed: 3399391] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-16.
[4]	"Isolation and characterization of complementary DNAs encoding human manganese-containing superoxide dismutase." Ho Y.-S., Crapo J.D. FEBS Lett. 229:256-260(1988) [PubMed: 2831093] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[5]	"Manganese superoxide dismutase: nucleotide and deduced amino acid sequence of a cDNA encoding a new human transcript." Church S.L. Biochim. Biophys. Acta 1087:250-252(1990) [PubMed: 1699607] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]	"Complementary DNA encoding human colon cancer manganese superoxide dismutase and the expression of its gene in human cells." St Clair D.K., Holland J.C. Cancer Res. 51:939-943(1991) [PubMed: 1988135] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Colon.
[7]	"Molecular structure and organization of the human manganese superoxide dismutase gene." Wan X.S., Devalaraja M.N., St Clair D.K. DNA Cell Biol. 13:1127-1136(1994) [PubMed: 7702755] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." 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. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-16.
[9]	NIEHS SNPs program Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ILE-10; VAL-16; VAL-66 AND TRP-156.
[10]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-16. Tissue: Hippocampus.
[11]	"The DNA sequence and analysis of human chromosome 6." 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. Beck S. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-16.
[12]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-16.
[13]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-16. Tissue: Lung.
[14]	"The primary structure of human liver manganese superoxide dismutase." Barra D., Schinina M.E., Simmaco M., Bannister J.V., Bannister W.H., Rotilio G., Bossa F. J. Biol. Chem. 259:12595-12601(1984) [PubMed: 6386798] [Abstract] Cited for: PROTEIN SEQUENCE OF 25-222.
[15]	"The human myocardial two-dimensional gel protein database: update 1994." Corbett J.M., Wheeler C.H., Baker C.S., Yacoub M.H., Dunn M.J. Electrophoresis 15:1459-1465(1994) [PubMed: 7895732] [Abstract] Cited for: PROTEIN SEQUENCE OF 25-39. Tissue: Heart.
[16]	"The major protein expression profile and two-dimensional protein database of human heart." Kovalyov L.I., Shishkin S.S., Efimochkin A.S., Kovalyova M.A., Ershova E.S., Egorov T.A., Musalyamov A.K. Electrophoresis 16:1160-1169(1995) [PubMed: 7498159] [Abstract] Cited for: PROTEIN SEQUENCE OF 25-39. Tissue: Heart.
[17]	"Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2." Rasmussen R.K., Ji H., Eddes J.S., Moritz R.L., Reid G.E., Simpson R.J., Dorow D.S. Electrophoresis 18:588-598(1997) [PubMed: 9150946] [Abstract] Cited for: PROTEIN SEQUENCE OF 25-39. Tissue: Mammary carcinoma.
[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: 10334867] [Abstract] Cited for: NITRATION, FUNCTION, MUTAGENESIS OF TYR-58.
[19]	"Detection of sequence-specific tyrosine nitration of manganese SOD and SERCA in cardiovascular disease and aging." 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. Am. J. Physiol. 290:H2220-H2227(2006) [PubMed: 16399855] [Abstract] Cited for: NITRATION AT TYR-58.
[20]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[21]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-68 AND LYS-130, MASS SPECTROMETRY.
[22]	"The structure of human mitochondrial manganese superoxide dismutase reveals a novel tetrameric interface of two 4-helix bundles." Borgstahl G.E.O., Parge H.E., Hickey M.J., Beyer W.F. Jr., Hallewell R.A., Tainer J.A. Cell 71:107-118(1992) [PubMed: 1394426] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[23]	"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: 8605177] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF VARIANT THR-82.
[24]	"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: 9537988] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT ASN-167.
[25]	"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: 9537987] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT TYR-58.
[26]	"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: 10852710] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS) OF MUTANT ALA-167.
[27]	"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: 11580280] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF MUTANT ALA-185.
[28]	"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: 19265433] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF MUTANTS ALA/ASN/HIS/VAL-58 IN COMPLEX WITH MANGANESE IONS, SUBUNIT.
[29]	"The polymorphism of manganese superoxide dismutase is associated with diabetic nephropathy in Japanese type 2 diabetic patients." Nomiyama T., Tanaka Y., Piao L., Nagasaka K., Sakai K., Ogihara T., Nakajima K., Watada H., Kawamori R. J. Hum. Genet. 48:138-141(2003) [PubMed: 12624725] [Abstract] Cited for: VARIANT VAL-16, ASSOCIATION WITH DIABETIC NEPHROPATHY SUSCEPTIBILITY.
+	Additional computationally mapped references.

Hide | Top

Web resources

NIEHS-SNPs

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Superoxide dismutase entry

Hide | Top

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.
AK313082 mRNA. Translation: BAG35908.1.
AL135914 Genomic DNA. Translation: CAI21845.1.
CH471051 Genomic DNA. Translation: EAW47630.1.
BC012423 mRNA. Translation: AAH12423.1.

IPI

IPI00022314.

PIR

DSHUN. S13162.

RefSeq

NP_000627.2.
NP_001019636.1.

UniGene

Hs.487046

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P04179. 20 interactions.

STRING

P04179.

PTM databases

PhosphoSite

P04179.

2-D gel databases

SWISS-2DPAGE

P04179.

DOSAC-COBS-2DPAGE

P04179.

HSC-2DPAGE

P04179.

OGP

P04179.

PMMA-2DPAGE

P04179.

Siena-2DPAGE

P04179.

Proteomic databases

PRIDE

P04179.

Genome annotation databases

Ensembl

ENST00000337404; ENSP00000337127; ENSG00000112096; Homo sapiens. [Genome view]
ENST00000367055; ENSP00000356022; ENSG00000112096; Homo sapiens. [Genome view]

GeneID

6648.

KEGG

hsa:6648.

Organism-specific databases

CTD

6648.

GeneCards

GC06M160020.

HGNC

HGNC:11180. SOD2.

HPA

CAB002013.
HPA001814.

MIM

147460. gene.
612634. phenotype.

PharmGKB

PA36017.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG18046.

HOGENOM

HBG507761.

HOVERGEN

P04179.

InParanoid

P04179.

PhylomeDB

P04179.

Enzyme and pathway databases

BRENDA

1.15.1.1. 247.

Pathway_Interaction_DB

foxopathway. FoxO family signaling.

Gene expression databases

ArrayExpress

P04179.

Bgee

P04179.

CleanEx

HS_SOD2.

Genevestigator

P04179.

GermOnline

ENSG00000112096. Homo sapiens.

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]

PANTHER

PTHR11404. SODismutase. 1 hit.

Pfam

PF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]

PIRSF

PIRSF000349. SODismutase. 1 hit.

PRINTS

PR01703. MNSODISMTASE.

PROSITE

PS00088. SOD_MN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

25907.

SOURCE

Search...

Hide | Top

Entry information

Entry name

SODM_HUMAN

Accession

Primary (citable) accession number: P04179
Secondary accession number(s): B2R7R1

Q9P2Z3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 1987
Last sequence update:	April 1, 1990
Last modified:	January 19, 2010
This is version 137 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.

Hide | Top

Relevant documents

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

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

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents