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P78417 (GSTO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione S-transferase omega-1

Short name=GSTO-1
EC=2.5.1.18
Alternative name(s):
Glutathione S-transferase omega 1-1
Short name=GSTO 1-1
Glutathione-dependent dehydroascorbate reductase
EC=1.8.5.1
Monomethylarsonic acid reductase
Short name=MMA(V) reductase
EC=1.20.4.2
S-(Phenacyl)glutathione reductase
Short name=SPG-R
Gene names
Name:GSTO1
Synonyms:GSTTLP28
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length241 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities. Has S-(phenacyl)glutathione reductase activity. Has also glutathione S-transferase activity. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) and dimethylarsonic acid. Ref.2 Ref.9 Ref.10 Ref.11 Ref.15

Catalytic activity

RX + glutathione = HX + R-S-glutathione. Ref.2 Ref.9 Ref.10 Ref.11 Ref.15

2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate. Ref.2 Ref.9 Ref.10 Ref.11 Ref.15

Methylarsonate + 2 glutathione = methylarsonite + glutathione disulfide + H2O. Ref.2 Ref.9 Ref.10 Ref.11 Ref.15

Enzyme regulation

Monomethylarsonic acid reductase activity is competitively inhibited by 1-chloro 2,4-dinitrobenzene (CDNB) and by deoxycholate.

Subunit structure

Homodimer. Ref.2 Ref.15

Subcellular location

Cytoplasmcytosol Ref.9.

Tissue specificity

Ubiquitous. Highest expression in liver, pancreas, skeletal muscle, spleen, thymus, colon, blood leukocyte and heart. Lowest expression in brain, placenta and lung. Ref.2

Sequence similarities

Belongs to the GST superfamily. Omega family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Biophysicochemical properties

pH dependence:

Optimum pH is 8. Ref.9 Ref.10

Sequence caution

The sequence CAD97673.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionOxidoreductase
Transferase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processL-ascorbic acid metabolic process

Inferred from direct assay Ref.9. Source: UniProtKB

cellular response to arsenic-containing substance

Inferred from direct assay Ref.9. Source: UniProtKB

glutathione derivative biosynthetic process

Traceable author statement. Source: Reactome

negative regulation of ryanodine-sensitive calcium-release channel activity

Inferred from direct assay PubMed 11035031. Source: BHF-UCL

positive regulation of ryanodine-sensitive calcium-release channel activity

Inferred from direct assay PubMed 11035031. Source: BHF-UCL

positive regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion

Inferred by curator PubMed 11035031. Source: BHF-UCL

regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion

Inferred by curator PubMed 11035031. Source: BHF-UCL

regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum

Inferred from direct assay PubMed 11035031. Source: BHF-UCL

small molecule metabolic process

Traceable author statement. Source: Reactome

xenobiotic catabolic process

Inferred from direct assay Ref.3. Source: UniProtKB

xenobiotic metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay Ref.9. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337PubMed 23376485. Source: UniProt

   Molecular_functionglutathione dehydrogenase (ascorbate) activity

Inferred from direct assay Ref.9. Source: UniProtKB

glutathione transferase activity

Inferred from direct assay Ref.9. Source: UniProtKB

methylarsonate reductase activity

Inferred from electronic annotation. Source: UniProtKB-EC

oxidoreductase activity

Inferred from direct assay Ref.9. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P78417-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P78417-2)

The sequence of this isoform differs from the canonical sequence as follows:
     123-155: Missing.
Isoform 3 (identifier: P78417-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-28: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.12
Chain2 – 241240Glutathione S-transferase omega-1
PRO_0000185884

Regions

Domain22 – 10180GST N-terminal
Domain106 – 230125GST C-terminal
Region85 – 862Glutathione binding

Sites

Active site321Nucleophile Ref.2
Binding site591Glutathione
Binding site721Glutathione; via amide nitrogen and carbonyl oxygen

Amino acid modifications

Modified residue21N-acetylserine Ref.12
Modified residue571N6-acetyllysine Ref.13
Modified residue1431N6-acetyllysine Ref.13
Modified residue1481N6-acetyllysine Ref.13
Modified residue1521N6-acetyllysine Ref.13

Natural variations

Alternative sequence1 – 2828Missing in isoform 3.
VSP_045819
Alternative sequence123 – 15533Missing in isoform 2.
VSP_045820
Natural variant321C → Y.
Corresponds to variant rs45529437 [ dbSNP | Ensembl ].
VAR_061231
Natural variant861S → C.
Corresponds to variant rs11509436 [ dbSNP | Ensembl ].
VAR_029269
Natural variant1401A → D in allele GSTO1*C; no effect on protein stability. Ref.3 Ref.15 Ref.16
Corresponds to variant rs4925 [ dbSNP | Ensembl ].
VAR_016811
Natural variant1551Missing in allele GSTO1*B; decreased protein stability. Ref.3 Ref.15 Ref.16
VAR_016813
Natural variant2081E → K. Ref.3
Corresponds to variant rs11509438 [ dbSNP | Ensembl ].
VAR_024484
Natural variant2361A → V. Ref.3
Corresponds to variant rs11509439 [ dbSNP | Ensembl ].
VAR_026583

Experimental info

Mutagenesis321C → A: Loss of activity. Ref.10

Secondary structure

........................................... 241
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 1, 1998. Version 2.
Checksum: 9134ABA265F5C87E

FASTA24127,566
        10         20         30         40         50         60 
MSGESARSLG KGSAPPGPVP EGSIRIYSMR FCPFAERTRL VLKAKGIRHE VININLKNKP 

        70         80         90        100        110        120 
EWFFKKNPFG LVPVLENSQG QLIYESAITC EYLDEAYPGK KLLPDDPYEK ACQKMILELF 

       130        140        150        160        170        180 
SKVPSLVGSF IRSQNKEDYA GLKEEFRKEF TKLEEVLTNK KTTFFGGNSI SMIDYLIWPW 

       190        200        210        220        230        240 
FERLEAMKLN ECVDHTPKLK LWMAAMKEDP TVSALLTSEK DWQGFLELYL QNSPEACDYG 


L 

« Hide

Isoform 2 [UniParc].

Checksum: F00CDE200E2A1738
Show »

FASTA20823,709
Isoform 3 [UniParc].

Checksum: C3F8EBA348399628
Show »

FASTA21324,796

References

« Hide 'large scale' references
[1]"Cloning of the human homolog to a mouse protein, differentially expressed in lymphoma cells with different susceptibility to radiation induced apoptosis."
Kodym R., Story M.D.
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Placenta.
[2]"Identification, characterization, and crystal structure of the Omega class glutathione transferases."
Board P.G., Coggan M., Chelvanayagam G., Easteal S., Jermiin L.S., Schulte G.K., Danley D.E., Hoth L.R., Griffor M.C., Kamath A.V., Rosner M.H., Chrunyk B.A., Perregaux D.E., Gabel C.A., Geoghegan K.F., Pandit J.
J. Biol. Chem. 275:24798-24806(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, TISSUE SPECIFICITY.
Tissue: Fetus.
[3]"Genetic variation in genes associated with arsenic metabolism: glutathione S-transferase omega 1-1 and purine nucleoside phosphorylase polymorphisms in European and indigenous Americans."
Yu L., Kalla K., Guthrie E., Vidrine A., Klimecki W.T.
Environ. Health Perspect. 111:1421-1427(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASP-140; GLU-155 DEL; LYS-208 AND VAL-236.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Uterus.
[5]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Eye.
[8]"Human ERp29: isolation, primary structural characterisation and two-dimensional gel mapping."
Hubbard M.J., McHugh N.J.
Electrophoresis 21:3785-3796(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 12-21; 58-65; 133-139 AND 149-156, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Liver.
[9]"Human monomethylarsonic acid (MMA(V)) reductase is a member of the glutathione-S-transferase superfamily."
Zakharyan R.A., Sampayo-Reyes A., Healy S.M., Tsaprailis G., Board P.G., Liebler D.C., Aposhian H.V.
Chem. Res. Toxicol. 14:1051-1057(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Liver.
[10]"Glutathione transferase omega 1 catalyzes the reduction of S-(phenacyl)glutathiones to acetophenones."
Board P.G., Anders M.W.
Chem. Res. Toxicol. 20:149-154(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF CYS-32, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY.
[11]"S-(4-Nitrophenacyl)glutathione is a specific substrate for glutathione transferase omega 1-1."
Board P.G., Coggan M., Cappello J., Zhou H., Oakley A.J., Anders M.W.
Anal. Biochem. 374:25-30(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
[12]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[13]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-57; LYS-143; LYS-148 AND LYS-152, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Novel folding and stability defects cause a deficiency of human glutathione transferase omega 1."
Zhou H., Brock J., Casarotto M.G., Oakley A.J., Board P.G.
J. Biol. Chem. 286:4271-4279(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF VARIANT GLU-155 DEL, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, CHARACTERIZATION OF VARIANTS ASP-140 AND GLU-155 DEL.
[16]"Characterization of the human Omega class glutathione transferase genes and associated polymorphisms."
Whitbread A.K., Tetlow N., Eyre H.J., Sutherland G.R., Board P.G.
Pharmacogenetics 13:131-144(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ASP-140 AND GLU-155 DEL.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U90313 mRNA. Translation: AAB70109.1.
AF212303 mRNA. Translation: AAF73376.1.
AY817669 Genomic DNA. Translation: AAV68046.1.
BX537431 mRNA. Translation: CAD97673.1. Different initiation.
AL139341 Genomic DNA. Translation: CAI17224.1.
CH471066 Genomic DNA. Translation: EAW49601.1.
CH471066 Genomic DNA. Translation: EAW49602.1.
CH471066 Genomic DNA. Translation: EAW49603.1.
BC000127 mRNA. Translation: AAH00127.1.
CCDSCCDS53572.1. [P78417-2]
CCDS53573.1. [P78417-3]
CCDS7555.1. [P78417-1]
RefSeqNP_001177931.1. NM_001191002.1. [P78417-2]
NP_001177932.1. NM_001191003.1. [P78417-3]
NP_004823.1. NM_004832.2. [P78417-1]
UniGeneHs.190028.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EEMX-ray2.00A1-241[»]
3LFLX-ray2.10A/B/C1-241[»]
3VLNX-ray1.70A1-241[»]
4IS0X-ray1.72A1-241[»]
ProteinModelPortalP78417.
SMRP78417. Positions 3-241.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114836. 11 interactions.
IntActP78417. 7 interactions.
MINTMINT-1384709.
STRING9606.ENSP00000358727.

Chemistry

BindingDBP78417.
ChEMBLCHEMBL3174.
DrugBankDB00143. Glutathione.

PTM databases

PhosphoSiteP78417.

Polymorphism databases

DMDM6016173.

2D gel databases

OGPP78417.
UCD-2DPAGEP78417.

Proteomic databases

MaxQBP78417.
PaxDbP78417.
PeptideAtlasP78417.
PRIDEP78417.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000369710; ENSP00000358724; ENSG00000148834. [P78417-2]
ENST00000369713; ENSP00000358727; ENSG00000148834. [P78417-1]
ENST00000539281; ENSP00000441488; ENSG00000148834. [P78417-3]
GeneID9446.
KEGGhsa:9446.
UCSCuc001kya.3. human. [P78417-1]

Organism-specific databases

CTD9446.
GeneCardsGC10P106004.
HGNCHGNC:13312. GSTO1.
HPAHPA037603.
HPA037604.
MIM605482. gene.
neXtProtNX_P78417.
PharmGKBPA133787054.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0625.
HOGENOMHOG000006560.
HOVERGENHBG051853.
InParanoidP78417.
KOK00799.
OMAHKAYLDS.
OrthoDBEOG71CFNG.
PhylomeDBP78417.
TreeFamTF105325.

Enzyme and pathway databases

BioCycMetaCyc:HS07564-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.

Gene expression databases

ArrayExpressP78417.
BgeeP78417.
CleanExHS_GSTO1.
GenevestigatorP78417.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR005442. GST_omega.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF13417. GST_N_3. 1 hit.
[Graphical view]
PRINTSPR01625. GSTRNSFRASEO.
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGSTO1. human.
EvolutionaryTraceP78417.
GeneWikiGSTO1.
GenomeRNAi9446.
NextBio35384.
PROP78417.
SOURCESearch...

Entry information

Entry nameGSTO1_HUMAN
AccessionPrimary (citable) accession number: P78417
Secondary accession number(s): D3DRA3 expand/collapse secondary AC list , F5H7H0, Q5TA03, Q7Z3T2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM