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P15559 (NQO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 158. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NAD(P)H dehydrogenase [quinone] 1

EC=1.6.5.2
Alternative name(s):
Azoreductase
DT-diaphorase
Short name=DTD
Menadione reductase
NAD(P)H:quinone oxidoreductase 1
Phylloquinone reductase
Quinone reductase 1
Short name=QR1
Gene names
Name:NQO1
Synonyms:DIA4, NMOR1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length274 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinons involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis.

Catalytic activity

NAD(P)H + a quinone = NAD(P)+ + a hydroquinone.

Cofactor

FAD.

Enzyme regulation

Inhibited by dicoumarol.

Subunit structure

Homodimer. Ref.9 Ref.12

Subcellular location

Cytoplasm.

Induction

By dioxin.

Polymorphism

The Ser-187 polymorphism may be linked to susceptibility to forms of cancers.

Miscellaneous

Quinone reductase accepts electrons from both NADH and NADPH with equal efficiency.

Sequence similarities

Belongs to the NAD(P)H dehydrogenase (quinone) family.

Mass spectrometry

Molecular mass is 30864±6 Da from positions 2 - 274. Determined by ESI. Ref.11

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandFAD
Flavoprotein
NAD
NADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Inferred from electronic annotation. Source: Ensembl

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

negative regulation of catalytic activity

Inferred from electronic annotation. Source: Ensembl

nitric oxide biosynthetic process

Traceable author statement PubMed 9579781. Source: ProtInc

positive regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

regulation of cellular amino acid metabolic process

Traceable author statement. Source: Reactome

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to nutrient

Inferred from electronic annotation. Source: Ensembl

response to toxic substance

Traceable author statement PubMed 10393963. Source: ProtInc

small molecule metabolic process

Traceable author statement. Source: Reactome

synaptic transmission, cholinergic

Traceable author statement PubMed 9579781. Source: ProtInc

xenobiotic metabolic process

Traceable author statement PubMed 10393963. Source: ProtInc

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionNAD(P)H dehydrogenase (quinone) activity

Traceable author statement PubMed 10393963. Source: ProtInc

cytochrome-b5 reductase activity, acting on NAD(P)H

Traceable author statement PubMed 9579781. Source: ProtInc

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 18388957PubMed 21042282. Source: IntAct

superoxide dismutase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ING1Q9UK533EBI-3989435,EBI-399198
Tp63O88898-22EBI-3989435,EBI-2338228From a different organism.
Tp63O88898-62EBI-3989435,EBI-2338244From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P15559-1)

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: P15559-2)

The sequence of this isoform differs from the canonical sequence as follows:
     140-173: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P15559-3)

The sequence of this isoform differs from the canonical sequence as follows:
     102-139: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 274273NAD(P)H dehydrogenase [quinone] 1
PRO_0000071622

Regions

Nucleotide binding18 – 192FAD
Nucleotide binding104 – 1074FAD
Nucleotide binding148 – 1514FAD
Region126 – 1283Substrate binding

Sites

Binding site121FAD
Binding site671FAD
Binding site1561FAD
Binding site2011FAD

Natural variations

Alternative sequence102 – 13938Missing in isoform 3.
VSP_044446
Alternative sequence140 – 17334Missing in isoform 2.
VSP_042716
Natural variant1391R → W.
Corresponds to variant rs1131341 [ dbSNP | Ensembl ].
VAR_016170
Natural variant1871P → S Lack of activity. Ref.3 Ref.4 Ref.14 Ref.15
Corresponds to variant rs1800566 [ dbSNP | Ensembl ].
VAR_008384
Natural variant2691Q → H.
Corresponds to variant rs34447156 [ dbSNP | Ensembl ].
VAR_050220

Experimental info

Sequence conflict2521F → S in BAG60289. Ref.4

Secondary structure

............................................................. 274
Helix Strand Turn

Details...

Sequences

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

Last modified April 1, 1990. Version 1.
Checksum: A4010462AD00F3FE

FASTA27430,868
        10         20         30         40         50         60 
MVGRRALIVL AHSERTSFNY AMKEAAAAAL KKKGWEVVES DLYAMNFNPI ISRKDITGKL 

        70         80         90        100        110        120 
KDPANFQYPA ESVLAYKEGH LSPDIVAEQK KLEAADLVIF QFPLQWFGVP AILKGWFERV 

       130        140        150        160        170        180 
FIGEFAYTYA AMYDKGPFRS KKAVLSITTG GSGSMYSLQG IHGDMNVILW PIQSGILHFC 

       190        200        210        220        230        240 
GFQVLEPQLT YSIGHTPADA RIQILEGWKK RLENIWDETP LYFAPSSLFD LNFQAGFLMK 

       250        260        270 
KEVQDEEKNK KFGLSVGHHL GKSIPTDNQI KARK 

« Hide

Isoform 2 [UniParc].

Checksum: 63EF4B34E6394793
Show »

FASTA24027,295
Isoform 3 [UniParc].

Checksum: 8BF801EAD71D02AB
Show »

FASTA23626,365

References

« Hide 'large scale' references
[1]"Human dioxin-inducible cytosolic NAD(P)H:menadione oxidoreductase. cDNA sequence and localization of gene to chromosome 16."
Jaiswal A.K., McBride O.W., Adesnik M., Nebert D.W.
J. Biol. Chem. 263:13572-13578(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Liver.
[2]"Human NAD(P)H:quinone oxidoreductase (NQO1) gene structure and induction by dioxin."
Jaiswal A.K.
Biochemistry 30:10647-10653(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]NIEHS SNPs program
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-187.
[4]"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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), VARIANT SER-187.
Tissue: Amygdala.
[5]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(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 (JUL-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: Colon.
[8]"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].
[9]"Crystal structure of human DT-diaphorase: a model for interaction with the cytotoxic prodrug 5-(aziridin-1-yl)-2,4-dinitrobenzamide (CB1954)."
Skelly J.V., Sanderson M.R., Suter D.A., Baumann U., Read M.A., Gregory D.S.J., Bennett M., Hobbs S.M., Neidle S.
J. Med. Chem. 42:4325-4330(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 4-274 IN COMPLEX WITH FAD, SUBUNIT.
[10]"Structures of recombinant human and mouse NAD(P)H:quinone oxidoreductases: species comparison and structural changes with substrate binding and release."
Faig M., Bianchet M.A., Talalay P., Chen S., Winski S., Ross D., Amzel L.M.
Proc. Natl. Acad. Sci. U.S.A. 97:3177-3182(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH FAD AND DUROQUINONE.
[11]"Characterization of a mechanism-based inhibitor of NAD(P)H:quinone oxidoreductase 1 by biochemical, X-ray crystallographic, and mass spectrometric approaches."
Winski S.L., Faig M., Bianchet M.A., Siegel D., Swann E., Fung K., Duncan M.W., Moody C.J., Amzel L.M., Ross D.
Biochemistry 40:15135-15142(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH FAD AND THE INHIBITOR ES936, MASS SPECTROMETRY.
[12]"Structure-based development of anticancer drugs: complexes of NAD(P)H:quinone oxidoreductase 1 with chemotherapeutic quinones."
Faig M., Bianchet M.A., Winski S., Hargreaves R., Moody C.J., Hudnott A.R., Ross D., Amzel L.M.
Structure 9:659-667(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEXES WITH FAD AND INHIBITORS, SUBUNIT.
[13]"The crystal structure of NAD(P)H quinone oxidoreductase 1 in complex with its potent inhibitor dicoumarol."
Asher G., Dym O., Tsvetkov P., Adler J., Shaul Y.
Biochemistry 45:6372-6378(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR DICOUMAROL.
[14]"NAD(P)H:quinone oxidoreductase gene expression in human colon carcinoma cells: characterization of a mutation which modulates DT-diaphorase activity and mitomycin sensitivity."
Traver R.D., Horikoshi T., Danenberg K.D., Stadlbauer T.H., Danenberg P.V., Ross D., Gibson N.W.
Cancer Res. 52:797-802(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SER-187.
[15]"No linkage of P187S polymorphism in NAD(P)H: quinone oxidoreductase (NQO1/DIA4) and type 1 diabetes in the Danish population."
Kristiansen O.P., Larsen Z.M., Johannesen J., Nerup J., Mandrup-Poulsen T., Pociot F.
Hum. Mutat. 14:67-70(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SER-187.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03934 mRNA. Translation: AAA59940.1.
M81600 expand/collapse EMBL AC list , M81596, M81597, M81598, M81599 Genomic DNA. Translation: AAB60701.1.
AY281093 Genomic DNA. Translation: AAP20940.1. Sequence problems.
AK297979 mRNA. Translation: BAG60289.1.
AK312368 mRNA. Translation: BAG35286.1.
AK316246 mRNA. Translation: BAH14617.1.
AC092115 Genomic DNA. No translation available.
CH471092 Genomic DNA. Translation: EAW83283.1.
CH471092 Genomic DNA. Translation: EAW83284.1.
BC007659 mRNA. Translation: AAH07659.1.
CCDSCCDS10883.1. [P15559-1]
CCDS32471.1. [P15559-3]
CCDS32472.1. [P15559-2]
PIRA30879. A41135.
RefSeqNP_000894.1. NM_000903.2. [P15559-1]
NP_001020604.1. NM_001025433.1. [P15559-2]
NP_001020605.1. NM_001025434.1. [P15559-3]
UniGeneHs.406515.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D4AX-ray1.70A/B/C/D2-274[»]
1DXOX-ray2.50A/B/C/D2-274[»]
1GG5X-ray2.50A/B/C/D2-274[»]
1H66X-ray2.00A/B/C/D3-274[»]
1H69X-ray1.86A/B/C/D3-274[»]
1KBOX-ray2.30A/B/C/D2-274[»]
1KBQX-ray1.80A/B/C/D2-274[»]
1QBGX-ray2.30A/B/C/D4-274[»]
2F1OX-ray2.75A/B/C/D/E/F/G/H2-274[»]
3JSXX-ray2.45A/B/C/D/E/F/G/H2-274[»]
ProteinModelPortalP15559.
SMRP15559. Positions 2-274.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108072. 16 interactions.
DIPDIP-24210N.
IntActP15559. 3 interactions.
MINTMINT-231407.
STRING9606.ENSP00000319788.

Chemistry

BindingDBP15559.
ChEMBLCHEMBL3623.
DrugBankDB00266. Dicumarol.
DB00170. Menadione.

PTM databases

PhosphoSiteP15559.

Polymorphism databases

DMDM118607.

Proteomic databases

MaxQBP15559.
PaxDbP15559.
PRIDEP15559.

Protocols and materials databases

DNASU1728.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000320623; ENSP00000319788; ENSG00000181019. [P15559-1]
ENST00000379046; ENSP00000368334; ENSG00000181019. [P15559-3]
ENST00000379047; ENSP00000368335; ENSG00000181019. [P15559-2]
GeneID1728.
KEGGhsa:1728.
UCSCuc002exp.3. human. [P15559-1]
uc002exq.3. human. [P15559-2]
uc002exr.3. human. [P15559-3]

Organism-specific databases

CTD1728.
GeneCardsGC16M069744.
HGNCHGNC:2874. NQO1.
HPACAB012421.
HPA007308.
MIM125860. gene.
neXtProtNX_P15559.
PharmGKBPA31744.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2249.
HOGENOMHOG000149970.
HOVERGENHBG029104.
InParanoidP15559.
KOK00355.
OMAYDKGPFQ.
PhylomeDBP15559.
TreeFamTF300296.

Enzyme and pathway databases

BRENDA1.6.5.2. 2681.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP15559.
BgeeP15559.
CleanExHS_NQO1.
GenevestigatorP15559.

Family and domain databases

Gene3D3.40.50.360. 1 hit.
InterProIPR003680. Flavodoxin_fold.
IPR029039. Flavoprotein-like.
[Graphical view]
PfamPF02525. Flavodoxin_2. 1 hit.
[Graphical view]
SUPFAMSSF52218. SSF52218. 1 hit.
ProtoNetSearch...

Other

ChiTaRSNQO1. human.
EvolutionaryTraceP15559.
GeneWikiNAD(P)H_dehydrogenase_(quinone_1).
GenomeRNAi1728.
NextBio35473648.
PROP15559.
SOURCESearch...

Entry information

Entry nameNQO1_HUMAN
AccessionPrimary (citable) accession number: P15559
Secondary accession number(s): B2R5Y9 expand/collapse secondary AC list , B4DNM7, B7ZAD1, Q86UK1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: July 9, 2014
This is version 158 of the entry and version 1 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 16

Human chromosome 16: entries, gene names and cross-references to MIM