Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P16083 (NQO2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 153. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribosyldihydronicotinamide dehydrogenase [quinone]

EC=1.10.99.2
Alternative name(s):
NRH dehydrogenase [quinone] 2
NRH:quinone oxidoreductase 2
Quinone reductase 2
Short name=QR2
Gene names
Name:NQO2
Synonyms:NMOR2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length231 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis. Ref.18

Catalytic activity

1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide + a quinone = 1-(beta-D-ribofuranosyl)nicotinamide + a hydroquinone. Ref.19

Cofactor

Binds 1 zinc ion per subunit.

FAD.

Enzyme regulation

Inhibited by melatonin, resveratrol and 5-hydroxytryptamine. Ref.18

Subunit structure

Homodimer. Ref.18

Subcellular location

Cytoplasm.

Miscellaneous

Uses dihydronicotinamide riboside (NRH) rather than NAD(P)H as an electron donor.

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

KM=28 µM for NRH Ref.9 Ref.12

KM=11.6 µM for menadione

KM=252 µM for NADH

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 231231Ribosyldihydronicotinamide dehydrogenase [quinone]
PRO_0000071626

Regions

Nucleotide binding18 – 214FAD
Nucleotide binding104 – 1074FAD
Nucleotide binding148 – 1514FAD
Region127 – 1293Substrate binding

Sites

Metal binding1741Zinc
Metal binding1781Zinc
Metal binding2231Zinc
Binding site121FAD
Binding site1561FAD
Binding site1941FAD
Binding site2011FAD

Amino acid modifications

Modified residue801Phosphoserine Ref.13
Modified residue1971Phosphoserine Ref.13

Natural variations

Natural variant161K → R. Ref.4
Corresponds to variant rs28383623 [ dbSNP | Ensembl ].
VAR_021399
Natural variant291E → G. Ref.4
Corresponds to variant rs17136117 [ dbSNP | Ensembl ].
VAR_021400
Natural variant471L → F. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.7 Ref.8
Corresponds to variant rs1143684 [ dbSNP | Ensembl ].
VAR_021401
Natural variant581G → D. Ref.4
Corresponds to variant rs17300141 [ dbSNP | Ensembl ].
VAR_021402
Natural variant1841V → A. Ref.4
Corresponds to variant rs28383651 [ dbSNP | Ensembl ].
VAR_021403

Experimental info

Mutagenesis1621N → H: Loss of activity toward CB1954, no effect toward menadione. Ref.17
Sequence conflict1401G → C in AAB60642. Ref.2

Secondary structure

................................................ 231
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P16083 [UniParc].

Last modified January 11, 2011. Version 5.
Checksum: FE1F4D577517B972

FASTA23125,919
        10         20         30         40         50         60 
MAGKKVLIVY AHQEPKSFNG SLKNVAVDEL SRQGCTVTVS DLYAMNLEPR ATDKDITGTL 

        70         80         90        100        110        120 
SNPEVFNYGV ETHEAYKQRS LASDITDEQK KVREADLVIF QFPLYWFSVP AILKGWMDRV 

       130        140        150        160        170        180 
LCQGFAFDIP GFYDSGLLQG KLALLSVTTG GTAEMYTKTG VNGDSRYFLW PLQHGTLHFC 

       190        200        210        220        230 
GFKVLAPQIS FAPEIASEEE RKGMVAAWSQ RLQTIWKEEP IPCTAHWHFG Q 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide and deduced amino acid sequence of a human cDNA (NQO2) corresponding to a second member of the NAD(P)H:quinone oxidoreductase gene family. Extensive polymorphism at the NQO2 gene locus on chromosome 6."
Jaiswal A.K., Burnett P., Adesnik M., McBride O.W.
Biochemistry 29:1899-1906(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PHE-47.
Tissue: Liver.
[2]"Human NAD(P)H:quinone oxidoreductase 2. Gene structure, activity, and tissue-specific expression."
Jaiswal A.K.
J. Biol. Chem. 269:14502-14508(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PHE-47.
Tissue: Liver.
[3]"Human NRH:quinone oxidoreductase 2, complete genomic sequence."
Iida A., Osawa S., Kitamura Y., Kitamoto T., Koyama K., Nakamura Y.
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PHE-47.
[4]NIEHS SNPs program
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-16; GLY-29; PHE-47; ASP-58 AND ALA-184.
[5]"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], VARIANT PHE-47.
Tissue: Cerebellum.
[6]"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. expand/collapse author list , 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.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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], VARIANT PHE-47.
[8]"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], VARIANT PHE-47.
Tissue: Brain.
[9]"Catalytic properties of NAD(P)H:quinone oxidoreductase-2 (NQO2), a dihydronicotinamide riboside dependent oxidoreductase."
Wu K., Knox R., Sun X.Z., Joseph P., Jaiswal A.K., Zhang D., Deng P.S.-K., Chen S.
Arch. Biochem. Biophys. 347:221-228(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES.
[10]"Unexpected genetic and structural relationships of a long-forgotten flavoenzyme to NAD(P)H:quinone reductase (DT-diaphorase)."
Zhao Q., Yang X.L., Holtzclaw W.D., Talalay P.
Proc. Natl. Acad. Sci. U.S.A. 94:1669-1674(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[11]Erratum
Zhao Q., Yang X.L., Holtzclaw W.D., Talalay P.
Proc. Natl. Acad. Sci. U.S.A. 94:5979-5979(1997)
[12]"Kinetic mechanism of quinone oxidoreductase 2 and its inhibition by the antimalarial quinolines."
Kwiek J.J., Haystead T.A.J., Rudolph J.
Biochemistry 43:4538-4547(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
[13]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-197, 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]"Crystal structure of human quinone reductase type 2, a metalloflavoprotein."
Foster C.E., Bianchet M.A., Talalay P., Zhao Q., Amzel L.M.
Biochemistry 38:9881-9886(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[16]"Crystal structure of quinone reductase 2 in complex with resveratrol."
Buryanovskyy L., Fu Y., Boyd M., Ma Y., Hsieh T.-C., Wu J.M., Zhang Z.
Biochemistry 43:11417-11426(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH RESVERATROL.
[17]"Crystal structure of quinone reductase 2 in complex with cancer prodrug CB1954."
Fu Y., Buryanovskyy L., Zhang Z.
Biochem. Biophys. Res. Commun. 336:332-338(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH CB1954, MUTAGENESIS OF ASN-162.
[18]"Kinetic, thermodynamic and X-ray structural insights into the interaction of melatonin and analogues with quinone reductase 2."
Calamini B., Santarsiero B.D., Boutin J.A., Mesecar A.D.
Biochem. J. 413:81-91(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH MELATONIN AND FAD, FUNCTION, SUBUNIT, ENZYME REGULATION.
[19]"Quinone reductase 2 is a catechol quinone reductase."
Fu Y., Buryanovskyy L., Zhang Z.
J. Biol. Chem. 283:23829-23835(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH DOPAMINE AND ADRENOCHROME, ENZYME ACTIVITY.
[20]"The structure of the leukemia drug imatinib bound to human quinone reductase 2 (NQO2)."
Winger J.A., Hantschel O., Superti-Furga G., Kuriyan J.
BMC Struct. Biol. 9:7-7(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH ZINC IONS; FAD AND IMATINIB.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02888 mRNA. Translation: AAA60239.1.
AY299456 Genomic DNA. Translation: AAB60642.3.
AB050248 Genomic DNA. Translation: BAB16974.1.
AY855291 Genomic DNA. Translation: AAW29945.1.
AK311746 mRNA. Translation: BAG34689.1.
AL133351 Genomic DNA. Translation: CAI23294.1.
CH471087 Genomic DNA. Translation: EAW55107.1.
BC006096 mRNA. Translation: AAH06096.1.
PIRA32667.
RefSeqNP_000895.2. NM_000904.3.
XP_005249204.1. XM_005249147.2.
XP_005249205.1. XM_005249148.2.
XP_005249206.1. XM_005249149.2.
XP_005249207.1. XM_005249150.2.
XP_005249208.1. XM_005249151.2.
UniGeneHs.145597.
Hs.533050.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QR2X-ray2.10A/B2-231[»]
1SG0X-ray1.50A/B2-231[»]
1XI2X-ray1.50A/B2-231[»]
1ZX1X-ray2.16A/B1-231[»]
2BZSX-ray2.00A/B2-230[»]
2QMYX-ray2.50A/B2-231[»]
2QMZX-ray2.10A/B2-231[»]
2QR2X-ray2.45A/B2-231[»]
2QWXX-ray1.50A/B1-231[»]
2QX4X-ray1.65A/B2-231[»]
2QX6X-ray1.75A/B2-231[»]
2QX8X-ray1.60A/B2-231[»]
2QX9X-ray2.31A/B2-231[»]
3FW1X-ray1.75A1-231[»]
3G5MX-ray1.84A/B1-231[»]
3GAMX-ray1.98A/B1-231[»]
3NFRX-ray1.57A/B2-231[»]
3NHFX-ray2.00A/B2-231[»]
3NHJX-ray2.33A/B2-231[»]
3NHKX-ray1.96A/B2-231[»]
3NHLX-ray1.57A/B2-231[»]
3NHPX-ray1.70A/B2-231[»]
3NHRX-ray1.80A/B2-231[»]
3NHSX-ray1.78A/B2-231[»]
3NHUX-ray1.90A/B2-231[»]
3NHWX-ray1.65A/B2-231[»]
3NHYX-ray1.90A/B2-231[»]
3O2NX-ray1.60A/B2-231[»]
3O73X-ray2.00A/B1-231[»]
3OVMX-ray2.09A/B1-231[»]
3OWHX-ray2.28A/B1-231[»]
3OWXX-ray1.85A/B1-231[»]
3OX1X-ray2.00A/B1-231[»]
3OX2X-ray2.41A/B1-231[»]
3OX3X-ray1.80A/B1-231[»]
3TE7X-ray1.70A/B3-230[»]
3TEMX-ray1.45A/B3-230[»]
3TZBX-ray2.19A/B/C/D3-230[»]
3UXEX-ray1.50A/B2-231[»]
3UXHX-ray1.53A/B2-231[»]
4FGJX-ray1.35A/B1-231[»]
4FGKX-ray1.40A/B1-231[»]
4FGLX-ray1.20A/B/C/D1-231[»]
4GQIX-ray1.95A/B2-231[»]
4GR9X-ray2.29A/B2-231[»]
DisProtDP00727.
ProteinModelPortalP16083.
SMRP16083. Positions 1-231.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110898. 8 interactions.
IntActP16083. 7 interactions.
MINTMINT-1133243.
STRING9606.ENSP00000337773.

Chemistry

BindingDBP16083.
ChEMBLCHEMBL3959.
DrugBankDB00170. Menadione.
DB00157. NADH.

PTM databases

PhosphoSiteP16083.

Polymorphism databases

DMDM317373581.

Proteomic databases

PaxDbP16083.
PRIDEP16083.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000338130; ENSP00000337773; ENSG00000124588.
ENST00000380430; ENSP00000369795; ENSG00000124588.
ENST00000380455; ENSP00000369822; ENSG00000124588.
GeneID4835.
KEGGhsa:4835.
UCSCuc003mus.2. human.

Organism-specific databases

CTD4835.
GeneCardsGC06P003006.
H-InvDBHIX0018967.
HGNCHGNC:7856. NQO2.
HPAHPA021283.
HPA021332.
MIM160998. gene.
neXtProtNX_P16083.
PharmGKBPA31745.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2249.
HOGENOMHOG000149970.
HOVERGENHBG029104.
InParanoidP16083.
KOK08071.
OMAEPKSFNG.
PhylomeDBP16083.
TreeFamTF300296.

Enzyme and pathway databases

BRENDA1.10.99.2. 2681.
SABIO-RKP16083.

Gene expression databases

ArrayExpressP16083.
BgeeP16083.
CleanExHS_NQO2.
GenevestigatorP16083.

Family and domain databases

InterProIPR003680. Flavodoxin_fold.
[Graphical view]
PfamPF02525. Flavodoxin_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP16083.
GeneWikiNAD(P)H_dehydrogenase,_quinone_2.
GenomeRNAi4835.
NextBio18630.
PROP16083.
SOURCESearch...

Entry information

Entry nameNQO2_HUMAN
AccessionPrimary (citable) accession number: P16083
Secondary accession number(s): B2R492, Q5TD04
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 11, 2011
Last modified: April 16, 2014
This is version 153 of the entry and version 5 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 6

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