ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q9JI75


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name NQO2_MOUSE
Primary accession number Q9JI75
Secondary accession numbers None
Integrated into Swiss-Prot on November 25, 2002
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    September 2, 2008 (Entry version 54)
Name and origin of the protein
Protein name Ribosyldihydronicotinamide dehydrogenase [quinone]
Synonyms EC 1.10.99.2
NRH dehydrogenase [quinone] 2
NRH:quinone oxidoreductase 2
Quinone reductase 2
QR2
Gene name
Name: Nqo2
Synonyms: Nmor2
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
TISSUE=Kidney;
DOI=10.1016/S0378-1119(00)00221-3; PubMed=10903442 [NCBI, ExPASy, EBI, Israel, Japan]
Long D.J. II, Jaiswal A.K.;
"Mouse NRH:quinone oxidoreductase (NQO2): cloning of cDNA and gene- and tissue-specific expression.";
Gene 252:107-117(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Embryonic liver;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Thymus;
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).
Comments
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
AF252260; AAF97785.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF254081; AAF97789.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF254076; AAF97789.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF254077; AAF97789.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF254078; AAF97789.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF254079; AAF97789.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF254080; AAF97789.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK010842; BAB27217.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC027629; AAH27629.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_064678.1; -.
UniGene Mm.252210
3D structure databases
HSSP P16083; 1QR2. [HSSP ENTRY / PDB]
SMR Q9JI75; 2-231.
ModBase Q9JI75.
Organism-specific databases
MGI MGI:104513; Nqo2.
Gene expression databases
ArrayExpress Q9JI75; -.
CleanEx MM_NQO2; -.
GermOnline ENSMUSG00000046949; Mus musculus.
Family and domain databases
InterPro IPR003680; Flavodoxin_fold.
Graphical view of domain structure.
Pfam PF02525; Flavodoxin_2; 1.
Pfam graphical view of domain structure.
BLOCKS Q9JI75.
Genome annotation databases
Ensembl ENSMUSG00000046949; Mus musculus. [Contig view]
GeneID 18105; -.
KEGG mmu:18105; -.
NMPDR fig|10090.3.peg.27682; -.
Phylogenomic databases
HOVERGEN Q9JI75; -.
Other
SOURCE Nqo2; Mus musculus.
ProtoNet Q9JI75.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cytoplasm; FAD; Flavoprotein; Metal-binding; Oxidoreductase; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   231  230     Ribosyldihydronicotinamide dehydrogenase [quinone]. PRO_0000071627
METAL   174   174        Zinc (By similarity). 
METAL   178   178        Zinc (By similarity). 
METAL   223   223        Zinc (By similarity). 
Sequence information
Length: 231 AA [This is the length of the unprocessed precursor] Molecular weight: 26248 Da [This is the MW of the unprocessed precursor] CRC64: D5D9AB805C4AD9F5 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAGKKVLIVY AHQEPKSFNG SLKKVAVEEL SKQGCTVTVS DLYSMNFEPR ATRNDITGAP 

        70         80         90        100        110        120 
SNPDVFSYGI ETHEAYKKKA LTSDIFEEQR KVQEADLVIF QFPLYWFSVP AILKGWMDRV 

       130        140        150        160        170        180 
LCRGFAFDIP GFYDSGFLKG KLALLSLTTG GTAEMYTKDG VSGDFRYFLW PLQHGTLHFC 

       190        200        210        220        230 
GFKVLAPQIS FGLDVSSEEE RKVMLASWAQ RLKSIWKEEP IHCTPPWYFQ E 

Q9JI75 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

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

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by kr flag YPRC Korea Mirror sites: Australia  Brazil  Canada  China  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!