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P11712 (CP2C9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 165. 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:
Cytochrome P450 2C9

EC=1.14.13.-
Alternative name(s):
(R)-limonene 6-monooxygenase
EC=1.14.13.80
(S)-limonene 6-monooxygenase
EC=1.14.13.48
(S)-limonene 7-monooxygenase
EC=1.14.13.49
CYPIIC9
Cytochrome P-450MP
Cytochrome P450 MP-4
Cytochrome P450 MP-8
Cytochrome P450 PB-1
S-mephenytoin 4-hydroxylase
Gene names
Name:CYP2C9
Synonyms:CYP2C10
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length490 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. This enzyme contributes to the wide pharmacokinetics variability of the metabolism of drugs such as S-warfarin, diclofenac, phenytoin, tolbutamide and losartan.

Catalytic activity

+-(R)-limonene + NADPH + O2 = (+)-trans-carveol + NADP+ + H2O.

--(S)-limonene + NADPH + O2 = (-)-trans-carveol + NADP+ + H2O.

--(S)-limonene + NADPH + O2 = (-)-perillyl alcohol + NADP+ + H2O.

Cofactor

Heme group.

Subcellular location

Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.

Induction

By rifampicin.

Sequence similarities

Belongs to the cytochrome P450 family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
Microsome
   Coding sequence diversityPolymorphism
   LigandHeme
Iron
Metal-binding
NADP
   Molecular functionMonooxygenase
Oxidoreductase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processarachidonic acid metabolic process

Traceable author statement. Source: Reactome

cellular amide metabolic process

Inferred from direct assay PubMed 19651758. Source: BHF-UCL

drug catabolic process

Inferred from mutant phenotype PubMed 18356043. Source: BHF-UCL

drug metabolic process

Inferred from mutant phenotype PubMed 21127708. Source: UniProtKB

epoxygenase P450 pathway

Traceable author statement. Source: Reactome

exogenous drug catabolic process

Inferred from direct assay PubMed 18619574. Source: BHF-UCL

monocarboxylic acid metabolic process

Inferred from direct assay PubMed 19651758. Source: BHF-UCL

monoterpenoid metabolic process

Inferred from direct assay PubMed 16401082. Source: BHF-UCL

omega-hydroxylase P450 pathway

Traceable author statement. Source: Reactome

oxidation-reduction process

Inferred from direct assay PubMed 16401082PubMed 19219744. Source: BHF-UCL

oxidative demethylation

Inferred from direct assay PubMed 18619574. Source: BHF-UCL

small molecule metabolic process

Traceable author statement. Source: Reactome

steroid metabolic process

Inferred from mutant phenotype PubMed 18356043. Source: BHF-UCL

urea metabolic process

Inferred from direct assay PubMed 19029318. Source: BHF-UCL

xenobiotic metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentendoplasmic reticulum membrane

Traceable author statement. Source: Reactome

intracellular membrane-bounded organelle

Inferred from direct assay PubMed 9618440. Source: UniProtKB

   Molecular_function(R)-limonene 6-monooxygenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

(S)-limonene 6-monooxygenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

(S)-limonene 7-monooxygenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

caffeine oxidase activity

Inferred from direct assay PubMed 18619574. Source: BHF-UCL

drug binding

Inferred from direct assay PubMed 19448135. Source: BHF-UCL

heme binding

Inferred from electronic annotation. Source: InterPro

iron ion binding

Inferred from electronic annotation. Source: InterPro

monooxygenase activity

Non-traceable author statement Ref.1. Source: UniProtKB

oxidoreductase activity

Inferred from direct assay PubMed 16401082PubMed 19219744. Source: BHF-UCL

steroid hydroxylase activity

Inferred from mutant phenotype PubMed 18356043. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 490490Cytochrome P450 2C9
PRO_0000051700

Sites

Metal binding4351Iron (heme axial ligand)

Natural variations

Natural variant191L → I in allele CYP2C9*7.
VAR_018862
Natural variant1441R → C in allele CYP2C9*2. Ref.1 Ref.2 Ref.3 Ref.19 Ref.20 Ref.24
Corresponds to variant rs1799853 [ dbSNP | Ensembl ].
VAR_008343
Natural variant1501R → H in allele CYP2C9*8. Ref.3 Ref.24
Corresponds to variant rs7900194 [ dbSNP | Ensembl ].
VAR_018863
Natural variant2511H → R in allele CYP2C9*9. Ref.3 Ref.24
Corresponds to variant rs2256871 [ dbSNP | Ensembl ].
VAR_018864
Natural variant2721E → G in allele CYP2C9*10. Ref.3
Corresponds to variant rs9332130 [ dbSNP | Ensembl ].
VAR_018865
Natural variant3351R → W in allele CYP2C9*11. Ref.23 Ref.24
Corresponds to variant rs28371685 [ dbSNP | Ensembl ].
VAR_018866
Natural variant3581Y → C. Ref.9 Ref.10 Ref.20
Corresponds to variant rs1057909 [ dbSNP | Ensembl ].
VAR_008344
Natural variant3591I → L in allele CYP2C9*3; responsible for the tolbutamide poor metabolizer phenotype. Ref.3 Ref.19 Ref.20 Ref.24
Corresponds to variant rs1057910 [ dbSNP | Ensembl ].
VAR_008345
Natural variant3591I → T in allele CYP2C9*4. Ref.21
Corresponds to variant rs56165452 [ dbSNP | Ensembl ].
VAR_013515
Natural variant3601D → E in allele CYP2C9*5; increases the K(m) value for substrates tested. Ref.22 Ref.24
Corresponds to variant rs28371686 [ dbSNP | Ensembl ].
VAR_013516
Natural variant4131L → P. Ref.24
Corresponds to variant rs28371687 [ dbSNP | Ensembl ].
VAR_024717
Natural variant4171G → D. Ref.9 Ref.10 Ref.20
VAR_008346
Natural variant4891P → S in allele CYP2C9*12. Ref.3
Corresponds to variant rs9332239 [ dbSNP | Ensembl ].
VAR_018867

Experimental info

Sequence conflict41L → I no nucleotide entry Ref.2
Sequence conflict61V → S no nucleotide entry Ref.2
Sequence conflict141L → M in AAB23864. Ref.11
Sequence conflict1751C → Y no nucleotide entry Ref.1
Sequence conflict2391F → L no nucleotide entry Ref.1

Secondary structure

............................................................................ 490
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11712 [UniParc].

Last modified May 30, 2000. Version 3.
Checksum: 4FDFC395303A4E3E

FASTA49055,628
        10         20         30         40         50         60 
MDSLVVLVLC LSCLLLLSLW RQSSGRGKLP PGPTPLPVIG NILQIGIKDI SKSLTNLSKV 

        70         80         90        100        110        120 
YGPVFTLYFG LKPIVVLHGY EAVKEALIDL GEEFSGRGIF PLAERANRGF GIVFSNGKKW 

       130        140        150        160        170        180 
KEIRRFSLMT LRNFGMGKRS IEDRVQEEAR CLVEELRKTK ASPCDPTFIL GCAPCNVICS 

       190        200        210        220        230        240 
IIFHKRFDYK DQQFLNLMEK LNENIKILSS PWIQICNNFS PIIDYFPGTH NKLLKNVAFM 

       250        260        270        280        290        300 
KSYILEKVKE HQESMDMNNP QDFIDCFLMK MEKEKHNQPS EFTIESLENT AVDLFGAGTE 

       310        320        330        340        350        360 
TTSTTLRYAL LLLLKHPEVT AKVQEEIERV IGRNRSPCMQ DRSHMPYTDA VVHEVQRYID 

       370        380        390        400        410        420 
LLPTSLPHAV TCDIKFRNYL IPKGTTILIS LTSVLHDNKE FPNPEMFDPH HFLDEGGNFK 

       430        440        450        460        470        480 
KSKYFMPFSA GKRICVGEAL AGMELFLFLT SILQNFNLKS LVDPKNLDTT PVVNGFASVP 

       490 
PFYQLCFIPV 

« Hide

References

« Hide 'large scale' references
[1]"Human cytochrome P-450 PB-1: a multigene family involved in mephenytoin and steroid oxidations that maps to chromosome 10."
Meehan R.R., Gosden J.R., Rout D., Hastie N.D., Friedberg T., Adesnik M., Buckland R., van Heyningen V., Fletcher J.M., Spurr N.K., Sweeney J., Wolf C.R.
Am. J. Hum. Genet. 42:26-37(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT CYS-144.
[2]"cDNA and amino acid sequences of two members of the human P450IIC gene subfamily."
Kimura S., Pastewka J., Gelboin H.V., Gonzalez F.J.
Nucleic Acids Res. 15:10053-10054(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT CYS-144.
[3]NIEHS SNPs program
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CYS-144; HIS-150; ARG-251; GLY-272; LEU-359 AND SER-489.
[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].
Tissue: Mammary gland.
[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., 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].
[8]"Nucleotide sequence of a human liver cytochrome P-450 related to the rat male specific form."
Yasumori T., Kawano S., Nagata K., Shimada M., Yamazoe Y., Kato R.
J. Biochem. 102:1075-1082(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-490.
Tissue: Liver.
[9]"Cloning and sequence determination of a complementary DNA related to human liver microsomal cytochrome P-450 S-mephenytoin 4-hydroxylase."
Umbenhauer D.R., Martin M.V., Lloyd R.S., Guengerich F.P.
Biochemistry 26:1094-1099(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-490, VARIANTS CYS-358 AND ASP-417.
Tissue: Liver.
[10]"Characterization of cDNAs, mRNAs, and proteins related to human liver microsomal cytochrome P-450 (S)-mephenytoin 4'-hydroxylase."
Ged C., Umbenhauer D.R., Bellew T.M., Bork R.W., Srivastava P.K., Shinriki N., Lloyd R.S., Guengerich F.P.
Biochemistry 27:6929-6940(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-490, VARIANTS CYS-358 AND ASP-417.
[11]"Six-base deletion occurring in messages of human cytochrome P-450 in the CYP2C subfamily results in reduction of tolbutamide hydroxylase activity."
Ohgiya S., Komori M., Ohi H., Shiramatsu K., Shinriki N., Kamataki T.
Biochem. Int. 27:1073-1081(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-490.
[12]"Human liver microsomal cytochrome P-450 mephenytoin 4-hydroxylase, a prototype of genetic polymorphism in oxidative drug metabolism. Purification and characterization of two similar forms involved in the reaction."
Shimada T., Misono K.S., Guengerich F.P.
J. Biol. Chem. 261:909-921(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-29, CHARACTERIZATION.
[13]"Cytochrome P-450 in human liver microsomes: high-performance liquid chromatographic isolation of three forms and their characterization."
Komori M., Hashizume T., Ohi H., Miura T., Kitada M., Nagashima K., Kamataki T.
J. Biochem. 104:912-916(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-25.
[14]"Separation of human liver microsomal tolbutamide hydroxylase and (S)-mephenytoin 4'-hydroxylase cytochrome P-450 enzymes."
Srivastava P.K., Yun C.H., Beaune P.H., Ged C., Guengerich F.P.
Mol. Pharmacol. 40:69-79(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
[15]"Allelic variants of human cytochrome P450 2C9: baculovirus-mediated expression, purification, structural characterization, substrate stereoselectivity, and prochiral selectivity of the wild-type and I359L mutant forms."
Haining R.L., Hunter A.P., Veronese M.E., Trager W.F., Rettie A.E.
Arch. Biochem. Biophys. 333:447-458(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-9; 21-157; 169-249; 264-424; 426-476 AND 484-487.
[16]"Expression of modified cytochrome P450 2C10 (2C9) in Escherichia coli, purification, and reconstitution of catalytic activity."
Sandhu P., Baba T., Guengerich F.P.
Arch. Biochem. Biophys. 306:443-450(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-20.
[17]"Metabolism of (+)- and (-)-limonenes to respective carveols and perillyl alcohols by CYP2C9 and CYP2C19 in human liver microsomes."
Miyazawa M., Shindo M., Shimada T.
Drug Metab. Dispos. 30:602-607(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[18]"Crystal structure of human cytochrome P450 2C9 with bound warfarin."
Williams P.A., Cosme J., Ward A., Angove H.C., Matak-Vinkovic D., Jhoti H.
Nature 424:464-468(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 30-490.
[19]"Genetic analysis of the human cytochrome P450 CYP2C9 locus."
Stubbins M.J., Harries L.W., Smith G., Tarbit M.H., Wolf C.R.
Pharmacogenetics 6:429-439(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CYP2C9*2 CYS-144 AND CYP2C9*3 LEU-359.
[20]"Allelic and functional variability of cytochrome P4502C9."
Bhasker C.R., Miners J.O., Coulter S., Birkett D.J.
Pharmacogenetics 7:51-58(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CYP2C9*2 CYS-144; CYS-358; CYP2C9*3 LEU-359 AND ASP-417.
[21]"Polymorphism of the cytochrome P450 (CYP) 2C9 gene in Japanese epileptic patients: genetic analysis of the CYP2C9 locus."
Imai J., Ieiri I., Mamiya K., Miyahara S., Furuumi H., Nanba E., Yamane M., Fukumaki Y., Ninomiya H., Tashiro N., Otsubo K., Higuchi S.
Pharmacogenetics 10:85-89(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CYP2C9*4 THR-359.
[22]"Identification and functional characterization of a new CYP2C9 variant (CYP2C9*5) expressed among African Americans."
Dickmann L.J., Rettie A.E., Kneller M.B., Kim R.B., Wood A.J., Stein C.M., Wilkinson G.R., Schwarz U.I.
Mol. Pharmacol. 60:382-387(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CYP2C9*5 GLU-360.
[23]"Association between CYP2C9 genetic variants and anticoagulation-related outcomes during warfarin therapy."
Higashi M.K., Veenstra D.L., Kondo L.M., Wittkowsky A.K., Srinouanprachanh S.L., Farin F.M., Rettie A.E.
JAMA 287:1690-1698(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CYP2C9*11 TRP-335.
[24]"Genetic variation in eleven phase I drug metabolism genes in an ethnically diverse population."
Solus J.F., Arietta B.J., Harris J.R., Sexton D.P., Steward J.Q., McMunn C., Ihrie P., Mehall J.M., Edwards T.L., Dawson E.P.
Pharmacogenomics 5:895-931(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CYS-144; HIS-150; ARG-251; TRP-335; LEU-359; GLU-360 AND PRO-413.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY341248 Genomic DNA. Translation: AAP88931.1.
AY702706 Genomic DNA. Translation: AAT94065.1.
AK289420 mRNA. Translation: BAF82109.1.
AL359672 Genomic DNA. Translation: CAH71303.1.
CH471066 Genomic DNA. Translation: EAW50020.1.
BC125054 mRNA. Translation: AAI25055.1.
D00173 mRNA. Translation: BAA00123.1.
M15331 mRNA. Translation: AAA52157.1.
M21939 mRNA. Translation: AAA52158.1.
M21940 mRNA. Translation: AAA52159.1.
S46963 mRNA. Translation: AAB23864.2. Sequence problems.
CCDSCCDS7437.1.
PIRB38462.
D28951.
RefSeqNP_000762.2. NM_000771.3.
UniGeneHs.282624.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OG2X-ray2.60A/B30-490[»]
1OG5X-ray2.55A/B30-490[»]
1R9OX-ray2.00A18-490[»]
ProteinModelPortalP11712.
SMRP11712. Positions 44-490.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107937. 9 interactions.
IntActP11712. 6 interactions.
STRING9606.ENSP00000260682.

Chemistry

BindingDBP11712.
ChEMBLCHEMBL3397.
DrugBankDB01418. Acenocoumarol.
DB00969. Alosetron.
DB01118. Amiodarone.
DB00025. Antihemophilic Factor.
DB00673. Aprepitant.
DB00559. Bosentan.
DB00821. Carprofen.
DB01136. Carvedilol.
DB00482. Celecoxib.
DB01242. Clomipramine.
DB00250. Dapsone.
DB00705. Delavirdine.
DB00967. Desloratadine.
DB00304. Desogestrel.
DB00586. Diclofenac.
DB00736. Esomeprazole.
DB00749. Etodolac.
DB00196. Fluconazole.
DB00472. Fluoxetine.
DB00712. Flurbiprofen.
DB01095. Fluvastatin.
DB00176. Fluvoxamine.
DB00983. Formoterol.
DB01241. Gemfibrozil.
DB01381. Ginkgo biloba.
DB01016. Glibenclamide.
DB00222. Glimepiride.
DB01067. Glipizide.
DB01018. Guanfacine.
DB00327. Hydromorphone.
DB01050. Ibuprofen.
DB00458. Imipramine.
DB01029. Irbesartan.
DB01026. Ketoconazole.
DB00448. Lansoprazole.
DB00678. Losartan.
DB01283. Lumiracoxib.
DB00470. Marinol.
DB00784. Mefenamic acid.
DB00814. Meloxicam.
DB00532. Mephenytoin.
DB00916. Metronidazole.
DB01110. Miconazole.
DB00683. Midazolam.
DB00471. Montelukast.
DB00731. Nateglinide.
DB00220. Nelfinavir.
DB00622. Nicardipine.
DB01192. Oxymorphone.
DB00213. Pantoprazole.
DB00617. Paramethadione.
DB00946. Phenprocoumon.
DB00252. Phenytoin.
DB00175. Pravastatin.
DB00908. Quinidine.
DB00503. Ritonavir.
DB00412. Rosiglitazone.
DB01104. Sertraline.
DB00203. Sildenafil.
DB01015. Sulfamethoxazole.
DB00870. Suprofen.
DB00675. Tamoxifen.
DB00469. Tenoxicam.
DB00342. Terfenadine.
DB01124. Tolbutamide.
DB00214. Torasemide.
DB01361. Troleandomycin.
DB00580. Valdecoxib.
DB00177. Valsartan.
DB00582. Voriconazole.
DB00682. Warfarin.
DB00549. Zafirlukast.
DB00744. Zileuton.

PTM databases

PhosphoSiteP11712.

Polymorphism databases

DMDM6686268.

Proteomic databases

PaxDbP11712.
PRIDEP11712.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000260682; ENSP00000260682; ENSG00000138109.
GeneID1559.
KEGGhsa:1559.
UCSCuc001kka.4. human.

Organism-specific databases

CTD1559.
GeneCardsGC10P096688.
HGNCHGNC:2623. CYP2C9.
HPACAB016123.
HPA015066.
MIM601130. gene.
neXtProtNX_P11712.
Orphanet240843. Acenocoumarol toxicity.
240859. Carbutamide toxicity.
240873. Fluindione toxicity.
240875. Glibenclamide toxicity.
240877. Gliclazide toxicity.
240879. Glimepiride toxicity.
240881. Glipizide toxicity.
240897. Phenprocoumon toxicity.
240991. Susceptibility to bleeding due to acenocoumarol treatment.
240993. Susceptibility to bleeding due to fluindione treatment.
240995. Susceptibility to bleeding due to phenprocoumon treatment.
240997. Susceptibility to bleeding due to warfarine treatment.
241007. Susceptibility to hypoglycemia due to carbutamide treatment.
241009. Susceptibility to hypoglycemia due to glibenclamide treatment.
241011. Susceptibility to hypoglycemia due to gliclazide treatment.
241013. Susceptibility to hypoglycemia due to glimepiride treatment.
241015. Susceptibility to hypoglycemia due to glipizide treatment.
241045. Warfarine dose selection in the treatment of venous thrombosis and atrial fibrillation.
240923. Warfarine toxicity.
PharmGKBPA126.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2124.
HOGENOMHOG000036992.
HOVERGENHBG015789.
InParanoidP11712.
KOK17719.
OMANVAFMKS.
OrthoDBEOG7RBZ85.
PhylomeDBP11712.
TreeFamTF352043.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
SABIO-RKP11712.

Gene expression databases

ArrayExpressP11712.
BgeeP11712.
CleanExHS_CYP2C9.
GenevestigatorP11712.

Family and domain databases

Gene3D1.10.630.10. 1 hit.
InterProIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00463. EP450I.
PR00385. P450.
SUPFAMSSF48264. SSF48264. 1 hit.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCYP2C9. human.
EvolutionaryTraceP11712.
GeneWikiCYP2C9.
GenomeRNAi1559.
NextBio6438.
PROP11712.
SOURCESearch...

Entry information

Entry nameCP2C9_HUMAN
AccessionPrimary (citable) accession number: P11712
Secondary accession number(s): P11713 expand/collapse secondary AC list , Q16756, Q16872, Q5VX92
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: May 30, 2000
Last modified: July 9, 2014
This is version 165 of the entry and version 3 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