P11712 (CP2C9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	490 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Endoplasmic reticulum Membrane Microsome
Coding sequence diversity	Polymorphism
Ligand	Heme Iron Metal-binding NADP
Molecular function	Monooxygenase Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	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 oxidative demethylation Inferred from direct assay PubMed 18619574. Source: BHF-UCL 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_component	endoplasmic reticulum membrane Traceable author statement. Source: Reactome
Molecular_function	(R)-limonene 6-monooxygenase activity Inferred from electronic annotation. Source: EC (S)-limonene 6-monooxygenase activity Inferred from electronic annotation. Source: EC (S)-limonene 7-monooxygenase activity Inferred from electronic annotation. Source: EC caffeine oxidase activity Inferred from direct assay PubMed 18619574. Source: BHF-UCL drug binding Inferred from direct assay PubMed 19448135. Source: BHF-UCL electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro steroid hydroxylase activity Inferred from mutant phenotype PubMed 18356043. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 490

490

Cytochrome P450 2C9

PRO_0000051700

Sites

Metal binding

435

1

Iron (heme axial ligand)

Natural variations

Natural variant

19

1

L → I in allele CYP2C9*7.

VAR_018862

Natural variant

144

1

R → 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 variant

150

1

R → H in allele CYP2C9*8. Ref.3 Ref.24
Corresponds to variant rs7900194 [ dbSNP | Ensembl ].

VAR_018863

Natural variant

251

1

H → R in allele CYP2C9*9. Ref.3 Ref.24
Corresponds to variant rs2256871 [ dbSNP | Ensembl ].

VAR_018864

Natural variant

272

1

E → G in allele CYP2C9*10. Ref.3
Corresponds to variant rs9332130 [ dbSNP | Ensembl ].

VAR_018865

Natural variant

335

1

R → W in allele CYP2C9*11. Ref.23 Ref.24
Corresponds to variant rs28371685 [ dbSNP | Ensembl ].

VAR_018866

Natural variant

358

1

Y → C. Ref.9 Ref.10 Ref.20
Corresponds to variant rs1057909 [ dbSNP | Ensembl ].

VAR_008344

Natural variant

359

1

I → 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 variant

359

1

I → T in allele CYP2C9*4. Ref.21
Corresponds to variant rs56165452 [ dbSNP | Ensembl ].

VAR_013515

Natural variant

360

1

D → 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 variant

413

1

L → P. Ref.24
Corresponds to variant rs28371687 [ dbSNP | Ensembl ].

VAR_024717

Natural variant

417

1

G → D. Ref.9 Ref.10 Ref.20

VAR_008346

Natural variant

489

1

P → S in allele CYP2C9*12. Ref.3
Corresponds to variant rs9332239 [ dbSNP | Ensembl ].

VAR_018867

Experimental info

Sequence conflict

4

1

L → I no nucleotide entry Ref.2

Sequence conflict

6

1

V → S no nucleotide entry Ref.2

Sequence conflict

14

1

L → M in AAB23864. Ref.11

Sequence conflict

175

1

C → Y no nucleotide entry Ref.1

Sequence conflict

239

1

F → L no nucleotide entry Ref.1

Secondary structure

1

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490

Helix Strand Turn

Details...

Beta strand

33 – 35

3

Turn

37 – 39

3

Helix

42 – 45

4

Helix

47 – 61

15

Beta strand

63 – 71

9

Beta strand

73 – 77

5

Helix

80 – 87

8

Turn

88 – 94

7

Turn

105 – 107

3

Beta strand

111 – 114

4

Helix

117 – 131

15

Beta strand

134 – 136

3

Helix

141 – 157

17

Turn

158 – 161

4

Helix

167 – 183

17

Helix

192 – 208

17

Helix

213 – 218

6

Helix

222 – 225

4

Helix

230 – 253

24

Helix

263 – 274

12

Beta strand

275 – 277

3

Helix

284 – 315

32

Helix

317 – 330

14

Beta strand

333 – 335

3

Helix

339 – 344

6

Helix

346 – 359

14

Beta strand

374 – 376

3

Beta strand

379 – 381

3

Beta strand

386 – 389

4

Helix

392 – 395

4

Turn

398 – 400

3

Beta strand

401 – 403

3

Helix

409 – 412

4

Beta strand

415 – 417

3

Helix

431 – 433

3

Helix

438 – 455

18

Beta strand

456 – 462

7

Helix

464 – 466

3

Beta strand

475 – 477

3

Beta strand

485 – 489

5

Sequences

	Sequence		Length	Mass (Da)
	P11712 [UniParc]. Last modified May 30, 2000. Version 3. Checksum: 4FDFC395303A4E3E	FASTA	490	55,628
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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.

Web resources

Cytochrome P450 Allele Nomenclature Committee

CYP2C9 alleles

NIEHS-SNPs

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.

IPI

IPI00007219.

PIR

B38462.
D28951.

RefSeq

NP_000762.2. NM_000771.3.

UniGene

Hs.282624.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OG2	X-ray	2.60	A/B	30-490	[»]
1OG5	X-ray	2.55	A/B	30-490	[»]
1R9O	X-ray	2.00	A	23-489	[»]

ProteinModelPortal

P11712.

ModBase

Search...

Protein-protein interaction databases

IntAct

P11712. 6 interactions.

STRING

9606.ENSP00000260682.

PTM databases

PhosphoSite

P11712.

Polymorphism databases

DMDM

6686268.

Proteomic databases

PaxDb

P11712.

PRIDE

P11712.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000260682; ENSP00000260682; ENSG00000138109.

GeneID

1559.

KEGG

hsa:1559.

UCSC

uc001kka.4. human.

Organism-specific databases

CTD

1559.

GeneCards

GC10P096688.

HGNC

HGNC:2623. CYP2C9.

HPA

CAB016123.
HPA015066.

MIM

601130. gene.

neXtProt

NX_P11712.

Orphanet

240843. 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.

PharmGKB

PA126.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2124.

HOGENOM

HOG000036992.

HOVERGEN

HBG015789.

InParanoid

P11712.

KO

K07413.

OMA

KHNQPSE.

OrthoDB

EOG48WC22.

PhylomeDB

P11712.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

SABIO-RK

P11712.

Gene expression databases

ArrayExpress

P11712.

Bgee

P11712.

CleanEx

HS_CYP2C9.

Genevestigator

P11712.

GermOnline

ENSG00000138109. Homo sapiens.

Family and domain databases

Gene3D

1.10.630.10. 1 hit.

InterPro

IPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]

Pfam

PF00067. p450. 1 hit.
[Graphical view]

PRINTS

PR00463. EP450I.
PR00385. P450.

SUPFAM

SSF48264. Cytochrome_P450. 1 hit.

PROSITE

PS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P11712.

ChEMBL

CHEMBL3397.

ChiTaRS

CYP2C9. human.

DrugBank

DB01418. 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.

EvolutionaryTrace

P11712.

GenomeRNAi

1559.

NextBio

6438.

SOURCE

Search...

Entry information

Entry name

CP2C9_HUMAN

Accession

Primary (citable) accession number: P11712
Secondary accession number(s): P11713 , Q16756, Q16872, Q5VX92

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	May 30, 2000
Last modified:	May 1, 2013
This is version 155 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.