P10632 (CP2C8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cytochrome P450 2C8
EC=1.14.14.1

Alternative name(s):
CYPIIC8
Cytochrome P450 IIC2
Cytochrome P450 MP-12
Cytochrome P450 MP-20
Cytochrome P450 form 1
S-mephenytoin 4-hydroxylase

Gene names

Name:

CYP2C8

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. In the epoxidation of arachidonic acid it generates only 14,15- and 11,12-cis-epoxyeicosatrienoic acids. It is the principal enzyme responsible for the metabolism the anti-cancer drug paclitaxel (taxol). Ref.10
Catalytic activity	RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O. Ref.10
Cofactor	Heme group.
Subcellular location	Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Induction	By phenobarbital.
Sequence similarities	Belongs to the cytochrome P450 family.
Caution	Alternative splicing has been shown to occur but the shorter forms are believed to be non-functional.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Heme Iron Metal-binding
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 organic acid metabolic process Inferred from direct assay PubMed 19651758. Source: BHF-UCL oxidative demethylation Inferred from direct assay PubMed 18619574. Source: BHF-UCL xenobiotic metabolic process Traceable author statement. Source: Reactome
Cellular_component	endoplasmic reticulum membrane Traceable author statement. Source: Reactome
Molecular_function	aromatase activity Inferred from electronic annotation. Source: EC caffeine oxidase activity Inferred from direct assay PubMed 18619574. 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 monooxygenase activity Inferred from direct assay PubMed 19651758. Source: BHF-UCL
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P10632-1)

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: P10632-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-8: MEPFVVLV → MFLQPIAK
     9-110: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 490

490

Cytochrome P450 2C8

PRO_0000051699

Sites

Metal binding

435

1

Iron (heme axial ligand)

Binding site

100

1

Substrate

Binding site

204

1

Substrate

Binding site

241

1

Substrate

Natural variations

Alternative sequence

1 – 8

8

MEPFVVLV → MFLQPIAK in isoform 2.

VSP_043306

Alternative sequence

9 – 110

102

Missing in isoform 2.

VSP_043307

Natural variant

139

1

R → K in allele CYP2C8*3. Ref.4 Ref.5 Ref.12 Ref.16 Ref.17 Ref.18
Corresponds to variant rs11572080 [ dbSNP | Ensembl ].

VAR_012238

Natural variant

154

1

E → D in clone MP-12. Ref.11

VAR_001250

Natural variant

193

1

N → K in MP-20. Ref.11

VAR_001251

Natural variant

244

1

I → V. Ref.5
Corresponds to variant rs11572102 [ dbSNP | Ensembl ].

VAR_018958

Natural variant

249

1

K → R in clone MP-12. Ref.11

VAR_001252

Natural variant

264

1

I → M in allele CYP2C8*4. Ref.1 Ref.3 Ref.5 Ref.17 Ref.18
Corresponds to variant rs1058930 [ dbSNP | Ensembl ].

VAR_011754

Natural variant

269

1

I → F in allele CYP2C8*2; only found in African-Americans. Ref.5 Ref.16 Ref.17 Ref.18
Corresponds to variant rs11572103 [ dbSNP | Ensembl ].

VAR_012239

Natural variant

390

1

L → S. Ref.17

VAR_016947

Natural variant

399

1

K → R in allele CYP2C8*3. Ref.4 Ref.5 Ref.13 Ref.16 Ref.17 Ref.18
Corresponds to variant rs10509681 [ dbSNP | Ensembl ].

VAR_012240

Natural variant

411

1

H → L in clone MP-20. Ref.10 Ref.11

VAR_001253

Experimental info

Sequence conflict

54

1

F → L no nucleotide entry Ref.12

Sequence conflict

67

1

V → L no nucleotide entry Ref.12

Sequence conflict

76

1

V → C no nucleotide entry Ref.12

Sequence conflict

82

1

A → S in AAH20596. Ref.8

Sequence conflict

130

1

T → N in AAA35739. Ref.1

Sequence conflict

130

1

T → N in AAA35740. Ref.1

Sequence conflict

130

1

T → N no nucleotide entry Ref.3

Sequence conflict

209

1

N → S no nucleotide entry Ref.12

Sequence conflict

384 – 393

10

GTTIMALLTS → SFDNKIMLAA in AAA35740. Ref.1

Sequence conflict

386

1

T → A in BAF85442. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

490

Helix Strand Turn

Details...

Turn

37 – 39

3

Helix

42 – 44

3

Beta strand

47 – 49

3

Helix

50 – 61

12

Beta strand

63 – 69

7

Beta strand

72 – 77

6

Helix

80 – 87

8

Turn

88 – 94

7

Helix

101 – 107

7

Turn

111 – 113

3

Helix

117 – 130

14

Turn

133 – 136

4

Beta strand

137 – 139

3

Helix

141 – 157

17

Turn

158 – 161

4

Helix

167 – 182

16

Beta strand

183 – 185

3

Helix

192 – 208

17

Helix

212 – 218

7

Helix

220 – 225

6

Helix

227 – 252

26

Helix

263 – 273

11

Helix

284 – 298

15

Helix

300 – 315

16

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

391 – 395

5

Turn

398 – 400

3

Beta strand

401 – 403

3

Helix

409 – 412

4

Helix

431 – 433

3

Helix

438 – 455

18

Beta strand

456 – 459

4

Helix

464 – 466

3

Beta strand

472 – 479

8

Beta strand

485 – 489

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1990. Version 2. Checksum: E920EB2084F477E1	FASTA	490	55,825
	10 20 30 40 50 60 MEPFVVLVLC LSFMLLFSLW RQSCRRRKLP PGPTPLPIIG NMLQIDVKDI CKSFTNFSKV 70 80 90 100 110 120 YGPVFTVYFG MNPIVVFHGY EAVKEALIDN GEEFSGRGNS PISQRITKGL GIISSNGKRW 130 140 150 160 170 180 KEIRRFSLTT LRNFGMGKRS IEDRVQEEAH CLVEELRKTK ASPCDPTFIL GCAPCNVICS 190 200 210 220 230 240 VVFQKRFDYK DQNFLTLMKR FNENFRILNS PWIQVCNNFP LLIDCFPGTH NKVLKNVALT 250 260 270 280 290 300 RSYIREKVKE HQASLDVNNP RDFIDCFLIK MEQEKDNQKS EFNIENLVGT VADLFVAGTE 310 320 330 340 350 360 TTSTTLRYGL LLLLKHPEVT AKVQEEIDHV IGRHRSPCMQ DRSHMPYTDA VVHEIQRYSD 370 380 390 400 410 420 LVPTGVPHAV TTDTKFRNYL IPKGTTIMAL LTSVLHDDKE FPNPNIFDPG HFLDKNGNFK 430 440 450 460 470 480 KSDYFMPFSA GKRICAGEGL ARMELFLFLT TILQNFNLKS VDDLKNLNTT AVTKGIVSLP 490 PSYQICFIPV
	Isoform 2 [UniParc]. Checksum: 0A9312FD6D4B9634	FASTA	388	44,358
	10 20 30 40 50 60 MFLQPIAKGI ISSNGKRWKE IRRFSLTTLR NFGMGKRSIE DRVQEEAHCL VEELRKTKAS 70 80 90 100 110 120 PCDPTFILGC APCNVICSVV FQKRFDYKDQ NFLTLMKRFN ENFRILNSPW IQVCNNFPLL 130 140 150 160 170 180 IDCFPGTHNK VLKNVALTRS YIREKVKEHQ ASLDVNNPRD FIDCFLIKME QEKDNQKSEF 190 200 210 220 230 240 NIENLVGTVA DLFVAGTETT STTLRYGLLL LLKHPEVTAK VQEEIDHVIG RHRSPCMQDR 250 260 270 280 290 300 SHMPYTDAVV HEIQRYSDLV PTGVPHAVTT DTKFRNYLIP KGTTIMALLT SVLHDDKEFP 310 320 330 340 350 360 NPNIFDPGHF LDKNGNFKKS DYFMPFSAGK RICAGEGLAR MELFLFLTTI LQNFNLKSVD 370 380 DLKNLNTTAV TKGIVSLPPS YQICFIPV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of multiple human cytochrome P-450 1 cDNAs. The chromosomal localization of the gene and evidence for alternate RNA splicing." Okino S.T., Quattrochi L.C., Pendurthi U.R., McBride O.W., Tukey R.H. J. Biol. Chem. 262:16072-16079(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MET-264. Tissue: Liver.
[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] (ISOFORM 1). Tissue: Liver.
[3]	"Cloning and expression of complementary DNAs for multiple members of the human cytochrome P450IIC subfamily." Romkes M., Faletto M.B., Blaisdell J.A., Raucy J.L., Goldstein J.A. Biochemistry 30:3247-3255(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MET-264.
[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] (ISOFORMS 1 AND 2), VARIANTS LYS-139 AND ARG-399. Tissue: Liver and Mammary gland.
[5]	NIEHS SNPs program Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-139; VAL-244; MET-264; PHE-269 AND ARG-399.
[6]	"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].
[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. , 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].
[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] (ISOFORM 1). Tissue: Liver.
[9]	"Isolation of the human cytochrome P-450 IIC8 gene: multiple glucocorticoid responsive elements in the 5' region." Ged C., Beaune P. Biochim. Biophys. Acta 1088:433-435(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56. Tissue: Blood.
[10]	"Molecular cloning, expression and characterization of an endogenous human cytochrome P450 arachidonic acid epoxygenase isoform." Zeldin D.C., DuBois R.N., Falck J.R., Capdevila J.H. Arch. Biochem. Biophys. 322:76-86(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-15, NUCLEOTIDE SEQUENCE [MRNA] OF 6-490, FUNCTION, CATALYTIC ACTIVITY, VARIANT LEU-411. Tissue: Kidney.
[11]	"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 11-490 (ISOFORM 1), VARIANTS ASP-154; LYS-193; ARG-249 AND LEU-411. Tissue: Liver.
[12]	"Cloning, expression and chromosomal localization of a member of the human cytochrome P450IIC gene sub-family." Shephard E.A., Phillips I.R., Santisteban I., Palmer C.N., Povey S. Ann. Hum. Genet. 53:23-31(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 34-382 (ISOFORM 1), VARIANT LYS-139.
[13]	"Sequence of a human liver cytochrome P-450 cDNA clone." Kolyada A.Y. Nucleic Acids Res. 18:5550-5550(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 281-490 (ISOFORM 1), VARIANT ARG-399.
[14]	"Structure of human microsomal cytochrome P450 2C8. Evidence for a peripheral fatty acid binding site." Schoch G.A., Yano J.K., Wester M.R., Griffin K.J., Stout C.D., Johnson E.F. J. Biol. Chem. 279:9497-9503(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 28-490.
[15]	"Determinants of cytochrome P450 2C8 substrate binding: structures of complexes with montelukast, troglitazone, felodipine, and 9-cis-retinoic acid." Schoch G.A., Yano J.K., Sansen S., Dansette P.M., Stout C.D., Johnson E.F. J. Biol. Chem. 283:17227-17237(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 28-490 IN COMPLEX WITH INHIBITORS, SUBSTRATE-BINDING SITES.
[16]	"Polymorphisms in human CYP2C8 decrease metabolism of the anticancer drug paclitaxel and arachidonic acid." Dai D., Zeldin D.C., Blaisdell J.A., Chanas B., Coulter S.J., Ghanayem B.I., Goldstein J.A. Pharmacogenetics 11:597-607(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS LYS-139; PHE-269 AND ARG-399.
[17]	"CYP2C8 polymorphisms in Caucasians and their relationship with paclitaxel 6alpha-hydroxylase activity in human liver microsomes." Bahadur N., Leathart J.B., Mutch E., Steimel-Crespi D., Dunn S.A., Gilissen R., Houdt J.V., Hendrickx J., Mannens G., Bohets H., Williams F.M., Armstrong M., Crespi C.L., Daly A.K. Biochem. Pharmacol. 64:1579-1589(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS LYS-139; MET-264; PHE-269; SER-390 AND ARG-399.
[18]	"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 LYS-139; MET-264; PHE-269 AND ARG-399.
+	Additional computationally mapped references.

Web resources

Cytochrome P450 Allele Nomenclature Committee

CYP2C8 alleles

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M17397 mRNA. Translation: AAA35739.1.
M17398 mRNA. Translation: AAA35740.1.
Y00498 mRNA. Translation: CAA68550.1.
AK292753 mRNA. Translation: BAF85442.1.
AK293328 mRNA. Translation: BAH11492.1.
AK315823 mRNA. Translation: BAF98714.1.
AY514490 Genomic DNA. Translation: AAR89907.1.
AL359672 Genomic DNA. Translation: CAH71307.1.
CH471066 Genomic DNA. Translation: EAW50018.1.
BC020596 mRNA. Translation: AAH20596.1.
X54807 Genomic DNA. Translation: CAA38578.1.
M21941 mRNA. Translation: AAA52160.1.
M21942 mRNA. Translation: AAA52161.1.
X51535 mRNA. Translation: CAA35915.1.

IPI

IPI00290301.

PIR

A29782.

RefSeq

NP_000761.3. NM_000770.3.
NP_001185782.1. NM_001198853.1.
NP_001185783.1. NM_001198854.1.
NP_001185784.1. NM_001198855.1.

UniGene

Hs.709188.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PQ2	X-ray	2.70	A/B	28-490	[»]
2NNH	X-ray	2.60	A/B	28-490	[»]
2NNI	X-ray	2.80	A	28-490	[»]
2NNJ	X-ray	2.28	A	28-490	[»]
2VN0	X-ray	2.70	A	28-490	[»]

ProteinModelPortal

P10632.

ModBase

Search...

Protein-protein interaction databases

IntAct

P10632. 9 interactions.

STRING

9606.ENSP00000360317.

PTM databases

PhosphoSite

P10632.

Polymorphism databases

DMDM

117225.

Proteomic databases

PaxDb

P10632.

PRIDE

P10632.

Protocols and materials databases

DNASU

1558.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000371270; ENSP00000360317; ENSG00000138115.
ENST00000535898; ENSP00000445062; ENSG00000138115.

GeneID

1558.

KEGG

hsa:1558.

UCSC

uc001kkb.3. human.

Organism-specific databases

CTD

1558.

GeneCards

GC10M096786.

HGNC

HGNC:2622. CYP2C8.

HPA

HPA013547.
HPA013970.
HPA015066.

MIM

601129. gene.

neXtProt

NX_P10632.

PharmGKB

PA125.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2124.

HOGENOM

HOG000036992.

HOVERGEN

HBG015789.

InParanoid

P10632.

KO

K07413.

OMA

MLQIDIK.

OrthoDB

EOG48WC22.

PhylomeDB

P10632.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

SABIO-RK

P10632.

Gene expression databases

ArrayExpress

P10632.

Bgee

P10632.

CleanEx

HS_CYP2C8.

Genevestigator

P10632.

GermOnline

ENSG00000138115. 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

P10632.

ChEMBL

CHEMBL3721.

ChiTaRS

CYP2C8. human.

DrugBank

DB01424. Aminophenazone.
DB01118. Amiodarone.
DB00613. Amodiaquine.
DB00865. Benzphetamine.
DB00564. Carbamazepine.
DB00439. Cerivastatin.
DB00586. Diclofenac.
DB01095. Fluvastatin.
DB01320. Fosphenytoin.
DB01241. Gemfibrozil.
DB01026. Ketoconazole.
DB01259. Lapatinib.
DB00227. Lovastatin.
DB00683. Midazolam.
DB00471. Montelukast.
DB00622. Nicardipine.
DB01229. Paclitaxel.
DB00252. Phenytoin.
DB01132. Pioglitazone.
DB00912. Repaglinide.
DB01045. Rifampin.
DB00412. Rosiglitazone.
DB00641. Simvastatin.
DB01261. Sitagliptin.
DB01124. Tolbutamide.
DB00214. Torasemide.
DB00755. Tretinoin.
DB00440. Trimethoprim.
DB00682. Warfarin.
DB00549. Zafirlukast.
DB01198. Zopiclone.

EvolutionaryTrace

P10632.

GenomeRNAi

1558.

NextBio

6434.

SOURCE

Search...

Entry information

Entry name

CP2C8_HUMAN

Accession

Primary (citable) accession number: P10632
Secondary accession number(s): A8K9N8 , B0AZN2, B7Z1F6, Q5VX93, Q8WWB1, Q9UCZ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	November 1, 1990
Last modified:	May 1, 2013
This is version 153 of the entry and version 2 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.