Reviewed, UniProtKB/Swiss-Prot P05177 (CP1A2_HUMAN)

Names and origin

Protein names

Recommended name:
    Cytochrome P450 1A2
    EC=1.14.14.1
Alternative name(s):
    CYPIA2
    Cytochrome P450-P3
    Cytochrome P(3)450
    Cytochrome P450 4

Gene names

Name:

CYP1A2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	515 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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. Most active in catalyzing 2-hydroxylation. Caffeine is metabolized primarily by cytochrome CYP1A2 in the liver through an initial N3-demethylation. Also acts in the metabolism of aflatoxin B1 and acetaminophen. Participates in the bioactivation of carcinogenic aromatic and heterocyclic amines. Catalizes the N-hydroxylation of heterocyclic amines and the O-deethylation of phenacetin. Ref.11
Catalytic activity	RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O.
Cofactor	Heme group By similarity.
Subcellular location	Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Tissue specificity	Liver.
Induction	By nicotine, omeprazole, phenobarbital, primidone and rifampicin.
Polymorphism	The CYP1A2*1F allele which is quite common (40 to 50%) is due to a substitution of a base in the non-coding region of the CYP1A2 gene and has the effect of decreasing the enzyme inducibility. Individuals who are homozygous for the CYP1A2*1F allele are 'slow' caffeine metabolizers. Thus for these individual increased intake of caffeine seems to be associated with a concommitant increase in the risk of non-fatal myocardial infraction (MI).
Sequence similarities	Belongs to the cytochrome P450 family.
Biophysicochemical properties	Kinetic parameters: KM=4 µM for 2-amino-6-methyldipyrido[1,2-a:3',2'-d]imidazole KM=21 µM for 2-amino-3-methylimidazo[4,5-f]quinoline KM=26 µM for 2-amino-2,4-dimethylimidazo[4,5-f]quinoline KM=27 µM for 2-amino-3,8-dimethylimidazo[4,5-f]quinoxaline KM=71 µM for 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine KM=25 µM for phenacetin

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Heme Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	alkaloid metabolic process Inferred from direct assay. Source: UniProtKB drug catabolic process Inferred from mutant phenotype. Source: UniProtKB monocarboxylic acid metabolic process Inferred from direct assay. Source: UniProtKB monoterpenoid metabolic process Inferred from direct assay. Source: UniProtKB oxidation reduction Inferred from direct assay. Source: UniProtKB steroid catabolic process Inferred from mutant phenotype. Source: UniProtKB toxin biosynthetic process Inferred from direct assay. Source: UniProtKB
Cellular component	endoplasmic reticulum membrane Inferred from Experiment. Source: Reactome extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell microsome Inferred from direct assay. Source: UniProtKB
Molecular function	aromatase activity Inferred from electronic annotation. Source: EC demethylase activity Inferred from direct assay. Source: UniProtKB electron carrier activity Traceable author statement. Source: UniProtKB heme binding Inferred from electronic annotation. Source: InterPro oxygen binding Inferred from Experiment. Source: Reactome
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: P05177-1)

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: P05177-2)

The sequence of this isoform differs from the canonical sequence as follows:
     510-510: R → RL

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.9

Chain

2 – 515

514

Cytochrome P450 1A2

PRO_0000051651

Sites

Metal binding

458

1

Iron (heme axial ligand) By similarity

Amino acid modifications

Modified residue

289

1

N6-acetyllysine By similarity

Natural variations

Alternative sequence

510

1

R → RL in isoform 2.

VSP_017123

Natural variant

18

1

S → C: dbSNP rs17861152. Ref.15 Ref.17

VAR_023196

Natural variant

21

1

F → L in allele CYP1A2*2. dbSNP rs56160784. Ref.12

VAR_008349

Natural variant

42

1

P → R in allele CYP1A2*15. Ref.16

VAR_025182

Natural variant

73

1

G → R: dbSNP rs45565238. Ref.7

VAR_025183

Natural variant

83

1

T → M in allele CYP1A2*9. Ref.14

VAR_020848

Natural variant

104

1

D → N: dbSNP rs34067076. Ref.7

VAR_025184

Natural variant

111

1

L → F: dbSNP rs45442197. Ref.7

VAR_025185

Natural variant

168

1

E → Q in allele CYP1A2*10. Ref.14

VAR_020849

Natural variant

186

1

F → L in allele CYP1A2*11; drastic reduction in O-deethylation of phenacetin and 7-ethoxyresorufin; has a Vmax of approximately 5% of that of the wild-type and 5-fold lower Km value. Ref.14

VAR_020850

Natural variant

205

1

F → V: dbSNP rs45540640. Ref.7

VAR_025186

Natural variant

212

1

S → C in allele CYP1A2*12. Ref.14

VAR_020851

Natural variant

281

1

R → W: dbSNP rs45468096. Ref.7

VAR_025187

Natural variant

298

1

S → R: dbSNP rs17861157. Ref.15

VAR_024709

Natural variant

299

1

G → S in allele CYP1A2*13. dbSNP rs35796837. Ref.14

VAR_020852

Natural variant

314

1

I → V: dbSNP rs28399418. Ref.15 Ref.5

VAR_024710

Natural variant

348

1

D → N in allele CYP1A2*3; increases N-hydroxylation activity of heterocyclic amines; reduces phenacetin O-deethylation activity. dbSNP rs56276455. Ref.11 Ref.13

VAR_020793

Natural variant

377

1

R → Q in allele CYP1A2*16. Ref.16

VAR_025188

Natural variant

386

1

I → F in allele CYP1A2*4; increases catalytic efficiency of N-hydroxylation towards some heterocyclic amines and reduces towards others; reduces catalytic efficiency of phenacetin O-deethylation due to a high decrease in the affinity for phenacetin. Ref.11 Ref.13

VAR_020794

Natural variant

406

1

C → Y in allele CYP1A2*5; increases N-hydroxylation activity of heterocyclic amines; reduces catalytic efficiency of phenacetin O-deethylation. dbSNP rs55889066. Ref.11 Ref.13

VAR_020795

Natural variant

431

1

R → W in allele CYP1A2*6; not detected when expressed in heterologous system as it may be critical for maintenance of protein tertiary structure. dbSNP rs28399424. Ref.11 Ref.15 Ref.13

VAR_020796

Natural variant

438

1

T → I in allele CYP1A2*14. dbSNP rs45486893. Ref.7 Ref.14

VAR_020853

Natural variant

456

1

R → H in allele CYP1A2*8. Ref.16

VAR_025189

Natural variant

457

1

R → W: dbSNP rs34151816.

VAR_055563

Experimental info

Sequence conflict

79

1

R → S in AAA35738. Ref.2

Sequence conflict

81

1

G → D in AAH67427. Ref.8

Sequence conflict

170

1

K → M in AAF13599. Ref.5

Sequence conflict

311

1

V → L in AAA52154. Ref.10

Sequence conflict

450 – 451

2

LF → MLV in AAA52154. Ref.10

Sequence conflict

492

1

T → I in AAF13599. Ref.5

Sequence conflict

511

1

R → LP Ref.2

Secondary structure

1

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515

Helix Strand Turn

Details...

Turn

49 – 51

3

Helix

54 – 57

4

Helix

61 – 72

12

Beta strand

74 – 80

7

Beta strand

83 – 88

6

Helix

91 – 98

8

Turn

99 – 101

3

Helix

102 – 104

3

Helix

112 – 115

4

Turn

123 – 125

3

Helix

131 – 146

16

Turn

147 – 149

3

Helix

160 – 181

22

Helix

188 – 205

18

Helix

206 – 208

3

Helix

214 – 220

7

Helix

221 – 223

3

Helix

224 – 227

4

Helix

235 – 237

3

Helix

240 – 244

5

Helix

248 – 273

26

Helix

283 – 293

11

Helix

305 – 308

4

Helix

310 – 335

26

Helix

337 – 350

14

Turn

351 – 353

3

Helix

359 – 361

3

Helix

366 – 379

14

Beta strand

394 – 396

3

Beta strand

399 – 401

3

Beta strand

406 – 410

5

Helix

411 – 416

6

Turn

418 – 420

3

Helix

429 – 432

4

Beta strand

437 – 440

4

Helix

442 – 445

4

Helix

454 – 456

3

Helix

461 – 478

18

Beta strand

480 – 482

3

Beta strand

496 – 498

3

Beta strand

507 – 510

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 23AEFEEBDF6806AB	FASTA	515	58,294
	10 20 30 40 50 60 MALSQSVPFS ATELLLASAI FCLVFWVLKG LRPRVPKGLK SPPEPWGWPL LGHVLTLGKN 70 80 90 100 110 120 PHLALSRMSQ RYGDVLQIRI GSTPVLVLSR LDTIRQALVR QGDDFKGRPD LYTSTLITDG 130 140 150 160 170 180 QSLTFSTDSG PVWAARRRLA QNALNTFSIA SDPASSSSCY LEEHVSKEAK ALISRLQELM 190 200 210 220 230 240 AGPGHFDPYN QVVVSVANVI GAMCFGQHFP ESSDEMLSLV KNTHEFVETA SSGNPLDFFP 250 260 270 280 290 300 ILRYLPNPAL QRFKAFNQRF LWFLQKTVQE HYQDFDKNSV RDITGALFKH SKKGPRASGN 310 320 330 340 350 360 LIPQEKIVNL VNDIFGAGFD TVTTAISWSL MYLVTKPEIQ RKIQKELDTV IGRERRPRLS 370 380 390 400 410 420 DRPQLPYLEA FILETFRHSS FLPFTIPHST TRDTTLNGFY IPKKCCVFVN QWQVNHDPEL 430 440 450 460 470 480 WEDPSEFRPE RFLTADGTAI NKPLSEKMML FGMGKRRCIG EVLAKWEIFL FLAILLQQLE 490 500 510 FSVPPGVKVD LTPIYGLTMK HARCEHVQAR RFSIN
	Isoform 2. Checksum: 8557AB02860C4806	FASTA	516	58,407
	10 20 30 40 50 60 MALSQSVPFS ATELLLASAI FCLVFWVLKG LRPRVPKGLK SPPEPWGWPL LGHVLTLGKN 70 80 90 100 110 120 PHLALSRMSQ RYGDVLQIRI GSTPVLVLSR LDTIRQALVR QGDDFKGRPD LYTSTLITDG 130 140 150 160 170 180 QSLTFSTDSG PVWAARRRLA QNALNTFSIA SDPASSSSCY LEEHVSKEAK ALISRLQELM 190 200 210 220 230 240 AGPGHFDPYN QVVVSVANVI GAMCFGQHFP ESSDEMLSLV KNTHEFVETA SSGNPLDFFP 250 260 270 280 290 300 ILRYLPNPAL QRFKAFNQRF LWFLQKTVQE HYQDFDKNSV RDITGALFKH SKKGPRASGN 310 320 330 340 350 360 LIPQEKIVNL VNDIFGAGFD TVTTAISWSL MYLVTKPEIQ RKIQKELDTV IGRERRPRLS 370 380 390 400 410 420 DRPQLPYLEA FILETFRHSS FLPFTIPHST TRDTTLNGFY IPKKCCVFVN QWQVNHDPEL 430 440 450 460 470 480 WEDPSEFRPE RFLTADGTAI NKPLSEKMML FGMGKRRCIG EVLAKWEIFL FLAILLQQLE 490 500 510 FSVPPGVKVD LTPIYGLTMK HARCEHVQAR LRFSIN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human P3(450): cDNA and complete amino acid sequence." Jaiswal A.K., Nebert D.W., Gonzalez F.J. Nucleic Acids Res. 14:6773-6774(1986) [PubMed: 3755823] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Human cytochrome P-450 4 mRNA and gene: part of a multigene family that contains Alu sequences in its mRNA." Quattrochi L.C., Pendurthi U.R., Okino S.T., Potenza C., Tukey R.H. Proc. Natl. Acad. Sci. U.S.A. 83:6731-6735(1986) [PubMed: 3462722] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[3]	"Human CYP1A2: sequence, gene structure, comparison with the mouse and rat orthologous gene, and differences in liver 1A2 mRNA expression." Ikeya K., Jaiswal A.K., Owens R.A., Jones J.E., Nebert D.W., Kimura S. Mol. Endocrinol. 3:1399-1408(1989) [PubMed: 2575218] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Human P(3)450: cDNA and complete protein sequence, repetitive Alu sequences in the 3' nontranslated region, and localization of gene to chromosome 15." Jaiswal A.K., Nebert D.W., McBride O.W., Gonzalez F.J. J. Exp. Pathol. 3:1-17(1987) [PubMed: 3681487] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Liver.
[5]	"Sequence of a new human cytochrome P450-1A2 cDNA." Zhuge J., Qian Y., Xie H., Yu Y. Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT VAL-314. Tissue: Liver.
[6]	"Organization of the CYP1A cluster on human chromosome 15: implications for gene regulation." Corchero J., Pimprale S., Kimura S., Gonzalez F.J. Pharmacogenetics 11:1-6(2001) [PubMed: 11207026] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]	NIEHS SNPs program Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-73; ASN-104; PHE-111; VAL-205; TRP-281 AND ILE-438.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[9]	"Identification of a human liver cytochrome P-450 homologous to the major isosafrole-inducible cytochrome P-450 in the rat." Wrighton S.A., Campanile C., Thomas P.E., Maines S.L., Watkins P.B., Parker G., Mendez-Picon G., Haniu M., Shively J.E., Levin W., Guzelian P.S. Mol. Pharmacol. 29:405-410(1986) [PubMed: 3517618] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-19.
[10]	"Cloning and isolation of human cytochrome P-450 cDNAs homologous to dioxin-inducible rabbit mRNAs encoding P-450 4 and P-450 6." Quattrochi L.C., Okino S.T., Pendurthi U.R., Tukey R.H. DNA 4:395-400(1985) [PubMed: 3000715] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 295-485. Tissue: Liver.
[11]	"Functional characterization of four allelic variants of human cytochrome P450 1A2." Zhou H., Josephy P.D., Kim D., Guengerich F.P. Arch. Biochem. Biophys. 422:23-30(2004) [PubMed: 14725854] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CHARACTERIZATION OF VARIANTS ASN-348; PHE-386; TYR-406 AND TRP-431.
[12]	"Detection of a novel cytochrome P-450 1A2 polymorphism (F21L) in Chinese." Huang J.D., Guo W.C., Lai M.D., Guo Y.L., Lambert G.H. Drug Metab. Dispos. 27:98-101(1999) [PubMed: 9884316] [Abstract] Cited for: VARIANT LEU-21.
[13]	"Five novel natural allelic variants-951A->C, 1042G->A (D348N), 1156A->T (I386F), 1217G->A (C406Y) and 1291C->T (C431Y)-of the human CYP1A2 gene in a French Caucasian population." Chevalier D., Cauffiez C., Allorge D., Lo-Guidice J.-M., Lhermitte M., Lafitte J.-J., Broly F. Hum. Mutat. 17:355-356(2001) [PubMed: 11295848] [Abstract] Cited for: VARIANTS ASN-348; PHE-386; TYR-406 AND TRP-431.
[14]	"Six novel nonsynonymous CYP1A2 gene polymorphisms: catalytic activities of the naturally occurring variant enzymes." Murayama N., Soyama A., Saito Y., Nakajima Y., Komamura K., Ueno K., Kamakura S., Kitakaze M., Kimura H., Goto Y., Saitoh O., Katoh M., Ohnuma T., Kawai M., Sugai K., Ohtsuki T., Suzuki C., Minami N., Ozawa S., Sawada J. J. Pharmacol. Exp. Ther. 308:300-306(2004) [PubMed: 14563787] [Abstract] Cited for: VARIANTS MET-83; GLN-168; LEU-186; CYS-212; SER-299 AND ILE-438.
[15]	"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: 15469410] [Abstract] Cited for: VARIANTS CYS-18; ARG-298; VAL-314 AND TRP-431.
[16]	"Single nucleotide polymorphisms and haplotypes of CYP1A2 in a Japanese population." Soyama A., Saito Y., Hanioka N., Maekawa K., Komamura K., Kamakura S., Kitakaze M., Tomoike H., Ueno K., Goto Y., Kimura H., Katoh M., Sugai K., Saitoh O., Kawai M., Ohnuma T., Ohtsuki T., Suzuki C. , Minami N., Kamatani N., Ozawa S., Sawada J. Drug Metab. Pharmacokinet. 20:24-33(2005) [PubMed: 15770072] [Abstract] Cited for: VARIANTS ARG-42; GLN-377 AND HIS-456.
[17]	"Toward the evaluation of function in genetic variability: characterizing human SNP frequencies and establishing BAC-transgenic mice carrying the human CYP1A1_CYP1A2 locus." Jiang Z., Dalton T.P., Jin L., Wang B., Tsuneoka Y., Shertzer H.G., Deka R., Nebert D.W. Hum. Mutat. 25:196-206(2005) [PubMed: 15643613] [Abstract] Cited for: VARIANT CYS-18.
[18]	"Coffee, CYP1A2 genotype, and risk of myocardial infarction." Cornelis M.C., El-Sohemy A., Kabagambe E.K., Campos H. JAMA 295:1135-1141(2006) [PubMed: 16522833] [Abstract] Cited for: EFFECT OF CAFFEINE METABOLISM ON RISKS OF MYOCARDIAL INFARCTION.
+	Additional computationally mapped references.

Web resources

Cytochrome P450 Allele Nomenclature Committee

CYP1A2 alleles

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z00036 mRNA. Translation: CAA77335.1.
M12078 mRNA. Translation: AAA52154.1.
M31667 , M31664, M31665, M31666 Genomic DNA. Translation: AAA52163.1.
L00389 , L00384, L00385, L00386, L00388, L00387 Genomic DNA. Translation: AAA35738.1.
AF182274 mRNA. Translation: AAF13599.1.
AF253322 Genomic DNA. Translation: AAK25728.1.
DQ022432 Genomic DNA. Translation: AAY26399.1.
BC067424 mRNA. Translation: AAH67424.1.
BC067425 mRNA. Translation: AAH67425.1.
BC067426 mRNA. Translation: AAH67426.1.
BC067427 mRNA. Translation: AAH67427.1.
BC067428 mRNA. Translation: AAH67428.1.
M55053 mRNA. Translation: AAA52146.1.

IPI

IPI00307246.
IPI00719591.

PIR

O4HU4. S16718.

RefSeq

NP_000752.2.

UniGene

Hs.1361

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2HI4	X-ray	1.95	A	27-514	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P05177.

PTM databases

PhosphoSite

P05177.

Proteomic databases

PRIDE

P05177.

Genome annotation databases

Ensembl

ENST00000343932; ENSP00000342007; ENSG00000140505; Homo sapiens. [Genome view]

GeneID

1544.

KEGG

hsa:1544.

UCSC

uc002ayr.1. human.

Organism-specific databases

CTD

1544.

GeneCards

GC15P072828.

H-InvDB

HIX0038087.

HGNC

HGNC:2596. CYP1A2.

HPA

CAB015446.
CAB016531.

MIM

108330. gene.
124060. gene+phenotype.

PharmGKB

PA27093.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG15606.

HOVERGEN

P05177.

InParanoid

P05177.

OMA

PESSDEM.

PhylomeDB

P05177.

Enzyme and pathway databases

BRENDA

1.14.14.1. 247.

Reactome

REACT_13433. Biological oxidations.
REACT_649. Phase 1 functionalization.

Gene expression databases

ArrayExpress

P05177.

Bgee

P05177.

CleanEx

HS_CYP1A2.

Genevestigator

P05177.

GermOnline

ENSG00000140505. Homo sapiens.

Family and domain databases

InterPro

IPR001128. Cyt_P450.
IPR017973. Cyt_P450_C.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
IPR008066. Cyt_P450_E_grp-I_CYP1.
[Graphical view]

Gene3D

G3DSA:1.10.630.10. Cyt_P450. 1 hit.

PANTHER

PTHR19383. Cyt_P450. 1 hit.
PTHR19383:SF63. Cyt_P450_E_grp-I_CYP1. 1 hit.

Pfam

PF00067. p450. 1 hit.
[Graphical view]

PRINTS

PR00463. EP450I.
PR01683. EP450ICYP1A.
PR00385. P450.

PROSITE

PS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB01418. Acenocoumarol.
DB00316. Acetaminophen.
DB00787. Aciclovir.
DB00969. Alosetron.
DB01424. Aminophenazone.
DB00321. Amitriptyline.
DB00261. Anagrelide.
DB00972. Azelastine.
DB00188. Bortezomib.
DB00201. Caffeine.
DB00262. Carmustine.
DB00475. Chlordiazepoxide.
DB00477. Chlorpromazine.
DB00356. Chlorzoxazone.
DB00501. Cimetidine.
DB01012. Cinacalcet.
DB00537. Ciprofloxacin.
DB01242. Clomipramine.
DB00257. Clotrimazole.
DB00363. Clozapine.
DB00286. Conjugated Estrogens.
DB00924. Cyclobenzaprine.
DB00851. Dacarbazine.
DB00967. Desloratadine.
DB00829. Diazepam.
DB00527. Dibucaine.
DB00586. Diclofenac.
DB00476. Duloxetine.
DB00467. Enoxacin.
DB00736. Esomeprazole.
DB00783. Estradiol.
DB00655. Estrone.
DB00544. Fluorouracil.
DB00499. Flutamide.
DB00176. Fluvoxamine.
DB00998. Frovatriptan.
DB00365. Grepafloxacin.
DB00502. Haloperidol.
DB01094. Hesperetin.
DB00458. Imipramine.
DB01026. Ketoconazole.
DB01097. Leflunomide.
DB01002. Levobupivacaine.
DB01137. Levofloxacin.
DB00281. Lidocaine.
DB00978. Lomefloxacin.
DB01065. Melatonin.
DB00532. Mephenytoin.
DB00379. Mexiletine.
DB00370. Mirtazapine.
DB01059. Norfloxacin.
DB00540. Nortriptyline.
DB01165. Ofloxacin.
DB00334. Olanzapine.
DB00904. Ondansetron.
DB00377. Palonosetron.
DB00213. Pantoprazole.
DB00487. Pefloxacin.
DB01100. Pimozide.
DB01182. Propafenone.
DB00571. Propranolol.
DB00908. Quinidine.
DB00980. Ramelteon.
DB00863. Ranitidine.
DB01367. Rasagiline.
DB01045. Rifampin.
DB00740. Riluzole.
DB00533. Rofecoxib.
DB00268. Ropinirole.
DB00296. Ropivacaine.
DB00382. Tacrine.
DB00976. Telithromycin.
DB00342. Terfenadine.
DB00277. Theophylline.
DB00730. Thiabendazole.
DB00697. Tizanidine.
DB01124. Tolbutamide.
DB00661. Verapamil.
DB00682. Warfarin.
DB00744. Zileuton.
DB00315. Zolmitriptan.

NextBio

6391.

SOURCE

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Entry information

Entry name

CP1A2_HUMAN

Accession

Primary (citable) accession number: P05177
Secondary accession number(s): Q16754 , Q6NWU5, Q9BXX7, Q9UK49

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 116 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.