Q16678 (CP1B1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cytochrome P450 1B1
EC=1.14.14.1

Alternative name(s):
CYPIB1

Gene names

Name:

CYP1B1

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	543 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. Ref.8 Ref.14 Participates in the metabolism of an as-yet-unknown biologically active molecule that is a participant in eye development. Ref.8 Ref.14
Catalytic activity	RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O. Ref.8 Ref.14
Cofactor	Heme group. Ref.9
Enzyme regulation	Enzyme activity is increased by liposomes containing anionic phospholipids, phosphatidic acid and cardiolipin. Ref.8
Subcellular location	Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Tissue specificity	Expressed in many tissues. Ref.1
Induction	By polycyclic aromatic hydrocarbons (PAH) and 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD). Ref.1 Ref.8
Polymorphism	Various CYP1B1 alleles are known. The sequence shown is that of allele CYP1B1*1.
Involvement in disease	Primary congenital glaucoma 3A (GLC3A) [MIM:231300]: An autosomal recessive form of primary congenital glaucoma (PCG). PCG is characterized by marked increase of intraocular pressure at birth or early childhood, large ocular globes (buphthalmos) and corneal edema. It results from developmental defects of the trabecular meshwork and anterior chamber angle of the eye that prevent adequate drainage of aqueous humor. Note: The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry. Ref.10 Ref.11 Ref.15 Ref.16 Ref.18 Ref.20 Ref.23 Ref.24 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.34 Ref.36 Primary open angle glaucoma (POAG) [MIM:137760]: A complex and genetically heterogeneous ocular disorder characterized by a specific pattern of optic nerve and visual field defects. The angle of the anterior chamber of the eye is open, and usually the intraocular pressure is increased. The disease is asymptomatic until the late stages, by which time significant and irreversible optic nerve damage has already taken place. In some cases, POAG shows digenic inheritance involving mutations in CYP1B1 and MYOC genes. Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. CYP1B1 mutations have been reported to pose a significant risk for early-onset POAG and also modify glaucoma phenotype in patients who do not carry a MYOC mutation (Ref.29). Ref.22 Ref.29 Ref.33 Ref.35 Ref.36 Primary open angle glaucoma 1A (GLC1A) [MIM:137750]: A form of primary open angle glaucoma (POAG). POAG is characterized by a specific pattern of optic nerve and visual field defects. The angle of the anterior chamber of the eye is open, and usually the intraocular pressure is increased. The disease is asymptomatic until the late stages, by which time significant and irreversible optic nerve damage has already taken place. Note: The gene represented in this entry acts as a disease modifier. Digenic mutations in CYP1B1 and MYOC have been found in a family segregating both primary adult-onset and juvenile forms of open angle glaucoma (Ref.22). All affected family members with mutations in both MYOC and CYP1B1 had juvenile glaucoma, whereas those with only the MYOC mutation had the adult-onset form (Ref.22). Ref.22 Peters anomaly (PAN) [MIM:604229]: Consists of a central corneal leukoma, absence of the posterior corneal stroma and Descemet membrane, and a variable degree of iris and lenticular attachments to the central aspect of the posterior cornea. Note: The disease is caused by mutations affecting the gene represented in this entry.
Sequence similarities	Belongs to the cytochrome P450 family.
Biophysicochemical properties	Kinetic parameters: KM=6.0 µM for 17-beta-estradiol Ref.14 KM=17.0 µM for testosterone KM=24.0 µM for progesterone Vmax=14.95 nmol/min/mg enzyme for 17-beta-estradiol 4-hydroxylation Vmax=6.9 nmol/min/mg enzyme for 17-beta-estradiol 2-hydroxylation Vmax=36.16 nmol/min/mg enzyme for testosterone 6-beta-hydroxylation Vmax=9.86 nmol/min/mg enzyme for progesterone 6-beta-hydroxylation Vmax=37.80 nmol/min/mg enzyme for progesterone 16-alpha-hydroxylation

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Coding sequence diversity	Polymorphism
Disease	Disease mutation Glaucoma Peters anomaly
Ligand	Heme Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	angiogenesis Inferred from electronic annotation. Source: Compara cellular aromatic compound metabolic process Inferred from electronic annotation. Source: Compara endothelial cell migration Inferred from electronic annotation. Source: Compara endothelial cell-cell adhesion Inferred from electronic annotation. Source: Compara response to toxin Inferred from electronic annotation. Source: Compara retina vasculature development in camera-type eye Inferred from electronic annotation. Source: Compara small molecule metabolic process Traceable author statement. Source: Reactome toxin metabolic process Inferred from electronic annotation. Source: Compara visual perception Traceable author statement PubMed 9097971. Source: UniProtKB 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 electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Traceable author statement PubMed 9097971. Source: UniProtKB iron ion binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen Inferred from direct assay PubMed 10871058. Source: MGI oxygen binding Traceable author statement PubMed 9097971. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 543

543

Cytochrome P450 1B1

PRO_0000051660

Sites

Metal binding

470

1

Iron (heme axial ligand)

Natural variations

Natural variant

28

1

S → W in POAG. Ref.35

VAR_054227

Natural variant

48

1

R → G in allele CYP1B1*2, allele CYP1B1*5, allele CYP1B1*6 and allele CYP1B1*7. Ref.5 Ref.7 Ref.16 Ref.20 Ref.23 Ref.24 Ref.25 Ref.27 Ref.28 Ref.29 Ref.30 Ref.33
Corresponds to variant rs10012 [ dbSNP | Ensembl ].

VAR_011752

Natural variant

52

1

P → L. Ref.35

VAR_054228

Natural variant

57

1

W → C in POAG; juvenile onset; allele CYP1B1*11. Ref.11 Ref.33

VAR_008350

Natural variant

61

1

G → E in GLC3A and POAG; allele CYP1B1*12; reduces enzymatic activity. Ref.10 Ref.11 Ref.16 Ref.23 Ref.32 Ref.34 Ref.35 Ref.36
Corresponds to variant rs28936700 [ dbSNP | Ensembl ].

VAR_001244

Natural variant

68

1

Q → R.
Corresponds to variant rs9282670 [ dbSNP | Ensembl ].

VAR_028735

Natural variant

77

1

L → P in GLC3A. Ref.16 Ref.30

VAR_054229

Natural variant

81

1

Y → N in POAG; adult-onset; hypomorphic allele; reduces the abundance of the enzyme. Ref.29 Ref.34 Ref.35 Ref.36
Corresponds to variant rs9282671 [ dbSNP | Ensembl ].

VAR_028736

Natural variant

115

1

A → P in GLC3A. Ref.30

VAR_054230

Natural variant

119

1

A → S in allele CYP1B1*2, allele CYP1B1*6 and allele CYP1B1*7; significantly associated with breast or lung cancer; no significant change in 17beta-estradiol 2- and 4-hydroxylation activities and 17beta-estradiol affinity; 1.5-fold reduction in testosterone affinity but nearly no change in testosterone 6beta-hydroxylation activity; 2-fold increase in progesterone 6beta- and 16alpha-hydroxylation activities and 5-fold reduction in progesterone affinity. Ref.5 Ref.14 Ref.16 Ref.19 Ref.20 Ref.24 Ref.25 Ref.27 Ref.28 Ref.30 Ref.33
Corresponds to variant rs1056827 [ dbSNP | Ensembl ].

VAR_011753

Natural variant

132

1

M → R in GLC3A. Ref.30

VAR_054231

Natural variant

144

1

Q → H. Ref.35

VAR_054232

Natural variant

144

1

Q → P in GLC3A. Ref.30

VAR_054233

Natural variant

144

1

Q → R in GLC3A. Ref.26

VAR_054234

Natural variant

145

1

R → W in POAG. Ref.35

VAR_054235

Natural variant

184

1

G → S. Ref.23

VAR_054236

Natural variant

189

1

A → P Associated with ocular hypertension susceptibility. Ref.35

VAR_054237

Natural variant

192

1

D → V in GLC3A. Ref.20

VAR_054238

Natural variant

193

1

P → L in GLC3A. Ref.23 Ref.30

VAR_054239

Natural variant

198

1

V → I in GLC3A. Ref.20
Corresponds to variant rs59472972 [ dbSNP | Ensembl ].

VAR_054240

Natural variant

203

1

N → S in GLC3A; reduces enzymatic activity. Ref.36

VAR_054241

Natural variant

206

1

S → N. Ref.5
Corresponds to variant rs9341248 [ dbSNP | Ensembl ].

VAR_018869

Natural variant

215

1

S → I in GLC3A. Ref.28

VAR_054242

Natural variant

229

1

E → K in GLC3A and POAG; juvenile-onset; hypomorphic allele; reduces the abundance of the enzyme. Ref.23 Ref.27 Ref.29 Ref.30 Ref.33 Ref.34 Ref.35 Ref.36
Corresponds to variant rs57865060 [ dbSNP | Ensembl ].

VAR_054243

Natural variant

232

1

G → R in GLC3A and POAG; adult-onset. Ref.27 Ref.29

VAR_054244

Natural variant

239

1

S → R in GLC3A. Ref.30

VAR_054245

Natural variant

266

1

R → L. Ref.5
Corresponds to variant rs9341250 [ dbSNP | Ensembl ].

VAR_018870

Natural variant

269 – 271

3

Missing in GLC3A and POAG.

VAR_054246

Natural variant

320

1

V → L in GLC3A. Ref.20

VAR_054247

Natural variant

330

1

A → F in GLC3A; requires 2 nucleotide substitutions; uncertain pathogenicity. Ref.20

VAR_054248

Natural variant

330

1

A → S Associated with ocular hypertension susceptibility. Ref.35

VAR_054249

Natural variant

343

1

Missing in GLC3A; reduces enzymatic activity and also the abundance of the enzyme. Ref.34 Ref.36

VAR_054250

Natural variant

345

1

L → F in POAG. Ref.22

VAR_054251

Natural variant

355 – 358

4

Missing in GLC3A.

VAR_054252

Natural variant

364

1

V → M in GLC3A. Ref.18 Ref.20 Ref.28

VAR_054253

Natural variant

365

1

G → W in GLC3A; allele CYP1B1*18. Ref.11
Corresponds to variant rs55771538 [ dbSNP | Ensembl ].

VAR_001245

Natural variant

368

1

R → H in GLC3A and GLC1A; acts as GLC1A disease modifier in patients also carrying Val-399 mutation in MYOC. Ref.16 Ref.22 Ref.23 Ref.24 Ref.30 Ref.32 Ref.33 Ref.34
Corresponds to variant rs28936414 [ dbSNP | Ensembl ].

VAR_016034

Natural variant

374

1

D → N in GLC3A. Ref.10 Ref.16
Corresponds to variant rs28936413 [ dbSNP | Ensembl ].

VAR_001246

Natural variant

379

1

P → L in allele CYP1B1*19. Ref.11
Corresponds to variant rs56305281 [ dbSNP | Ensembl ].

VAR_008351

Natural variant

387

1

E → K in GLC3A and POAG; allele CYP1B1*20. Ref.11 Ref.15 Ref.24 Ref.27 Ref.29 Ref.34
Corresponds to variant rs55989760 [ dbSNP | Ensembl ].

VAR_008352

Natural variant

388

1

A → T in GLC3A. Ref.32

VAR_054254

Natural variant

390

1

R → C in GLC3A. Ref.30 Ref.31

VAR_054255

Natural variant

390

1

R → H in GLC3A; allele CYP1B1*21. Ref.11 Ref.29 Ref.30
Corresponds to variant rs56010818 [ dbSNP | Ensembl ].

VAR_008353

Natural variant

390

1

R → S in GLC3A. Ref.16 Ref.27

VAR_054256

Natural variant

399

1

I → S in GLC3A. Ref.27

VAR_054257

Natural variant

409

1

V → F in POAG. Ref.35

VAR_054258

Natural variant

422

1

V → G. Ref.32

VAR_054259

Natural variant

423

1

N → Y in GLC3A and POAG; juvenile-onset. Ref.27 Ref.29

VAR_054260

Natural variant

432

1

L → V in allele CYP1B1*3, allele CYP1B1*5, allele CYP1B1*6 and allele CYP1B1*7; 1.6-fold increase in 17beta-estradiol 4-hydroxylation activity but no change in 17beta-estradiol 2-hydroxylation activity; 2-fold reduction in testosterone 6beta-hydroxylation activity and 3-fold reduction in testosterone affinity; 6-fold and 4-fold increase in progesterone 6beta- and 16alpha-hydroxylation activity, respectively and 7-fold reduction in progesterone affinity. Ref.5 Ref.11 Ref.12 Ref.14 Ref.16 Ref.19 Ref.20 Ref.22 Ref.23 Ref.24 Ref.25 Ref.27 Ref.28 Ref.29 Ref.30 Ref.33
Corresponds to variant rs1056836 [ dbSNP | Ensembl ].

VAR_001248

Natural variant

437

1

P → L in GLC3A; allele CYP1B1*23. Ref.11 Ref.24 Ref.30
Corresponds to variant rs56175199 [ dbSNP | Ensembl ].

VAR_008354

Natural variant

441

1

D → H.
Corresponds to variant rs4986887 [ dbSNP | Ensembl ].

VAR_028737

Natural variant

443

1

A → G in GLC3A and POAG; allele CYP1B1*7; unproven pathogenicity. Ref.24 Ref.25 Ref.29 Ref.35
Corresponds to variant rs4986888 [ dbSNP | Ensembl ].

VAR_018774

Natural variant

444

1

R → Q in GLC3A. Ref.20

VAR_054261

Natural variant

445

1

F → C in GLC3A. Ref.26

VAR_054262

Natural variant

449

1

D → E.
Corresponds to variant rs1056837 [ dbSNP | Ensembl ].

VAR_028738

Natural variant

453

1

N → S in allele CYP1B1*4. Ref.4 Ref.5 Ref.12 Ref.16 Ref.24 Ref.25 Ref.27 Ref.28 Ref.29 Ref.30 Ref.33
Corresponds to variant rs1800440 [ dbSNP | Ensembl ].

VAR_008355

Natural variant

466

1

G → D in GLC3A. Ref.30

VAR_054263

Natural variant

469

1

R → W in GLC3A; allele CYP1B1*25. Ref.10 Ref.11 Ref.16 Ref.34
Corresponds to variant rs28936701 [ dbSNP | Ensembl ].

VAR_001247

Natural variant

499

1

E → G in GLC3A. Ref.20

VAR_054264

Natural variant

515

1

S → L in POAG; uncertain pathogenicity. Ref.33

VAR_054265

Natural variant

518

1

V → A. Ref.33

VAR_054266

Natural variant

523

1

R → T in POAG; juvenile-onset. Ref.33

VAR_054267

Natural variant

530

1

D → G in POAG. Ref.33

VAR_054268

Secondary structure

1

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543

Helix Strand Turn

Details...

Helix

70 – 81

12

Beta strand

83 – 89

7

Beta strand

92 – 97

6

Helix

100 – 107

8

Turn

108 – 113

6

Helix

121 – 125

5

Helix

126 – 129

4

Beta strand

132 – 135

4

Helix

139 – 154

16

Helix

162 – 183

22

Helix

184 – 188

5

Helix

194 – 209

16

Helix

219 – 224

6

Helix

228 – 235

8

Turn

241 – 243

3

Helix

245 – 249

5

Helix

253 – 282

30

Helix

292 – 304

13

Helix

317 – 319

3

Helix

320 – 348

29

Helix

350 – 363

14

Helix

372 – 377

6

Helix

379 – 392

14

Beta strand

407 – 409

3

Beta strand

412 – 414

3

Beta strand

419 – 424

6

Helix

425 – 428

4

Turn

431 – 433

3

Beta strand

435 – 439

5

Helix

442 – 445

4

Helix

454 – 457

4

Helix

473 – 490

18

Beta strand

491 – 495

5

Beta strand

505 – 513

9

Beta strand

518 – 524

7

Sequences

	Sequence		Length	Mass (Da)
	Q16678 [UniParc]. Last modified June 7, 2004. Version 2. Checksum: 46B6DA7368F63EA2	FASTA	543	60,846
	10 20 30 40 50 60 MGTSLSPNDP WPLNPLSIQQ TTLLLLLSVL ATVHVGQRLL RQRRRQLRSA PPGPFAWPLI 70 80 90 100 110 120 GNAAAVGQAA HLSFARLARR YGDVFQIRLG SCPIVVLNGE RAIHQALVQQ GSAFADRPAF 130 140 150 160 170 180 ASFRVVSGGR SMAFGHYSEH WKVQRRAAHS MMRNFFTRQP RSRQVLEGHV LSEARELVAL 190 200 210 220 230 240 LVRGSADGAF LDPRPLTVVA VANVMSAVCF GCRYSHDDPE FRELLSHNEE FGRTVGAGSL 250 260 270 280 290 300 VDVMPWLQYF PNPVRTVFRE FEQLNRNFSN FILDKFLRHC ESLRPGAAPR DMMDAFILSA 310 320 330 340 350 360 EKKAAGDSHG GGARLDLENV PATITDIFGA SQDTLSTALQ WLLLLFTRYP DVQTRVQAEL 370 380 390 400 410 420 DQVVGRDRLP CMGDQPNLPY VLAFLYEAMR FSSFVPVTIP HATTANTSVL GYHIPKDTVV 430 440 450 460 470 480 FVNQWSVNHD PLKWPNPENF DPARFLDKDG LINKDLTSRV MIFSVGKRRC IGEELSKMQL 490 500 510 520 530 540 FLFISILAHQ CDFRANPNEP AKMNFSYGLT IKPKSFKVNV TLRESMELLD SAVQNLQAKE TCQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete cDNA sequence of a human dioxin-inducible mRNA identifies a new gene subfamily of cytochrome P450 that maps to chromosome 2." Sutter T.R., Tang Y.M., Hayes C.L., Wo Y.-Y.P., Jabs E.W., Li X., Yin H., Cody C.W., Greenlee W.F. J. Biol. Chem. 269:13092-13099(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
[2]	"Isolation and characterization of the human cytochrome P450 CYP1B1 gene." Tang Y.M., Wo Y.-Y.P., Stewart J., Hawkins A.L., Griffin C.A., Sutter T.R., Greenlee W.F. J. Biol. Chem. 271:28324-28330(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Physical/genetic map of the 2p22-2p21 region on chromosome 2." Gorry M.C., Zhang Y., Marks J.J., Suppe B., Hart P.S., Cortelli J.R., Pallos D., Hart T.C. Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-453.
[5]	NIEHS SNPs program Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLY-48; SER-119; ASN-206; LEU-266; VAL-432 AND SER-453.
[6]	"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]. Tissue: Lung.
[7]	Guillemette C. Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-112, VARIANT GLY-48.
[8]	"Increase of human CYP1B1 activities by acidic phospholipids and kinetic deuterium isotope effects on CYP1B1 substrate oxidation." Jang H.H., Kim S.Y., Kang J.Y., Park S.H., Ryu S.H., Ahn T., Yun C.H. J. Biochem. 152:433-442(2012) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, FUNCTION.
[9]	"Structural characterization of the complex between alpha-naphthoflavone and human cytochrome P450 1B1." Wang A., Savas U., Stout C.D., Johnson E.F. J. Biol. Chem. 286:5736-5743(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 51-543 IN COMPLEX WITH HEME AND THE INHIBITOR ALPHA-NAPHTOFLAVONE, COFACTOR.
[10]	"Mutations in CYP1B1, the gene for cytochrome P4501B1, are the predominant cause of primary congenital glaucoma in Saudi Arabia." Bejjani B.A., Lewis R.A., Tomey K.F., Anderson K.L., Dueker D.K., Jabak M., Astle W.F., Otterud B., Leppert M., Lupski J.R. Am. J. Hum. Genet. 62:325-333(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GLC3A GLU-61; ASN-374 AND TRP-469.
[11]	"Sequence analysis and homology modeling suggest that primary congenital glaucoma on 2p21 results from mutations disrupting either the hinge region or the conserved core structures of cytochrome P4501B1." Stoilov I., Akarsu A.N., Alozie I., Child A., Barsoum-Homsy M., Turacli M.E., Or M., Lewis R.A., Ozdemir N., Brice G., Aktan S.G., Chevrette L., Coca-Prados M., Sarfarazi M. Am. J. Hum. Genet. 62:573-584(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GLC3A TRP-365, VARIANTS CYS-57; GLU-61; TRP-365; LEU-379; LYS-387; HIS-390; VAL-432; LEU-437 AND TRP-469.
[12]	"Association of cytochrome P450 1B1 (CYP1B1) polymorphism with steroid receptor status in breast cancer." Bailey L.R., Roodi N., Dupont W.D., Parl F.F. Cancer Res. 58:5038-5041(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS VAL-432 AND SER-453.
[13]	Erratum Bailey L.R., Roodi N., Dupont W.D., Parl F.F. Cancer Res. 59:1388-1388(1999)
[14]	"Catalytic properties of polymorphic human cytochrome P450 1B1 variants." Shimada T., Watanabe J., Kawajiri K., Sutter T.R., Guengerich F.P., Gillam E.M.J., Inoue K. Carcinogenesis 20:1607-1613(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, CHARACTERIZATION OF VARIANTS SER-119 AND VAL-432.
[15]	"Identification of a single ancestral CYP1B1 mutation in Slovak Gypsies (Roms) affected with primary congenital glaucoma." Plasilova M., Stoilov I., Sarfarazi M., Kadasi L., Ferakova E., Ferak V. J. Med. Genet. 36:290-294(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GLC3A LYS-387.
[16]	"Multiple CYP1B1 mutations and incomplete penetrance in an inbred population segregating primary congenital glaucoma suggest frequent de novo events and a dominant modifier locus." Bejjani B.A., Stockton D.W., Lewis R.A., Tomey K.F., Dueker D.K., Jabak M., Astle W.F., Lupski J.R. Hum. Mol. Genet. 9:367-374(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GLC3A GLU-61; PRO-77; 269-SER--PHE-271 DEL; HIS-368; ASN-374; SER-390 AND TRP-469, VARIANTS GLY-48; SER-119; VAL-432 AND SER-453.
[17]	Erratum Bejjani B.A., Stockton D.W., Lewis R.A., Tomey K.F., Dueker D.K., Jabak M., Astle W.F., Lupski J.R. Hum. Mol. Genet. 9:1141-1141(2000)
[18]	"Novel compound heterozygous mutations in the cytochrome P4501B1 gene (CYP1B1) in a Japanese patient with primary congenital glaucoma." Ohtake Y., Kubota R., Tanino T., Miyata H., Mashima Y. Ophthalmic Genet. 21:191-193(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GLC3A MET-364.
[19]	"Association of CYP1B1 genetic polymorphism with incidence to breast and lung cancer." Watanabe J., Shimada T., Gillam E.M., Ikuta T., Suemasu K., Higashi Y., Gotoh O., Kawajiri K. Pharmacogenetics 10:25-33(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS SER-119 AND VAL-432, ASSOCIATION WITH BREAST OR LUNG CANCER.
[20]	"Novel cytochrome P4501B1 (CYP1B1) gene mutations in Japanese patients with primary congenital glaucoma." Mashima Y., Suzuki Y., Sergeev Y., Ohtake Y., Tanino T., Kimura I., Miyata H., Aihara M., Tanihara H., Inatani M., Azuma N., Iwata T., Araie M. Invest. Ophthalmol. Vis. Sci. 42:2211-2216(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GLC3A VAL-192; ILE-198; LEU-320; PHE-330; MET-364; GLN-444 AND GLY-499, VARIANTS GLY-48; SER-119 AND VAL-432.
[21]	Erratum Mashima Y., Suzuki Y., Sergeev Y., Ohtake Y., Tanino T., Kimura I., Miyata H., Aihara M., Tanihara H., Inatani M., Azuma N., Iwata T., Araie M. Invest. Ophthalmol. Vis. Sci. 42:2775-2775(2001)
[22]	"Digenic inheritance of early-onset glaucoma: CYP1B1, a potential modifier gene." Vincent A.L., Billingsley G., Buys Y., Levin A.V., Priston M., Trope G., Williams-Lyn D., Heon E. Am. J. Hum. Genet. 70:448-460(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT POAG PHE-345, VARIANT GLC1A HIS-368, VARIANT VAL-432.
[23]	"Identification of novel mutations causing familial primary congenital glaucoma in Indian pedigrees." Panicker S.G., Reddy A.B.M., Mandal A.K., Ahmed N., Nagarajaram H.A., Hasnain S.E., Balasubramanian D. Invest. Ophthalmol. Vis. Sci. 43:1358-1366(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GLC3A GLU-61; LEU-193; LYS-229 AND HIS-368, VARIANTS GLY-48; SER-184 AND VAL-432.
[24]	"Molecular genetics of primary congenital glaucoma in Brazil." Stoilov I.R., Costa V.P., Vasconcellos J.P.C., Melo M.B., Betinjane A.J., Carani J.C.E., Oltrogge E.V., Sarfarazi M. Invest. Ophthalmol. Vis. Sci. 43:1820-1827(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GLC3A HIS-368; LYS-387; LEU-437 AND GLY-443, VARIANTS GLY-48; SER-119; VAL-432 AND SER-453.
[25]	"Functional analysis of six different polymorphic CYP1B1 enzyme variants found in an Ethiopian population." Aklillu E., Oscarson M., Hidestrand M., Leidvik B., Otter C., Ingelman-Sundberg M. Mol. Pharmacol. 61:586-594(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GLY-48; SER-119; VAL-432; GLY-443 AND SER-453.
[26]	"Gene symbol: CYP1B1. Disease: glaucoma, primary congenital." Chakrabarti S., Komatireddy S., Mandal A.K., Balasubramanian D. Hum. Genet. 113:556-556(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GLC3A ARG-144 AND CYS-445.
[27]	"Novel cytochrome P450 1B1 (CYP1B1) mutations in patients with primary congenital glaucoma in France." Colomb E., Kaplan J., Garchon H.-J. Hum. Mutat. 22:496-496(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GLC3A LYS-229; ARG-232; LYS-387; SER-390; SER-399 AND TYR-423, VARIANTS GLY-48; SER-119; VAL-432 AND SER-453.
[28]	"CYP1B1 gene analysis in primary congenital glaucoma in Indonesian and European patients." Sitorus R., Ardjo S.M., Lorenz B., Preising M. J. Med. Genet. 40:E9-E9(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GLC3A ILE-215; 355-ARG--ALA-358 DEL AND MET-364, VARIANTS GLY-48; SER-119; VAL-432 AND SER-453.
[29]	"CYP1B1 mutations in French patients with early-onset primary open-angle glaucoma." Melki R., Colomb E., Lefort N., Brezin A.P., Garchon H.-J. J. Med. Genet. 41:647-651(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS POAG ASN-81; LYS-229; ARG-232; SER-269--PHE-271 DEL; LYS-387; HIS-390; TYR-423 AND GLY-443, VARIANTS GLC3A ARG-232; LYS-387 AND TYR-423, VARIANTS GLY-48; SER119; VAL-432 AND SER-453.
[30]	"Mutation spectrum of the CYP1B1 gene in Indian primary congenital glaucoma patients." Reddy A.B.M., Kaur K., Mandal A.K., Panicker S.G., Thomas R., Hasnain S.E., Balasubramanian D., Chakrabarti S. Mol. Vis. 10:696-702(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GLC3A PRO-77; PRO-115; ARG-132; PRO-144; LEU-193; LYS-229; ARG-239; HIS-368; HIS-390; CYS-390; LEU-437 AND ASP-466, VARIANTS GLY-48; SER-119; VAL-432 AND SER-453.
[31]	"Cytochrome P4501B1 mutations cause only part of primary congenital glaucoma in Ecuador." Curry S.M., Daou A.G., Hermanns P., Molinari A., Lewis R.A., Bejjani B.A. Ophthalmic Genet. 25:3-9(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GLC3A CYS-390.
[32]	"Molecular and clinical evaluation of primary congenital glaucoma in Kuwait." Alfadhli S., Behbehani A., Elshafey A., Abdelmoaty S., Al-Awadi S. Am. J. Ophthalmol. 141:512-516(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GLC3A GLU-61; HIS-368 AND THR-388, VARIANT GLY-422.
[33]	"Primary role of CYP1B1 in Indian juvenile-onset POAG patients." Acharya M., Mookherjee S., Bhattacharjee A., Bandyopadhyay A.K., Daulat Thakur S.K., Bhaduri G., Sen A., Ray K. Mol. Vis. 12:399-404(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS POAG CYS-57; LYS-229; HIS-368; LEU-515; THR-523 AND GLY-530, VARIANTS GLY-48; SER-119; VAL-432; SER-453 AND ALA-518.
[34]	"Primary congenital glaucoma and Rieger's anomaly: extended haplotypes reveal founder effects for eight distinct CYP1B1 mutations." Chavarria-Soley G., Michels-Rautenstrauss K., Pasutto F., Flikier D., Flikier P., Cirak S., Bejjani B., Winters D.L., Lewis R.A., Mardin C., Reis A., Rautenstrauss B. Mol. Vis. 12:523-531(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GLC3A GLU-61; ASN-81; LYS-229; LEU-343 DEL; HIS-368; LYS-387 AND TRP-469.
[35]	"Heterozygous CYP1B1 gene mutations in Spanish patients with primary open-angle glaucoma." Lopez-Garrido M.-P., Sanchez-Sanchez F., Lopez-Martinez F., Aroca-Aguilar J.-D., Blanco-Marchite C., Coca-Prados M., Escribano J. Mol. Vis. 12:748-755(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS POAG TRP-28; GLU-61; ASN-81; TRP-145; LYS-229; PHE-409 AND GLY-443, VARIANTS LEU-52; HIS-144; PRO-189 AND SER-330.
[36]	"Mutations in CYP1B1 cause primary congenital glaucoma by reduction of either activity or abundance of the enzyme." Chavarria-Soley G., Sticht H., Aklillu E., Ingelman-Sundberg M., Pasutto F., Reis A., Rautenstrauss B. Hum. Mutat. 29:1147-1153(2008) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS GLC3A GLU-61; SER-203; LYS-229 AND LEU-343 DEL, CHARACTERIZATION OF VARIANT POAG ASN-81.
+	Additional computationally mapped references.

Web resources

Cytochrome P450 Allele Nomenclature Committee

CYP1B1 alleles

GeneReviews

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U03688 mRNA. Translation: AAA19567.1.
U56438 Genomic DNA. Translation: AAC50809.1.
AF450132, AF450131 Genomic DNA. Translation: AAM50512.1.
BT019979 mRNA. Translation: AAV38782.1.
AY393998 Genomic DNA. Translation: AAQ87875.1.
BC012049 mRNA. Translation: AAH12049.1.
AF171066 Genomic DNA. Translation: AAG43404.1.

IPI

IPI00003451.

PIR

A54116.

RefSeq

NP_000095.2. NM_000104.3.

UniGene

Hs.154654.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3PM0	X-ray	2.70	A	51-543	[»]

ProteinModelPortal

Q16678.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q16678. 1 interaction.

STRING

9606.ENSP00000260630.

PTM databases

PhosphoSite

Q16678.

Polymorphism databases

DMDM

48429256.

Proteomic databases

PaxDb

Q16678.

PRIDE

Q16678.

Protocols and materials databases

DNASU

1545.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000260630; ENSP00000260630; ENSG00000138061.
ENST00000407341; ENSP00000384972; ENSG00000138061.

GeneID

1545.

KEGG

hsa:1545.

UCSC

uc002rqo.2. human.

Organism-specific databases

CTD

1545.

GeneCards

GC02M038206.

H-InvDB

HIX0001979.

HGNC

HGNC:2597. CYP1B1.

HPA

CAB011705.
HPA026863.

MIM

137750. phenotype.
137760. phenotype.
231300. phenotype.
601771. gene.
604229. phenotype.

neXtProt

NX_Q16678.

Orphanet

98976. Congenital glaucoma.
98977. Juvenile glaucoma.
708. Peters anomaly.

PharmGKB

PA27094.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2124.

HOGENOM

HOG000036991.

HOVERGEN

HBG106944.

InParanoid

Q16678.

KO

K07410.

OrthoDB

EOG48WC1T.

Enzyme and pathway databases

BioCyc

MetaCyc:HS06443-MONOMER.

Reactome

REACT_111217. Metabolism.

SABIO-RK

Q16678.

Gene expression databases

ArrayExpress

Q16678.

Bgee

Q16678.

CleanEx

HS_CYP1B1.

Genevestigator

Q16678.

GermOnline

ENSG00000138061. 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

Q16678.

ChEMBL

CHEMBL4878.

DrugBank

DB00655. Estrone.

EvolutionaryTrace

Q16678.

GenomeRNAi

1545.

NextBio

6395.

SOURCE

Search...

Entry information

Entry name

CP1B1_HUMAN

Accession

Primary (citable) accession number: Q16678
Secondary accession number(s): Q5TZW8, Q93089, Q9H316

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	June 7, 2004
Last modified:	May 1, 2013
This is version 151 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.