Reviewed, UniProtKB/Swiss-Prot Q16678 (CP1B1_HUMAN)

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) [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	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. Participates in the metabolism of an as-yet-unknown biologically active molecule that is a participant in eye development.
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	Expressed in many tissues.
Induction	By polycyclic aromatic hydrocarbons (PAH) and 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD).
Polymorphism	Various CYP1B1 alleles are known. The sequence shown is that of allele CYP1B1*1.
Involvement in disease	Defects in CYP1B1 are the cause of primary congenital glaucoma type 3A (GLC3A) [MIM:231300]. GLC3A is 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. Ref.8 Ref.9 Ref.13 Ref.14 Ref.16 Ref.18 Ref.20 Ref.21 Ref.22 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.32 Ref.34 Defects in CYP1B1 are a cause of primary open angle glaucoma (POAG) [MIM:137760]. POAG is 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. Ref.20 Ref.27 Ref.34 Ref.31 Ref.33 Defects in CYP1B1 are a cause of Peters anomaly [MIM:604229]. Peters anomaly is a congenital defect of the anterior chamber of the eye.
Sequence similarities	Belongs to the cytochrome P450 family.
Biophysicochemical properties	Kinetic parameters: KM=6.0 µM for 17-beta-estradiol 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	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Traceable author statement. Source: UniProtKB visual perception Traceable author statement. 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 electronic annotation. Source: UniProtKB-KW
Molecular function	aromatase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Traceable author statement. Source: UniProtKB oxygen binding Traceable author statement. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SAE1	Q9UBE0	1	EBI-1055133,EBI-743154

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) By similarity
Natural variations
	Natural variant	28	1	S → W in POAG. Ref.33		VAR_054227
	Natural variant	48	1	R → G in allele CYP1B1*2, allele CYP1B1*5, allele CYP1B1*6 and allele CYP1B1*7. dbSNP rs10012. Ref.14 Ref.18 Ref.21 Ref.22 Ref.25 Ref.26 Ref.27 Ref.28 Ref.31 Ref.5 Ref.7 Ref.23		VAR_011752
	Natural variant	52	1	P → L		VAR_054228
	Natural variant	57	1	W → C in POAG; juvenile onset; allele CYP1B1*11. Ref.9 Ref.31		VAR_008350
	Natural variant	61	1	G → E in GLC3A and POAG; allele CYP1B1*12; reduces enzymatic activity. dbSNP rs28936700. Ref.8 Ref.9 Ref.14 Ref.21 Ref.30 Ref.32 Ref.34 Ref.33		VAR_001244
	Natural variant	68	1	Q → R: dbSNP rs9282670.		VAR_028735
	Natural variant	77	1	L → P in GLC3A. Ref.14 Ref.28		VAR_054229
	Natural variant	81	1	Y → N in POAG; adult-onset; hypomorphic allele; reduces the abundance of the enzyme. dbSNP rs9282671. Ref.27 Ref.32 Ref.34 Ref.33		VAR_028736
	Natural variant	115	1	A → P in GLC3A. Ref.28		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. dbSNP rs1056827. Ref.14 Ref.18 Ref.22 Ref.25 Ref.26 Ref.28 Ref.31 Ref.5 Ref.23 Ref.12 Ref.17		VAR_011753
	Natural variant	132	1	M → R in GLC3A. Ref.28		VAR_054231
	Natural variant	144	1	Q → H		VAR_054232
	Natural variant	144	1	Q → P in GLC3A. Ref.28		VAR_054233
	Natural variant	144	1	Q → R in GLC3A. Ref.24		VAR_054234
	Natural variant	145	1	R → W in POAG. Ref.33		VAR_054235
	Natural variant	184	1	G → S		VAR_054236
	Natural variant	189	1	A → P Associated with ocular hypertension susceptibility. Ref.33		VAR_054237
	Natural variant	192	1	D → V in GLC3A. Ref.18		VAR_054238
	Natural variant	193	1	P → L in GLC3A. Ref.21 Ref.28		VAR_054239
	Natural variant	198	1	V → I in GLC3A. dbSNP rs59472972. Ref.18		VAR_054240
	Natural variant	203	1	N → S in GLC3A; reduces enzymatic activity. Ref.34		VAR_054241
	Natural variant	206	1	S → N: dbSNP rs9341248. Ref.5		VAR_018869
	Natural variant	215	1	S → I in GLC3A. Ref.26		VAR_054242
	Natural variant	229	1	E → K in GLC3A and POAG; juvenile-onset; hypomorphic allele; reduces the abundance of the enzyme. dbSNP rs57865060. Ref.21 Ref.25 Ref.27 Ref.28 Ref.32 Ref.34 Ref.31 Ref.33		VAR_054243
	Natural variant	232	1	G → R in GLC3A and POAG; adult-onset. Ref.25 Ref.27		VAR_054244
	Natural variant	239	1	S → R in GLC3A. Ref.28		VAR_054245
	Natural variant	266	1	R → L: dbSNP rs9341250. Ref.5		VAR_018870
	Natural variant	269 – 271	3	Missing in GLC3A and POAG.		VAR_054246
	Natural variant	320	1	V → L in GLC3A. Ref.18		VAR_054247
	Natural variant	330	1	A → F in GLC3A; requires 2 nucleotide substitutions; uncertain pathogenicity. Ref.18		VAR_054248
	Natural variant	330	1	A → S Associated with ocular hypertension susceptibility. Ref.33		VAR_054249
	Natural variant	343	1	Missing in GLC3A; reduces enzymatic activity and also the abundance of the enzyme.		VAR_054250
	Natural variant	345	1	L → F in POAG. Ref.20		VAR_054251
	Natural variant	355 – 358	4	Missing in GLC3A.		VAR_054252
	Natural variant	364	1	V → M in GLC3A. Ref.16 Ref.18 Ref.26		VAR_054253
	Natural variant	365	1	G → W in GLC3A; allele CYP1B1*18. dbSNP rs55771538. Ref.9		VAR_001245
	Natural variant	368	1	R → H in GLC3A and glaucoma; digenic early-onset; this mutation may act as a modifier of MYOC mutant phenotype. dbSNP rs28936414. Ref.14 Ref.20 Ref.21 Ref.22 Ref.28 Ref.30 Ref.32 Ref.31		VAR_016034
	Natural variant	374	1	D → N in GLC3A. dbSNP rs28936413. Ref.8 Ref.14		VAR_001246
	Natural variant	379	1	P → L in allele CYP1B1*19. dbSNP rs56305281. Ref.9		VAR_008351
	Natural variant	387	1	E → K in GLC3A and POAG; allele CYP1B1*20. dbSNP rs55989760. Ref.9 Ref.13 Ref.22 Ref.25 Ref.27 Ref.32		VAR_008352
	Natural variant	388	1	A → T in GLC3A. Ref.30		VAR_054254
	Natural variant	390	1	R → C in GLC3A. Ref.28 Ref.29		VAR_054255
	Natural variant	390	1	R → H in GLC3A; allele CYP1B1*21. dbSNP rs56010818. Ref.9 Ref.27 Ref.28		VAR_008353
	Natural variant	390	1	R → S in GLC3A. Ref.14 Ref.25		VAR_054256
	Natural variant	399	1	I → S in GLC3A. Ref.25		VAR_054257
	Natural variant	409	1	V → F in POAG. Ref.33		VAR_054258
	Natural variant	422	1	V → G		VAR_054259
	Natural variant	423	1	N → Y in GLC3A and POAG; juvenile-onset. Ref.25 Ref.27		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. dbSNP rs1056836. Ref.9 Ref.14 Ref.18 Ref.20 Ref.21 Ref.22 Ref.25 Ref.26 Ref.27 Ref.28 Ref.31 Ref.5 Ref.23 Ref.12 Ref.17 Ref.10		VAR_001248
	Natural variant	437	1	P → L in GLC3A; allele CYP1B1*23. dbSNP rs56175199. Ref.9 Ref.22 Ref.28		VAR_008354
	Natural variant	441	1	D → H: dbSNP rs4986887.		VAR_028737
	Natural variant	443	1	A → G in GLC3A and POAG; allele CYP1B1*7; unproven pathogenicity. dbSNP rs4986888. Ref.22 Ref.27 Ref.33 Ref.23		VAR_018774
	Natural variant	444	1	R → Q in GLC3A. Ref.18		VAR_054261
	Natural variant	445	1	F → C in GLC3A. Ref.24		VAR_054262
	Natural variant	449	1	D → E: dbSNP rs1056837.		VAR_028738
	Natural variant	453	1	N → S in allele CYP1B1*4. dbSNP rs1800440. Ref.14 Ref.22 Ref.25 Ref.26 Ref.27 Ref.28 Ref.31 Ref.5 Ref.23 Ref.10 Ref.4		VAR_008355
	Natural variant	466	1	G → D in GLC3A. Ref.28		VAR_054263
	Natural variant	469	1	R → W in GLC3A; allele CYP1B1*25. dbSNP rs28936701. Ref.8 Ref.9 Ref.14 Ref.32		VAR_001247
	Natural variant	499	1	E → G in GLC3A. Ref.18		VAR_054264
	Natural variant	515	1	S → L in POAG; uncertain pathogenicity. Ref.31		VAR_054265
	Natural variant	518	1	V → A		VAR_054266
	Natural variant	523	1	R → T in POAG; juvenile-onset. Ref.31		VAR_054267
	Natural variant	530	1	D → G in POAG. Ref.31		VAR_054268

Sequences

	Sequence		Length	Mass (Da)
	Q16678-1 [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

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[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: 8175734] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 8910454] [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: 15489334] [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]	"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: 9463332] [Abstract] Cited for: VARIANTS GLC3A GLU-61; ASN-374 AND TRP-469.
[9]	"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: 9497261] [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.
[10]	"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: 9823305] [Abstract] Cited for: VARIANTS VAL-432 AND SER-453.
[11]	Erratum Bailey L.R., Roodi N., Dupont W.D., Parl F.F. Cancer Res. 59:1388-1388(1999)
[12]	"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: 10426814] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, CHARACTERIZATION OF VARIANTS SER-119 AND VAL-432.
[13]	"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: 10227395] [Abstract] Cited for: VARIANT GLC3A LYS-387.
[14]	"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: 10655546] [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.
[15]	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)
[16]	"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: 11184479] [Abstract] Cited for: VARIANT GLC3A MET-364.
[17]	"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: 10739169] [Abstract] Cited for: VARIANTS SER-119 AND VAL-432, ASSOCIATION WITH BREAST OR LUNG CANCER.
[18]	"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: 11527932] [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.
[19]	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)
[20]	"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: 11774072] [Abstract] Cited for: VARIANT POAG PHE-345, VARIANT GLC3A HIS-368, VARIANT VAL-432.
[21]	"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: 11980847] [Abstract] Cited for: VARIANTS GLC3A GLU-61; LEU-193; LYS-229 AND HIS-368, VARIANTS GLY-48; SER-184 AND VAL-432.
[22]	"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: 12036985] [Abstract] Cited for: VARIANTS GLC3A HIS-368; LYS-387; LEU-437 AND GLY-443, VARIANTS GLY-48; SER-119; VAL-432 AND SER-453.
[23]	"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: 11854439] [Abstract] Cited for: VARIANTS GLY-48; SER-119; VAL-432; GLY-443 AND SER-453.
[24]	"Gene symbol: CYP1B1. Disease: glaucoma, primary congenital." Chakrabarti S., Komatireddy S., Mandal A.K., Balasubramanian D. Hum. Genet. 113:556-556(2003) [PubMed: 14640115] [Abstract] Cited for: VARIANTS GLC3A ARG-144 AND CYS-445.
[25]	"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: 14635112] [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.
[26]	"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: 12525557] [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.
[27]	"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: 15342693] [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.
[28]	"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: 15475877] [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.
[29]	"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: 15255109] [Abstract] Cited for: VARIANT GLC3A CYS-390.
[30]	"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: 16490498] [Abstract] Cited for: VARIANTS GLC3A GLU-61; HIS-368 AND THR-388, VARIANT GLY-422.
[31]	"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: 16688110] [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.
[32]	"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: 16735994] [Abstract] Cited for: VARIANTS GLC3A GLU-61; ASN-81; LYS-229; LEU-343 DEL; HIS-368; LYS-387 AND TRP-469.
[33]	"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: 16862072] [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.
[34]	"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: 18470941] [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.
UniGene	Hs.154654 Hs.715731
3D structure databases
SMR	Q16678. Positions 49-515.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q16678. 1 interaction.
STRING	Q16678.
Proteomic databases
PRIDE	Q16678.
Genome annotation databases
Ensembl	ENST00000260630; ENSP00000260630; ENSG00000138061; Homo sapiens. [Genome view] ENST00000407341; ENSP00000384972; ENSG00000138061; Homo sapiens. [Genome view]
GeneID	1545.
KEGG	hsa:1545.
UCSC	uc002rqo.2. human.
Organism-specific databases
CTD	1545.
GeneCards	GC02M038206.
HGNC	HGNC:2597. CYP1B1.
HPA	CAB011705.
MIM	137760. phenotype. 231300. phenotype. 601771. gene. 604229. phenotype.
Orphanet	98976. Glaucoma, congenital. 359. Glaucoma, hereditary. 708. Peters anomaly.
PharmGKB	PA27094.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG11826.
HOGENOM	HBG749920.
HOVERGEN	Q16678.
InParanoid	Q16678.
OrthoDB	EOG9SXQZX.
Enzyme and pathway databases
BRENDA	1.14.14.1. 247.
Reactome	REACT_13433. Biological oxidations.
Gene expression databases
ArrayExpress	Q16678.
Bgee	Q16678.
CleanEx	HS_CYP1B1.
Genevestigator	Q16678.
GermOnline	ENSG00000138061. Homo sapiens.
Family and domain databases
InterPro	IPR001128. Cyt_P450. IPR017973. Cyt_P450_C. IPR017972. Cyt_P450_CS. IPR002401. Cyt_P450_E_grp-I. [Graphical view]
Gene3D	G3DSA:1.10.630.10. Cyt_P450. 1 hit.
PANTHER	PTHR19383. Cyt_P450. 1 hit.
Pfam	PF00067. p450. 1 hit. [Graphical view]
PRINTS	PR00463. EP450I. PR00385. P450.
PROSITE	PS00086. CYTOCHROME_P450. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
DrugBank	DB00655. Estrone.
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:	February 9, 2010
This is version 119 of the entry and version 2 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.