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Entry version 221 (16 Oct 2019)
Sequence version 2 (07 Jun 2004)
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Protein

Cytochrome P450 1B1

Gene

CYP1B1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins (PubMed:20972997, PubMed:11555828, PubMed:12865317, PubMed:10681376, PubMed:15258110). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase) (PubMed:20972997, PubMed:11555828, PubMed:12865317, PubMed:10681376, PubMed:15258110). Exhibits catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2- and 4-hydroxy E1 and E2. Displays a predominant hydroxylase activity toward E2 at the C-4 position (PubMed:11555828, PubMed:12865317). Metabolizes testosterone and progesterone to B or D ring hydroxylated metabolites (PubMed:10426814). May act as a major enzyme for all-trans retinoic acid biosynthesis in extrahepatic tissues. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid (PubMed:10681376, PubMed:15258110). Catalyzes the epoxidation of double bonds of certain PUFA. Converts arachidonic acid toward epoxyeicosatrienoic acid (EpETrE) regioisomers, 8,9-, 11,12-, and 14,15- EpETrE, that function as lipid mediators in the vascular system (PubMed:20972997). Additionally, displays dehydratase activity toward oxygenated eicosanoids hydroperoxyeicosatetraenoates (HpETEs). This activity is independent of cytochrome P450 reductase, NADPH, and O2 (PubMed:21068195). Also involved in the oxidative metabolism of xenobiotics, particularly converting polycyclic aromatic hydrocarbons and heterocyclic aryl amines procarcinogens to DNA-damaging products (PubMed:10426814). Plays an important role in retinal vascular development. Under hyperoxic O2 conditions, promotes retinal angiogenesis and capillary morphogenesis, likely by metabolizing the oxygenated products generated during the oxidative stress. Also, contributes to oxidative homeostasis and ultrastructural organization and function of trabecular meshwork tissue through modulation of POSTN expression (By similarity).By similarity7 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

heme1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Enzyme activity is increased by liposomes containing anionic phospholipids, phosphatidic acid and cardiolipin. Inhibited by naringenin with an IC50 of 5 µM (PubMed:22888116, PubMed:22935222). Enzyme activity is increased by cytochrome b5.2 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 0.15 min(-1) for retinol, 0.77 min(-1) for retinal, 2.86 min(-1) for 7,12-dimethyltetraphene, 0.48 min(-1) for arachidonic acid.1 Publication
  1. KM=6.9 µM for 17-beta-estradiol (2-hydroxylation)1 Publication
  2. KM=5.1 µM for 17-beta-estradiol (4-hydroxylation)1 Publication
  3. KM=17.0 µM for testosterone(6-beta-hydroxylation)1 Publication
  4. KM=25.0 µM for progesterone (6-beta-hydroxylation)1 Publication
  5. KM=23.0 µM for progesterone (16-alpha-hydroxylation)1 Publication
  6. KM=18.5 µM for all-trans-retinol1 Publication
  7. KM=11 µM for all-trans retinol1 Publication
  8. KM=8.5 µM for all-trans-retinal1 Publication
  9. KM=29.8 µM for arachidonic acid1 Publication
  10. KM=212.8 µM for 7,12-dimethyltetraphene1 Publication
  1. Vmax=0.42 nmol/min/nmol enzyme for 17-beta-estradiol (2-hydroxylation)1 Publication
  2. Vmax=0.91 nmol/min/nmol enzyme for 17-beta-estradiol (4-hydroxylation)1 Publication
  3. Vmax=2.2 nmol/min/nmol enzyme for testosterone (6-beta-hydroxylation)1 Publication
  4. Vmax=0.6 nmol/min/nmol enzyme for progesterone (6-beta-hydroxylation)1 Publication
  5. Vmax=2.3 nmol/min/nmol enzyme for progesterone (16-alpha-hydroxylation)1 Publication
  6. Vmax=493 pmol/min/nmol enzyme toward all-trans retinol1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: Steroid hormone biosynthesis

This protein is involved in Steroid hormone biosynthesis.2 Publications
View all proteins of this organism that are known to be involved in Steroid hormone biosynthesis.

Pathwayi: retinol metabolism

This protein is involved in the pathway retinol metabolism, which is part of Cofactor metabolism.2 Publications
View all proteins of this organism that are known to be involved in the pathway retinol metabolism and in Cofactor metabolism.

Pathwayi: arachidonate metabolism

This protein is involved in the pathway arachidonate metabolism, which is part of Lipid metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway arachidonate metabolism and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei395Major determinant of CYP1B1 17beta-estradiol hydroxylation regiospecificity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi470Iron (heme axial ligand)Combined sources1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionLyase, Monooxygenase, Oxidoreductase
Biological processFatty acid metabolism, Lipid metabolism, Steroid metabolism
LigandHeme, Iron, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
MetaCyc:HS06443-MONOMER

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-211976 Endogenous sterols
R-HSA-2142670 Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET)
R-HSA-2142816 Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE)
R-HSA-5579000 Defective CYP1B1 causes Glaucoma

SABIO-RK: Biochemical Reaction Kinetics Database

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SABIO-RKi
Q16678

SIGNOR Signaling Network Open Resource

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SIGNORi
Q16678

UniPathway: a resource for the exploration and annotation of metabolic pathways

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UniPathwayi
UPA00383
UPA00912

Chemistry databases

SwissLipids knowledge resource for lipid biology

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SwissLipidsi
SLP:000001331

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Cytochrome P450 1B11 Publication (EC:1.14.14.12 Publications)
Alternative name(s):
CYPIB1
Hydroperoxy icosatetraenoate dehydratase1 Publication (EC:4.2.1.1521 Publication)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CYP1B11 PublicationImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 2

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:2597 CYP1B1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
601771 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q16678

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome, Mitochondrion

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Anterior segment dysgenesis 6 (ASGD6)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of anterior segment dysgenesis, a group of defects affecting anterior structures of the eye including cornea, iris, lens, trabecular meshwork, and Schlemm canal. Anterior segment dysgeneses result from abnormal migration or differentiation of the neural crest derived mesenchymal cells that give rise to components of the anterior chamber during eye development. Different anterior segment anomalies may exist alone or in combination, including iris hypoplasia, enlarged or reduced corneal diameter, corneal vascularization and opacity, posterior embryotoxon, corectopia, polycoria, abnormal iridocorneal angle, ectopia lentis, and anterior synechiae between the iris and posterior corneal surface. Clinical conditions falling within the phenotypic spectrum of anterior segment dysgeneses include aniridia, Axenfeld anomaly, Reiger anomaly/syndrome, Peters anomaly, and iridogoniodysgenesis. ASGD6 patients predominantly manifest Peters anomaly. Peters anomaly consists of corneal leukoma, defects in the posterior structures of the cornea such as absence of the posterior corneal stroma and Descemet membrane, and a variable degree of iridocorneal and/or keratolenticular adhesions. Over 50% of patients develop glaucoma in childhood.
Related information in OMIM
Glaucoma 3, primary congenital, A (GLC3A)20 Publications
The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry.
Disease descriptionAn 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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_05422728S → W in GLC3A. 1 PublicationCorresponds to variant dbSNP:rs780002791Ensembl.1
Natural variantiVAR_00835057W → C in GLC3A; juvenile onset; allele CYP1B1*11. 2 PublicationsCorresponds to variant dbSNP:rs72549387Ensembl.1
Natural variantiVAR_00124461G → E in GLC3A; allele CYP1B1*12; reduces enzymatic activity. 8 PublicationsCorresponds to variant dbSNP:rs28936700EnsemblClinVar.1
Natural variantiVAR_05422977L → P in GLC3A. 2 Publications1
Natural variantiVAR_02873681Y → N in GLC3A; adult-onset; hypomorphic allele; reduces the abundance of the enzyme. 4 PublicationsCorresponds to variant dbSNP:rs9282671EnsemblClinVar.1
Natural variantiVAR_054230115A → P in GLC3A. 1 PublicationCorresponds to variant dbSNP:rs764338357Ensembl.1
Natural variantiVAR_054231132M → R in GLC3A. 1 Publication1
Natural variantiVAR_054233144Q → P in GLC3A. 1 Publication1
Natural variantiVAR_054234144Q → R in GLC3A. 1 PublicationCorresponds to variant dbSNP:rs753847648Ensembl.1
Natural variantiVAR_054235145R → W in GLC3A. 1 Publication1
Natural variantiVAR_054238192D → V in GLC3A. 1 Publication1
Natural variantiVAR_054239193P → L in GLC3A. 2 PublicationsCorresponds to variant dbSNP:rs529769268Ensembl.1
Natural variantiVAR_054240198V → I in GLC3A. 1 PublicationCorresponds to variant dbSNP:rs59472972Ensembl.1
Natural variantiVAR_054241203N → S in GLC3A; reduces enzymatic activity. 1 PublicationCorresponds to variant dbSNP:rs1426636145Ensembl.1
Natural variantiVAR_054242215S → I in GLC3A. 1 PublicationCorresponds to variant dbSNP:rs72549384Ensembl.1
Natural variantiVAR_054243229E → K in GLC3A; juvenile-onset; hypomorphic allele; reduces the abundance of the enzyme. 8 PublicationsCorresponds to variant dbSNP:rs57865060EnsemblClinVar.1
Natural variantiVAR_054244232G → R in GLC3A; adult-onset. 2 PublicationsCorresponds to variant dbSNP:rs104893628EnsemblClinVar.1
Natural variantiVAR_054245239S → R in GLC3A. 1 Publication1
Natural variantiVAR_054246269 – 271Missing in GLC3A. 1 Publication3
Natural variantiVAR_054247320V → L in GLC3A. 1 PublicationCorresponds to variant dbSNP:rs72549382EnsemblClinVar.1
Natural variantiVAR_054248330A → F in GLC3A; requires 2 nucleotide substitutions; unknown pathological significance. 1 Publication1
Natural variantiVAR_054250343Missing in GLC3A; reduces enzymatic activity and also the abundance of the enzyme. 2 Publications1
Natural variantiVAR_054251345L → F in GLC3A. 1 PublicationCorresponds to variant dbSNP:rs66583685Ensembl.1
Natural variantiVAR_054252355 – 358Missing in GLC3A. 1 Publication4
Natural variantiVAR_054253364V → M in GLC3A. 3 PublicationsCorresponds to variant dbSNP:rs72549379Ensembl.1
Natural variantiVAR_001245365G → W in GLC3A; allele CYP1B1*18. 1 PublicationCorresponds to variant dbSNP:rs55771538EnsemblClinVar.1
Natural variantiVAR_016034368R → H in GLC3A and GLC1A; acts as GLC1A disease modifier in patients also carrying Val-399 mutation in MYOC. 8 PublicationsCorresponds to variant dbSNP:rs79204362EnsemblClinVar.1
Natural variantiVAR_001246374D → N in GLC3A. 2 PublicationsCorresponds to variant dbSNP:rs104893622EnsemblClinVar.1
Natural variantiVAR_008352387E → K in GLC3A; allele CYP1B1*20. 6 PublicationsCorresponds to variant dbSNP:rs55989760EnsemblClinVar.1
Natural variantiVAR_054254388A → T in GLC3A. 1 Publication1
Natural variantiVAR_054255390R → C in GLC3A. 2 PublicationsCorresponds to variant dbSNP:rs148542782EnsemblClinVar.1
Natural variantiVAR_008353390R → H in GLC3A; allele CYP1B1*21. 3 PublicationsCorresponds to variant dbSNP:rs56010818Ensembl.1
Natural variantiVAR_054256390R → S in GLC3A. 2 PublicationsCorresponds to variant dbSNP:rs148542782EnsemblClinVar.1
Natural variantiVAR_054257399I → S in GLC3A. 1 PublicationCorresponds to variant dbSNP:rs72549378Ensembl.1
Natural variantiVAR_054258409V → F in GLC3A. 1 PublicationCorresponds to variant dbSNP:rs957253424Ensembl.1
Natural variantiVAR_054260423N → Y in GLC3A; juvenile-onset. 2 PublicationsCorresponds to variant dbSNP:rs104893629EnsemblClinVar.1
Natural variantiVAR_008354437P → L in GLC3A; allele CYP1B1*23. 3 PublicationsCorresponds to variant dbSNP:rs56175199Ensembl.1
Natural variantiVAR_018774443A → G in GLC3A; allele CYP1B1*7; unknown pathological significance. 4 PublicationsCorresponds to variant dbSNP:rs4986888EnsemblClinVar.1
Natural variantiVAR_054261444R → Q in GLC3A. 1 PublicationCorresponds to variant dbSNP:rs72549376Ensembl.1
Natural variantiVAR_054262445F → C in GLC3A. 1 Publication1
Natural variantiVAR_054263466G → D in GLC3A. 1 PublicationCorresponds to variant dbSNP:rs868208502Ensembl.1
Natural variantiVAR_001247469R → W in GLC3A; allele CYP1B1*25. 4 PublicationsCorresponds to variant dbSNP:rs28936701EnsemblClinVar.1
Natural variantiVAR_054264499E → G in GLC3A. 1 PublicationCorresponds to variant dbSNP:rs72549372Ensembl.1
Natural variantiVAR_054265515S → L in GLC3A; unknown pathological significance. 1 Publication1
Natural variantiVAR_054267523R → T in GLC3A; juvenile-onset. 1 Publication1
Natural variantiVAR_054268530D → G in GLC3A. 1 Publication1
Glaucoma 1, open angle, A (GLC1A)1 Publication
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 (PubMed:11774072). 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 (PubMed:11774072).1 Publication
Disease descriptionA 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. However, glaucoma can occur at any intraocular pressure. The disease is generally asymptomatic until the late stages, by which time significant and irreversible optic nerve damage has already taken place.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_016034368R → H in GLC3A and GLC1A; acts as GLC1A disease modifier in patients also carrying Val-399 mutation in MYOC. 8 PublicationsCorresponds to variant dbSNP:rs79204362EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi395V → L: Invertes the 4OH E2:2OH E2 hydroxylation preference from 5.1 to 0.45. 1 Publication1

Keywords - Diseasei

Disease mutation, Glaucoma, Peters anomaly

Organism-specific databases

DisGeNET

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DisGeNETi
1545

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
CYP1B1

MalaCards human disease database

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MalaCardsi
CYP1B1
MIMi137750 phenotype
231300 phenotype
617315 phenotype

Open Targets

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OpenTargetsi
ENSG00000138061

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
98976 Congenital glaucoma
98977 Juvenile glaucoma
353225 NON RARE IN EUROPE: Primary adult open-angle glaucoma
708 Peters anomaly

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA27094

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
Q16678

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL4878

Drug and drug target database

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DrugBanki
DB02342 2-Methoxyestradiol
DB00613 Amodiaquine
DB01169 Arsenic trioxide
DB06732 beta-Naphthoflavone
DB00121 Biotin
DB00201 Caffeine
DB09061 Cannabidiol
DB00363 Clozapine
DB01254 Dasatinib
DB00694 Daunorubicin
DB01234 Dexamethasone
DB01248 Docetaxel
DB00997 Doxorubicin
DB00530 Erlotinib
DB00783 Estradiol
DB13952 Estradiol acetate
DB13953 Estradiol benzoate
DB13954 Estradiol cypionate
DB13955 Estradiol dienanthate
DB13956 Estradiol valerate
DB00655 Estrone
DB07776 Flavone
DB00499 Flutamide
DB01645 Genistein
DB01026 Ketoconazole
DB00448 Lansoprazole
DB14009 Medical Cannabis
DB01065 Melatonin
DB01204 Mitoxantrone
DB14011 Nabiximols
DB03467 Naringenin
DB00338 Omeprazole
DB00526 Oxaliplatin
DB01229 Paclitaxel
DB01174 Phenobarbital
DB01087 Primaquine
DB01168 Procarbazine
DB00396 Progesterone
DB00818 Propofol
DB04216 Quercetin
DB02709 Resveratrol
DB00675 Tamoxifen
DB00624 Testosterone
DB13943 Testosterone cypionate
DB13944 Testosterone enanthate
DB13946 Testosterone undecanoate
DB00277 Theophylline
DB12245 Triclabendazole
DB11155 Triclocarban

DrugCentral

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DrugCentrali
Q16678

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
1320

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
CYP1B1

Domain mapping of disease mutations (DMDM)

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DMDMi
48429256

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000516601 – 543Cytochrome P450 1B1Add BLAST543

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q16678

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q16678

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q16678

MaxQB - The MaxQuant DataBase

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MaxQBi
Q16678

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q16678

PeptideAtlas

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PeptideAtlasi
Q16678

PRoteomics IDEntifications database

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PRIDEi
Q16678

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
61033

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q16678

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q16678

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in heart, brain, lung, skeletal muscle, kidney, spleen, thymus, prostate, testis, ovary, small intestine, colon, and peripheral blood leukocytes (PubMed:8175734). Expressed in retinal endothelial cells and umbilical vein endothelial cells (at protein level) (PubMed:19005183).2 Publications

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By polycyclic aromatic hydrocarbons (PAH) and 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000138061 Expressed in 235 organ(s), highest expression level in tendon

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q16678 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q16678 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB011705
HPA026863

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
107925, 7 interactors

Protein interaction database and analysis system

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IntActi
Q16678, 4 interactors

STRING: functional protein association networks

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STRINGi
9606.ENSP00000478561

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q16678

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1543
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q16678

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q16678

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0156 Eukaryota
COG2124 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00950000183037

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000036991

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q16678

KEGG Orthology (KO)

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KOi
K07410

Identification of Orthologs from Complete Genome Data

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OMAi
LPCLDDQ

Database of Orthologous Groups

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OrthoDBi
888304at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q16678

TreeFam database of animal gene trees

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TreeFami
TF105095

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.630.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR032971 CYP1B1
IPR001128 Cyt_P450
IPR017972 Cyt_P450_CS
IPR002401 Cyt_P450_E_grp-I
IPR036396 Cyt_P450_sf

The PANTHER Classification System

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PANTHERi
PTHR24299:SF11 PTHR24299:SF11, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00067 p450, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00463 EP450I
PR00385 P450

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48264 SSF48264, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00086 CYTOCHROME_P450, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

Q16678-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGTSLSPNDP WPLNPLSIQQ TTLLLLLSVL ATVHVGQRLL RQRRRQLRSA
60 70 80 90 100
PPGPFAWPLI GNAAAVGQAA HLSFARLARR YGDVFQIRLG SCPIVVLNGE
110 120 130 140 150
RAIHQALVQQ GSAFADRPAF ASFRVVSGGR SMAFGHYSEH WKVQRRAAHS
160 170 180 190 200
MMRNFFTRQP RSRQVLEGHV LSEARELVAL LVRGSADGAF LDPRPLTVVA
210 220 230 240 250
VANVMSAVCF GCRYSHDDPE FRELLSHNEE FGRTVGAGSL VDVMPWLQYF
260 270 280 290 300
PNPVRTVFRE FEQLNRNFSN FILDKFLRHC ESLRPGAAPR DMMDAFILSA
310 320 330 340 350
EKKAAGDSHG GGARLDLENV PATITDIFGA SQDTLSTALQ WLLLLFTRYP
360 370 380 390 400
DVQTRVQAEL DQVVGRDRLP CMGDQPNLPY VLAFLYEAMR FSSFVPVTIP
410 420 430 440 450
HATTANTSVL GYHIPKDTVV FVNQWSVNHD PLKWPNPENF DPARFLDKDG
460 470 480 490 500
LINKDLTSRV MIFSVGKRRC IGEELSKMQL FLFISILAHQ CDFRANPNEP
510 520 530 540
AKMNFSYGLT IKPKSFKVNV TLRESMELLD SAVQNLQAKE TCQ
Length:543
Mass (Da):60,846
Last modified:June 7, 2004 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i46B6DA7368F63EA2
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A087WW26A0A087WW26_HUMAN
Cytochrome P450 1B1
CYP1B1
172Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A087WUQ7A0A087WUQ7_HUMAN
Cytochrome P450 1B1
CYP1B1
143Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement_in_disease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi

Various CYP1B1 alleles are known. The sequence shown is that of allele CYP1B1*1.

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05422728S → W in GLC3A. 1 PublicationCorresponds to variant dbSNP:rs780002791Ensembl.1
Natural variantiVAR_01175248R → G in allele CYP1B1*2, allele CYP1B1*5, allele CYP1B1*6 and allele CYP1B1*7. 12 PublicationsCorresponds to variant dbSNP:rs10012EnsemblClinVar.1
Natural variantiVAR_05422852P → L1 PublicationCorresponds to variant dbSNP:rs201824781EnsemblClinVar.1
Natural variantiVAR_00835057W → C in GLC3A; juvenile onset; allele CYP1B1*11. 2 PublicationsCorresponds to variant dbSNP:rs72549387Ensembl.1
Natural variantiVAR_00124461G → E in GLC3A; allele CYP1B1*12; reduces enzymatic activity. 8 PublicationsCorresponds to variant dbSNP:rs28936700EnsemblClinVar.1
Natural variantiVAR_02873568Q → R. Corresponds to variant dbSNP:rs9282670Ensembl.1
Natural variantiVAR_05422977L → P in GLC3A. 2 Publications1
Natural variantiVAR_02873681Y → N in GLC3A; adult-onset; hypomorphic allele; reduces the abundance of the enzyme. 4 PublicationsCorresponds to variant dbSNP:rs9282671EnsemblClinVar.1
Natural variantiVAR_054230115A → P in GLC3A. 1 PublicationCorresponds to variant dbSNP:rs764338357Ensembl.1
Natural variantiVAR_011753119A → 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. 11 PublicationsCorresponds to variant dbSNP:rs1056827EnsemblClinVar.1
Natural variantiVAR_054231132M → R in GLC3A. 1 Publication1
Natural variantiVAR_054232144Q → H1 Publication1
Natural variantiVAR_054233144Q → P in GLC3A. 1 Publication1
Natural variantiVAR_054234144Q → R in GLC3A. 1 PublicationCorresponds to variant dbSNP:rs753847648Ensembl.1
Natural variantiVAR_054235145R → W in GLC3A. 1 Publication1
Natural variantiVAR_054236184G → S1 Publication1
Natural variantiVAR_054237189A → P Associated with ocular hypertension susceptibility. 1 PublicationCorresponds to variant dbSNP:rs1326854156Ensembl.1
Natural variantiVAR_054238192D → V in GLC3A. 1 Publication1
Natural variantiVAR_054239193P → L in GLC3A. 2 PublicationsCorresponds to variant dbSNP:rs529769268Ensembl.1
Natural variantiVAR_054240198V → I in GLC3A. 1 PublicationCorresponds to variant dbSNP:rs59472972Ensembl.1
Natural variantiVAR_054241203N → S in GLC3A; reduces enzymatic activity. 1 PublicationCorresponds to variant dbSNP:rs1426636145Ensembl.1
Natural variantiVAR_018869206S → N1 PublicationCorresponds to variant dbSNP:rs9341248Ensembl.