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Aromatase (EC 1.14.14.14) (CYPXIX) (Cytochrome P-450AROM) (Cytochrome P450 19A1) (Estrogen synthase)

 CP19A_HUMAN             Reviewed;         503 AA.
P11511; Q16731; Q3B764; Q58FA0; Q8IYJ7;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
28-FEB-2018, entry version 200.
RecName: Full=Aromatase;
EC=1.14.14.14 {ECO:0000269|PubMed:27702664};
AltName: Full=CYPXIX;
AltName: Full=Cytochrome P-450AROM;
AltName: Full=Cytochrome P450 19A1;
AltName: Full=Estrogen synthase;
Name=CYP19A1; Synonyms=ARO1, CYAR, CYP19;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=2973313; DOI=10.1016/S0006-291X(88)80903-3;
Harada N.;
"Cloning of a complete cDNA encoding human aromatase: immunochemical
identification and sequence analysis.";
Biochem. Biophys. Res. Commun. 156:725-732(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3390233; DOI=10.1089/dna.1988.7.27;
Chen S., Besman M.J., Sparkes R.S., Zollman S., Klisak I.,
Mohandas T., Hall P.F., Shively J.E.;
"Human aromatase: cDNA cloning, Southern blot analysis, and assignment
of the gene to chromosome 15.";
DNA 7:27-38(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT CYS-264.
PubMed=2848247; DOI=10.1073/pnas.85.23.8948;
Corbin C.J., Graham-Lorence S., McPhaul M., Mason J.I.,
Mendelson C.R., Simpson E.R.;
"Isolation of a full-length cDNA insert encoding human aromatase
system cytochrome P-450 and its expression in nonsteroidogenic
cells.";
Proc. Natl. Acad. Sci. U.S.A. 85:8948-8952(1988).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=2541021; DOI=10.1016/0014-5793(89)81373-0;
Toda K., Terashima M., Mitsuuchi Y., Yamasaki Y., Yokoyama Y.,
Nojima S., Ushiro H., Maeda T., Yamamoto Y., Sagara Y., Shizuta Y.;
"Alternative usage of different poly(A) addition signals for two major
species of mRNA encoding human aromatase P-450.";
FEBS Lett. 247:371-376(1989).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2808431;
Means G.D., Mahendroo M.S., Corbin C.J., Mathis J.M., Powell F.E.,
Mendelson C.R., Simpson E.R.;
"Structural analysis of the gene encoding human aromatase cytochrome
P-450, the enzyme responsible for estrogen biosynthesis.";
J. Biol. Chem. 264:19385-19391(1989).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=2691883; DOI=10.1210/mend-3-9-1477;
Pompon D., Liu R.Y., Besman M.J., Wang P.L., Shively J.E., Chen S.;
"Expression of human placental aromatase in Saccharomyces
cerevisiae.";
Mol. Endocrinol. 3:1477-1487(1989).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1371509;
Harada N., Ogawa H., Shozu M., Yamada K., Suhara K., Nishida E.,
Takagi Y.;
"Biochemical and molecular genetic analyses on placental aromatase (P-
450AROM) deficiency.";
J. Biol. Chem. 267:4781-4785(1992).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-39; MET-201 AND
CYS-264.
NIEHS SNPs program;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
MET-201.
TISSUE=Ovary, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 85-503 (ISOFORM 1), AND TISSUE
SPECIFICITY.
TISSUE=Placenta;
PubMed=3018730; DOI=10.1073/pnas.83.17.6387;
Evans C.T., Ledesma D.B., Schulz T.Z., Simpson E.R., Mendelson C.R.;
"Isolation and characterization of a complementary DNA specific for
human aromatase-system cytochrome P-450 mRNA.";
Proc. Natl. Acad. Sci. U.S.A. 83:6387-6391(1986).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 85-503 (ISOFORM 1), AND VARIANT CYS-264.
PubMed=3653507; DOI=10.1016/0303-7207(87)90054-2;
Simpson E.R., Evans C.T., Corbin C.J., Powell F.E., Ledesma D.B.,
Mendelson C.R.;
"Sequencing of cDNA inserts encoding aromatase cytochrome P-450 (P-
450AROM).";
Mol. Cell. Endocrinol. 52:267-272(1987).
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49, AND TISSUE SPECIFICITY.
PubMed=2040633;
Mahendroo M.S., Means G.D., Mendelson C.R., Simpson E.R.;
"Tissue-specific expression of human P-450AROM. The promoter
responsible for expression in adipose tissue is different from that
utilized in placenta.";
J. Biol. Chem. 266:11276-11281(1991).
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49, TISSUE SPECIFICITY, AND
ALTERNATIVE PROMOTER USAGE.
PubMed=7690033;
Mahendroo M.S., Mendelson C.R., Simpson E.R.;
"Tissue-specific and hormonally controlled alternative promoters
regulate aromatase cytochrome P450 gene expression in human adipose
tissue.";
J. Biol. Chem. 268:19463-19470(1993).
[15]
PRELIMINARY PROTEIN SEQUENCE OF N-TERMINUS.
TISSUE=Placenta;
PubMed=3964273; DOI=10.1016/0006-291X(86)90987-3;
Chen S., Shively J.E., Nakajin S., Shinoda M., Hall P.F.;
"Amino terminal sequence analysis of human placenta aromatase.";
Biochem. Biophys. Res. Commun. 135:713-719(1986).
[16]
ALTERNATIVE PROMOTER USAGE, AND TISSUE SPECIFICITY.
PubMed=8117272; DOI=10.1006/bbrc.1994.1163;
Honda S., Harada N., Takagi Y.;
"Novel exon 1 of the aromatase gene specific for aromatase transcripts
in human brain.";
Biochem. Biophys. Res. Commun. 198:1153-1160(1994).
[17]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH ANDROSTENEDIONE,
AND HEME.
PubMed=19129847; DOI=10.1038/nature07614;
Ghosh D., Griswold J., Erman M., Pangborn W.;
"Structural basis for androgen specificity and oestrogen synthesis in
human aromatase.";
Nature 457:219-223(2009).
[18]
VARIANTS AROD CYS-435 AND TYR-437.
PubMed=8265607; DOI=10.1073/pnas.90.24.11673;
Ito Y., Fisher C.R., Conte F.A., Grumbach M.M., Simpson E.R.;
"Molecular basis of aromatase deficiency in an adult female with
sexual infantilism and polycystic ovaries.";
Proc. Natl. Acad. Sci. U.S.A. 90:11673-11677(1993).
[19]
VARIANT AROD CYS-375.
PubMed=8530621; DOI=10.1210/jcem.80.12.8530621;
Morishima A., Grumbach M.M., Simpson E.R., Fisher C., Qin K.;
"Aromatase deficiency in male and female siblings caused by a novel
mutation and the physiological role of estrogens.";
J. Clin. Endocrinol. Metab. 80:3689-3698(1995).
[20]
VARIANT AROD GLN-365.
PubMed=9211678; DOI=10.1056/NEJM199707103370204;
Carani C., Qin K., Simoni M., Faustini-Fustini M., Serpente S.,
Boyd J., Korach K.S., Simpson E.R.;
"Effect of testosterone and estradiol in a man with aromatase
deficiency.";
N. Engl. J. Med. 337:91-95(1997).
[21]
VARIANT CYS-264.
PubMed=9352581;
Watanabe J., Harada N., Suemasu K., Higashi Y., Gotoh O., Kawajiri K.;
"Arginine-cysteine polymorphism at codon 264 of the human CYP19 gene
does not affect aromatase activity.";
Pharmacogenetics 7:419-424(1997).
[22]
VARIANTS ARG-39 AND CYS-264.
PubMed=10956405;
DOI=10.1002/1097-0215(20000720)89:4<325::AID-IJC2>3.0.CO;2-3;
Miyoshi Y., Iwao K., Ikeda N., Egawa C., Noguchi S.;
"Breast cancer risk associated with polymorphism in CYP19 in Japanese
women.";
Int. J. Cancer 89:325-328(2000).
[23]
VARIANT [LARGE SCALE ANALYSIS] LEU-375.
PubMed=18987736; DOI=10.1038/nature07485;
Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K.,
Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L.,
Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A.,
Abbott S., Locke D., Hillier L.W., Miner T., Fulton L., Magrini V.,
Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R.,
Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E.,
Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J.,
Heath S., Shannon W.D., Nagarajan R., Walter M.J., Link D.C.,
Graubert T.A., DiPersio J.F., Wilson R.K.;
"DNA sequencing of a cytogenetically normal acute myeloid leukaemia
genome.";
Nature 456:66-72(2008).
[24]
VARIANT AROD HIS-192, AND CHARACTERIZATION OF VARIANT AROD HIS-192.
PubMed=24705274; DOI=10.1016/j.mce.2014.03.008;
Bouchoucha N., Samara-Boustani D., Pandey A.V., Bony-Trifunovic H.,
Hofer G., Aigrain Y., Polak M., Fluck C.E.;
"Characterization of a novel CYP19A1 (aromatase) R192H mutation
causing virilization of a 46,XX newborn, undervirilization of the
46,XY brother, but no virilization of the mother during pregnancies.";
Mol. Cell. Endocrinol. 390:8-17(2014).
[25]
VARIANT PRO-314.
PubMed=27657680; DOI=10.1038/gim.2016.142;
Chen D.Y., Liu X.F., Lin X.J., Zhang D., Chai Y.C., Yu D.H., Sun C.L.,
Wang X.L., Zhu W.D., Chen Y., Sun L.H., Wang X.W., Shi F.X.,
Huang Z.W., Yang T., Wu H.;
"A dominant variant in DMXL2 is linked to nonsyndromic hearing loss.";
Genet. Med. 19:553-558(2017).
[26]
CHARACTERIZATION OF VARIANTS CYS-264 AND HIS-264, PHOSPHORYLATION,
CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=27702664; DOI=10.1016/j.jsbmb.2016.09.022;
Baravalle R., Di Nardo G., Bandino A., Barone I., Catalano S.,
Ando S., Gilardi G.;
"Impact of R264C and R264H polymorphisms in human aromatase
function.";
J. Steroid Biochem. Mol. Biol. 167:23-32(2017).
-!- FUNCTION: Catalyzes the formation of aromatic C18 estrogens from
C19 androgens.
-!- CATALYTIC ACTIVITY: Testosterone + 3 [reduced NADPH--hemoprotein
reductase] + 3 O(2) = 17-beta-estradiol + formate + 4 H(2)O + 3
[oxidized NADPH--hemoprotein reductase].
{ECO:0000269|PubMed:27702664}.
-!- CATALYTIC ACTIVITY: Androst-4-ene-3,17-dione + 3 [reduced NADPH--
hemoprotein reductase] + 3 O(2) = estrone + formate + 4 H(2)O + 3
[oxidized NADPH--hemoprotein reductase].
{ECO:0000269|PubMed:27702664}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.46 uM for androstenedione {ECO:0000269|PubMed:27702664};
-!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P11511-1; Sequence=Displayed;
Name=2;
IsoId=P11511-2; Sequence=VSP_055583, VSP_055584;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed, including in adult and fetal
brain, placenta, skin fibroblasts, adipose tissue and gonads.
{ECO:0000269|PubMed:2040633, ECO:0000269|PubMed:3018730,
ECO:0000269|PubMed:7690033, ECO:0000269|PubMed:8117272}.
-!- PTM: Phosphorylated in vitro by PKA and PKG/PRKG1. These
phosphorylations inhibit the catalytic activity as measured by
estrone synthesis from androstenedione (36% decrease for PKA and
30% for PKG/PRKG1). {ECO:0000269|PubMed:27702664}.
-!- DISEASE: Aromatase excess syndrome (AEXS) [MIM:139300]: An
autosomal dominant disorder characterized by increased
extraglandular aromatization of steroids that presents with
heterosexual precocity in males and isosexual precocity in
females. Note=The disease is caused by mutations affecting the
gene represented in this entry.
-!- DISEASE: Aromatase deficiency (AROD) [MIM:613546]: A rare disease
in which fetal androgens are not converted into estrogens due to
placental aromatase deficiency. Thus, pregnant women exhibit a
hirsutism, which spontaneously resolves after post-partum. At
birth, female babies present with pseudohermaphroditism due to
virilization of extern genital organs. In adult females,
manifestations include delay of puberty, breast hypoplasia and
primary amenorrhoea with multicystic ovaries.
{ECO:0000269|PubMed:24705274, ECO:0000269|PubMed:8265607,
ECO:0000269|PubMed:8530621, ECO:0000269|PubMed:9211678}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Aromatase entry;
URL="https://en.wikipedia.org/wiki/Aromatase";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/cyp19a1/";
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EMBL; M22246; AAA35557.1; -; mRNA.
EMBL; X13589; CAA31929.1; -; mRNA.
EMBL; M18856; AAA35556.1; -; mRNA.
EMBL; J04127; AAA52132.1; -; mRNA.
EMBL; Y07508; CAA68807.1; -; mRNA.
EMBL; M30804; AAA35728.1; -; Genomic_DNA.
EMBL; M30796; AAA35728.1; JOINED; Genomic_DNA.
EMBL; M30797; AAA35728.1; JOINED; Genomic_DNA.
EMBL; M30798; AAA35728.1; JOINED; Genomic_DNA.
EMBL; M30800; AAA35728.1; JOINED; Genomic_DNA.
EMBL; M30801; AAA35728.1; JOINED; Genomic_DNA.
EMBL; M30802; AAA35728.1; JOINED; Genomic_DNA.
EMBL; M30803; AAA35728.1; JOINED; Genomic_DNA.
EMBL; AY957953; AAX44046.1; -; Genomic_DNA.
EMBL; AC012169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC020891; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC035714; AAH35714.1; -; mRNA.
EMBL; BC107785; AAI07786.1; -; mRNA.
EMBL; M28420; AAA52141.1; -; mRNA.
CCDS; CCDS10139.1; -. [P11511-1]
PIR; A34451; O4HU19.
RefSeq; NP_000094.2; NM_000103.3. [P11511-1]
RefSeq; NP_001334177.1; NM_001347248.1. [P11511-1]
RefSeq; NP_001334178.1; NM_001347249.1. [P11511-1]
RefSeq; NP_001334179.1; NM_001347250.1. [P11511-1]
RefSeq; NP_001334180.1; NM_001347251.1. [P11511-1]
RefSeq; NP_001334181.1; NM_001347252.1. [P11511-1]
RefSeq; NP_001334182.1; NM_001347253.1. [P11511-1]
RefSeq; NP_001334183.1; NM_001347254.1. [P11511-1]
RefSeq; NP_001334184.1; NM_001347255.1. [P11511-1]
RefSeq; NP_001334185.1; NM_001347256.1. [P11511-1]
RefSeq; NP_112503.1; NM_031226.2. [P11511-1]
UniGene; Hs.260074; -.
PDB; 1TQA; Model; -; A=53-495.
PDB; 3EQM; X-ray; 2.90 A; A=1-503.
PDB; 3S79; X-ray; 2.75 A; A=1-503.
PDB; 3S7S; X-ray; 3.21 A; A=1-503.
PDB; 4GL5; X-ray; 3.48 A; A=1-503.
PDB; 4GL7; X-ray; 3.90 A; A=1-503.
PDB; 4KQ8; X-ray; 3.29 A; A=45-503.
PDB; 5JKV; X-ray; 2.75 A; A=1-503.
PDB; 5JKW; X-ray; 3.00 A; A=1-503.
PDB; 5JL6; X-ray; 3.00 A; A=1-503.
PDB; 5JL7; X-ray; 3.10 A; A=1-503.
PDB; 5JL9; X-ray; 3.10 A; A=1-503.
PDBsum; 1TQA; -.
PDBsum; 3EQM; -.
PDBsum; 3S79; -.
PDBsum; 3S7S; -.
PDBsum; 4GL5; -.
PDBsum; 4GL7; -.
PDBsum; 4KQ8; -.
PDBsum; 5JKV; -.
PDBsum; 5JKW; -.
PDBsum; 5JL6; -.
PDBsum; 5JL7; -.
PDBsum; 5JL9; -.
ProteinModelPortal; P11511; -.
SMR; P11511; -.
BioGrid; 107960; 7.
IntAct; P11511; 1.
MINT; P11511; -.
STRING; 9606.ENSP00000260433; -.
BindingDB; P11511; -.
ChEMBL; CHEMBL1978; -.
DrugBank; DB02342; 2-Methoxyestradiol.
DrugBank; DB00357; Aminoglutethimide.
DrugBank; DB01217; Anastrozole.
DrugBank; DB05338; atamestane-plus-toremifene.
DrugBank; DB00443; Betamethasone.
DrugBank; DB04794; Bifonazole.
DrugBank; DB06719; Buserelin.
DrugBank; DB00389; Carbimazole.
DrugBank; DB00269; Chlorotrianisene.
DrugBank; DB00856; Chlorphenesin.
DrugBank; DB00882; Clomifene.
DrugBank; DB00257; Clotrimazole.
DrugBank; DB04839; Cyproterone acetate.
DrugBank; DB01406; Danazol.
DrugBank; DB05804; dehydroepiandrosterone sulfate.
DrugBank; DB01234; Dexamethasone.
DrugBank; DB00255; Diethylstilbestrol.
DrugBank; DB02901; Dihydrotestosterone.
DrugBank; DB00917; Dinoprostone.
DrugBank; DB00858; Drostanolone.
DrugBank; DB01127; Econazole.
DrugBank; DB00974; Edetic Acid.
DrugBank; DB00292; Etomidate.
DrugBank; DB00926; Etretinate.
DrugBank; DB00990; Exemestane.
DrugBank; DB01026; Ketoconazole.
DrugBank; DB01006; Letrozole.
DrugBank; DB01227; Levomethadyl Acetate.
DrugBank; DB00367; Levonorgestrel.
DrugBank; DB00358; Mefloquine.
DrugBank; DB01065; Melatonin.
DrugBank; DB00333; Methadone.
DrugBank; DB06710; Methyltestosterone.
DrugBank; DB01110; Miconazole.
DrugBank; DB05749; MPI-674.
DrugBank; DB08804; Nandrolone decanoate.
DrugBank; DB00984; Nandrolone phenpropionate.
DrugBank; DB00184; Nicotine.
DrugBank; DB09389; Norgestrel.
DrugBank; DB01229; Paclitaxel.
DrugBank; DB00481; Raloxifene.
DrugBank; DB05875; substance P.
DrugBank; DB06147; Sulfathiazole.
DrugBank; DB00675; Tamoxifen.
DrugBank; DB00857; Terbinafine.
DrugBank; DB00894; Testolactone.
DrugBank; DB00624; Testosterone.
DrugBank; DB01007; Tioconazole.
DrugBank; DB00072; Trastuzumab.
DrugBank; DB00197; Troglitazone.
GuidetoPHARMACOLOGY; 1362; -.
SwissLipids; SLP:000001716; -.
iPTMnet; P11511; -.
PhosphoSitePlus; P11511; -.
BioMuta; CYP19A1; -.
DMDM; 117293; -.
PaxDb; P11511; -.
PeptideAtlas; P11511; -.
PRIDE; P11511; -.
DNASU; 1588; -.
Ensembl; ENST00000396402; ENSP00000379683; ENSG00000137869. [P11511-1]
Ensembl; ENST00000396404; ENSP00000379685; ENSG00000137869. [P11511-1]
Ensembl; ENST00000405913; ENSP00000383930; ENSG00000137869. [P11511-2]
Ensembl; ENST00000557858; ENSP00000452627; ENSG00000137869. [P11511-2]
Ensembl; ENST00000559878; ENSP00000453149; ENSG00000137869. [P11511-1]
GeneID; 1588; -.
KEGG; hsa:1588; -.
UCSC; uc001zyz.5; human. [P11511-1]
CTD; 1588; -.
DisGeNET; 1588; -.
EuPathDB; HostDB:ENSG00000137869.13; -.
GeneCards; CYP19A1; -.
HGNC; HGNC:2594; CYP19A1.
HPA; CAB000355; -.
HPA; HPA051194; -.
MalaCards; CYP19A1; -.
MIM; 107910; gene.
MIM; 139300; phenotype.
MIM; 613546; phenotype.
neXtProt; NX_P11511; -.
OpenTargets; ENSG00000137869; -.
Orphanet; 91; Aromatase deficiency.
Orphanet; 178345; Aromatase excess syndrome.
PharmGKB; PA27091; -.
eggNOG; KOG0157; Eukaryota.
eggNOG; COG2124; LUCA.
GeneTree; ENSGT00840000129915; -.
HOGENOM; HOG000111912; -.
HOVERGEN; HBG050750; -.
InParanoid; P11511; -.
KO; K07434; -.
OMA; MRRIMLD; -.
OrthoDB; EOG091G056R; -.
PhylomeDB; P11511; -.
TreeFam; TF352039; -.
BioCyc; MetaCyc:HS06413-MONOMER; -.
BRENDA; 1.14.14.14; 2681.
Reactome; R-HSA-193144; Estrogen biosynthesis.
Reactome; R-HSA-211976; Endogenous sterols.
Reactome; R-HSA-5579030; Defective CYP19A1 causes Aromatase excess syndrome (AEXS).
SABIO-RK; P11511; -.
SIGNOR; P11511; -.
ChiTaRS; CYP19A1; human.
EvolutionaryTrace; P11511; -.
GeneWiki; Aromatase; -.
GenomeRNAi; 1588; -.
PRO; PR:P11511; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000137869; -.
CleanEx; HS_CYP19A1; -.
ExpressionAtlas; P11511; baseline and differential.
Genevisible; P11511; HS.
GO; GO:0005783; C:endoplasmic reticulum; IDA:LIFEdb.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0070330; F:aromatase activity; IDA:UniProtKB.
GO; GO:0009055; F:electron transfer activity; TAS:UniProtKB.
GO; GO:0020037; F:heme binding; IDA:UniProtKB.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0016712; F: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; TAS:UniProtKB.
GO; GO:0019825; F:oxygen binding; TAS:ProtInc.
GO; GO:0008395; F:steroid hydroxylase activity; TAS:Reactome.
GO; GO:0006710; P:androgen catabolic process; IDA:CAFA.
GO; GO:0006703; P:estrogen biosynthetic process; TAS:Reactome.
GO; GO:0030540; P:female genitalia development; IEA:Ensembl.
GO; GO:0008585; P:female gonad development; IEA:Ensembl.
GO; GO:0030879; P:mammary gland development; IEA:Ensembl.
GO; GO:0002677; P:negative regulation of chronic inflammatory response; IEA:Ensembl.
GO; GO:0010760; P:negative regulation of macrophage chemotaxis; IEA:Ensembl.
GO; GO:2000866; P:positive regulation of estradiol secretion; IDA:CAFA.
GO; GO:0060736; P:prostate gland growth; IEA:Ensembl.
GO; GO:0006694; P:steroid biosynthetic process; TAS:ProtInc.
GO; GO:0016125; P:sterol metabolic process; TAS:Reactome.
GO; GO:0061370; P:testosterone biosynthetic process; IEA:Ensembl.
GO; GO:0060065; P:uterus development; IEA:Ensembl.
Gene3D; 1.10.630.10; -; 1.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR002401; Cyt_P450_E_grp-I.
InterPro; IPR036396; Cyt_P450_sf.
Pfam; PF00067; p450; 1.
PRINTS; PR00463; EP450I.
PRINTS; PR00385; P450.
SUPFAM; SSF48264; SSF48264; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Direct protein sequencing; Disease mutation; Heme; Iron; Membrane;
Metal-binding; Monooxygenase; Oxidoreductase; Polymorphism;
Pseudohermaphroditism; Reference proteome.
CHAIN 1 503 Aromatase.
/FTId=PRO_0000051955.
METAL 437 437 Iron (heme axial ligand).
BINDING 309 309 Substrate.
BINDING 374 374 Substrate; via amide nitrogen.
VAR_SEQ 210 218 ESAIVVKIQ -> GTEIFTLTS (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_055583.
VAR_SEQ 219 503 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_055584.
VARIANT 39 39 W -> R (in dbSNP:rs2236722).
{ECO:0000269|PubMed:10956405,
ECO:0000269|Ref.8}.
/FTId=VAR_023428.
VARIANT 192 192 R -> H (in AROD; strongly reduced
aromatase activity; 81% reduction of
androstenedione metabolism compared to
wild-type; dbSNP:rs765057534).
{ECO:0000269|PubMed:24705274}.
/FTId=VAR_072784.
VARIANT 201 201 T -> M (in dbSNP:rs28757184).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.8}.
/FTId=VAR_023429.
VARIANT 264 264 R -> C (1.6 fold decrease in affinity for
androstenedione substrate; slightly
affects PKA-mediated reduction in
catalytic activity as measured in vitro
by estrone synthesis from androstenedione
(49% decrease compared with 36% for the
wild-type protein); no effect on PKG/
PRKG1-mediated reduction in catalytic
activity in vitro; dbSNP:rs700519).
{ECO:0000269|PubMed:10956405,
ECO:0000269|PubMed:27702664,
ECO:0000269|PubMed:2848247,
ECO:0000269|PubMed:3653507,
ECO:0000269|PubMed:9352581,
ECO:0000269|Ref.8}.
/FTId=VAR_018406.
VARIANT 264 264 R -> H (2.5 fold decrease in affinity for
androstenedione substrate; slightly
affects PKA-mediated reduction in
catalytic activity as measured by estrone
synthesis from androstenedione in vitro
(28% decrease compared with 36% for the
wild-type protein) and PKG/PRKG1-mediated
reduction in catalytic activity in vitro
(15% decrease compared with 30% for the
wild-type protein); dbSNP:rs2304462).
{ECO:0000269|PubMed:27702664}.
/FTId=VAR_077526.
VARIANT 314 314 S -> P (found in deaf patients; unknown
pathological significance).
{ECO:0000269|PubMed:27657680}.
/FTId=VAR_079486.
VARIANT 365 365 R -> Q (in AROD; 0.4% of wild-type
activity; dbSNP:rs80051519).
{ECO:0000269|PubMed:9211678}.
/FTId=VAR_016962.
VARIANT 375 375 R -> C (in AROD; dbSNP:rs121434536).
{ECO:0000269|PubMed:8530621}.
/FTId=VAR_016963.
VARIANT 375 375 R -> L. {ECO:0000269|PubMed:18987736}.
/FTId=VAR_054152.
VARIANT 435 435 R -> C (in AROD; 1.1% of wild-type
activity; dbSNP:rs121434534).
{ECO:0000269|PubMed:8265607}.
/FTId=VAR_016964.
VARIANT 437 437 C -> Y (in AROD; complete loss of
activity; dbSNP:rs78310315).
{ECO:0000269|PubMed:8265607}.
/FTId=VAR_016965.
CONFLICT 496 496 N -> S (in Ref. 1; AAA35557/CAA31929).
{ECO:0000305}.
STRAND 54 56 {ECO:0000244|PDB:3S79}.
HELIX 57 68 {ECO:0000244|PDB:3S79}.
HELIX 70 80 {ECO:0000244|PDB:3S79}.
STRAND 83 97 {ECO:0000244|PDB:3S79}.
HELIX 100 108 {ECO:0000244|PDB:3S79}.
HELIX 110 112 {ECO:0000244|PDB:3S79}.
HELIX 119 125 {ECO:0000244|PDB:3S79}.
STRAND 130 132 {ECO:0000244|PDB:3S79}.
HELIX 138 151 {ECO:0000244|PDB:3S79}.
HELIX 155 172 {ECO:0000244|PDB:3S79}.
HELIX 173 177 {ECO:0000244|PDB:3S79}.
STRAND 183 185 {ECO:0000244|PDB:5JKW}.
HELIX 187 203 {ECO:0000244|PDB:3S79}.
HELIX 210 227 {ECO:0000244|PDB:3S79}.
HELIX 232 236 {ECO:0000244|PDB:3S79}.
HELIX 238 240 {ECO:0000244|PDB:3S79}.
HELIX 242 267 {ECO:0000244|PDB:3S79}.
TURN 270 275 {ECO:0000244|PDB:3S79}.
HELIX 278 287 {ECO:0000244|PDB:3S79}.
TURN 288 290 {ECO:0000244|PDB:3EQM}.
HELIX 293 324 {ECO:0000244|PDB:3S79}.
HELIX 326 339 {ECO:0000244|PDB:3S79}.
TURN 340 342 {ECO:0000244|PDB:3S79}.
HELIX 347 349 {ECO:0000244|PDB:3S79}.
TURN 350 352 {ECO:0000244|PDB:3S79}.
HELIX 354 366 {ECO:0000244|PDB:3S79}.
STRAND 373 376 {ECO:0000244|PDB:3S79}.
STRAND 381 383 {ECO:0000244|PDB:3S79}.
STRAND 386 388 {ECO:0000244|PDB:3S79}.
STRAND 393 396 {ECO:0000244|PDB:3S79}.
HELIX 398 401 {ECO:0000244|PDB:3S79}.
TURN 402 404 {ECO:0000244|PDB:3S79}.
HELIX 415 418 {ECO:0000244|PDB:3S79}.
TURN 424 426 {ECO:0000244|PDB:3S79}.
HELIX 433 435 {ECO:0000244|PDB:5JL6}.
HELIX 440 455 {ECO:0000244|PDB:3S79}.
STRAND 458 463 {ECO:0000244|PDB:3S79}.
TURN 468 470 {ECO:0000244|PDB:3S79}.
STRAND 473 481 {ECO:0000244|PDB:3S79}.
STRAND 483 485 {ECO:0000244|PDB:4KQ8}.
STRAND 490 494 {ECO:0000244|PDB:3S79}.
SEQUENCE 503 AA; 57883 MW; 9BD9B28651D9A69A CRC64;
MVLEMLNPIH YNITSIVPEA MPAATMPVLL LTGLFLLVWN YEGTSSIPGP GYCMGIGPLI
SHGRFLWMGI GSACNYYNRV YGEFMRVWIS GEETLIISKS SSMFHIMKHN HYSSRFGSKL
GLQCIGMHEK GIIFNNNPEL WKTTRPFFMK ALSGPGLVRM VTVCAESLKT HLDRLEEVTN
ESGYVDVLTL LRRVMLDTSN TLFLRIPLDE SAIVVKIQGY FDAWQALLIK PDIFFKISWL
YKKYEKSVKD LKDAIEVLIA EKRRRISTEE KLEECMDFAT ELILAEKRGD LTRENVNQCI
LEMLIAAPDT MSVSLFFMLF LIAKHPNVEE AIIKEIQTVI GERDIKIDDI QKLKVMENFI
YESMRYQPVV DLVMRKALED DVIDGYPVKK GTNIILNIGR MHRLEFFPKP NEFTLENFAK
NVPYRYFQPF GFGPRGCAGK YIAMVMMKAI LVTLLRRFHV KTLQGQCVES IQKIHDLSLH
PDETKNMLEM IFTPRNSDRC LEH


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