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P11511

- CP19A_HUMAN

UniProt

P11511 - CP19A_HUMAN

Protein

Aromatase

Gene

CYP19A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 165 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the formation of aromatic C18 estrogens from C19 androgens.

    Catalytic activityi

    Testosterone + 3 O2 + 3 reduced flavoproteins = 17-beta-estradiol + formate + 4 H2O + 3 oxidized flavoproteins.
    Androst-4-ene-3,17-dione + 3 O2 + 3 reduced flavoproteins = estrone + formate + 4 H2O + 3 oxidized flavoproteins.

    Cofactori

    Heme group.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei309 – 3091Substrate
    Binding sitei374 – 3741Substrate; via amide nitrogen
    Metal bindingi437 – 4371Iron (heme axial ligand)

    GO - Molecular functioni

    1. aromatase activity Source: UniProtKB
    2. electron carrier activity Source: UniProtKB
    3. heme binding Source: UniProtKB
    4. iron ion binding Source: InterPro
    5. oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen Source: InterPro
    6. 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 Source: UniProtKB
    7. oxygen binding Source: ProtInc

    GO - Biological processi

    1. androgen metabolic process Source: Ensembl
    2. estrogen biosynthetic process Source: Reactome
    3. prostate gland growth Source: Ensembl
    4. small molecule metabolic process Source: Reactome
    5. steroid biosynthetic process Source: ProtInc
    6. steroid metabolic process Source: Reactome
    7. sterol metabolic process Source: Reactome
    8. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06413-MONOMER.
    ReactomeiREACT_11037. Estrogen biosynthesis.
    REACT_13812. Endogenous sterols.
    SABIO-RKP11511.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aromatase (EC:1.14.14.14)
    Alternative name(s):
    CYPXIX
    Cytochrome P-450AROM
    Cytochrome P450 19A1
    Estrogen synthase
    Gene namesi
    Name:CYP19A1
    Synonyms:ARO1, CYAR, CYP19
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:2594. CYP19A1.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: LIFEdb
    2. endoplasmic reticulum membrane Source: Reactome
    3. membrane Source: ProtInc

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Involvement in diseasei

    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.
    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.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti365 – 3651R → Q in AROD; 0.4% of wild-type activity. 1 Publication
    VAR_016962
    Natural varianti375 – 3751R → C in AROD. 1 Publication
    VAR_016963
    Natural varianti435 – 4351R → C in AROD; 1.1% of wild-type activity. 1 Publication
    VAR_016964
    Natural varianti437 – 4371C → Y in AROD; complete loss of activity. 1 Publication
    VAR_016965

    Keywords - Diseasei

    Disease mutation, Pseudohermaphroditism

    Organism-specific databases

    MIMi139300. phenotype.
    613546. phenotype.
    Orphaneti91. Aromatase deficiency.
    178345. Aromatase excess syndrome.
    PharmGKBiPA27091.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 503503AromatasePRO_0000051955Add
    BLAST

    Proteomic databases

    PaxDbiP11511.
    PRIDEiP11511.

    PTM databases

    PhosphoSiteiP11511.

    Expressioni

    Tissue specificityi

    Brain, placenta and gonads.4 Publications

    Gene expression databases

    ArrayExpressiP11511.
    BgeeiP11511.
    CleanExiHS_CYP19A1.
    GenevestigatoriP11511.

    Organism-specific databases

    HPAiCAB000355.
    HPA051194.

    Interactioni

    Protein-protein interaction databases

    IntActiP11511. 1 interaction.
    MINTiMINT-4054553.
    STRINGi9606.ENSP00000260433.

    Structurei

    Secondary structure

    1
    503
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi54 – 563
    Helixi57 – 6812
    Helixi70 – 8011
    Beta strandi83 – 9715
    Helixi100 – 1089
    Helixi110 – 1123
    Helixi119 – 1257
    Beta strandi130 – 1323
    Helixi138 – 15114
    Helixi155 – 17218
    Helixi173 – 1775
    Beta strandi183 – 1853
    Helixi187 – 20317
    Helixi210 – 22718
    Helixi232 – 2365
    Helixi238 – 2403
    Helixi242 – 26726
    Turni270 – 2756
    Helixi278 – 28710
    Turni288 – 2903
    Helixi293 – 32432
    Helixi326 – 33914
    Turni340 – 3423
    Helixi347 – 3493
    Turni350 – 3523
    Helixi354 – 36613
    Beta strandi373 – 3764
    Beta strandi381 – 3833
    Beta strandi386 – 3883
    Beta strandi393 – 3964
    Helixi398 – 4014
    Turni402 – 4043
    Helixi415 – 4184
    Turni424 – 4263
    Helixi433 – 4353
    Helixi440 – 45516
    Beta strandi458 – 4636
    Turni468 – 4703
    Beta strandi473 – 4819
    Beta strandi483 – 4853
    Beta strandi490 – 4945

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TQAmodel-A53-495[»]
    3EQMX-ray2.90A1-503[»]
    3S79X-ray2.75A1-503[»]
    3S7SX-ray3.21A1-503[»]
    4GL5X-ray3.48A1-503[»]
    4GL7X-ray3.90A1-503[»]
    4KQ8X-ray3.29A45-503[»]
    ProteinModelPortaliP11511.
    SMRiP11511. Positions 45-496.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11511.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cytochrome P450 family.Curated

    Phylogenomic databases

    eggNOGiCOG2124.
    HOGENOMiHOG000111912.
    HOVERGENiHBG050750.
    InParanoidiP11511.
    KOiK07434.
    OMAiNFAKNVP.
    OrthoDBiEOG7D85W5.
    PhylomeDBiP11511.
    TreeFamiTF352039.

    Family and domain databases

    Gene3Di1.10.630.10. 1 hit.
    InterProiIPR001128. Cyt_P450.
    IPR017972. Cyt_P450_CS.
    IPR002401. Cyt_P450_E_grp-I.
    [Graphical view]
    PfamiPF00067. p450. 1 hit.
    [Graphical view]
    PRINTSiPR00463. EP450I.
    PR00385. P450.
    SUPFAMiSSF48264. SSF48264. 1 hit.
    PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P11511-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MVLEMLNPIH YNITSIVPEA MPAATMPVLL LTGLFLLVWN YEGTSSIPGP    50
    GYCMGIGPLI SHGRFLWMGI GSACNYYNRV YGEFMRVWIS GEETLIISKS 100
    SSMFHIMKHN HYSSRFGSKL GLQCIGMHEK GIIFNNNPEL WKTTRPFFMK 150
    ALSGPGLVRM VTVCAESLKT HLDRLEEVTN ESGYVDVLTL LRRVMLDTSN 200
    TLFLRIPLDE SAIVVKIQGY FDAWQALLIK PDIFFKISWL YKKYEKSVKD 250
    LKDAIEVLIA EKRRRISTEE KLEECMDFAT ELILAEKRGD LTRENVNQCI 300
    LEMLIAAPDT MSVSLFFMLF LIAKHPNVEE AIIKEIQTVI GERDIKIDDI 350
    QKLKVMENFI YESMRYQPVV DLVMRKALED DVIDGYPVKK GTNIILNIGR 400
    MHRLEFFPKP NEFTLENFAK NVPYRYFQPF GFGPRGCAGK YIAMVMMKAI 450
    LVTLLRRFHV KTLQGQCVES IQKIHDLSLH PDETKNMLEM IFTPRNSDRC 500
    LEH 503
    Length:503
    Mass (Da):57,883
    Last modified:January 23, 2007 - v3
    Checksum:i9BD9B28651D9A69A
    GO
    Isoform 2 (identifier: P11511-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         210-218: ESAIVVKIQ → GTEIFTLTS
         219-503: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:218
    Mass (Da):24,518
    Checksum:i9C15EFD1B411087C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti496 – 4961N → S in AAA35557. (PubMed:2973313)Curated
    Sequence conflicti496 – 4961N → S in CAA31929. (PubMed:2973313)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti39 – 391W → R.1 Publication
    Corresponds to variant rs2236722 [ dbSNP | Ensembl ].
    VAR_023428
    Natural varianti201 – 2011T → M.2 Publications
    Corresponds to variant rs28757184 [ dbSNP | Ensembl ].
    VAR_023429
    Natural varianti264 – 2641R → C.3 Publications
    Corresponds to variant rs700519 [ dbSNP | Ensembl ].
    VAR_018406
    Natural varianti365 – 3651R → Q in AROD; 0.4% of wild-type activity. 1 Publication
    VAR_016962
    Natural varianti375 – 3751R → C in AROD. 1 Publication
    VAR_016963
    Natural varianti375 – 3751R → L.1 Publication
    VAR_054152
    Natural varianti435 – 4351R → C in AROD; 1.1% of wild-type activity. 1 Publication
    VAR_016964
    Natural varianti437 – 4371C → Y in AROD; complete loss of activity. 1 Publication
    VAR_016965

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei210 – 2189ESAIVVKIQ → GTEIFTLTS in isoform 2. 1 PublicationVSP_055583
    Alternative sequencei219 – 503285Missing in isoform 2. 1 PublicationVSP_055584Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22246 mRNA. Translation: AAA35557.1.
    X13589 mRNA. Translation: CAA31929.1.
    M18856 mRNA. Translation: AAA35556.1.
    J04127 mRNA. Translation: AAA52132.1.
    Y07508 mRNA. Translation: CAA68807.1.
    M30804
    , M30796, M30797, M30798, M30800, M30801, M30802, M30803 Genomic DNA. Translation: AAA35728.1.
    AY957953 Genomic DNA. Translation: AAX44046.1.
    AC012169 Genomic DNA. No translation available.
    AC020891 Genomic DNA. No translation available.
    BC035714 mRNA. Translation: AAH35714.1.
    BC107785 mRNA. Translation: AAI07786.1.
    M28420 mRNA. Translation: AAA52141.1.
    CCDSiCCDS10139.1.
    PIRiA34451. O4HU19.
    RefSeqiNP_000094.2. NM_000103.3.
    NP_112503.1. NM_031226.2.
    XP_005254247.1. XM_005254190.1.
    XP_005254248.1. XM_005254191.1.
    UniGeneiHs.260074.

    Genome annotation databases

    EnsembliENST00000260433; ENSP00000260433; ENSG00000137869. [P11511-1]
    ENST00000396402; ENSP00000379683; ENSG00000137869. [P11511-1]
    ENST00000396404; ENSP00000379685; ENSG00000137869. [P11511-1]
    ENST00000405913; ENSP00000383930; ENSG00000137869. [P11511-2]
    ENST00000557858; ENSP00000452627; ENSG00000137869. [P11511-2]
    ENST00000559878; ENSP00000453149; ENSG00000137869. [P11511-1]
    GeneIDi1588.
    KEGGihsa:1588.
    UCSCiuc001zyz.4. human.

    Polymorphism databases

    DMDMi117293.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Aromatase entry

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22246 mRNA. Translation: AAA35557.1 .
    X13589 mRNA. Translation: CAA31929.1 .
    M18856 mRNA. Translation: AAA35556.1 .
    J04127 mRNA. Translation: AAA52132.1 .
    Y07508 mRNA. Translation: CAA68807.1 .
    M30804
    , M30796 , M30797 , M30798 , M30800 , M30801 , M30802 , M30803 Genomic DNA. Translation: AAA35728.1 .
    AY957953 Genomic DNA. Translation: AAX44046.1 .
    AC012169 Genomic DNA. No translation available.
    AC020891 Genomic DNA. No translation available.
    BC035714 mRNA. Translation: AAH35714.1 .
    BC107785 mRNA. Translation: AAI07786.1 .
    M28420 mRNA. Translation: AAA52141.1 .
    CCDSi CCDS10139.1.
    PIRi A34451. O4HU19.
    RefSeqi NP_000094.2. NM_000103.3.
    NP_112503.1. NM_031226.2.
    XP_005254247.1. XM_005254190.1.
    XP_005254248.1. XM_005254191.1.
    UniGenei Hs.260074.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1TQA model - A 53-495 [» ]
    3EQM X-ray 2.90 A 1-503 [» ]
    3S79 X-ray 2.75 A 1-503 [» ]
    3S7S X-ray 3.21 A 1-503 [» ]
    4GL5 X-ray 3.48 A 1-503 [» ]
    4GL7 X-ray 3.90 A 1-503 [» ]
    4KQ8 X-ray 3.29 A 45-503 [» ]
    ProteinModelPortali P11511.
    SMRi P11511. Positions 45-496.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P11511. 1 interaction.
    MINTi MINT-4054553.
    STRINGi 9606.ENSP00000260433.

    Chemistry

    BindingDBi P11511.
    ChEMBLi CHEMBL1978.
    DrugBanki DB00357. Aminoglutethimide.
    DB01217. Anastrozole.
    DB00286. Conjugated Estrogens.
    DB01406. Danazol.
    DB00255. Diethylstilbestrol.
    DB00990. Exemestane.
    DB01006. Letrozole.
    DB00894. Testolactone.
    DB00624. Testosterone.
    GuidetoPHARMACOLOGYi 1362.

    PTM databases

    PhosphoSitei P11511.

    Polymorphism databases

    DMDMi 117293.

    Proteomic databases

    PaxDbi P11511.
    PRIDEi P11511.

    Protocols and materials databases

    DNASUi 1588.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000260433 ; ENSP00000260433 ; ENSG00000137869 . [P11511-1 ]
    ENST00000396402 ; ENSP00000379683 ; ENSG00000137869 . [P11511-1 ]
    ENST00000396404 ; ENSP00000379685 ; ENSG00000137869 . [P11511-1 ]
    ENST00000405913 ; ENSP00000383930 ; ENSG00000137869 . [P11511-2 ]
    ENST00000557858 ; ENSP00000452627 ; ENSG00000137869 . [P11511-2 ]
    ENST00000559878 ; ENSP00000453149 ; ENSG00000137869 . [P11511-1 ]
    GeneIDi 1588.
    KEGGi hsa:1588.
    UCSCi uc001zyz.4. human.

    Organism-specific databases

    CTDi 1588.
    GeneCardsi GC15M051500.
    HGNCi HGNC:2594. CYP19A1.
    HPAi CAB000355.
    HPA051194.
    MIMi 107910. gene.
    139300. phenotype.
    613546. phenotype.
    neXtProti NX_P11511.
    Orphaneti 91. Aromatase deficiency.
    178345. Aromatase excess syndrome.
    PharmGKBi PA27091.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2124.
    HOGENOMi HOG000111912.
    HOVERGENi HBG050750.
    InParanoidi P11511.
    KOi K07434.
    OMAi NFAKNVP.
    OrthoDBi EOG7D85W5.
    PhylomeDBi P11511.
    TreeFami TF352039.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS06413-MONOMER.
    Reactomei REACT_11037. Estrogen biosynthesis.
    REACT_13812. Endogenous sterols.
    SABIO-RK P11511.

    Miscellaneous databases

    ChiTaRSi CYP19A1. human.
    EvolutionaryTracei P11511.
    GeneWikii Aromatase.
    GenomeRNAii 1588.
    NextBioi 6526.
    PROi P11511.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P11511.
    Bgeei P11511.
    CleanExi HS_CYP19A1.
    Genevestigatori P11511.

    Family and domain databases

    Gene3Di 1.10.630.10. 1 hit.
    InterProi IPR001128. Cyt_P450.
    IPR017972. Cyt_P450_CS.
    IPR002401. Cyt_P450_E_grp-I.
    [Graphical view ]
    Pfami PF00067. p450. 1 hit.
    [Graphical view ]
    PRINTSi PR00463. EP450I.
    PR00385. P450.
    SUPFAMi SSF48264. SSF48264. 1 hit.
    PROSITEi PS00086. CYTOCHROME_P450. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of a complete cDNA encoding human aromatase: immunochemical identification and sequence analysis."
      Harada N.
      Biochem. Biophys. Res. Commun. 156:725-732(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Placenta.
    2. "Human aromatase: cDNA cloning, Southern blot analysis, and assignment of the gene to chromosome 15."
      Chen S., Besman M.J., Sparkes R.S., Zollman S., Klisak I., Mohandas T., Hall P.F., Shively J.E.
      DNA 7:27-38(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Isolation of a full-length cDNA insert encoding human aromatase system cytochrome P-450 and its expression in nonsteroidogenic cells."
      Corbin C.J., Graham-Lorence S., McPhaul M., Mason J.I., Mendelson C.R., Simpson E.R.
      Proc. Natl. Acad. Sci. U.S.A. 85:8948-8952(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT CYS-264.
    4. "Alternative usage of different poly(A) addition signals for two major species of mRNA encoding human aromatase P-450."
      Toda K., Terashima M., Mitsuuchi Y., Yamasaki Y., Yokoyama Y., Nojima S., Ushiro H., Maeda T., Yamamoto Y., Sagara Y., Shizuta Y.
      FEBS Lett. 247:371-376(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Placenta.
    5. "Structural analysis of the gene encoding human aromatase cytochrome P-450, the enzyme responsible for estrogen biosynthesis."
      Means G.D., Mahendroo M.S., Corbin C.J., Mathis J.M., Powell F.E., Mendelson C.R., Simpson E.R.
      J. Biol. Chem. 264:19385-19391(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. "Expression of human placental aromatase in Saccharomyces cerevisiae."
      Pompon D., Liu R.Y., Besman M.J., Wang P.L., Shively J.E., Chen S.
      Mol. Endocrinol. 3:1477-1487(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Placenta.
    7. "Biochemical and molecular genetic analyses on placental aromatase (P-450AROM) deficiency."
      Harada N., Ogawa H., Shozu M., Yamada K., Suhara K., Nishida E., Takagi Y.
      J. Biol. Chem. 267:4781-4785(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    8. NIEHS SNPs program
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-39; MET-201 AND CYS-264.
    9. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      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.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT MET-201.
      Tissue: Ovary and Placenta.
    11. "Isolation and characterization of a complementary DNA specific for human aromatase-system cytochrome P-450 mRNA."
      Evans C.T., Ledesma D.B., Schulz T.Z., Simpson E.R., Mendelson C.R.
      Proc. Natl. Acad. Sci. U.S.A. 83:6387-6391(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 85-503 (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Placenta.
    12. "Sequencing of cDNA inserts encoding aromatase cytochrome P-450 (P-450AROM)."
      Simpson E.R., Evans C.T., Corbin C.J., Powell F.E., Ledesma D.B., Mendelson C.R.
      Mol. Cell. Endocrinol. 52:267-272(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 85-503 (ISOFORM 1), VARIANT CYS-264.
    13. "Tissue-specific expression of human P-450AROM. The promoter responsible for expression in adipose tissue is different from that utilized in placenta."
      Mahendroo M.S., Means G.D., Mendelson C.R., Simpson E.R.
      J. Biol. Chem. 266:11276-11281(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49, TISSUE SPECIFICITY.
    14. "Tissue-specific and hormonally controlled alternative promoters regulate aromatase cytochrome P450 gene expression in human adipose tissue."
      Mahendroo M.S., Mendelson C.R., Simpson E.R.
      J. Biol. Chem. 268:19463-19470(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49, TISSUE SPECIFICITY, ALTERNATIVE PROMOTER USAGE.
    15. "Amino terminal sequence analysis of human placenta aromatase."
      Chen S., Shively J.E., Nakajin S., Shinoda M., Hall P.F.
      Biochem. Biophys. Res. Commun. 135:713-719(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY PROTEIN SEQUENCE OF N-TERMINUS.
      Tissue: Placenta.
    16. "Novel exon 1 of the aromatase gene specific for aromatase transcripts in human brain."
      Honda S., Harada N., Takagi Y.
      Biochem. Biophys. Res. Commun. 198:1153-1160(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE PROMOTER USAGE, TISSUE SPECIFICITY.
    17. "Structural basis for androgen specificity and oestrogen synthesis in human aromatase."
      Ghosh D., Griswold J., Erman M., Pangborn W.
      Nature 457:219-223(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH ANDROSTENEDIONE, HEME.
    18. "Molecular basis of aromatase deficiency in an adult female with sexual infantilism and polycystic ovaries."
      Ito Y., Fisher C.R., Conte F.A., Grumbach M.M., Simpson E.R.
      Proc. Natl. Acad. Sci. U.S.A. 90:11673-11677(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS AROD CYS-435 AND TYR-437.
    19. "Aromatase deficiency in male and female siblings caused by a novel mutation and the physiological role of estrogens."
      Morishima A., Grumbach M.M., Simpson E.R., Fisher C., Qin K.
      J. Clin. Endocrinol. Metab. 80:3689-3698(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT AROD CYS-375.
    20. "Effect of testosterone and estradiol in a man with aromatase deficiency."
      Carani C., Qin K., Simoni M., Faustini-Fustini M., Serpente S., Boyd J., Korach K.S., Simpson E.R.
      N. Engl. J. Med. 337:91-95(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT AROD GLN-365.
    21. Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-375.

    Entry informationi

    Entry nameiCP19A_HUMAN
    AccessioniPrimary (citable) accession number: P11511
    Secondary accession number(s): Q16731
    , Q3B764, Q58FA0, Q8IYJ7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 165 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3