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Protein

Cholesterol 24-hydroxylase

Gene

CYP46A1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the turnover of cholesterol. It converts cholesterol into 24S-hydroxycholesterol and, to a lesser extent, 25-hydroxycholesterol. Has also activity with xenobiotic compounds, such as clotrimazole.2 Publications

Catalytic activityi

Cholesterol + NADPH + O2 = (24S)-24-hydroxycholesterol + NADP+ + H2O.1 Publication

Cofactori

heme3 Publications

Kineticsi

  1. KM=2.2 µM for 24(S)-hydroxycholesterol1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi437 – 4371Iron (heme axial ligand)

    GO - Molecular functioni

    • cholesterol 24-hydroxylase activity Source: UniProtKB
    • heme binding Source: UniProtKB
    • iron ion binding Source: InterPro
    • steroid hydroxylase activity Source: ProtInc

    GO - Biological processi

    • bile acid biosynthetic process Source: Reactome
    • bile acid metabolic process Source: Reactome
    • cholesterol catabolic process Source: UniProtKB
    • nervous system development Source: ProtInc
    • small molecule metabolic process Source: Reactome
    • sterol metabolic process Source: Reactome
    • xenobiotic metabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Cholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism

    Keywords - Ligandi

    Heme, Iron, Metal-binding, NADP

    Enzyme and pathway databases

    BRENDAi1.14.13.98. 2681.
    ReactomeiREACT_11053. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
    REACT_13812. Endogenous sterols.
    SABIO-RKQ9Y6A2.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cholesterol 24-hydroxylase (EC:1.14.13.98)
    Short name:
    CH24H
    Alternative name(s):
    Cytochrome P450 46A1
    Gene namesi
    Name:CYP46A1
    Synonyms:CYP46
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:2641. CYP46A1.

    Subcellular locationi

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei3 – 2321HelicalSequence AnalysisAdd
    BLAST

    GO - Cellular componenti

    • endoplasmic reticulum Source: ProtInc
    • endoplasmic reticulum membrane Source: Reactome
    • integral component of membrane Source: UniProtKB-KW
    Complete GO annotation...

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Microsome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27117.

    Polymorphism and mutation databases

    BioMutaiCYP46A1.
    DMDMi12585217.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 500500Cholesterol 24-hydroxylasePRO_0000051994Add
    BLAST

    Proteomic databases

    PaxDbiQ9Y6A2.
    PRIDEiQ9Y6A2.

    PTM databases

    PhosphoSiteiQ9Y6A2.

    Expressioni

    Tissue specificityi

    Expressed in brain. The mRNA was broadly distributed with higher levels in gray matter zones and lower levels in regions rich in white matter. Not detected in fetal sample but its expression increases linearly with age.

    Gene expression databases

    BgeeiQ9Y6A2.
    CleanExiHS_CYP46A1.
    ExpressionAtlasiQ9Y6A2. baseline and differential.
    GenevisibleiQ9Y6A2. HS.

    Organism-specific databases

    HPAiHPA040702.

    Interactioni

    Protein-protein interaction databases

    IntActiQ9Y6A2. 1 interaction.
    STRINGi9606.ENSP00000261835.

    Structurei

    Secondary structure

    1
    500
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi60 – 7112Combined sources
    Beta strandi73 – 797Combined sources
    Beta strandi82 – 876Combined sources
    Helixi90 – 978Combined sources
    Helixi106 – 1138Combined sources
    Beta strandi118 – 1214Combined sources
    Turni125 – 1273Combined sources
    Helixi131 – 14111Combined sources
    Helixi142 – 1454Combined sources
    Helixi147 – 1515Combined sources
    Helixi154 – 17017Combined sources
    Beta strandi173 – 1764Combined sources
    Helixi180 – 19718Combined sources
    Helixi203 – 2053Combined sources
    Helixi209 – 22719Combined sources
    Helixi230 – 2323Combined sources
    Helixi234 – 2363Combined sources
    Helixi237 – 26630Combined sources
    Helixi275 – 2828Combined sources
    Turni283 – 2853Combined sources
    Beta strandi287 – 2893Combined sources
    Helixi290 – 30213Combined sources
    Helixi305 – 31814Combined sources
    Helixi322 – 33514Combined sources
    Turni336 – 3383Combined sources
    Helixi344 – 3496Combined sources
    Helixi351 – 36313Combined sources
    Beta strandi370 – 3745Combined sources
    Beta strandi378 – 3803Combined sources
    Beta strandi383 – 3853Combined sources
    Beta strandi387 – 3937Combined sources
    Helixi395 – 3995Combined sources
    Turni402 – 4043Combined sources
    Beta strandi405 – 4073Combined sources
    Helixi413 – 4164Combined sources
    Beta strandi424 – 4263Combined sources
    Helixi433 – 4353Combined sources
    Helixi440 – 45718Combined sources
    Beta strandi458 – 4625Combined sources
    Beta strandi470 – 48011Combined sources
    Beta strandi483 – 4886Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2Q9FX-ray1.90A51-500[»]
    2Q9GX-ray2.40A51-500[»]
    3MDMX-ray1.60A51-500[»]
    3MDRX-ray2.00A/B51-500[»]
    3MDTX-ray2.30A/B51-500[»]
    3MDVX-ray2.40A/B51-500[»]
    4ENHX-ray2.50A51-500[»]
    4FIAX-ray2.10A51-500[»]
    4J14X-ray2.50A51-500[»]
    ProteinModelPortaliQ9Y6A2.
    SMRiQ9Y6A2. Positions 57-491.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y6A2.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi493 – 4997Poly-Pro

    Sequence similaritiesi

    Belongs to the cytochrome P450 family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG2124.
    GeneTreeiENSGT00760000119243.
    HOGENOMiHOG000290190.
    HOVERGENiHBG102502.
    InParanoidiQ9Y6A2.
    KOiK07440.
    OMAiDYEDLGR.
    PhylomeDBiQ9Y6A2.
    TreeFamiTF352037.

    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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q9Y6A2-1) [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

            10         20         30         40         50
    MSPGLLLLGS AVLLAFGLCC TFVHRARSRY EHIPGPPRPS FLLGHLPCFW
    60 70 80 90 100
    KKDEVGGRVL QDVFLDWAKK YGPVVRVNVF HKTSVIVTSP ESVKKFLMST
    110 120 130 140 150
    KYNKDSKMYR ALQTVFGERL FGQGLVSECN YERWHKQRRV IDLAFSRSSL
    160 170 180 190 200
    VSLMETFNEK AEQLVEILEA KADGQTPVSM QDMLTYTAMD ILAKAAFGME
    210 220 230 240 250
    TSMLLGAQKP LSQAVKLMLE GITASRNTLA KFLPGKRKQL REVRESIRFL
    260 270 280 290 300
    RQVGRDWVQR RREALKRGEE VPADILTQIL KAEEGAQDDE GLLDNFVTFF
    310 320 330 340 350
    IAGHETSANH LAFTVMELSR QPEIVARLQA EVDEVIGSKR YLDFEDLGRL
    360 370 380 390 400
    QYLSQVLKES LRLYPPAWGT FRLLEEETLI DGVRVPGNTP LLFSTYVMGR
    410 420 430 440 450
    MDTYFEDPLT FNPDRFGPGA PKPRFTYFPF SLGHRSCIGQ QFAQMEVKVV
    460 470 480 490 500
    MAKLLQRLEF RLVPGQRFGL QEQATLKPLD PVLCTLRPRG WQPAPPPPPC
    Length:500
    Mass (Da):56,821
    Last modified:November 1, 1999 - v1
    Checksum:iAB9307749D9E5FDA
    GO
    Isoform 2 (identifier: Q9Y6A2-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-97: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:403
    Mass (Da):45,976
    Checksum:iE47E531F99EAA940
    GO
    Isoform 3 (identifier: Q9Y6A2-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-153: Missing.
         383-392: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:337
    Mass (Da):38,315
    Checksum:i43E23CB22A230FD7
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 153153Missing in isoform 3. 1 PublicationVSP_053858Add
    BLAST
    Alternative sequencei1 – 9797Missing in isoform 2. 1 PublicationVSP_053859Add
    BLAST
    Alternative sequencei383 – 39210Missing in isoform 3. 1 PublicationVSP_053860

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF094480 mRNA. Translation: AAD41244.1.
    AK090886 mRNA. Translation: BAC03539.1.
    AK295216 mRNA. Translation: BAG58210.1.
    AL136000 Genomic DNA. No translation available.
    AL160313 Genomic DNA. No translation available.
    BC022539 mRNA. Translation: AAH22539.1.
    CCDSiCCDS9954.1. [Q9Y6A2-1]
    RefSeqiNP_006659.1. NM_006668.1. [Q9Y6A2-1]
    UniGeneiHs.25121.

    Genome annotation databases

    EnsembliENST00000261835; ENSP00000261835; ENSG00000036530. [Q9Y6A2-1]
    ENST00000380228; ENSP00000369577; ENSG00000036530. [Q9Y6A2-2]
    GeneIDi10858.
    KEGGihsa:10858.
    UCSCiuc001ygo.3. human. [Q9Y6A2-1]
    uc001ygp.3. human.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF094480 mRNA. Translation: AAD41244.1.
    AK090886 mRNA. Translation: BAC03539.1.
    AK295216 mRNA. Translation: BAG58210.1.
    AL136000 Genomic DNA. No translation available.
    AL160313 Genomic DNA. No translation available.
    BC022539 mRNA. Translation: AAH22539.1.
    CCDSiCCDS9954.1. [Q9Y6A2-1]
    RefSeqiNP_006659.1. NM_006668.1. [Q9Y6A2-1]
    UniGeneiHs.25121.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2Q9FX-ray1.90A51-500[»]
    2Q9GX-ray2.40A51-500[»]
    3MDMX-ray1.60A51-500[»]
    3MDRX-ray2.00A/B51-500[»]
    3MDTX-ray2.30A/B51-500[»]
    3MDVX-ray2.40A/B51-500[»]
    4ENHX-ray2.50A51-500[»]
    4FIAX-ray2.10A51-500[»]
    4J14X-ray2.50A51-500[»]
    ProteinModelPortaliQ9Y6A2.
    SMRiQ9Y6A2. Positions 57-491.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiQ9Y6A2. 1 interaction.
    STRINGi9606.ENSP00000261835.

    PTM databases

    PhosphoSiteiQ9Y6A2.

    Polymorphism and mutation databases

    BioMutaiCYP46A1.
    DMDMi12585217.

    Proteomic databases

    PaxDbiQ9Y6A2.
    PRIDEiQ9Y6A2.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000261835; ENSP00000261835; ENSG00000036530. [Q9Y6A2-1]
    ENST00000380228; ENSP00000369577; ENSG00000036530. [Q9Y6A2-2]
    GeneIDi10858.
    KEGGihsa:10858.
    UCSCiuc001ygo.3. human. [Q9Y6A2-1]
    uc001ygp.3. human.

    Organism-specific databases

    CTDi10858.
    GeneCardsiGC14P100150.
    HGNCiHGNC:2641. CYP46A1.
    HPAiHPA040702.
    MIMi604087. gene.
    neXtProtiNX_Q9Y6A2.
    PharmGKBiPA27117.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG2124.
    GeneTreeiENSGT00760000119243.
    HOGENOMiHOG000290190.
    HOVERGENiHBG102502.
    InParanoidiQ9Y6A2.
    KOiK07440.
    OMAiDYEDLGR.
    PhylomeDBiQ9Y6A2.
    TreeFamiTF352037.

    Enzyme and pathway databases

    BRENDAi1.14.13.98. 2681.
    ReactomeiREACT_11053. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
    REACT_13812. Endogenous sterols.
    SABIO-RKQ9Y6A2.

    Miscellaneous databases

    ChiTaRSiCYP46A1. human.
    EvolutionaryTraceiQ9Y6A2.
    GeneWikiiCYP46A1.
    GenomeRNAii10858.
    NextBioi35472068.
    PROiQ9Y6A2.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9Y6A2.
    CleanExiHS_CYP46A1.
    ExpressionAtlasiQ9Y6A2. baseline and differential.
    GenevisibleiQ9Y6A2. HS.

    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "cDNA cloning of cholesterol 24-hydroxylase, a mediator of cholesterol homeostasis in the brain."
      Lund E.G., Guileyardo J.M., Russell D.W.
      Proc. Natl. Acad. Sci. U.S.A. 96:7238-7243(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Fetal brain.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
      Tissue: Amygdala and Caudate nucleus.
    3. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORM 1).
      Tissue: Brain.
    5. "Broad substrate specificity of human cytochrome P450 46A1 which initiates cholesterol degradation in the brain."
      Mast N., Norcross R., Andersson U., Shou M., Nakayama K., Bjoerkhem I., Pikuleva I.A.
      Biochemistry 42:14284-14292(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES.
    6. "Crystal structures of substrate-bound and substrate-free cytochrome P450 46A1, the principal cholesterol hydroxylase in the brain."
      Mast N., White M.A., Bjorkhem I., Johnson E.F., Stout C.D., Pikuleva I.A.
      Proc. Natl. Acad. Sci. U.S.A. 105:9546-9551(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 51-500 IN COMPLEX WITH HEME AND CHOLESTEROL 3-SULFATE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR.
    7. "Structural basis of drug binding to CYP46A1, an enzyme that controls cholesterol turnover in the brain."
      Mast N., Charvet C., Pikuleva I.A., Stout C.D.
      J. Biol. Chem. 285:31783-31795(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 51-500 IN COMPLEXES WITH HEME AND INHIBITORS, FUNCTION, COFACTOR.
    8. "Binding of a cyano- and fluoro-containing drug bicalutamide to cytochrome P450 46A1: unusual features and spectral response."
      Mast N., Zheng W., Stout C.D., Pikuleva I.A.
      J. Biol. Chem. 288:4613-4624(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 51-500 IN COMPLEXES WITH HEME AND THE INHIBITOR BICALUTAMIDE, COFACTOR.

    Entry informationi

    Entry nameiCP46A_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y6A2
    Secondary accession number(s): B4DHP8, E7EQG9, Q8N2B0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: November 1, 1999
    Last modified: June 24, 2015
    This is version 138 of the entry and version 1 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, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.