Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9NYL5

- CP39A_HUMAN

UniProt

Q9NYL5 - CP39A_HUMAN

Protein

24-hydroxycholesterol 7-alpha-hydroxylase

Gene

CYP39A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (17 Apr 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Involved in the bile acid metabolism. Has a preference for 24-hydroxycholesterol, and converts it into a 7-alpha-hydroxylated product.

    Catalytic activityi

    (24R)-cholest-5-ene-3-beta,24-diol + NADPH + O2 = (24R)-cholest-5-ene-3-beta,7-alpha,24-triol + NADP+ + H2O.

    Cofactori

    Heme group.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi414 – 4141Iron (heme axial ligand)Sequence Analysis

    GO - Molecular functioni

    1. 24-hydroxycholesterol 7alpha-hydroxylase activity Source: UniProtKB-EC
    2. heme binding Source: InterPro
    3. iron ion binding Source: InterPro
    4. oxysterol 7-alpha-hydroxylase activity Source: UniProtKB
    5. steroid 7-alpha-hydroxylase activity Source: Ensembl

    GO - Biological processi

    1. bile acid biosynthetic process Source: UniProtKB
    2. bile acid catabolic process Source: UniProtKB-KW
    3. bile acid metabolic process Source: Reactome
    4. cholesterol catabolic process Source: Ensembl
    5. digestion Source: UniProtKB
    6. small molecule metabolic process Source: Reactome
    7. sterol metabolic process Source: Reactome
    8. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Bile acid catabolism, Lipid degradation, Lipid metabolism, Steroid metabolism

    Keywords - Ligandi

    Heme, Iron, Metal-binding, NADP

    Enzyme and pathway databases

    BRENDAi1.14.13.60. 2681.
    ReactomeiREACT_11053. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
    REACT_13812. Endogenous sterols.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    24-hydroxycholesterol 7-alpha-hydroxylase (EC:1.14.13.99)
    Alternative name(s):
    Cytochrome P450 39A1
    Short name:
    hCYP39A1
    Oxysterol 7-alpha-hydroxylase
    Gene namesi
    Name:CYP39A1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:17449. CYP39A1.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: Reactome
    2. intracellular membrane-bounded organelle Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Microsome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA38452.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 46946924-hydroxycholesterol 7-alpha-hydroxylasePRO_0000051992Add
    BLAST

    Proteomic databases

    PaxDbiQ9NYL5.
    PRIDEiQ9NYL5.

    Expressioni

    Tissue specificityi

    Liver specific.

    Gene expression databases

    BgeeiQ9NYL5.
    CleanExiHS_CYP39A1.
    GenevestigatoriQ9NYL5.

    Organism-specific databases

    HPAiHPA029892.

    Interactioni

    Protein-protein interaction databases

    BioGridi119453. 4 interactions.
    IntActiQ9NYL5. 4 interactions.
    STRINGi9606.ENSP00000275016.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NYL5.
    SMRiQ9NYL5. Positions 23-468.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cytochrome P450 family.Curated

    Phylogenomic databases

    eggNOGiCOG2124.
    HOGENOMiHOG000290686.
    HOVERGENiHBG106232.
    InParanoidiQ9NYL5.
    KOiK07439.
    OMAiNLRRPPC.
    OrthoDBiEOG7W153H.
    PhylomeDBiQ9NYL5.
    TreeFamiTF105090.

    Family and domain databases

    Gene3Di1.10.630.10. 1 hit.
    InterProiIPR001128. Cyt_P450.
    IPR024204. Cyt_P450_CYP7A1-type.
    IPR002403. Cyt_P450_E_grp-IV.
    [Graphical view]
    PfamiPF00067. p450. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000047. Cytochrome_CYPVIIA1. 1 hit.
    PRINTSiPR00465. EP450IV.
    SUPFAMiSSF48264. SSF48264. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9NYL5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MELISPTVII ILGCLALFLL LQRKNLRRPP CIKGWIPWIG VGFEFGKAPL    50
    EFIEKARIKY GPIFTVFAMG NRMTFVTEEE GINVFLKSKK VDFELAVQNI 100
    VYRTASIPKN VFLALHEKLY IMLKGKMGTV NLHQFTGQLT EELHEQLENL 150
    GTHGTMDLNN LVRHLLYPVT VNMLFNKSLF STNKKKIKEF HQYFQVYDED 200
    FEYGSQLPEC LLRNWSKSKK WFLELFEKNI PDIKACKSAK DNSMTLLQAT 250
    LDIVETETSK ENSPNYGLLL LWASLSNAVP VAFWTLAYVL SHPDIHKAIM 300
    EGISSVFGKA GKDKIKVSED DLENLLLIKW CVLETIRLKA PGVITRKVVK 350
    PVEILNYIIP SGDLLMLSPF WLHRNPKYFP EPELFKPERW KKANLEKHSF 400
    LDCFMAFGSG KFQCPARWFA LLEVQMCIIL ILYKYDCSLL DPLPKQSYLH 450
    LVGVPQPEGQ CRIEYKQRI 469
    Length:469
    Mass (Da):54,116
    Last modified:April 17, 2007 - v2
    Checksum:i74B013055257275C
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti23 – 231R → P.1 Publication
    Corresponds to variant rs12192544 [ dbSNP | Ensembl ].
    VAR_031609
    Natural varianti103 – 1031R → H.
    Corresponds to variant rs2277119 [ dbSNP | Ensembl ].
    VAR_031610
    Natural varianti288 – 2881Y → H.1 Publication
    Corresponds to variant rs17856332 [ dbSNP | Ensembl ].
    VAR_031611
    Natural varianti324 – 3241N → K.1 Publication
    Corresponds to variant rs7761731 [ dbSNP | Ensembl ].
    VAR_031612

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF237982 mRNA. Translation: AAF63329.1.
    AK292263 mRNA. Translation: BAF84952.1.
    AL591242, AL035670 Genomic DNA. Translation: CAH73899.1.
    AL035670, AL591242 Genomic DNA. Translation: CAI20276.1.
    BC010358 mRNA. Translation: AAH10358.1.
    CCDSiCCDS4916.1.
    RefSeqiNP_001265667.1. NM_001278738.1.
    NP_001265668.1. NM_001278739.1.
    NP_057677.2. NM_016593.4.
    UniGeneiHs.387367.

    Genome annotation databases

    EnsembliENST00000275016; ENSP00000275016; ENSG00000146233.
    GeneIDi51302.
    KEGGihsa:51302.
    UCSCiuc003oyf.1. human.

    Polymorphism databases

    DMDMi145559458.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF237982 mRNA. Translation: AAF63329.1 .
    AK292263 mRNA. Translation: BAF84952.1 .
    AL591242 , AL035670 Genomic DNA. Translation: CAH73899.1 .
    AL035670 , AL591242 Genomic DNA. Translation: CAI20276.1 .
    BC010358 mRNA. Translation: AAH10358.1 .
    CCDSi CCDS4916.1.
    RefSeqi NP_001265667.1. NM_001278738.1.
    NP_001265668.1. NM_001278739.1.
    NP_057677.2. NM_016593.4.
    UniGenei Hs.387367.

    3D structure databases

    ProteinModelPortali Q9NYL5.
    SMRi Q9NYL5. Positions 23-468.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119453. 4 interactions.
    IntActi Q9NYL5. 4 interactions.
    STRINGi 9606.ENSP00000275016.

    Polymorphism databases

    DMDMi 145559458.

    Proteomic databases

    PaxDbi Q9NYL5.
    PRIDEi Q9NYL5.

    Protocols and materials databases

    DNASUi 51302.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000275016 ; ENSP00000275016 ; ENSG00000146233 .
    GeneIDi 51302.
    KEGGi hsa:51302.
    UCSCi uc003oyf.1. human.

    Organism-specific databases

    CTDi 51302.
    GeneCardsi GC06M046564.
    H-InvDB HIX0005936.
    HGNCi HGNC:17449. CYP39A1.
    HPAi HPA029892.
    MIMi 605994. gene.
    neXtProti NX_Q9NYL5.
    PharmGKBi PA38452.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2124.
    HOGENOMi HOG000290686.
    HOVERGENi HBG106232.
    InParanoidi Q9NYL5.
    KOi K07439.
    OMAi NLRRPPC.
    OrthoDBi EOG7W153H.
    PhylomeDBi Q9NYL5.
    TreeFami TF105090.

    Enzyme and pathway databases

    BRENDAi 1.14.13.60. 2681.
    Reactomei REACT_11053. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
    REACT_13812. Endogenous sterols.

    Miscellaneous databases

    GeneWikii CYP39A1.
    GenomeRNAii 51302.
    NextBioi 54605.
    PROi Q9NYL5.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9NYL5.
    CleanExi HS_CYP39A1.
    Genevestigatori Q9NYL5.

    Family and domain databases

    Gene3Di 1.10.630.10. 1 hit.
    InterProi IPR001128. Cyt_P450.
    IPR024204. Cyt_P450_CYP7A1-type.
    IPR002403. Cyt_P450_E_grp-IV.
    [Graphical view ]
    Pfami PF00067. p450. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000047. Cytochrome_CYPVIIA1. 1 hit.
    PRINTSi PR00465. EP450IV.
    SUPFAMi SSF48264. SSF48264. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Expression cloning of an oxysterol 7alpha-hydroxylase selective for 24-hydroxycholesterol."
      Li-Hawkins J., Lund E.G., Bronson A.D., Russell D.W.
      J. Biol. Chem. 275:16543-16549(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LYS-324.
      Tissue: Liver.
    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].
      Tissue: Testis.
    3. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(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], VARIANTS PRO-23 AND HIS-288.
      Tissue: Skin.

    Entry informationi

    Entry nameiCP39A_HUMAN
    AccessioniPrimary (citable) accession number: Q9NYL5
    Secondary accession number(s): Q5VTT0, Q96FW5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2002
    Last sequence update: April 17, 2007
    Last modified: October 1, 2014
    This is version 124 of the entry and version 2 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3