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O15528

- CP27B_HUMAN

UniProt

O15528 - CP27B_HUMAN

Protein

25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial

Gene

CYP27B1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    Catalyzes the conversion of 25-hydroxyvitamin D3 (25(OH)D) to 1-alpha,25-dihydroxyvitamin D3 (1,25(OH)2D) plays an important role in normal bone growth, calcium metabolism, and tissue differentiation.

    Catalytic activityi

    Calcidiol + NADPH + O2 = calcitriol + NADP+ + H2O.

    Cofactori

    Heme group.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi455 – 4551Iron (heme axial ligand)By similarity

    GO - Molecular functioni

    1. calcidiol 1-monooxygenase activity Source: BHF-UCL
    2. heme binding Source: InterPro
    3. iron ion binding Source: InterPro

    GO - Biological processi

    1. bone mineralization Source: BHF-UCL
    2. calcitriol biosynthetic process from calciol Source: BHF-UCL
    3. calcium ion homeostasis Source: BHF-UCL
    4. calcium ion transport Source: BHF-UCL
    5. decidualization Source: BHF-UCL
    6. G1 to G0 transition Source: BHF-UCL
    7. negative regulation of calcidiol 1-monooxygenase activity Source: BHF-UCL
    8. negative regulation of cell growth Source: BHF-UCL
    9. negative regulation of cell proliferation Source: BHF-UCL
    10. positive regulation of keratinocyte differentiation Source: BHF-UCL
    11. positive regulation of vitamin D 24-hydroxylase activity Source: BHF-UCL
    12. positive regulation of vitamin D receptor signaling pathway Source: BHF-UCL
    13. regulation of bone mineralization Source: BHF-UCL
    14. response to estrogen Source: BHF-UCL
    15. response to interferon-gamma Source: BHF-UCL
    16. response to lipopolysaccharide Source: BHF-UCL
    17. response to vitamin D Source: BHF-UCL
    18. small molecule metabolic process Source: Reactome
    19. steroid metabolic process Source: Reactome
    20. vitamin D catabolic process Source: Ensembl
    21. vitamin D metabolic process Source: BHF-UCL
    22. vitamin metabolic process Source: Reactome
    23. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Ligandi

    Heme, Iron, Metal-binding, NADP

    Enzyme and pathway databases

    BRENDAi1.14.13.13. 2681.
    ReactomeiREACT_13450. Vitamins.
    REACT_13523. Vitamin D (calciferol) metabolism.
    UniPathwayiUPA00955.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial (EC:1.14.13.13)
    Alternative name(s):
    25-OHD-1 alpha-hydroxylase
    25-hydroxyvitamin D(3) 1-alpha-hydroxylase
    Short name:
    VD3 1A hydroxylase
    Calcidiol 1-monooxygenase
    Cytochrome P450 subfamily XXVIIB polypeptide 1
    Cytochrome P450C1 alpha
    Cytochrome P450VD1-alpha
    Cytochrome p450 27B1
    Gene namesi
    Name:CYP27B1
    Synonyms:CYP1ALPHA, CYP27B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:2606. CYP27B1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: BHF-UCL
    2. mitochondrial outer membrane Source: Reactome
    3. mitochondrion Source: BHF-UCL

    Keywords - Cellular componenti

    Membrane, Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Rickets vitamin D-dependent 1A (VDDR1A) [MIM:264700]: A disorder caused by a selective deficiency of the active form of vitamin D (1,25-dihydroxyvitamin D3) and resulting in defective bone mineralization and clinical features of rickets.5 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti65 – 651Q → H in VDDR1A. 1 Publication
    VAR_016969
    Natural varianti107 – 1071R → H in VDDR1A; complete loss of activity. 1 Publication
    Corresponds to variant rs28934604 [ dbSNP | Ensembl ].
    VAR_016952
    Natural varianti125 – 1251G → E in VDDR1A; complete loss of activity. 1 Publication
    Corresponds to variant rs28934605 [ dbSNP | Ensembl ].
    VAR_016953
    Natural varianti189 – 1891E → G in VDDR1A; 22% of wild-type activity. 1 Publication
    VAR_016954
    Natural varianti189 – 1891E → K in VDDR1A; 11% of wild-type activity. 1 Publication
    VAR_016967
    Natural varianti321 – 3211T → R in VDDR1A; complete loss of activity. 1 Publication
    VAR_016955
    Natural varianti323 – 3231S → Y in VDDR1A. 1 Publication
    VAR_016970
    Natural varianti335 – 3351R → P in VDDR1A; complete loss of activity. 1 Publication
    Corresponds to variant rs28934606 [ dbSNP | Ensembl ].
    VAR_016956
    Natural varianti343 – 3431L → F in VDDR1A; 2.3% of wild-type activity. 1 Publication
    VAR_016957
    Natural varianti382 – 3821P → S in VDDR1A; complete loss of activity. 1 Publication
    Corresponds to variant rs28934607 [ dbSNP | Ensembl ].
    VAR_016958
    Natural varianti389 – 3891R → C in VDDR1A; complete loss of activity. 1 Publication
    VAR_016968
    Natural varianti389 – 3891R → G in VDDR1A; complete loss of activity. 1 Publication
    VAR_016960
    Natural varianti389 – 3891R → H in VDDR1A; complete loss of activity. 2 Publications
    VAR_016959
    Natural varianti409 – 4091T → I in VDDR1A. 2 Publications
    VAR_016961
    Natural varianti429 – 4291R → P in VDDR1A. 1 Publication
    VAR_016971
    Natural varianti453 – 4531R → C in VDDR1A. 1 Publication
    VAR_016972
    Natural varianti478 – 4781V → G in VDDR1A. 1 Publication
    VAR_016973
    Natural varianti497 – 4971P → R in VDDR1A. 1 Publication
    VAR_016974

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi264700. phenotype.
    Orphaneti289157. Hypocalcemic vitamin D-dependent rickets.
    PharmGKBiPA27099.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 50825-hydroxyvitamin D-1 alpha hydroxylase, mitochondrialPRO_0000003622
    Transit peptidei1 – ?MitochondrionSequence Analysis

    Proteomic databases

    PaxDbiO15528.
    PRIDEiO15528.

    PTM databases

    PhosphoSiteiO15528.

    Expressioni

    Tissue specificityi

    Kidney.

    Gene expression databases

    ArrayExpressiO15528.
    BgeeiO15528.
    CleanExiHS_CYP27B1.
    GenevestigatoriO15528.

    Organism-specific databases

    HPAiHPA043358.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000228606.

    Structurei

    3D structure databases

    ProteinModelPortaliO15528.
    SMRiO15528. Positions 35-505.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cytochrome P450 family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG2124.
    HOGENOMiHOG000253961.
    HOVERGENiHBG106909.
    InParanoidiO15528.
    KOiK07438.
    OMAiLHSEITA.
    OrthoDBiEOG7ZGX4B.
    PhylomeDBiO15528.
    TreeFamiTF105094.

    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]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O15528-1 [UniParc]FASTAAdd to Basket

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    MTQTLKYASR VFHRVRWAPE LGASLGYREY HSARRSLADI PGPSTPSFLA    50
    ELFCKGGLSR LHELQVQGAA HFGPVWLASF GTVRTVYVAA PALVEELLRQ 100
    EGPRPERCSF SPWTEHRRCR QRACGLLTAE GEEWQRLRSL LAPLLLRPQA 150
    AARYAGTLNN VVCDLVRRLR RQRGRGTGPP ALVRDVAGEF YKFGLEGIAA 200
    VLLGSRLGCL EAQVPPDTET FIRAVGSVFV STLLTMAMPH WLRHLVPGPW 250
    GRLCRDWDQM FAFAQRHVER REAEAAMRNG GQPEKDLESG AHLTHFLFRE 300
    ELPAQSILGN VTELLLAGVD TVSNTLSWAL YELSRHPEVQ TALHSEITAA 350
    LSPGSSAYPS ATVLSQLPLL KAVVKEVLRL YPVVPGNSRV PDKDIHVGDY 400
    IIPKNTLVTL CHYATSRDPA QFPEPNSFRP ARWLGEGPTP HPFASLPFGF 450
    GKRSCMGRRL AELELQMALA QILTHFEVQP EPGAAPVRPK TRTVLVPERS 500
    INLQFLDR 508
    Length:508
    Mass (Da):56,504
    Last modified:January 1, 1998 - v1
    Checksum:i7F0611EFAD1B5C1C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti320 – 3201D → N in BAG37458. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti65 – 651Q → H in VDDR1A. 1 Publication
    VAR_016969
    Natural varianti107 – 1071R → H in VDDR1A; complete loss of activity. 1 Publication
    Corresponds to variant rs28934604 [ dbSNP | Ensembl ].
    VAR_016952
    Natural varianti125 – 1251G → E in VDDR1A; complete loss of activity. 1 Publication
    Corresponds to variant rs28934605 [ dbSNP | Ensembl ].
    VAR_016953
    Natural varianti166 – 1661V → L.1 Publication
    Corresponds to variant rs8176344 [ dbSNP | Ensembl ].
    VAR_018841
    Natural varianti189 – 1891E → G in VDDR1A; 22% of wild-type activity. 1 Publication
    VAR_016954
    Natural varianti189 – 1891E → K in VDDR1A; 11% of wild-type activity. 1 Publication
    VAR_016967
    Natural varianti321 – 3211T → R in VDDR1A; complete loss of activity. 1 Publication
    VAR_016955
    Natural varianti323 – 3231S → Y in VDDR1A. 1 Publication
    VAR_016970
    Natural varianti335 – 3351R → P in VDDR1A; complete loss of activity. 1 Publication
    Corresponds to variant rs28934606 [ dbSNP | Ensembl ].
    VAR_016956
    Natural varianti343 – 3431L → F in VDDR1A; 2.3% of wild-type activity. 1 Publication
    VAR_016957
    Natural varianti382 – 3821P → S in VDDR1A; complete loss of activity. 1 Publication
    Corresponds to variant rs28934607 [ dbSNP | Ensembl ].
    VAR_016958
    Natural varianti389 – 3891R → C in VDDR1A; complete loss of activity. 1 Publication
    VAR_016968
    Natural varianti389 – 3891R → G in VDDR1A; complete loss of activity. 1 Publication
    VAR_016960
    Natural varianti389 – 3891R → H in VDDR1A; complete loss of activity. 2 Publications
    VAR_016959
    Natural varianti409 – 4091T → I in VDDR1A. 2 Publications
    VAR_016961
    Natural varianti429 – 4291R → P in VDDR1A. 1 Publication
    VAR_016971
    Natural varianti453 – 4531R → C in VDDR1A. 1 Publication
    VAR_016972
    Natural varianti478 – 4781V → G in VDDR1A. 1 Publication
    VAR_016973
    Natural varianti497 – 4971P → R in VDDR1A. 1 Publication
    VAR_016974

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF027152 Genomic DNA. Translation: AAC51854.1.
    AB005038 mRNA. Translation: BAA23416.1.
    AB005989 mRNA. Translation: BAA22656.1.
    AB005990 Genomic DNA. Translation: BAA22657.1.
    AB006987 Genomic DNA. Translation: BAA23418.1.
    AF020192 mRNA. Translation: AAC51853.1.
    AF256213 Genomic DNA. Translation: AAG00416.1.
    AF246895 mRNA. Translation: AAF64299.1.
    AY288916 Genomic DNA. Translation: AAP31972.1.
    AK314953 mRNA. Translation: BAG37458.1.
    CH471054 Genomic DNA. Translation: EAW97067.1.
    BC136386 mRNA. Translation: AAI36387.1.
    CCDSiCCDS8954.1.
    PIRiJC5713.
    RefSeqiNP_000776.1. NM_000785.3.
    UniGeneiHs.524528.

    Genome annotation databases

    EnsembliENST00000228606; ENSP00000228606; ENSG00000111012.
    GeneIDi1594.
    KEGGihsa:1594.
    UCSCiuc001spz.1. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF027152 Genomic DNA. Translation: AAC51854.1 .
    AB005038 mRNA. Translation: BAA23416.1 .
    AB005989 mRNA. Translation: BAA22656.1 .
    AB005990 Genomic DNA. Translation: BAA22657.1 .
    AB006987 Genomic DNA. Translation: BAA23418.1 .
    AF020192 mRNA. Translation: AAC51853.1 .
    AF256213 Genomic DNA. Translation: AAG00416.1 .
    AF246895 mRNA. Translation: AAF64299.1 .
    AY288916 Genomic DNA. Translation: AAP31972.1 .
    AK314953 mRNA. Translation: BAG37458.1 .
    CH471054 Genomic DNA. Translation: EAW97067.1 .
    BC136386 mRNA. Translation: AAI36387.1 .
    CCDSi CCDS8954.1.
    PIRi JC5713.
    RefSeqi NP_000776.1. NM_000785.3.
    UniGenei Hs.524528.

    3D structure databases

    ProteinModelPortali O15528.
    SMRi O15528. Positions 35-505.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000228606.

    Chemistry

    BindingDBi O15528.
    ChEMBLi CHEMBL5993.
    DrugBanki DB00146. Calcidiol.
    DB00136. Calcitriol.
    DB00153. Ergocalciferol.

    PTM databases

    PhosphoSitei O15528.

    Proteomic databases

    PaxDbi O15528.
    PRIDEi O15528.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000228606 ; ENSP00000228606 ; ENSG00000111012 .
    GeneIDi 1594.
    KEGGi hsa:1594.
    UCSCi uc001spz.1. human.

    Organism-specific databases

    CTDi 1594.
    GeneCardsi GC12M058156.
    H-InvDB HIX0171662.
    HGNCi HGNC:2606. CYP27B1.
    HPAi HPA043358.
    MIMi 264700. phenotype.
    609506. gene.
    neXtProti NX_O15528.
    Orphaneti 289157. Hypocalcemic vitamin D-dependent rickets.
    PharmGKBi PA27099.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2124.
    HOGENOMi HOG000253961.
    HOVERGENi HBG106909.
    InParanoidi O15528.
    KOi K07438.
    OMAi LHSEITA.
    OrthoDBi EOG7ZGX4B.
    PhylomeDBi O15528.
    TreeFami TF105094.

    Enzyme and pathway databases

    UniPathwayi UPA00955 .
    BRENDAi 1.14.13.13. 2681.
    Reactomei REACT_13450. Vitamins.
    REACT_13523. Vitamin D (calciferol) metabolism.

    Miscellaneous databases

    GeneWikii 25-Hydroxyvitamin_D3_1-alpha-hydroxylase.
    GenomeRNAii 1594.
    NextBioi 35468145.
    PROi O15528.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O15528.
    Bgeei O15528.
    CleanExi HS_CYP27B1.
    Genevestigatori O15528.

    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. "Complete structure of the human gene for the vitamin D 1alpha-hydroxylase, P450c1alpha."
      Fu G.K., Portale A.P., Miller W.L.
      DNA Cell Biol. 16:1499-1507(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Molecular cloning of cDNA and genomic DNA for human 25-hydroxyvitamin D3 1 alpha-hydroxylase."
      Monkawa T., Yoshida T., Wakino S., Shinki T., Anazawa H., Deluca H.F., Suda T., Hayashi M., Saruta T.
      Biochem. Biophys. Res. Commun. 239:527-533(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Tissue: Kidney.
    3. "Cloning of human 25-hydroxyvitamin D-1 alpha-hydroxylase and mutations causing vitamin D-dependent rickets type 1."
      Fu G.K., Lin D., Zhang Y.H., Bikle D.D., Shackleton C.H., Miller W.L., Portale A.A.
      Mol. Endocrinol. 11:1961-1970(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Targeted disruption of the 25-hydroxyvitamin D3 1alpha-hydroxylase gene in ras-transformed keratinocytes demonstrates that locally produced 1alpha,25-dihydroxyvitamin D3 suppresses growth and induces differentiation in an autocrine fashion."
      Huang D.C., Papavasiliou V., Rhim J.S., Horst R.L., Kremer R.
      Mol. Cancer Res. 1:56-67(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Targeted disruption of the 25-hydroxyvitamin D3 1 a-hydroxylase gene in a Ras-transformed human keratinocyte cell line: evidence for an autocrine growth regulatory function of 1 alpha, 25-dihydroxyvitamin D3 in vitro and in vivo."
      Huang D.C., Papavasiliou J., Rhim J., Kremer R.
      Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    6. NIEHS SNPs program
      Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-166.
    7. "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: Kidney.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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].
    10. "Inactivating mutations in the 25-hydroxyvitamin D3 1alpha-hydroxylase gene in patients with pseudovitamin D-deficiency rickets."
      Kitanaka S., Takeyama K., Murayama A., Sato T., Okumura K., Nogami M., Hasegawa Y., Niimi H., Yanagisawa J., Tanaka T., Kato S.
      N. Engl. J. Med. 338:653-661(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS VDDR1A HIS-107; GLU-125; PRO-335 AND SER-382.
    11. "Genetics of vitamin D 1-alpha-hydroxylase deficiency in 17 families."
      Wang J.T., Lin C.-J., Burridge S.M., Fu G.K., Labuda M., Portale A.A., Miller W.L.
      Am. J. Hum. Genet. 63:1694-1702(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS VDDR1A HIS-65; LYS-189; HIS-389; ILE-409; PRO-429; CYS-453 AND ARG-497.
    12. "Novel mutations in the 1alpha-hydroxylase (P450c1) gene in three families with pseudovitamin D-deficiency rickets resulting in loss of functional enzyme activity in blood-derived macrophages."
      Smith S.J., Rucka A.K., Berry J.L., Davies M., Mylchreest S., Paterson C.R., Heath D.A., Tassabehji M., Read A.P., Mee A.P., Mawer E.B.
      J. Bone Miner. Res. 14:730-739(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS VDDR1A TYR-323 AND GLY-478.
    13. "No enzyme activity of 25-hydroxyvitamin D3 1alpha-hydroxylase gene product in pseudovitamin D deficiency rickets, including that with mild clinical manifestation."
      Kitanaka S., Murayama A., Sakaki T., Inouye K., Seino Y., Fukumoto S., Shima M., Yukizane S., Takayanagi M., Niimi H., Takeyama K., Kato S.
      J. Clin. Endocrinol. Metab. 84:4111-4117(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS VDDR1A ARG-321 AND CYS-389.
    14. "Novel gene mutations in patients with 1alpha-hydroxylase deficiency that confer partial enzyme activity in vitro."
      Wang X., Zhang M.Y., Miller W.L., Portale A.A.
      J. Clin. Endocrinol. Metab. 87:2424-2430(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS VDDR1A GLY-189; PHE-343; GLY-389; HIS-389 AND ILE-409.

    Entry informationi

    Entry nameiCP27B_HUMAN
    AccessioniPrimary (citable) accession number: O15528
    Secondary accession number(s): B2RC61, Q548T3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 140 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3