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P11473

- VDR_HUMAN

UniProt

P11473 - VDR_HUMAN

Protein

Vitamin D3 receptor

Gene

VDR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 183 (01 Oct 2014)
      Sequence version 1 (01 Oct 1989)
      Previous versions | rss
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    Functioni

    Nuclear hormone receptor. Transcription factor that mediates the action of vitamin D3 by controlling the expression of hormone sensitive genes. Regulates transcription of hormone sensitive genes via its association with the WINAC complex, a chromatin-remodeling complex. Recruited to promoters via its interaction with the WINAC complex subunit BAZ1B/WSTF, which mediates the interaction with acetylated histones, an essential step for VDR-promoter association. Plays a central role in calcium homeostasis.4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei143 – 1431Vitamin D3
    Binding sitei305 – 3051Vitamin D3
    Binding sitei397 – 3971Vitamin D3

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi21 – 9676Nuclear receptorPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri24 – 4421NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri60 – 8425NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. calcitriol binding Source: UniProtKB
    2. calcitriol receptor activity Source: UniProtKB
    3. DNA binding Source: MGI
    4. lithocholic acid binding Source: UniProtKB
    5. lithocholic acid receptor activity Source: UniProtKB
    6. protein binding Source: UniProtKB
    7. retinoid X receptor binding Source: BHF-UCL
    8. sequence-specific DNA binding Source: InterPro
    9. steroid hormone receptor activity Source: InterPro
    10. zinc ion binding Source: InterPro

    GO - Biological processi

    1. bile acid signaling pathway Source: UniProtKB
    2. calcium ion transport Source: Ensembl
    3. cell morphogenesis Source: UniProtKB
    4. cellular calcium ion homeostasis Source: Ensembl
    5. decidualization Source: BHF-UCL
    6. gene expression Source: Reactome
    7. intestinal absorption Source: Ensembl
    8. lactation Source: Ensembl
    9. mammary gland branching involved in pregnancy Source: Ensembl
    10. negative regulation of cell proliferation Source: BHF-UCL
    11. negative regulation of keratinocyte proliferation Source: UniProtKB
    12. negative regulation of transcription, DNA-templated Source: MGI
    13. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    14. organ morphogenesis Source: Ensembl
    15. positive regulation of apoptotic process involved in mammary gland involution Source: Ensembl
    16. positive regulation of gene expression Source: UniProtKB
    17. positive regulation of keratinocyte differentiation Source: UniProtKB
    18. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    19. positive regulation of vitamin D 24-hydroxylase activity Source: BHF-UCL
    20. regulation of calcidiol 1-monooxygenase activity Source: BHF-UCL
    21. signal transduction Source: ProtInc
    22. skeletal system development Source: Ensembl
    23. transcription initiation from RNA polymerase II promoter Source: Reactome
    24. vitamin D receptor signaling pathway Source: BHF-UCL

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_15525. Nuclear Receptor transcription pathway.
    SignaLinkiP11473.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Vitamin D3 receptor
    Short name:
    VDR
    Alternative name(s):
    1,25-dihydroxyvitamin D3 receptor
    Nuclear receptor subfamily 1 group I member 1
    Gene namesi
    Name:VDR
    Synonyms:NR1I1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:12679. VDR.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Rickets vitamin D-dependent 2A (VDDR2A) [MIM:277440]: A disorder of vitamin D metabolism resulting in severe rickets, hypocalcemia and secondary hyperparathyroidism. Most patients have total alopecia in addition to rickets.10 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti33 – 331G → D in VDDR2A. 1 Publication
    VAR_004656
    Natural varianti35 – 351H → Q in VDDR2A. 1 Publication
    VAR_004657
    Natural varianti45 – 451K → E in VDDR2A. 1 Publication
    VAR_004658
    Natural varianti46 – 461G → D in VDDR2A. 1 Publication
    VAR_004659
    Natural varianti47 – 471F → I in VDDR2A. 1 Publication
    VAR_004660
    Natural varianti50 – 501R → Q in VDDR2A. 1 Publication
    VAR_004661
    Natural varianti73 – 731R → Q in VDDR2A. 1 Publication
    VAR_004662
    Natural varianti80 – 801R → Q in VDDR2A. 2 Publications
    VAR_004663
    Natural varianti274 – 2741R → L in VDDR2A; decreases affinity for ligand by a factor of 1000. 1 Publication
    VAR_004664
    Natural varianti305 – 3051H → Q in VDDR2A. 1 Publication
    VAR_004665
    Natural varianti314 – 3141I → S in VDDR2A. 1 Publication
    VAR_004666
    Natural varianti391 – 3911R → C in VDDR2A. 1 Publication
    VAR_004667

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi61 – 622PF → AA: Promotes heterodimerization with RXRA; when associated with A-75.
    Mutagenesisi75 – 751H → A: Promotes heterodimerization with RXRA; when associated with A-61 and A-62. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi277440. phenotype.
    607948. phenotype.
    Orphaneti93160. Hypocalcemic vitamin D-resistant rickets.
    PharmGKBiPA37301.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 427427Vitamin D3 receptorPRO_0000053542Add
    BLAST

    Proteomic databases

    MaxQBiP11473.
    PaxDbiP11473.
    PRIDEiP11473.

    PTM databases

    PhosphoSiteiP11473.

    Expressioni

    Gene expression databases

    ArrayExpressiP11473.
    BgeeiP11473.
    CleanExiHS_VDR.
    GenevestigatoriP11473.

    Organism-specific databases

    HPAiCAB004617.
    HPA047740.

    Interactioni

    Subunit structurei

    Homodimer in the absence of bound vitamin D3. Heterodimer with RXRA after vitamin D3 binding. Interacts with SMAD3. Interacts with MED1, NCOA1, NCOA2, NCOA3 and NCOA6 coactivators, leading to a strong increase of transcription of target genes. Interacts (in a ligand-dependent manner) with BAZ1B/WSTF. Interacts with SNW1. Interacts with IRX4, the interaction doesn't affect its transactivation activity.9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EP300Q094723EBI-286357,EBI-447295
    Ncoa6Q9JLI42EBI-286357,EBI-286271From a different organism.
    PTPN3P260454EBI-286357,EBI-1047946
    SNW1Q135735EBI-286357,EBI-632715
    TP53P046376EBI-286357,EBI-366083

    Protein-protein interaction databases

    BioGridi113264. 95 interactions.
    DIPiDIP-32624N.
    IntActiP11473. 19 interactions.
    MINTiMINT-236408.
    STRINGi9606.ENSP00000229022.

    Structurei

    Secondary structure

    1
    427
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni25 – 273
    Beta strandi33 – 353
    Beta strandi38 – 403
    Helixi42 – 5312
    Beta strandi61 – 644
    Turni70 – 756
    Helixi77 – 8610
    Helixi91 – 933
    Helixi97 – 10711
    Beta strandi108 – 1103
    Turni111 – 1133
    Helixi126 – 14217
    Helixi150 – 1523
    Helixi217 – 2237
    Helixi227 – 24721
    Helixi251 – 2533
    Helixi256 – 27419
    Helixi275 – 2773
    Turni281 – 2844
    Beta strandi285 – 2873
    Helixi291 – 2933
    Helixi297 – 3015
    Turni302 – 3043
    Helixi307 – 32115
    Turni322 – 3243
    Helixi327 – 33812
    Beta strandi341 – 3433
    Helixi349 – 37022
    Turni373 – 3786
    Helixi379 – 40426
    Helixi410 – 4134
    Helixi416 – 4227

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DB1X-ray1.80A118-427[»]
    1IE8X-ray1.52A118-427[»]
    1IE9X-ray1.40A118-427[»]
    1KB2X-ray2.70A/B16-125[»]
    1KB4X-ray2.80A/B16-125[»]
    1KB6X-ray2.70A/B16-125[»]
    1S0ZX-ray2.50A118-427[»]
    1S19X-ray2.10A118-427[»]
    1TXIX-ray1.90A118-427[»]
    1YNWX-ray3.00A16-125[»]
    2HAMX-ray1.90A118-427[»]
    2HARX-ray1.90A118-427[»]
    2HASX-ray1.96A118-427[»]
    2HB7X-ray1.80A118-427[»]
    2HB8X-ray2.00A118-427[»]
    3A2IX-ray3.27A118-427[»]
    3A2JX-ray2.70A118-427[»]
    3A3ZX-ray1.72X118-427[»]
    3A40X-ray1.45X118-427[»]
    3A78X-ray1.90A118-427[»]
    3AUQX-ray2.64A118-427[»]
    3AURX-ray2.21A118-427[»]
    3AX8X-ray2.60A118-427[»]
    3AZ1X-ray1.50A120-423[»]
    3AZ2X-ray1.69A120-423[»]
    3AZ3X-ray1.36A120-423[»]
    3B0TX-ray1.30A120-423[»]
    3CS4X-ray2.00A118-427[»]
    3CS6X-ray1.80A118-427[»]
    3KPZX-ray1.90A118-427[»]
    3M7RX-ray1.80A120-423[»]
    3OGTX-ray1.75A118-427[»]
    3P8XX-ray1.70A118-164[»]
    A217-427[»]
    3TKCX-ray1.75A118-427[»]
    3VHWX-ray2.43A118-427[»]
    3W0AX-ray1.80A120-423[»]
    3W0CX-ray1.90A120-423[»]
    3W0YX-ray1.98A120-423[»]
    4G2IX-ray1.80A118-427[»]
    4ITEX-ray2.49A118-427[»]
    4ITFX-ray2.84A118-427[»]
    DisProtiDP00184.
    ProteinModelPortaliP11473.
    SMRiP11473. Positions 21-425.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11473.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni97 – 19195HingeAdd
    BLAST
    Regioni192 – 427236Ligand-bindingAdd
    BLAST
    Regioni227 – 23711Vitamin D3 bindingAdd
    BLAST
    Regioni271 – 2788Vitamin D3 binding

    Domaini

    Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.

    Sequence similaritiesi

    Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri24 – 4421NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri60 – 8425NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG283526.
    HOGENOMiHOG000220844.
    HOVERGENiHBG108655.
    InParanoidiP11473.
    KOiK08539.
    OMAiFCQFRPP.
    PhylomeDBiP11473.
    TreeFamiTF316304.

    Family and domain databases

    Gene3Di1.10.565.10. 2 hits.
    3.30.50.10. 1 hit.
    InterProiIPR008946. Nucl_hormone_rcpt_ligand-bd.
    IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
    IPR001723. Str_hrmn_rcpt.
    IPR000324. VitD_rcpt.
    IPR001628. Znf_hrmn_rcpt.
    IPR013088. Znf_NHR/GATA.
    [Graphical view]
    PfamiPF00104. Hormone_recep. 1 hit.
    PF00105. zf-C4. 1 hit.
    [Graphical view]
    PRINTSiPR00398. STRDHORMONER.
    PR00047. STROIDFINGER.
    PR00350. VITAMINDR.
    SMARTiSM00430. HOLI. 1 hit.
    SM00399. ZnF_C4. 1 hit.
    [Graphical view]
    SUPFAMiSSF48508. SSF48508. 1 hit.
    PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
    PS51030. NUCLEAR_REC_DBD_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P11473-1) [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

    MEAMAASTSL PDPGDFDRNV PRICGVCGDR ATGFHFNAMT CEGCKGFFRR    50
    SMKRKALFTC PFNGDCRITK DNRRHCQACR LKRCVDIGMM KEFILTDEEV 100
    QRKREMILKR KEEEALKDSL RPKLSEEQQR IIAILLDAHH KTYDPTYSDF 150
    CQFRPPVRVN DGGGSHPSRP NSRHTPSFSG DSSSSCSDHC ITSSDMMDSS 200
    SFSNLDLSEE DSDDPSVTLE LSQLSMLPHL ADLVSYSIQK VIGFAKMIPG 250
    FRDLTSEDQI VLLKSSAIEV IMLRSNESFT MDDMSWTCGN QDYKYRVSDV 300
    TKAGHSLELI EPLIKFQVGL KKLNLHEEEH VLLMAICIVS PDRPGVQDAA 350
    LIEAIQDRLS NTLQTYIRCR HPPPGSHLLY AKMIQKLADL RSLNEEHSKQ 400
    YRCLSFQPEC SMKLTPLVLE VFGNEIS 427
    Length:427
    Mass (Da):48,289
    Last modified:October 1, 1989 - v1
    Checksum:iF95F300D042C4CB7
    GO
    Isoform 2 (identifier: P11473-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MEWRNKKRSDWLSMVLRTAGVEEAFGSEVSVRPHRRAPLGSTYLPPAPSGM

    Note: No experimental confirmation available.

    Show »
    Length:477
    Mass (Da):53,883
    Checksum:i7E4B93646169F6A8
    GO

    Sequence cautioni

    The sequence AAH60832.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAP88938.1 differs from that shown. Reason: Erroneous gene model prediction.

    Polymorphismi

    Genetic variations in VDR may determine Mycobacterium tuberculosis susceptibility [MIMi:607948].

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti33 – 331G → D in VDDR2A. 1 Publication
    VAR_004656
    Natural varianti35 – 351H → Q in VDDR2A. 1 Publication
    VAR_004657
    Natural varianti45 – 451K → E in VDDR2A. 1 Publication
    VAR_004658
    Natural varianti46 – 461G → D in VDDR2A. 1 Publication
    VAR_004659
    Natural varianti47 – 471F → I in VDDR2A. 1 Publication
    VAR_004660
    Natural varianti50 – 501R → Q in VDDR2A. 1 Publication
    VAR_004661
    Natural varianti73 – 731R → Q in VDDR2A. 1 Publication
    VAR_004662
    Natural varianti80 – 801R → Q in VDDR2A. 2 Publications
    VAR_004663
    Natural varianti230 – 2301L → V.1 Publication
    Corresponds to variant rs11574090 [ dbSNP | Ensembl ].
    VAR_029309
    Natural varianti274 – 2741R → L in VDDR2A; decreases affinity for ligand by a factor of 1000. 1 Publication
    VAR_004664
    Natural varianti305 – 3051H → Q in VDDR2A. 1 Publication
    VAR_004665
    Natural varianti314 – 3141I → S in VDDR2A. 1 Publication
    VAR_004666
    Natural varianti362 – 3621T → I.1 Publication
    Corresponds to variant rs11574115 [ dbSNP | Ensembl ].
    VAR_029310
    Natural varianti391 – 3911R → C in VDDR2A. 1 Publication
    VAR_004667

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MEWRNKKRSDWLSMVLRTAG VEEAFGSEVSVRPHRRAPLG STYLPPAPSGM in isoform 2. 1 PublicationVSP_047218

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03258 mRNA. Translation: AAA61273.1.
    X67482 mRNA. Translation: CAA47824.1.
    AF026260 mRNA. Translation: AAB95155.1.
    AB002168 Genomic DNA. Translation: BAA83389.1.
    AY342401 Genomic DNA. Translation: AAP88938.1. Sequence problems.
    AK312267 mRNA. Translation: BAG35198.1.
    AC004466 Genomic DNA. No translation available.
    AC121338 Genomic DNA. No translation available.
    CH471111 Genomic DNA. Translation: EAW57960.1.
    CH471111 Genomic DNA. Translation: EAW57961.1.
    BC060832 mRNA. Translation: AAH60832.1. Different initiation.
    M65208 mRNA. Translation: AAA61274.1.
    AY827087 Genomic DNA. Translation: AAV85448.1.
    CCDSiCCDS55820.1. [P11473-2]
    CCDS8757.1. [P11473-1]
    PIRiA28200.
    RefSeqiNP_000367.1. NM_000376.2. [P11473-1]
    NP_001017535.1. NM_001017535.1. [P11473-1]
    NP_001017536.1. NM_001017536.1. [P11473-2]
    XP_006719650.1. XM_006719587.1. [P11473-1]
    UniGeneiHs.524368.

    Genome annotation databases

    EnsembliENST00000229022; ENSP00000229022; ENSG00000111424. [P11473-1]
    ENST00000395324; ENSP00000378734; ENSG00000111424. [P11473-1]
    ENST00000549336; ENSP00000449573; ENSG00000111424. [P11473-1]
    ENST00000550325; ENSP00000447173; ENSG00000111424. [P11473-2]
    GeneIDi7421.
    KEGGihsa:7421.
    UCSCiuc001rql.3. human.
    uc001rqm.3. human. [P11473-1]

    Polymorphism databases

    DMDMi137617.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    SHMPD

    The Singapore human mutation and polymorphism database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03258 mRNA. Translation: AAA61273.1 .
    X67482 mRNA. Translation: CAA47824.1 .
    AF026260 mRNA. Translation: AAB95155.1 .
    AB002168 Genomic DNA. Translation: BAA83389.1 .
    AY342401 Genomic DNA. Translation: AAP88938.1 . Sequence problems.
    AK312267 mRNA. Translation: BAG35198.1 .
    AC004466 Genomic DNA. No translation available.
    AC121338 Genomic DNA. No translation available.
    CH471111 Genomic DNA. Translation: EAW57960.1 .
    CH471111 Genomic DNA. Translation: EAW57961.1 .
    BC060832 mRNA. Translation: AAH60832.1 . Different initiation.
    M65208 mRNA. Translation: AAA61274.1 .
    AY827087 Genomic DNA. Translation: AAV85448.1 .
    CCDSi CCDS55820.1. [P11473-2 ]
    CCDS8757.1. [P11473-1 ]
    PIRi A28200.
    RefSeqi NP_000367.1. NM_000376.2. [P11473-1 ]
    NP_001017535.1. NM_001017535.1. [P11473-1 ]
    NP_001017536.1. NM_001017536.1. [P11473-2 ]
    XP_006719650.1. XM_006719587.1. [P11473-1 ]
    UniGenei Hs.524368.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DB1 X-ray 1.80 A 118-427 [» ]
    1IE8 X-ray 1.52 A 118-427 [» ]
    1IE9 X-ray 1.40 A 118-427 [» ]
    1KB2 X-ray 2.70 A/B 16-125 [» ]
    1KB4 X-ray 2.80 A/B 16-125 [» ]
    1KB6 X-ray 2.70 A/B 16-125 [» ]
    1S0Z X-ray 2.50 A 118-427 [» ]
    1S19 X-ray 2.10 A 118-427 [» ]
    1TXI X-ray 1.90 A 118-427 [» ]
    1YNW X-ray 3.00 A 16-125 [» ]
    2HAM X-ray 1.90 A 118-427 [» ]
    2HAR X-ray 1.90 A 118-427 [» ]
    2HAS X-ray 1.96 A 118-427 [» ]
    2HB7 X-ray 1.80 A 118-427 [» ]
    2HB8 X-ray 2.00 A 118-427 [» ]
    3A2I X-ray 3.27 A 118-427 [» ]
    3A2J X-ray 2.70 A 118-427 [» ]
    3A3Z X-ray 1.72 X 118-427 [» ]
    3A40 X-ray 1.45 X 118-427 [» ]
    3A78 X-ray 1.90 A 118-427 [» ]
    3AUQ X-ray 2.64 A 118-427 [» ]
    3AUR X-ray 2.21 A 118-427 [» ]
    3AX8 X-ray 2.60 A 118-427 [» ]
    3AZ1 X-ray 1.50 A 120-423 [» ]
    3AZ2 X-ray 1.69 A 120-423 [» ]
    3AZ3 X-ray 1.36 A 120-423 [» ]
    3B0T X-ray 1.30 A 120-423 [» ]
    3CS4 X-ray 2.00 A 118-427 [» ]
    3CS6 X-ray 1.80 A 118-427 [» ]
    3KPZ X-ray 1.90 A 118-427 [» ]
    3M7R X-ray 1.80 A 120-423 [» ]
    3OGT X-ray 1.75 A 118-427 [» ]
    3P8X X-ray 1.70 A 118-164 [» ]
    A 217-427 [» ]
    3TKC X-ray 1.75 A 118-427 [» ]
    3VHW X-ray 2.43 A 118-427 [» ]
    3W0A X-ray 1.80 A 120-423 [» ]
    3W0C X-ray 1.90 A 120-423 [» ]
    3W0Y X-ray 1.98 A 120-423 [» ]
    4G2I X-ray 1.80 A 118-427 [» ]
    4ITE X-ray 2.49 A 118-427 [» ]
    4ITF X-ray 2.84 A 118-427 [» ]
    DisProti DP00184.
    ProteinModelPortali P11473.
    SMRi P11473. Positions 21-425.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113264. 95 interactions.
    DIPi DIP-32624N.
    IntActi P11473. 19 interactions.
    MINTi MINT-236408.
    STRINGi 9606.ENSP00000229022.

    Chemistry

    BindingDBi P11473.
    ChEMBLi CHEMBL1977.
    DrugBanki DB00146. Calcidiol.
    DB02300. Calcipotriol.
    DB00136. Calcitriol.
    DB01070. Dihydrotachysterol.
    DB00153. Ergocalciferol.
    DB00910. Paricalcitol.
    GuidetoPHARMACOLOGYi 605.

    PTM databases

    PhosphoSitei P11473.

    Polymorphism databases

    DMDMi 137617.

    Proteomic databases

    MaxQBi P11473.
    PaxDbi P11473.
    PRIDEi P11473.

    Protocols and materials databases

    DNASUi 7421.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000229022 ; ENSP00000229022 ; ENSG00000111424 . [P11473-1 ]
    ENST00000395324 ; ENSP00000378734 ; ENSG00000111424 . [P11473-1 ]
    ENST00000549336 ; ENSP00000449573 ; ENSG00000111424 . [P11473-1 ]
    ENST00000550325 ; ENSP00000447173 ; ENSG00000111424 . [P11473-2 ]
    GeneIDi 7421.
    KEGGi hsa:7421.
    UCSCi uc001rql.3. human.
    uc001rqm.3. human. [P11473-1 ]

    Organism-specific databases

    CTDi 7421.
    GeneCardsi GC12M048247.
    HGNCi HGNC:12679. VDR.
    HPAi CAB004617.
    HPA047740.
    MIMi 277440. phenotype.
    601769. gene.
    607948. phenotype.
    neXtProti NX_P11473.
    Orphaneti 93160. Hypocalcemic vitamin D-resistant rickets.
    PharmGKBi PA37301.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG283526.
    HOGENOMi HOG000220844.
    HOVERGENi HBG108655.
    InParanoidi P11473.
    KOi K08539.
    OMAi FCQFRPP.
    PhylomeDBi P11473.
    TreeFami TF316304.

    Enzyme and pathway databases

    Reactomei REACT_15525. Nuclear Receptor transcription pathway.
    SignaLinki P11473.

    Miscellaneous databases

    ChiTaRSi VDR. human.
    EvolutionaryTracei P11473.
    GeneWikii Calcitriol_receptor.
    GenomeRNAii 7421.
    NextBioi 29054.
    PROi P11473.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P11473.
    Bgeei P11473.
    CleanExi HS_VDR.
    Genevestigatori P11473.

    Family and domain databases

    Gene3Di 1.10.565.10. 2 hits.
    3.30.50.10. 1 hit.
    InterProi IPR008946. Nucl_hormone_rcpt_ligand-bd.
    IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
    IPR001723. Str_hrmn_rcpt.
    IPR000324. VitD_rcpt.
    IPR001628. Znf_hrmn_rcpt.
    IPR013088. Znf_NHR/GATA.
    [Graphical view ]
    Pfami PF00104. Hormone_recep. 1 hit.
    PF00105. zf-C4. 1 hit.
    [Graphical view ]
    PRINTSi PR00398. STRDHORMONER.
    PR00047. STROIDFINGER.
    PR00350. VITAMINDR.
    SMARTi SM00430. HOLI. 1 hit.
    SM00399. ZnF_C4. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48508. SSF48508. 1 hit.
    PROSITEi PS00031. NUCLEAR_REC_DBD_1. 1 hit.
    PS51030. NUCLEAR_REC_DBD_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "A single receptor identical with that from intestine/T47D cells mediates the action of 1,25-dihydroxyvitamin D-3 in HL-60 cells."
      Goto H., Chen K.S., Prahl J.M., Deluca H.F.
      Biochim. Biophys. Acta 1132:103-108(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. Rae J.L., Shepard A.R.
      Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Lens epithelium.
    4. "Structural organization of the human vitamin D receptor chromosomal gene and its promoter."
      Miyamoto K., Kesterson R.A., Yamamoto H., Taketani Y., Nishiwaki E., Tatsumi S., Inoue Y., Morita K., Takeda E., Pike J.W.
      Mol. Endocrinol. 11:1165-1179(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. NIEHS SNPs program
      Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-230 AND ILE-362.
    6. "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] (ISOFORM 1).
    7. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORM 2).
      Tissue: Placenta.
    10. "Vitamin D receptor expression in human lymphocytes. Signal requirements and characterization by western blots and DNA sequencing."
      Yu X.-P., Mocharla H., Hustmyer F.G., Manolagas S.C.
      J. Biol. Chem. 266:7588-7595(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 24-90 (ISOFORM 1/2).
      Tissue: Peripheral blood.
    11. "Promoter and 3'-untranslated-region haplotypes in the vitamin D receptor gene predispose to osteoporotic fracture: the Rotterdam study."
      Fang Y., van Meurs J.B., d'Alesio A., Jhamai M., Zhao H., Rivadeneira F., Hofman A., van Leeuwen J.P., Jehan F., Pols H.A., Uitterlinden A.G.
      Am. J. Hum. Genet. 77:807-823(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 343-427.
    12. "Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300."
      Chen H., Lin R.J., Schiltz R.L., Chakravarti D., Nash A., Nagy L., Privalsky M.L., Nakatani Y., Evans R.M.
      Cell 90:569-580(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NCOA3.
    13. "Isolation and characterization of a novel coactivator protein, NCoA-62, involved in vitamin D-mediated transcription."
      Baudino T.A., Kraichely D.M., Jefcoat S.C. Jr., Winchester S.K., Partridge N.C., Macdonald P.N.
      J. Biol. Chem. 273:16434-16441(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SNW1.
    14. "A new family of nuclear receptor coregulators that integrates nuclear receptor signaling through CBP."
      Mahajan M.A., Samuels H.H.
      Mol. Cell. Biol. 20:5048-5063(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NCOA6.
    15. "Ligand-induced transrepression by VDR through association of WSTF with acetylated histones."
      Fujiki R., Kim M.-S., Sasaki Y., Yoshimura K., Kitagawa H., Kato S.
      EMBO J. 24:3881-3894(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BAZ1B.
    16. "IRX4 at 5p15 suppresses prostate cancer growth through the interaction with vitamin D receptor, conferring prostate cancer susceptibility."
      Nguyen H.H., Takata R., Akamatsu S., Shigemizu D., Tsunoda T., Furihata M., Takahashi A., Kubo M., Kamatani N., Ogawa O., Fujioka T., Nakamura Y., Nakagawa H.
      Hum. Mol. Genet. 21:2076-2085(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IRX4.
      Tissue: Prostate.
    17. "The crystal structure of the nuclear receptor for vitamin D bound to its natural ligand."
      Rochel N., Wurtz J.-M., Mitschler A., Klaholz B., Moras D.
      Mol. Cell 5:173-179(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 118-427 IN COMPLEX WITH DIHYDROXYVITAMIN D3, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION.
    18. "Crystal structures of the vitamin D receptor complexed to superagonist 20-epi ligands."
      Tocchini-Valentini G., Rochel N., Wurtz J.-M., Mitschler A., Moras D.
      Proc. Natl. Acad. Sci. U.S.A. 98:5491-5496(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 118-427 IN COMPLEXES WITH VITAMIN D3 AND VITAMIN D3 ANALOGS.
    19. "Structural basis of VDR-DNA interactions on direct repeat response elements."
      Shaffer P.L., Gewirth D.T.
      EMBO J. 21:2242-2252(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 16-125 IN COMPLEX WITH DNA, MUTAGENESIS OF 61-PRO-PHE-62 AND HIS-75, SUBUNIT.
    20. "Crystal structures of the vitamin D nuclear receptor liganded with the vitamin D side chain analogues calcipotriol and seocalcitol, receptor agonists of clinical importance. Insights into a structural basis for the switching of calcipotriol to a receptor antagonist by further side chain modification."
      Tocchini-Valentini G., Rochel N., Wurtz J.-M., Moras D.
      J. Med. Chem. 47:1956-1961(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 188-427 IN COMPLEXES WITH VITAMIN D3 ANALOGS.
    21. "Structural analysis of RXR-VDR interactions on DR3 DNA."
      Shaffer P.L., Gewirth D.T.
      J. Steroid Biochem. Mol. Biol. 89:215-219(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 16-125 OF MUTANT ALA-61/ALA-62/ALA-75 IN COMPLEX WITH RXRA AND DNA, SUBUNIT.
    22. "Superagonistic action of 14-epi-analogs of 1,25-dihydroxyvitamin D explained by vitamin D receptor-coactivator interaction."
      Eelen G., Verlinden L., Rochel N., Claessens F., De Clercq P., Vandewalle M., Tocchini-Valentini G., Moras D., Bouillon R., Verstuyf A.
      Mol. Pharmacol. 67:1566-1573(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 188-427 IN COMPLEX WITH VITAMIN D3 ANALOG, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH NCOA1; NCOA2 AND MED1.
    23. "Probing a water channel near the A-ring of receptor-bound 1 alpha,25-dihydroxyvitamin D3 with selected 2 alpha-substituted analogues."
      Hourai S., Fujishima T., Kittaka A., Suhara Y., Takayama H., Rochel N., Moras D.
      J. Med. Chem. 49:5199-5205(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 188-427 IN COMPLEXES WITH DIHYDROXYVITAMIN D3 AND VITAMIN D3 ANALOGS, FUNCTION.
    24. "Point mutations in the human vitamin D receptor gene associated with hypocalcemic rickets."
      Hughes M.R., Malloy P.J., Kieback D.G., Kesterson R.A., Pike J.W., Feldman D., O'Malley B.W.
      Science 242:1702-1705(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS VDDR2A ASP-33 AND GLN-73.
    25. "A new point mutation in the deoxyribonucleic acid-binding domain of the vitamin D receptor in a kindred with hereditary 1,25-dihydroxyvitamin D-resistant rickets."
      Yagi H., Ozono K., Miyake H., Nagashima K., Kuroume T., Pike J.W.
      J. Clin. Endocrinol. Metab. 76:509-512(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VDDR2A GLN-35.
    26. "A unique mutation in the vitamin D receptor gene in three Japanese patients with vitamin D-dependent rickets type II: utility of single-strand conformation polymorphism analysis for heterozygous carrier detection."
      Saijo T., Ito M., Takeda E., Mahbubul Huq A.H.M., Naito E., Yokota I., Sone T., Pike J.W., Kuroda Y.
      Am. J. Hum. Genet. 49:668-673(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VDDR2A GLN-50.
    27. "A unique point mutation in the human vitamin D receptor chromosomal gene confers hereditary resistance to 1,25-dihydroxyvitamin D3."
      Sone T., Marx S.J., Liberman U.A., Pike J.W.
      Mol. Endocrinol. 4:623-631(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VDDR2A GLN-80.
    28. "Hereditary 1 alpha,25-dihydroxyvitamin D-resistant rickets resulting from a mutation in the vitamin D receptor deoxyribonucleic acid-binding domain."
      Malloy P.J., Weisman Y., Feldman D.
      J. Clin. Endocrinol. Metab. 78:313-316(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VDDR2A GLN-80.
    29. "Two mutations in the hormone binding domain of the vitamin D receptor cause tissue resistance to 1,25 dihydroxyvitamin D3."
      Kristjansson K., Rut A.R., Hewison M., O'Riordan J.L.H., Hughes M.R.
      J. Clin. Invest. 92:12-16(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VDDR2A LEU-274.
    30. "Two mutations causing vitamin D resistant rickets: modelling on the basis of steroid hormone receptor DNA-binding domain crystal structures."
      Rut A.R., Hewison M., Kristjansson K., Luisi B., Hughes M.R., O'Riordan J.L.H.
      Clin. Endocrinol. (Oxf.) 41:581-590(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS VDDR2A GLU-45 AND ILE-47.
    31. "A novel mutation in the deoxyribonucleic acid-binding domain of the vitamin D receptor causes hereditary 1,25-dihydroxyvitamin D-resistant rickets."
      Lin U.-T., Malloy P.J., Sakati N., Al-Ashwal A., Feldman D.
      J. Clin. Endocrinol. Metab. 81:2564-2569(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VDDR2A ASP-46.
    32. "Vitamin D receptors from patients with resistance to 1,25-dihydroxyvitamin D(3): point mutations confer reduced transactivation in response to ligand and impaired interaction with the retinoid X receptor heterodimeric partner."
      Whitfield G.K., Selznick S.H., Haussler C.A., Hsieh J.-C., Galligan M.A., Jurutka P.W., Thompson P.D., Lee S.M., Zerwekh J.E., Haussler M.R.
      Mol. Endocrinol. 10:1617-1631(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS VDDR2A SER-314 AND CYS-391.
    33. "Hereditary vitamin D resistant rickets caused by a novel mutation in the vitamin D receptor that results in decreased affinity for hormone and cellular hyporesponsiveness."
      Malloy P.J., Eccleshall T.R., Gross C., van Maldergem L., Bouillon R., Feldman D.
      J. Clin. Invest. 99:297-304(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VDDR2A GLN-305.
    34. "Vitamin D receptor gene variants of BsmI, ApaI, TaqI, and FokI polymorphisms in spinal tuberculosis."
      Selvaraj P., Kurian S.M., Chandra G., Reetha A.M., Charles N., Narayanan P.R.
      Clin. Genet. 65:73-76(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN MYCOBACTERIUM TUBERCULOSIS SUSCEPTIBILITY.

    Entry informationi

    Entry nameiVDR_HUMAN
    AccessioniPrimary (citable) accession number: P11473
    Secondary accession number(s): B2R5Q1, G3V1V9, Q5PSV3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: October 1, 1989
    Last modified: October 1, 2014
    This is version 183 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 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3