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P11473 (VDR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 181. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vitamin D3 receptor

Short name=VDR
Alternative name(s):
1,25-dihydroxyvitamin D3 receptor
Nuclear receptor subfamily 1 group I member 1
Gene names
Name:VDR
Synonyms:NR1I1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length427 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.15 Ref.17 Ref.22 Ref.23

Subunit structure

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. Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.19 Ref.21 Ref.22

Subcellular location

Nucleus.

Domain

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

Polymorphism

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

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33

Sequence similarities

Belongs to the nuclear hormone receptor family. NR1 subfamily.

Contains 1 nuclear receptor DNA-binding domain.

Caution

It is uncertain whether Met-1 or Met-4 is the initiator.

Sequence caution

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.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionReceptor
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbile acid signaling pathway

Inferred from direct assay PubMed 12016314. Source: UniProtKB

calcium ion transport

Inferred from electronic annotation. Source: Ensembl

cell morphogenesis

Inferred from mutant phenotype PubMed 17223341. Source: UniProtKB

cellular calcium ion homeostasis

Inferred from electronic annotation. Source: Ensembl

decidualization

Inferred from expression pattern PubMed 16720713. Source: BHF-UCL

gene expression

Traceable author statement. Source: Reactome

intestinal absorption

Inferred from electronic annotation. Source: Ensembl

lactation

Inferred from electronic annotation. Source: Ensembl

mammary gland branching involved in pregnancy

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from direct assay PubMed 16549446. Source: BHF-UCL

negative regulation of keratinocyte proliferation

Inferred from mutant phenotype PubMed 17223341. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 17426122. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 11891224. Source: MGI

organ morphogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process involved in mammary gland involution

Inferred from electronic annotation. Source: Ensembl

positive regulation of gene expression

Inferred from mutant phenotype PubMed 17223341. Source: UniProtKB

positive regulation of keratinocyte differentiation

Inferred from mutant phenotype PubMed 17082781. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 17082781PubMed 17254542. Source: UniProtKB

positive regulation of vitamin D 24-hydroxylase activity

Inferred from direct assay PubMed 16549446. Source: BHF-UCL

regulation of calcidiol 1-monooxygenase activity

Inferred from sequence or structural similarity. Source: BHF-UCL

signal transduction

Traceable author statement Ref.24. Source: ProtInc

skeletal system development

Inferred from electronic annotation. Source: Ensembl

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

vitamin D receptor signaling pathway

Inferred from direct assay PubMed 16549446. Source: BHF-UCL

   Cellular_componentnucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 17082781. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from direct assay PubMed 11891224. Source: MGI

calcitriol binding

Inferred from direct assay Ref.17PubMed 12016314. Source: UniProtKB

calcitriol receptor activity

Inferred from direct assay PubMed 12016314PubMed 17082781. Source: UniProtKB

lithocholic acid binding

Inferred from direct assay PubMed 12016314. Source: UniProtKB

lithocholic acid receptor activity

Inferred from direct assay PubMed 12016314. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 10409738PubMed 10744685Ref.15PubMed 17254542PubMed 20413580PubMed 9653119. Source: UniProtKB

retinoid X receptor binding

Inferred from physical interaction PubMed 17426122. Source: BHF-UCL

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

steroid hormone receptor activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P11473-1)

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.
Isoform 2 (identifier: P11473-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEWRNKKRSDWLSMVLRTAGVEEAFGSEVSVRPHRRAPLGSTYLPPAPSGM
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 427427Vitamin D3 receptor
PRO_0000053542

Regions

DNA binding21 – 9676Nuclear receptor
Zinc finger24 – 4421NR C4-type
Zinc finger60 – 8425NR C4-type
Region97 – 19195Hinge
Region192 – 427236Ligand-binding
Region227 – 23711Vitamin D3 binding
Region271 – 2788Vitamin D3 binding

Sites

Binding site1431Vitamin D3
Binding site3051Vitamin D3
Binding site3971Vitamin D3

Natural variations

Alternative sequence11M → MEWRNKKRSDWLSMVLRTAG VEEAFGSEVSVRPHRRAPLG STYLPPAPSGM in isoform 2.
VSP_047218
Natural variant331G → D in VDDR2A. Ref.24
VAR_004656
Natural variant351H → Q in VDDR2A. Ref.25
VAR_004657
Natural variant451K → E in VDDR2A. Ref.30
VAR_004658
Natural variant461G → D in VDDR2A. Ref.31
VAR_004659
Natural variant471F → I in VDDR2A. Ref.30
VAR_004660
Natural variant501R → Q in VDDR2A. Ref.26
VAR_004661
Natural variant731R → Q in VDDR2A. Ref.24
VAR_004662
Natural variant801R → Q in VDDR2A. Ref.27 Ref.28
VAR_004663
Natural variant2301L → V. Ref.5
Corresponds to variant rs11574090 [ dbSNP | Ensembl ].
VAR_029309
Natural variant2741R → L in VDDR2A; decreases affinity for ligand by a factor of 1000. Ref.29
VAR_004664
Natural variant3051H → Q in VDDR2A. Ref.33
VAR_004665
Natural variant3141I → S in VDDR2A. Ref.32
VAR_004666
Natural variant3621T → I. Ref.5
Corresponds to variant rs11574115 [ dbSNP | Ensembl ].
VAR_029310
Natural variant3911R → C in VDDR2A. Ref.32
VAR_004667

Experimental info

Mutagenesis61 – 622PF → AA: Promotes heterodimerization with RXRA; when associated with A-75.
Mutagenesis751H → A: Promotes heterodimerization with RXRA; when associated with A-61 and A-62. Ref.19

Secondary structure

.......................................................... 427
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: F95F300D042C4CB7

FASTA42748,289
        10         20         30         40         50         60 
MEAMAASTSL PDPGDFDRNV PRICGVCGDR ATGFHFNAMT CEGCKGFFRR SMKRKALFTC 

        70         80         90        100        110        120 
PFNGDCRITK DNRRHCQACR LKRCVDIGMM KEFILTDEEV QRKREMILKR KEEEALKDSL 

       130        140        150        160        170        180 
RPKLSEEQQR IIAILLDAHH KTYDPTYSDF CQFRPPVRVN DGGGSHPSRP NSRHTPSFSG 

       190        200        210        220        230        240 
DSSSSCSDHC ITSSDMMDSS SFSNLDLSEE DSDDPSVTLE LSQLSMLPHL ADLVSYSIQK 

       250        260        270        280        290        300 
VIGFAKMIPG FRDLTSEDQI VLLKSSAIEV IMLRSNESFT MDDMSWTCGN QDYKYRVSDV 

       310        320        330        340        350        360 
TKAGHSLELI EPLIKFQVGL KKLNLHEEEH VLLMAICIVS PDRPGVQDAA LIEAIQDRLS 

       370        380        390        400        410        420 
NTLQTYIRCR HPPPGSHLLY AKMIQKLADL RSLNEEHSKQ YRCLSFQPEC SMKLTPLVLE 


VFGNEIS 

« Hide

Isoform 2 [UniParc].

Checksum: 7E4B93646169F6A8
Show »

FASTA47753,883

References

« Hide 'large scale' references
[1]"Cloning and expression of full-length cDNA encoding human vitamin D receptor."
Baker A.R., McDonnell D.P., Hughes M., Crisp T.M., Mangelsdorf D.J., Haussler M.R., Pike J.W., Shine J., O'Malley B.W.
Proc. Natl. Acad. Sci. U.S.A. 85:3294-3298(1988) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Web resources

NIEHS-SNPs
SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS55820.1. [P11473-2]
CCDS8757.1. [P11473-1]
PIRA28200.
RefSeqNP_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]
UniGeneHs.524368.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
DisProtDP00184.
ProteinModelPortalP11473.
SMRP11473. Positions 21-425.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113264. 95 interactions.
DIPDIP-32624N.
IntActP11473. 19 interactions.
MINTMINT-236408.
STRING9606.ENSP00000229022.

Chemistry

BindingDBP11473.
ChEMBLCHEMBL1977.
DrugBankDB00146. Calcidiol.
DB02300. Calcipotriol.
DB00136. Calcitriol.
DB01070. Dihydrotachysterol.
DB00153. Ergocalciferol.
DB00910. Paricalcitol.
GuidetoPHARMACOLOGY605.

PTM databases

PhosphoSiteP11473.

Polymorphism databases

DMDM137617.

Proteomic databases

MaxQBP11473.
PaxDbP11473.
PRIDEP11473.

Protocols and materials databases

DNASU7421.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000229022; ENSP00000229022; ENSG00000111424. [P11473-1]
ENST00000395324; ENSP00000378734; ENSG00000111424. [P11473-1]
ENST00000549336; ENSP00000449573; ENSG00000111424. [P11473-1]
ENST00000550325; ENSP00000447173; ENSG00000111424. [P11473-2]
GeneID7421.
KEGGhsa:7421.
UCSCuc001rql.3. human.
uc001rqm.3. human. [P11473-1]

Organism-specific databases

CTD7421.
GeneCardsGC12M048247.
HGNCHGNC:12679. VDR.
HPACAB004617.
HPA047740.
MIM277440. phenotype.
601769. gene.
607948. phenotype.
neXtProtNX_P11473.
Orphanet93160. Hypocalcemic vitamin D-resistant rickets.
PharmGKBPA37301.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG283526.
HOGENOMHOG000220844.
HOVERGENHBG108655.
InParanoidP11473.
KOK08539.
OMAFCQFRPP.
PhylomeDBP11473.
TreeFamTF316304.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.
SignaLinkP11473.

Gene expression databases

ArrayExpressP11473.
BgeeP11473.
CleanExHS_VDR.
GenevestigatorP11473.

Family and domain databases

Gene3D1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProIPR008946. 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]
PfamPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSPR00398. STRDHORMONER.
PR00047. STROIDFINGER.
PR00350. VITAMINDR.
SMARTSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMSSF48508. SSF48508. 1 hit.
PROSITEPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSVDR. human.
EvolutionaryTraceP11473.
GeneWikiCalcitriol_receptor.
GenomeRNAi7421.
NextBio29054.
PROP11473.
SOURCESearch...

Entry information

Entry nameVDR_HUMAN
AccessionPrimary (citable) accession number: P11473
Secondary accession number(s): B2R5Q1, G3V1V9, Q5PSV3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: July 9, 2014
This is version 181 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM