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Protein

Vitamin D3 receptor

Gene

VDR

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

Functioni

Nuclear receptor for calcitriol, the active form of vitamin D3 which mediates the action of this vitamin on cells. Enters the nucleus upon vitamin D3 binding where it forms heterodimers with the retinoid X receptor/RXR. The VDR-RXR heterodimers bind to specific response elements on DNA and activate the transcription of vitamin D3-responsive target genes. Recruited to promoters via its interaction with BAZ1B/WSTF which mediates the interaction with acetylated histones, an essential step for VDR-promoter association. Plays a central role in calcium homeostasis.5 Publications

Caution

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei143Vitamin D31
Binding sitei305Vitamin D31
Binding sitei397Vitamin D31

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi21 – 96Nuclear receptorPROSITE-ProRule annotationAdd BLAST76
Zinc fingeri24 – 44NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri60 – 84NR C4-typePROSITE-ProRule annotationAdd BLAST25

GO - Molecular functioni

  • calcitriol binding Source: UniProtKB
  • calcitriol receptor activity Source: UniProtKB
  • DNA binding Source: MGI
  • lithocholic acid binding Source: UniProtKB
  • lithocholic acid receptor activity Source: UniProtKB
  • retinoid X receptor binding Source: UniProtKB
  • RNA polymerase II transcription factor activity, sequence-specific DNA binding Source: NTNU_SB
  • sequence-specific DNA binding Source: InterPro
  • steroid hormone receptor activity Source: InterPro
  • zinc ion binding Source: InterPro

GO - Biological processi

  • bile acid signaling pathway Source: UniProtKB
  • calcium ion transport Source: Ensembl
  • cell morphogenesis Source: UniProtKB
  • cellular calcium ion homeostasis Source: Ensembl
  • decidualization Source: BHF-UCL
  • intestinal absorption Source: Ensembl
  • lactation Source: Ensembl
  • mammary gland branching involved in pregnancy Source: Ensembl
  • negative regulation of cell proliferation Source: BHF-UCL
  • negative regulation of keratinocyte proliferation Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: MGI
  • negative regulation of transcription by RNA polymerase II Source: BHF-UCL
  • positive regulation of apoptotic process involved in mammary gland involution Source: Ensembl
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of keratinocyte differentiation Source: UniProtKB
  • positive regulation of transcription by RNA polymerase II Source: UniProtKB
  • positive regulation of vitamin D 24-hydroxylase activity Source: BHF-UCL
  • regulation of calcidiol 1-monooxygenase activity Source: BHF-UCL
  • signal transduction Source: ProtInc
  • skeletal system development Source: Ensembl
  • transcription initiation from RNA polymerase II promoter Source: Reactome
  • vitamin D metabolic process Source: Reactome
  • vitamin D receptor signaling pathway Source: BHF-UCL

Keywordsi

Molecular functionDNA-binding, Receptor
Biological processTranscription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-196791 Vitamin D (calciferol) metabolism
R-HSA-383280 Nuclear Receptor transcription pathway
SignaLinkiP11473
SIGNORiP11473

Protein family/group databases

MoonDBiP11473 Predicted
TCDBi9.B.208.1.1 the vitamin d3 receptor (vdr) family

Chemistry databases

SwissLipidsiSLP:000001571

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
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

EuPathDBiHostDB:ENSG00000111424.10
HGNCiHGNC:12679 VDR
MIMi601769 gene
neXtProtiNX_P11473

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Rickets vitamin D-dependent 2A (VDDR2A)12 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder of vitamin D metabolism resulting in severe rickets, hypocalcemia and secondary hyperparathyroidism. Most patients have total alopecia in addition to rickets.
See also OMIM:277440
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00465633G → D in VDDR2A. 1 PublicationCorresponds to variant dbSNP:rs121909790EnsemblClinVar.1
Natural variantiVAR_00465735H → Q in VDDR2A. 1 Publication1
Natural variantiVAR_00465845K → E in VDDR2A. 1 Publication1
Natural variantiVAR_00465946G → D in VDDR2A. 1 PublicationCorresponds to variant dbSNP:rs121909797EnsemblClinVar.1
Natural variantiVAR_00466047F → I in VDDR2A. 1 Publication1
Natural variantiVAR_00466150R → Q in VDDR2A. 1 PublicationCorresponds to variant dbSNP:rs121909794EnsemblClinVar.1
Natural variantiVAR_00466273R → Q in VDDR2A. 1 PublicationCorresponds to variant dbSNP:rs121909791EnsemblClinVar.1
Natural variantiVAR_00466380R → Q in VDDR2A. 2 PublicationsCorresponds to variant dbSNP:rs121909793EnsemblClinVar.1
Natural variantiVAR_079325152 – 427Missing in VDDR2A; loss of calcitriol receptor activity; loss of affinity for calcitriol; no effect on ligand-independent localization to the nucleus. 2 PublicationsCorresponds to variant dbSNP:rs121909795Add BLAST276
Natural variantiVAR_004664274R → L in VDDR2A; loss of calcitriol receptor activity; decreased affinity for calcitriol by a factor of 1000; no effect on interaction with RXRA; changed interaction with NCOR1; loss of interaction with NCOA1; no effect on sequence-specific DNA-binding. 2 PublicationsCorresponds to variant dbSNP:rs121909796EnsemblClinVar.1
Natural variantiVAR_004665305H → Q in VDDR2A; loss of calcitriol receptor activity; no effect on interaction with RXRA; changed interaction with NCOR1; loss of interaction with NCOA1; no effect on sequence-specific DNA-binding. 2 PublicationsCorresponds to variant dbSNP:rs121909798EnsemblClinVar.1
Natural variantiVAR_004666314I → S in VDDR2A. 1 PublicationCorresponds to variant dbSNP:rs121909799EnsemblClinVar.1
Natural variantiVAR_079326346V → M in VDDR2A; decreased calcitriol receptor activity; decreased affinity for calcitriol; decreased ligand-independent localization to the nucleus; loss of interaction with RXRA; decreased interaction with NCOR1; decreased interaction with NCOA1; decreased sequence-specific DNA-binding. 2 PublicationsCorresponds to variant dbSNP:rs267607169EnsemblClinVar.1
Natural variantiVAR_079327360S → P in VDDR2A; loss of calcitriol receptor activity; loss of affinity for calcitriol; decreased ligand-independent localization to the nucleus; loss of interaction with RXRA; loss of interaction with NCOR1; loss of interaction with NCOA1; loss of sequence-specific DNA-binding. 1 Publication1
Natural variantiVAR_004667391R → C in VDDR2A. 1 PublicationCorresponds to variant dbSNP:rs121909800EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi61 – 62PF → AA: Promotes heterodimerization with RXRA; when associated with A-75. 1 Publication2
Mutagenesisi75H → A: Promotes heterodimerization with RXRA; when associated with A-61 and A-62. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi7421
MalaCardsiVDR
MIMi277440 phenotype
607948 phenotype
OpenTargetsiENSG00000111424
Orphaneti93160 Hypocalcemic vitamin D-resistant rickets
PharmGKBiPA37301

Chemistry databases

ChEMBLiCHEMBL1977
DrugBankiDB01436 Alfacalcidol
DB00146 Calcidiol
DB02300 Calcipotriol
DB00136 Calcitriol
DB00169 Cholecalciferol
DB05024 CTA018
DB01070 Dihydrotachysterol
DB06410 Doxercalciferol
DB05295 Eldecalcitol
DB00153 Ergocalciferol
DB04796 Inecalcitol
DB00910 Paricalcitol
DB04258 Seocalcitol
GuidetoPHARMACOLOGYi605

Polymorphism and mutation databases

BioMutaiVDR
DMDMi137617

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000535421 – 427Vitamin D3 receptorAdd BLAST427

Proteomic databases

MaxQBiP11473
PaxDbiP11473
PeptideAtlasiP11473
PRIDEiP11473
ProteomicsDBi52780

PTM databases

iPTMnetiP11473
PhosphoSitePlusiP11473

Expressioni

Gene expression databases

BgeeiENSG00000111424
CleanExiHS_VDR
ExpressionAtlasiP11473 baseline and differential
GenevisibleiP11473 HS

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 with the corepressor NCOR1. Interacts (in a ligand-dependent manner) with BAZ1B/WSTF. Interacts with SNW1. Interacts with IRX4, the interaction doesn't affect its transactivation activity.10 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • retinoid X receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi113264, 93 interactors
ComplexPortaliCPX-631 RXRalpha-VDR nuclear hormone receptor complex
CPX-871 RXRbeta-VDR nuclear hormone receptor complex
CORUMiP11473
DIPiDIP-32624N
ELMiP11473
IntActiP11473, 29 interactors
MINTiP11473
STRINGi9606.ENSP00000447173

Chemistry databases

BindingDBiP11473

Structurei

Secondary structure

1427
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni25 – 27Combined sources3
Beta strandi33 – 35Combined sources3
Beta strandi38 – 40Combined sources3
Helixi42 – 53Combined sources12
Beta strandi61 – 64Combined sources4
Turni70 – 75Combined sources6
Helixi77 – 86Combined sources10
Helixi91 – 93Combined sources3
Helixi97 – 107Combined sources11
Beta strandi108 – 110Combined sources3
Turni111 – 113Combined sources3
Helixi115 – 119Combined sources5
Helixi126 – 142Combined sources17
Helixi150 – 152Combined sources3
Turni162 – 164Combined sources3
Helixi217 – 223Combined sources7
Helixi227 – 247Combined sources21
Helixi251 – 253Combined sources3
Helixi256 – 274Combined sources19
Helixi275 – 277Combined sources3
Turni281 – 284Combined sources4
Beta strandi285 – 287Combined sources3
Helixi291 – 293Combined sources3
Helixi297 – 301Combined sources5
Turni302 – 304Combined sources3
Helixi307 – 321Combined sources15
Turni322 – 324Combined sources3
Helixi327 – 338Combined sources12
Beta strandi341 – 343Combined sources3
Helixi349 – 370Combined sources22
Turni373 – 378Combined sources6
Helixi379 – 404Combined sources26
Helixi410 – 413Combined sources4
Helixi416 – 422Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
3WGPX-ray2.00A120-423[»]
3WWRX-ray3.18A118-427[»]
3X31X-ray2.11A118-427[»]
3X36X-ray1.93A118-427[»]
4G2IX-ray1.80A118-427[»]
4ITEX-ray2.49A118-427[»]
4ITFX-ray2.84A118-427[»]
5GT4X-ray1.83A118-423[»]
5V39X-ray2.20A119-425[»]
5YSYX-ray2.00A118-423[»]
5YT2X-ray2.00A118-423[»]
DisProtiDP00184
ProteinModelPortaliP11473
SMRiP11473
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11473

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini127 – 423NR LBDPROSITE-ProRule annotationAdd BLAST297

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni97 – 126HingeAdd BLAST30
Regioni227 – 237Vitamin D3 bindingAdd BLAST11
Regioni271 – 278Vitamin D3 binding8

Domaini

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

Sequence similaritiesi

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri24 – 44NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri60 – 84NR C4-typePROSITE-ProRule annotationAdd BLAST25

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG3575 Eukaryota
ENOG410XRZC LUCA
GeneTreeiENSGT00870000136372
HOGENOMiHOG000220844
HOVERGENiHBG108655
InParanoidiP11473
KOiK08539
OMAiPECSMKL
OrthoDBiEOG091G05X3
PhylomeDBiP11473
TreeFamiTF316304

Family and domain databases

Gene3Di3.30.50.10, 1 hit
InterProiView protein in InterPro
IPR035500 NHR_like_dom_sf
IPR000536 Nucl_hrmn_rcpt_lig-bd
IPR001723 Nuclear_hrmn_rcpt
IPR000324 VitD_rcpt
IPR001628 Znf_hrmn_rcpt
IPR013088 Znf_NHR/GATA
PfamiView protein in Pfam
PF00104 Hormone_recep, 1 hit
PF00105 zf-C4, 1 hit
PRINTSiPR00398 STRDHORMONER
PR00047 STROIDFINGER
PR00350 VITAMINDR
SMARTiView protein in SMART
SM00430 HOLI, 1 hit
SM00399 ZnF_C4, 1 hit
SUPFAMiSSF48508 SSF48508, 1 hit
PROSITEiView protein in PROSITE
PS51843 NR_LBD, 1 hit
PS00031 NUCLEAR_REC_DBD_1, 1 hit
PS51030 NUCLEAR_REC_DBD_2, 1 hit

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

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

        10         20         30         40         50
MEAMAASTSL PDPGDFDRNV PRICGVCGDR ATGFHFNAMT CEGCKGFFRR
60 70 80 90 100
SMKRKALFTC PFNGDCRITK DNRRHCQACR LKRCVDIGMM KEFILTDEEV
110 120 130 140 150
QRKREMILKR KEEEALKDSL RPKLSEEQQR IIAILLDAHH KTYDPTYSDF
160 170 180 190 200
CQFRPPVRVN DGGGSHPSRP NSRHTPSFSG DSSSSCSDHC ITSSDMMDSS
210 220 230 240 250
SFSNLDLSEE DSDDPSVTLE LSQLSMLPHL ADLVSYSIQK VIGFAKMIPG
260 270 280 290 300
FRDLTSEDQI VLLKSSAIEV IMLRSNESFT MDDMSWTCGN QDYKYRVSDV
310 320 330 340 350
TKAGHSLELI EPLIKFQVGL KKLNLHEEEH VLLMAICIVS PDRPGVQDAA
360 370 380 390 400
LIEAIQDRLS NTLQTYIRCR HPPPGSHLLY AKMIQKLADL RSLNEEHSKQ
410 420
YRCLSFQPEC SMKLTPLVLE VFGNEIS
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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAP88938 differs from that shown. Reason: Erroneous gene model prediction.Curated

Polymorphismi

Genetic variations in VDR may determine Mycobacterium tuberculosis susceptibility [MIMi:607948].1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00465633G → D in VDDR2A. 1 PublicationCorresponds to variant dbSNP:rs121909790EnsemblClinVar.1
Natural variantiVAR_00465735H → Q in VDDR2A. 1 Publication1
Natural variantiVAR_00465845K → E in VDDR2A. 1 Publication1
Natural variantiVAR_00465946G → D in VDDR2A. 1 PublicationCorresponds to variant dbSNP:rs121909797EnsemblClinVar.1
Natural variantiVAR_00466047F → I in VDDR2A. 1 Publication1
Natural variantiVAR_00466150R → Q in VDDR2A. 1 PublicationCorresponds to variant dbSNP:rs121909794EnsemblClinVar.1
Natural variantiVAR_00466273R → Q in VDDR2A. 1 PublicationCorresponds to variant dbSNP:rs121909791EnsemblClinVar.1
Natural variantiVAR_00466380R → Q in VDDR2A. 2 PublicationsCorresponds to variant dbSNP:rs121909793EnsemblClinVar.1
Natural variantiVAR_079325152 – 427Missing in VDDR2A; loss of calcitriol receptor activity; loss of affinity for calcitriol; no effect on ligand-independent localization to the nucleus. 2 PublicationsCorresponds to variant dbSNP:rs121909795Add BLAST276
Natural variantiVAR_029309230L → V1 PublicationCorresponds to variant dbSNP:rs11574090Ensembl.1
Natural variantiVAR_004664274R → L in VDDR2A; loss of calcitriol receptor activity; decreased affinity for calcitriol by a factor of 1000; no effect on interaction with RXRA; changed interaction with NCOR1; loss of interaction with NCOA1; no effect on sequence-specific DNA-binding. 2 PublicationsCorresponds to variant dbSNP:rs121909796EnsemblClinVar.1
Natural variantiVAR_004665305H → Q in VDDR2A; loss of calcitriol receptor activity; no effect on interaction with RXRA; changed interaction with NCOR1; loss of interaction with NCOA1; no effect on sequence-specific DNA-binding. 2 PublicationsCorresponds to variant dbSNP:rs121909798EnsemblClinVar.1
Natural variantiVAR_004666314I → S in VDDR2A. 1 PublicationCorresponds to variant dbSNP:rs121909799EnsemblClinVar.1
Natural variantiVAR_079326346V → M in VDDR2A; decreased calcitriol receptor activity; decreased affinity for calcitriol; decreased ligand-independent localization to the nucleus; loss of interaction with RXRA; decreased interaction with NCOR1; decreased interaction with NCOA1; decreased sequence-specific DNA-binding. 2 PublicationsCorresponds to variant dbSNP:rs267607169EnsemblClinVar.1
Natural variantiVAR_079327360S → P in VDDR2A; loss of calcitriol receptor activity; loss of affinity for calcitriol; decreased ligand-independent localization to the nucleus; loss of interaction with RXRA; loss of interaction with NCOR1; loss of interaction with NCOA1; loss of sequence-specific DNA-binding. 1 Publication1
Natural variantiVAR_029310362T → I1 PublicationCorresponds to variant dbSNP:rs11574115Ensembl.1
Natural variantiVAR_004667391R → C in VDDR2A. 1 PublicationCorresponds to variant dbSNP:rs121909800EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0472181M → MEWRNKKRSDWLSMVLRTAG VEEAFGSEVSVRPHRRAPLG STYLPPAPSGM in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_006719587.3 [P11473-1]
XP_011537022.1, XM_011538720.2 [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.4 human [P11473-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiVDR_HUMAN
AccessioniPrimary (citable) accession number: P11473
Secondary accession number(s): B2R5Q1, G3V1V9, Q5PSV3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: June 20, 2018
This is version 220 of the entry and version 1 of the sequence. See 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

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