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Protein

Vitamin D3 receptor

Gene

VDR

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Nuclear hormone receptor. Transcription factor that mediates the action of vitamin D3 by controlling the expression of hormone sensitive 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.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

  • 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: BHF-UCL
  • 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
  • gene expression Source: Reactome
  • 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 from RNA polymerase II promoter 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 from RNA polymerase II promoter 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 receptor signaling pathway Source: BHF-UCL
Complete GO annotation...

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 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:12679. VDR.

Subcellular locationi

GO - Cellular componenti

  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • receptor complex Source: BHF-UCL
  • RNA polymerase II transcription factor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Rickets vitamin D-dependent 2A (VDDR2A)10 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)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. 1 Publication
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.

Chemistry

DrugBankiDB01436. Alfacalcidol.
DB00146. Calcidiol.
DB02300. Calcipotriol.
DB00136. Calcitriol.
DB00169. Cholecalciferol.
DB01070. Dihydrotachysterol.
DB00153. Ergocalciferol.
DB00910. Paricalcitol.

Polymorphism and mutation databases

BioMutaiVDR.
DMDMi137617.

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

BgeeiP11473.
CleanExiHS_VDR.
ExpressionAtlasiP11473. baseline and differential.
GenevisibleiP11473. HS.

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. 96 interactions.
DIPiDIP-32624N.
IntActiP11473. 19 interactions.
MINTiMINT-236408.
STRINGi9606.ENSP00000447173.

Structurei

Secondary structure

1
427
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni25 – 273Combined sources
Beta strandi33 – 353Combined sources
Beta strandi38 – 403Combined sources
Helixi42 – 5312Combined sources
Beta strandi61 – 644Combined sources
Turni70 – 756Combined sources
Helixi77 – 8610Combined sources
Helixi91 – 933Combined sources
Helixi97 – 10711Combined sources
Beta strandi108 – 1103Combined sources
Turni111 – 1133Combined sources
Helixi115 – 1195Combined sources
Helixi126 – 14217Combined sources
Helixi150 – 1523Combined sources
Helixi217 – 2237Combined sources
Helixi227 – 24721Combined sources
Helixi251 – 2533Combined sources
Helixi256 – 27419Combined sources
Helixi275 – 2773Combined sources
Turni281 – 2844Combined sources
Beta strandi285 – 2873Combined sources
Helixi291 – 2933Combined sources
Helixi297 – 3015Combined sources
Turni302 – 3043Combined sources
Helixi307 – 32115Combined sources
Turni322 – 3243Combined sources
Helixi327 – 33812Combined sources
Beta strandi341 – 3433Combined sources
Helixi349 – 37022Combined sources
Turni373 – 3786Combined sources
Helixi379 – 40426Combined sources
Helixi410 – 4134Combined sources
Helixi416 – 4227Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
3WGPX-ray2.00A120-423[»]
3WWRX-ray3.18A118-427[»]
4G2IX-ray1.80A118-427[»]
4ITEX-ray2.49A118-427[»]
4ITFX-ray2.84A118-427[»]
4PA2X-ray2.00A118-427[»]
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.
GeneTreeiENSGT00780000121834.
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. 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 AAH60832.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAP88938.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

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:
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_006719587.2. [P11473-1]
XP_011537022.1. XM_011538720.1. [P11473-1]
UniGeneiHs.524368.

Genome annotation databases

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

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:
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_006719587.2. [P11473-1]
XP_011537022.1. XM_011538720.1. [P11473-1]
UniGeneiHs.524368.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
3WGPX-ray2.00A120-423[»]
3WWRX-ray3.18A118-427[»]
4G2IX-ray1.80A118-427[»]
4ITEX-ray2.49A118-427[»]
4ITFX-ray2.84A118-427[»]
4PA2X-ray2.00A118-427[»]
DisProtiDP00184.
ProteinModelPortaliP11473.
SMRiP11473. Positions 21-425.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113264. 96 interactions.
DIPiDIP-32624N.
IntActiP11473. 19 interactions.
MINTiMINT-236408.
STRINGi9606.ENSP00000447173.

Chemistry

BindingDBiP11473.
ChEMBLiCHEMBL1977.
DrugBankiDB01436. Alfacalcidol.
DB00146. Calcidiol.
DB02300. Calcipotriol.
DB00136. Calcitriol.
DB00169. Cholecalciferol.
DB01070. Dihydrotachysterol.
DB00153. Ergocalciferol.
DB00910. Paricalcitol.
GuidetoPHARMACOLOGYi605.

PTM databases

PhosphoSiteiP11473.

Polymorphism and mutation databases

BioMutaiVDR.
DMDMi137617.

Proteomic databases

MaxQBiP11473.
PaxDbiP11473.
PRIDEiP11473.

Protocols and materials databases

DNASUi7421.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi7421.
GeneCardsiGC12M048247.
HGNCiHGNC:12679. VDR.
MIMi277440. phenotype.
601769. gene.
607948. phenotype.
neXtProtiNX_P11473.
Orphaneti93160. Hypocalcemic vitamin D-resistant rickets.
PharmGKBiPA37301.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG283526.
GeneTreeiENSGT00780000121834.
HOGENOMiHOG000220844.
HOVERGENiHBG108655.
InParanoidiP11473.
KOiK08539.
OMAiFCQFRPP.
PhylomeDBiP11473.
TreeFamiTF316304.

Enzyme and pathway databases

ReactomeiREACT_15525. Nuclear Receptor transcription pathway.
SignaLinkiP11473.

Miscellaneous databases

ChiTaRSiVDR. human.
EvolutionaryTraceiP11473.
GeneWikiiCalcitriol_receptor.
GenomeRNAii7421.
NextBioi29054.
PROiP11473.
SOURCEiSearch...

Gene expression databases

BgeeiP11473.
CleanExiHS_VDR.
ExpressionAtlasiP11473. baseline and differential.
GenevisibleiP11473. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: July 22, 2015
This is version 191 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

Caution

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

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.