VDR_HUMAN - dbPTM
VDR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VDR_HUMAN
UniProt AC P11473
Protein Name Vitamin D3 receptor
Gene Name VDR
Organism Homo sapiens (Human).
Sequence Length 427
Subcellular Localization Nucleus . Cytoplasm . Localizes mainly to the nucleus. Localization to the nucleus is enhanced by vitamin D3.
Protein Description 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..
Protein Sequence MEAMAASTSLPDPGDFDRNVPRICGVCGDRATGFHFNAMTCEGCKGFFRRSMKRKALFTCPFNGDCRITKDNRRHCQACRLKRCVDIGMMKEFILTDEEVQRKREMILKRKEEEALKDSLRPKLSEEQQRIIAILLDAHHKTYDPTYSDFCQFRPPVRVNDGGGSHPSRPNSRHTPSFSGDSSSSCSDHCITSSDMMDSSSFSNLDLSEEDSDDPSVTLELSQLSMLPHLADLVSYSIQKVIGFAKMIPGFRDLTSEDQIVLLKSSAIEVIMLRSNESFTMDDMSWTCGNQDYKYRVSDVTKAGHSLELIEPLIKFQVGLKKLNLHEEEHVLLMAICIVSPDRPGVQDAALIEAIQDRLSNTLQTYIRCRHPPPGSHLLYAKMIQKLADLRSLNEEHSKQYRCLSFQPECSMKLTPLVLEVFGNEIS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
7Phosphorylation-MEAMAASTSLPDPG
-CCCCCCCCCCCCCC
14.7028122231
8PhosphorylationMEAMAASTSLPDPGD
CCCCCCCCCCCCCCC
29.5628122231
9PhosphorylationEAMAASTSLPDPGDF
CCCCCCCCCCCCCCC
35.1028122231
9 (in isoform 2)Phosphorylation-35.10-
13 (in isoform 2)Phosphorylation-42.17-
51PhosphorylationCKGFFRRSMKRKALF
CCHHHHHHCCCCEEE
25.131656468
117UbiquitinationRKEEEALKDSLRPKL
HHHHHHHHHHHCCCC
52.93-
123UbiquitinationLKDSLRPKLSEEQQR
HHHHHCCCCCHHHHH
59.20-
165PhosphorylationRVNDGGGSHPSRPNS
EECCCCCCCCCCCCC
35.1823898821
168PhosphorylationDGGGSHPSRPNSRHT
CCCCCCCCCCCCCCC
55.7527251275
172PhosphorylationSHPSRPNSRHTPSFS
CCCCCCCCCCCCCCC
28.2810687851
175PhosphorylationSRPNSRHTPSFSGDS
CCCCCCCCCCCCCCC
21.3710687851
182PhosphorylationTPSFSGDSSSSCSDH
CCCCCCCCCCCCCCC
35.3322817900
208PhosphorylationSFSNLDLSEEDSDDP
CCCCCCCCCCCCCCC
38.3122817900
222 (in isoform 2)Phosphorylation-21.5027251275
293PhosphorylationWTCGNQDYKYRVSDV
CCCCCCCEEEEHHHC
10.52-
302UbiquitinationYRVSDVTKAGHSLEL
EEHHHCCCCCCCHHH
52.8221906983
380PhosphorylationPPGSHLLYAKMIQKL
CCCCHHHHHHHHHHH
15.55-
386UbiquitinationLYAKMIQKLADLRSL
HHHHHHHHHHHHHHC
34.42-
392PhosphorylationQKLADLRSLNEEHSK
HHHHHHHHCCHHHHH
42.7324719451
399UbiquitinationSLNEEHSKQYRCLSF
HCCHHHHHHHCEEEC
53.94-
411PhosphorylationLSFQPECSMKLTPLV
EECCCCHHCCCCHHH
19.7924719451
442 (in isoform 2)Phosphorylation-24719451
461 (in isoform 2)Phosphorylation-24719451

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
51SPhosphorylationKinasePRKCAP17252
GPS
51SPhosphorylationKinasePRKCBP68403
GPS
182SPhosphorylationKinasePRKACAP17612
GPS
182SPhosphorylationKinasePKA-FAMILY-GPS
182SPhosphorylationKinasePKA_GROUP-PhosphoELM
208SPhosphorylationKinaseCSNK2A1P68399
GPS
208SPhosphorylationKinaseCSK21P68400
PhosphoELM
208SPhosphorylationKinaseCK2-FAMILY-GPS
208SPhosphorylationKinaseCK2_GROUP-PhosphoELM

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VDR_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of VDR_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KDM5A_HUMANKDM5Aphysical
11358960
STAT1_HUMANSTAT1physical
11909970
VDR_HUMANVDRphysical
11980721
JUN_HUMANJUNphysical
10330159
FOS_HUMANFOSphysical
10330159
MED13_HUMANMED13physical
10198638
MED12_HUMANMED12physical
10198638
MED1_HUMANMED1physical
10198638
MED14_HUMANMED14physical
10198638
TR150_HUMANTHRAP3physical
10198638
MED6_HUMANMED6physical
10198638
MED21_HUMANMED21physical
10198638
MED24_HUMANMED24physical
10198638
MED16_HUMANMED16physical
10198638
BAG1_HUMANBAG1genetic
10967105
SNW1_HUMANSNW1physical
9632709
RXRA_HUMANRXRAphysical
9632709
ZBT16_HUMANZBTB16physical
12460926
RUNX1_HUMANRUNX1physical
12460926
MTG8_HUMANRUNX1T1physical
12460926
VDR_HUMANVDRphysical
11514567
RXRA_HUMANRXRAphysical
11514567
SNW1_HUMANSNW1physical
11514567
NCOA2_MOUSENcoa2physical
11514567
NCOA2_HUMANNCOA2physical
11514567
NCOA2_HUMANNCOA2physical
12612084
NCOR1_HUMANNCOR1physical
19098224
CBP_HUMANCREBBPphysical
16434701
SRC_HUMANSRCphysical
16434701
MED1_HUMANMED1physical
16434701
CEBPA_HUMANCEBPAphysical
16357103
SRC_HUMANSRCphysical
12893883
NCOA2_HUMANNCOA2physical
12893883
NCOA3_HUMANNCOA3physical
12893883
RXRG_HUMANRXRGphysical
15919723
SRC_HUMANSRCphysical
15919723
NCOA2_HUMANNCOA2physical
15919723
NR2E3_HUMANNR2E3physical
15919092
NCOA3_HUMANNCOA3physical
15919092
MED1_HUMANMED1physical
15919092
RPB1_HUMANPOLR2Aphysical
15919092
RXRA_HUMANRXRAphysical
15890193
RPB1_HUMANPOLR2Aphysical
15890193
NCOA4_HUMANNCOA4physical
15805579
RXRA_HUMANRXRAphysical
15805579
RXRA_HUMANRXRAphysical
15647825
EP300_HUMANEP300physical
15647825
NCOA1_HUMANNCOA1physical
11149488
RXRA_HUMANRXRAphysical
11075811
NCOA1_HUMANNCOA1physical
11075811
VDR_HUMANVDRphysical
11075811
NCOR1_HUMANNCOR1physical
10877839
CSN2_HUMANCOPS2physical
10877839
TAF11_HUMANTAF11physical
10744685
TAF7_HUMANTAF7physical
10409738
RXRA_HUMANRXRAphysical
10224118
NCOA1_HUMANNCOA1physical
10224118
SMAD3_HUMANSMAD3physical
10037600
RXRA_HUMANRXRAphysical
10037600
MED1_HUMANMED1physical
17786964
RXRA_HUMANRXRAphysical
17786964
NCOA1_HUMANNCOA1physical
17786964
SRC_HUMANSRCphysical
20371703
HNF4A_HUMANHNF4Aphysical
20371703
P53_HUMANTP53physical
20227041
HAIR_HUMANHRphysical
20512927
FOXO3_HUMANFOXO3physical
20733005
FOXO4_HUMANFOXO4physical
20733005
NCOA3_HUMANNCOA3physical
20733005
SIR1_HUMANSIRT1physical
20733005
PP1G_HUMANPPP1CCphysical
20733005
MED12_HUMANMED12physical
10235266
MED13_HUMANMED13physical
10235266
MED1_HUMANMED1physical
10235266
MED14_HUMANMED14physical
10235266
MED24_HUMANMED24physical
10235266
MED23_HUMANMED23physical
10235266
MED16_HUMANMED16physical
10235266
MED4_HUMANMED4physical
10235266
MED7_HUMANMED7physical
10235266
MED6_HUMANMED6physical
10235266
CDN1A_HUMANCDKN1Aphysical
21088000
ACTN4_HUMANACTN4physical
21078666
RXRA_HUMANRXRAphysical
15604093
NRIP1_HUMANNRIP1physical
15604093
HMGN3_HUMANHMGN3physical
15604093
RXRG_HUMANRXRGphysical
15604093
CLASR_HUMANCLASRPphysical
15604093
NR1H2_HUMANNR1H2physical
15604093
GBRL2_HUMANGABARAPL2physical
15604093
GNPAT_HUMANGNPATphysical
15604093
NR0B2_HUMANNR0B2physical
15604093
RXRB_HUMANRXRBphysical
15604093
GBRL1_HUMANGABARAPL1physical
15604093
CASC4_HUMANCASC4physical
15604093
MED1_HUMANMED1physical
12796488
CD11B_HUMANCDK11Bphysical
19538938
PP1G_HUMANPPP1CCphysical
12036952
SRC_HUMANSRCphysical
21917910
NCOR1_HUMANNCOR1physical
11124027
NCOA1_HUMANNCOA1physical
11124027
PRS8_HUMANPSMC5physical
9831079
BRCA1_HUMANBRCA1physical
19074549
RXRA_HUMANRXRAphysical
15829977
HAIR_HUMANHRphysical
12847098
PTN3_HUMANPTPN3physical
21119599
RXRA_HUMANRXRAphysical
16750418
RXRA_HUMANRXRAphysical
17500032
NCOA1_HUMANNCOA1physical
23975195
RXRA_HUMANRXRAphysical
20153625
RXRA_HUMANRXRAphysical
15888456
NCOA3_HUMANNCOA3physical
15888456
PRS8_HUMANPSMC5physical
15604093
NCOA1_HUMANNCOA1physical
15604093
NCOA1_HUMANNCOA1physical
12796488
NCOA1_HUMANNCOA1physical
9121466
MDM2_HUMANMDM2physical
25969952
AFF1_HUMANAFF1physical
26329759
RXRA_HUMANRXRAphysical
26329759

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
277440Rickets vitamin D-dependent 2A (VDDR2A)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB01436Alfacalcidol
DB00146Calcidiol
DB02300Calcipotriol
DB00136Calcitriol
DB00169Cholecalciferol
DB01070Dihydrotachysterol
DB00153Ergocalciferol
DB00910Paricalcitol
Regulatory Network of VDR_HUMAN

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Related Literatures of Post-Translational Modification

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