Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Nuclear receptor subfamily 1 group I member 2  

UniProtKB / Swiss-Prot ID :  NR1I2_HUMAN

Gene Name (Synonyms) : 
NR1I2, PXR  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. 

Protein Function :  Nuclear receptor that binds and is activated by variety of endogenous and xenobiotic compounds. Transcription factor that activates the transcription of multiple genes involved in the metabolism and secretion of potentially harmful xenobiotics, drugs and endogenous compounds. Activated by the antibiotic rifampicin and various plant metabolites, such as hyperforin, guggulipid, colupulone, and isoflavones. Response to specific ligands is species-specific. Activated by naturally occurring steroids, such as pregnenolone and progesterone. Binds to a response element in the promoters of the CYP3A4 and ABCB1/MDR1 genes. 

Protein Sequence MEVRPKESWNHADFVHCEDTESVPGKPSVNADEEVGGPQICRVCGDKATGYHFNVMTCEGCKGFFRRAMK...
Predicted Secondary Structure  -
Protein Variant
LocationDescription
12A -> T (in dbSNP:rs1063955). VAR_050581
18E -> K (in dbSNP:rs59371185). VAR_033237
27P -> S (in allele PXR*2;dbSNP:rs12721613).
36G -> R (in allele PXR*3). VAR_012229
98R -> C. VAR_018340
122R -> Q (in allele PXR*4; rarepolymorphism).
148R -> Q. VAR_018341
370A -> T (in dbSNP:rs35761343). VAR_033238
381R -> W. VAR_018342
403I -> V. VAR_018343
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
8PhosphoserineRPKESWNHA
39.03Phosphositeplus
Link-
57PhosphothreonineFNVMTCEGC
11.79Phosphositeplus
Link-
208PhosphoserineKDLCSLKVS
38.22Phosphositeplus
Link
305PhosphoserineCGRLSYCLE
16.67Phosphositeplus
Link
350PhosphoserineISLFSPDRP
31.05Phosphositeplus
Link
408PhosphothreonineNAQHTQRLL
11.87Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
PIT1_HUMANin vitroHPRD:04346HPRD11891224
RXRA_HUMANin vitroHPRD:04346HPRD9727070
9489701
RXRB_HUMANin vitroHPRD:04346HPRD9727070
NCOA1_HUMANin vitroHPRD:04346HPRD12909012
NR1I2_HUMANin vitroHPRD:04346HPRD12909012
NCOR2_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:04346HPRD16219912
12072427
ST2A1_HUMANENSP00000336528STRING
ST2A1_HUMANENSP00000336528STRING
ST2A1_HUMANENSP00000336528STRING
NR0B2_HUMANENSP00000336528STRING
NR0B2_HUMANENSP00000336528STRING
NR0B2_HUMANENSP00000336528STRING
CP2C9_HUMANENSP00000336528STRING
CP2C9_HUMANENSP00000336528STRING
CP2C9_HUMANENSP00000336528STRING
PRGC1_HUMANENSP00000336528STRING
PRGC1_HUMANENSP00000336528STRING
PRGC1_HUMANENSP00000336528STRING
MDR1_HUMANENSP00000336528STRING
MDR1_HUMANENSP00000336528STRING
MDR1_HUMANENSP00000336528STRING
NCOR1_HUMANENSP00000336528STRING
NCOR1_HUMANENSP00000336528STRING
NCOR1_HUMANENSP00000336528STRING
CP7A1_HUMANENSP00000336528STRING
CP7A1_HUMANENSP00000336528STRING
CP7A1_HUMANENSP00000336528STRING
NCOA1_HUMANENSP00000336528STRING
NCOA1_HUMANENSP00000336528STRING
NCOA1_HUMANENSP00000336528STRING
NCOA1_HUMANENSP00000336528STRING
NCOA1_HUMANENSP00000336528STRING
NCOA1_HUMANENSP00000336528STRING
CP2B6_HUMANENSP00000336528STRING
CP2B6_HUMANENSP00000336528STRING
CP2B6_HUMANENSP00000336528STRING
UD14_HUMANENSP00000336528STRING
UD14_HUMANENSP00000336528STRING
UD14_HUMANENSP00000336528STRING
CP3A4_HUMANENSP00000336528STRING
CP3A4_HUMANENSP00000336528STRING
CP3A4_HUMANENSP00000336528STRING
CP3A4_HUMANENSP00000336528STRING
CP3A4_HUMANENSP00000336528STRING
CP3A4_HUMANENSP00000336528STRING
NCOR2_HUMANENSP00000336528STRING
NCOR2_HUMANENSP00000336528STRING
NCOR2_HUMANENSP00000336528STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
DrugBank
DB01248Docetaxel
DB00530Erlotinib
DB00783Estradiol
DB00977Ethinyl Estradiol
DB01229Paclitaxel
DB01045Rifampicin
DB01220Rifaximin
DB08864Rilpivirine
DB00163Vitamin E
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Related Literatures of Post-Translational Modification
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures