O75469 (NR1I2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nuclear receptor subfamily 1 group I member 2

Alternative name(s):
Orphan nuclear receptor PAR1
Orphan nuclear receptor PXR
Pregnane X receptor
Steroid and xenobiotic receptor
Short name=SXR

Gene names

Name:	NR1I2
Synonyms:	PXR

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	434 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.2 Ref.4 Ref.9 Ref.11 Ref.13 Ref.17
Subunit structure	Heterodimer with RXR. Interacts with NCOA1. Ref.13 Ref.16
Subcellular location	Nucleus Ref.10.
Tissue specificity	Expressed in liver, colon and small intestine.
Sequence similarities	Belongs to the nuclear hormone receptor family. NR1 subfamily. Contains 1 nuclear receptor DNA-binding domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator Receptor
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Uncategorized	regulation of transcription from RNA polymerase II promoter by nuclear hormone receptor Traceable author statement. Source: Reactome
Biological process	drug export Inferred from direct assay Ref.13. Source: UniProtKB exogenous drug catabolic process Inferred from direct assay Ref.13. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from direct assay. Source: MGI positive regulation of transcription, DNA-dependent Inferred from direct assay Ref.13. Source: UniProtKB steroid metabolic process Traceable author statement. Source: ProtInc transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW xenobiotic metabolic process Inferred from direct assay Ref.13. Source: UniProtKB xenobiotic transport Inferred from direct assay Ref.13. Source: UniProtKB
Cellular component	nucleoplasm Traceable author statement. Source: Reactome
Molecular function	drug binding Inferred from direct assay Ref.13. Source: UniProtKB protein binding Inferred from physical interaction Ref.13. Source: UniProtKB sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: InterPro steroid hormone receptor activity Inferred from electronic annotation. Source: InterPro transcription coactivator activity Traceable author statement. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1A (identifier: O75469-1)

Also known as: 1; PRR1-A;

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 1B (identifier: O75469-2)

Also known as: PRR1-B;

The sequence of this isoform differs from the canonical sequence as follows:
     1-55: Missing.

Isoform 1C (identifier: O75469-3)

Also known as: PRR1-C;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MDPRGEVGAKNLPPNSPRGPEANL

Isoform 2A (identifier: O75469-4)

Also known as: 2; PRR2-A;

The sequence of this isoform differs from the canonical sequence as follows:
     174-210: Missing.

Isoform 2B (identifier: O75469-5)

Also known as: PRR2-B;

The sequence of this isoform differs from the canonical sequence as follows:
     1-55: Missing.
     174-210: Missing.

Isoform 2C (identifier: O75469-6)

Also known as: PRR2-C;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MDPRGEVGAKNLPPNSPRGPEANL
     174-210: Missing.

Isoform 3 (identifier: O75469-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MTVTRTHHFKEGSLRAPAIPLHSAAAELASNHPRGPEANL

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 434

434

Nuclear receptor subfamily 1 group I member 2

PRO_0000053547

Regions

DNA binding

38 – 107

70

Nuclear receptor

Zinc finger

41 – 61

21

NR C4-type

Zinc finger

77 – 102

26

NR C4-type

Region

108 – 204

97

Hinge

Region

205 – 434

230

Ligand-binding

Motif

66 – 92

27

Bipartite nuclear localization signal

Sites

Binding site

247

1

Agonist

Binding site

285

1

Agonist

Binding site

288

1

Agonist

Binding site

299

1

Agonist

Binding site

407

1

Agonist

Natural variations

Alternative sequence

1 – 55

55

Missing in isoform 1B and isoform 2B.

VSP_003668

Alternative sequence

1

1

M → MDPRGEVGAKNLPPNSPRGP EANL in isoform 1C and isoform 2C.

VSP_003667

Alternative sequence

1

1

M → MTVTRTHHFKEGSLRAPAIP LHSAAAELASNHPRGPEANL in isoform 3.

VSP_026669

Alternative sequence

174 – 210

37

Missing in isoform 2A, isoform 2B and isoform 2C.

VSP_003669

Natural variant

12

1

A → T. Ref.5
Corresponds to variant rs1063955 [ dbSNP | Ensembl ].

VAR_050581

Natural variant

18

1

E → K. Ref.7
Corresponds to variant rs59371185 [ dbSNP | Ensembl ].

VAR_033237

Natural variant

27

1

P → S in allele PXR*2. Ref.4 Ref.7
Corresponds to variant rs12721613 [ dbSNP | Ensembl ].

VAR_012228

Natural variant

36

1

G → R in allele PXR*3. Ref.4

VAR_012229

Natural variant

98

1

R → C. Ref.18

VAR_018340

Natural variant

122

1

R → Q in allele PXR*4; rare polymorphism. Ref.4

VAR_012230

Natural variant

148

1

R → Q. Ref.18

VAR_018341

Natural variant

370

1

A → T. Ref.7
Corresponds to variant rs35761343 [ dbSNP | Ensembl ].

VAR_033238

Natural variant

381

1

R → W. Ref.18

VAR_018342

Natural variant

403

1

I → V. Ref.18

VAR_018343

Experimental info

Mutagenesis

66 – 67

2

RR → AA: Abolishes nuclear localization; when associated with 91-A-A-92. Ref.10

Mutagenesis

91 – 92

2

RR → AA: Abolishes nuclear localization; when associated with 66-A-A-67. Ref.10

Sequence conflict

109

1

K → N in CAB55489. Ref.5

Sequence conflict

109

1

K → N in CAB55490. Ref.5

Sequence conflict

109

1

K → N in CAB55491. Ref.5

Sequence conflict

109

1

K → N in CAB55492. Ref.5

Sequence conflict

109

1

K → N in CAB55493. Ref.5

Sequence conflict

109

1

K → N in CAB55494. Ref.5

Sequence conflict

174

1

Missing in AAH17304. Ref.8

Secondary structure

1

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434

Helix Strand Turn

Details...

Helix

145 – 161

17

Helix

199 – 203

5

Helix

204 – 208

5

Beta strand

211 – 216

6

Beta strand

222 – 226

5

Beta strand

231 – 233

3

Helix

234 – 237

4

Helix

240 – 260

21

Helix

262 – 265

4

Helix

269 – 290

22

Turn

294 – 297

4

Beta strand

298 – 301

4

Beta strand

304 – 308

5

Helix

314 – 318

5

Helix

322 – 332

11

Helix

337 – 348

12

Helix

359 – 380

22

Helix

384 – 386

3

Helix

389 – 417

29

Helix

423 – 429

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1A (1) (PRR1-A) [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 1DF6A2AE3109C4DA	FASTA	434	49,762
	10 20 30 40 50 60 MEVRPKESWN HADFVHCEDT ESVPGKPSVN ADEEVGGPQI CRVCGDKATG YHFNVMTCEG 70 80 90 100 110 120 CKGFFRRAMK RNARLRCPFR KGACEITRKT RRQCQACRLR KCLESGMKKE MIMSDEAVEE 130 140 150 160 170 180 RRALIKRKKS ERTGTQPLGV QGLTEEQRMM IRELMDAQMK TFDTTFSHFK NFRLPGVLSS 190 200 210 220 230 240 GCELPESLQA PSREEAAKWS QVRKDLCSLK VSLQLRGEDG SVWNYKPPAD SGGKEIFSLL 250 260 270 280 290 300 PHMADMSTYM FKGIISFAKV ISYFRDLPIE DQISLLKGAA FELCQLRFNT VFNAETGTWE 310 320 330 340 350 360 CGRLSYCLED TAGGFQQLLL EPMLKFHYML KKLQLHEEEY VLMQAISLFS PDRPGVLQHR 370 380 390 400 410 420 VVDQLQEQFA ITLKSYIECN RPQPAHRFLF LKIMAMLTEL RSINAQHTQR LLRIQDIHPF 430 ATPLMQELFG ITGS
	Isoform 1B (PRR1-B) [UniParc]. Checksum: 7B79CBF8A100C0F0	FASTA	379	43,706
	10 20 30 40 50 60 MTCEGCKGFF RRAMKRNARL RCPFRKGACE ITRKTRRQCQ ACRLRKCLES GMKKEMIMSD 70 80 90 100 110 120 EAVEERRALI KRKKSERTGT QPLGVQGLTE EQRMMIRELM DAQMKTFDTT FSHFKNFRLP 130 140 150 160 170 180 GVLSSGCELP ESLQAPSREE AAKWSQVRKD LCSLKVSLQL RGEDGSVWNY KPPADSGGKE 190 200 210 220 230 240 IFSLLPHMAD MSTYMFKGII SFAKVISYFR DLPIEDQISL LKGAAFELCQ LRFNTVFNAE 250 260 270 280 290 300 TGTWECGRLS YCLEDTAGGF QQLLLEPMLK FHYMLKKLQL HEEEYVLMQA ISLFSPDRPG 310 320 330 340 350 360 VLQHRVVDQL QEQFAITLKS YIECNRPQPA HRFLFLKIMA MLTELRSINA QHTQRLLRIQ 370 DIHPFATPLM QELFGITGS
	Isoform 1C (PRR1-C) [UniParc]. Checksum: 37EFF759461EFE94	FASTA	457	52,129
	10 20 30 40 50 60 MDPRGEVGAK NLPPNSPRGP EANLEVRPKE SWNHADFVHC EDTESVPGKP SVNADEEVGG 70 80 90 100 110 120 PQICRVCGDK ATGYHFNVMT CEGCKGFFRR AMKRNARLRC PFRKGACEIT RKTRRQCQAC 130 140 150 160 170 180 RLRKCLESGM KKEMIMSDEA VEERRALIKR KKSERTGTQP LGVQGLTEEQ RMMIRELMDA 190 200 210 220 230 240 QMKTFDTTFS HFKNFRLPGV LSSGCELPES LQAPSREEAA KWSQVRKDLC SLKVSLQLRG 250 260 270 280 290 300 EDGSVWNYKP PADSGGKEIF SLLPHMADMS TYMFKGIISF AKVISYFRDL PIEDQISLLK 310 320 330 340 350 360 GAAFELCQLR FNTVFNAETG TWECGRLSYC LEDTAGGFQQ LLLEPMLKFH YMLKKLQLHE 370 380 390 400 410 420 EEYVLMQAIS LFSPDRPGVL QHRVVDQLQE QFAITLKSYI ECNRPQPAHR FLFLKIMAML 430 440 450 TELRSINAQH TQRLLRIQDI HPFATPLMQE LFGITGS
	Isoform 2A (2) (PRR2-A) [UniParc]. Checksum: 5F0007EFD27260F9	FASTA	397	45,766
	10 20 30 40 50 60 MEVRPKESWN HADFVHCEDT ESVPGKPSVN ADEEVGGPQI CRVCGDKATG YHFNVMTCEG 70 80 90 100 110 120 CKGFFRRAMK RNARLRCPFR KGACEITRKT RRQCQACRLR KCLESGMKKE MIMSDEAVEE 130 140 150 160 170 180 RRALIKRKKS ERTGTQPLGV QGLTEEQRMM IRELMDAQMK TFDTTFSHFK NFRVSLQLRG 190 200 210 220 230 240 EDGSVWNYKP PADSGGKEIF SLLPHMADMS TYMFKGIISF AKVISYFRDL PIEDQISLLK 250 260 270 280 290 300 GAAFELCQLR FNTVFNAETG TWECGRLSYC LEDTAGGFQQ LLLEPMLKFH YMLKKLQLHE 310 320 330 340 350 360 EEYVLMQAIS LFSPDRPGVL QHRVVDQLQE QFAITLKSYI ECNRPQPAHR FLFLKIMAML 370 380 390 TELRSINAQH TQRLLRIQDI HPFATPLMQE LFGITGS
	Isoform 2B (PRR2-B) [UniParc]. Checksum: 7D4EA16E5A132B0B	FASTA	342	39,710
	10 20 30 40 50 60 MTCEGCKGFF RRAMKRNARL RCPFRKGACE ITRKTRRQCQ ACRLRKCLES GMKKEMIMSD 70 80 90 100 110 120 EAVEERRALI KRKKSERTGT QPLGVQGLTE EQRMMIRELM DAQMKTFDTT FSHFKNFRVS 130 140 150 160 170 180 LQLRGEDGSV WNYKPPADSG GKEIFSLLPH MADMSTYMFK GIISFAKVIS YFRDLPIEDQ 190 200 210 220 230 240 ISLLKGAAFE LCQLRFNTVF NAETGTWECG RLSYCLEDTA GGFQQLLLEP MLKFHYMLKK 250 260 270 280 290 300 LQLHEEEYVL MQAISLFSPD RPGVLQHRVV DQLQEQFAIT LKSYIECNRP QPAHRFLFLK 310 320 330 340 IMAMLTELRS INAQHTQRLL RIQDIHPFAT PLMQELFGIT GS
	Isoform 2C (PRR2-C) [UniParc]. Checksum: CE6179469491C1EF	FASTA	420	48,134
	10 20 30 40 50 60 MDPRGEVGAK NLPPNSPRGP EANLEVRPKE SWNHADFVHC EDTESVPGKP SVNADEEVGG 70 80 90 100 110 120 PQICRVCGDK ATGYHFNVMT CEGCKGFFRR AMKRNARLRC PFRKGACEIT RKTRRQCQAC 130 140 150 160 170 180 RLRKCLESGM KKEMIMSDEA VEERRALIKR KKSERTGTQP LGVQGLTEEQ RMMIRELMDA 190 200 210 220 230 240 QMKTFDTTFS HFKNFRVSLQ LRGEDGSVWN YKPPADSGGK EIFSLLPHMA DMSTYMFKGI 250 260 270 280 290 300 ISFAKVISYF RDLPIEDQIS LLKGAAFELC QLRFNTVFNA ETGTWECGRL SYCLEDTAGG 310 320 330 340 350 360 FQQLLLEPML KFHYMLKKLQ LHEEEYVLMQ AISLFSPDRP GVLQHRVVDQ LQEQFAITLK 370 380 390 400 410 420 SYIECNRPQP AHRFLFLKIM AMLTELRSIN AQHTQRLLRI QDIHPFATPL MQELFGITGS
	Isoform 3 [UniParc]. Checksum: 3049D23C9B903016	FASTA	473	53,899
	10 20 30 40 50 60 MTVTRTHHFK EGSLRAPAIP LHSAAAELAS NHPRGPEANL EVRPKESWNH ADFVHCEDTE 70 80 90 100 110 120 SVPGKPSVNA DEEVGGPQIC RVCGDKATGY HFNVMTCEGC KGFFRRAMKR NARLRCPFRK 130 140 150 160 170 180 GACEITRKTR RQCQACRLRK CLESGMKKEM IMSDEAVEER RALIKRKKSE RTGTQPLGVQ 190 200 210 220 230 240 GLTEEQRMMI RELMDAQMKT FDTTFSHFKN FRLPGVLSSG CELPESLQAP SREEAAKWSQ 250 260 270 280 290 300 VRKDLCSLKV SLQLRGEDGS VWNYKPPADS GGKEIFSLLP HMADMSTYMF KGIISFAKVI 310 320 330 340 350 360 SYFRDLPIED QISLLKGAAF ELCQLRFNTV FNAETGTWEC GRLSYCLEDT AGGFQQLLLE 370 380 390 400 410 420 PMLKFHYMLK KLQLHEEEYV LMQAISLFSP DRPGVLQHRV VDQLQEQFAI TLKSYIECNR 430 440 450 460 470 PQPAHRFLFL KIMAMLTELR SINAQHTQRL LRIQDIHPFA TPLMQELFGI TGS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"SXR, a novel steroid and xenobiotic-sensing nuclear receptor." Blumberg B., Sabbagh W. Jr., Juguilon H., Bolado J. Jr., van Meter C.M., Ong E.S., Evans R.M. Genes Dev. 12:3195-3205(1998) [PubMed: 9784494] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A).
[2]	"The human orphan nuclear receptor PXR is activated by compounds that regulate CYP3A4 gene expression and cause drug interactions." Lehmann J.M., McKee D.D., Watson M.A., Willson T.M., Moore J.T., Kliewer S.A. J. Clin. Invest. 102:1016-1023(1998) [PubMed: 9727070] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A), FUNCTION. Tissue: Liver.
[3]	"Identification of a human nuclear receptor defines a new signaling pathway for CYP3A induction." Bertilsson G., Heidrich J., Svensson K., Asman M., Jendeberg L., Sydow-Baeckman M., Ohlsson R., Postlind H., Blomquist P., Berkenstam A. Proc. Natl. Acad. Sci. U.S.A. 95:12208-12213(1998) [PubMed: 9770465] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A AND 3). Tissue: Liver.
[4]	"The human pregnane X receptor: genomic structure and identification and functional characterization of natural allelic variants." Zhang J., Kuehl P., Green E.D., Touchman J.W., Watkins P.B., Daly A., Hall S.D., Maurel P., Relling M., Brimer C., Yasuda K., Wrighton S.A., Hancock M., Kim R.B., Strom S., Thummel K., Russell C.G., Hudson J.R. Jr., Schuetz E.G., Boguski M.S. Pharmacogenetics 11:555-572(2001) [PubMed: 11668216] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1A AND 3), FUNCTION, VARIANTS SER-27; ARG-36 AND GLN-122.
[5]	"Identification of a novel protein isoform of the human nuclear hormone receptor PXR/SXR and localization to chromosome 3q12.1 -13.3." Heard D.J., Holloway J., Hansen C., Tommerup N., Aagaard L., Vissing H. Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A; 1B; 1C; 2A; 2B AND 2C), VARIANT THR-12. Tissue: Liver.
[6]	Wang X., Li J., Deng X., Chen J., Huang M. Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]	SeattleSNPs variation discovery resource Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-18; SER-27 AND THR-370.
[8]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1A). Tissue: Hepatoma.
[9]	"Nuclear receptor response elements mediate induction of intestinal MDR1 by rifampin." Geick A., Eichelbaum M., Burk O. J. Biol. Chem. 276:14581-14587(2001) [PubMed: 11297522] [Abstract] Cited for: FUNCTION.
[10]	"Molecular mechanism of nuclear translocation of an orphan nuclear receptor, SXR." Kawana K., Ikuta T., Kobayashi Y., Gotoh O., Takeda K., Kawajiri K. Mol. Pharmacol. 63:524-531(2003) [PubMed: 12606758] [Abstract] Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF 66-ARG-ARG-67 AND 91-ARG-ARG-92, NUCLEAR LOCALIZATION SIGNAL.
[11]	"Human CYP3A4 and murine Cyp3A11 are regulated by equol and genistein via the pregnane X receptor in a species-specific manner." Li Y., Ross-Viola J.S., Shay N.F., Moore D.D., Ricketts M.L. J. Nutr. 139:898-904(2009) [PubMed: 19297428] [Abstract] Cited for: FUNCTION.
[12]	"The human nuclear xenobiotic receptor PXR: structural determinants of directed promiscuity." Watkins R.E., Wisely G.B., Moore L.B., Collins J.L., Lambert M.H., Williams S.P., Willson T.M., Kliewer S.A., Redinbo M.R. Science 292:2329-2333(2001) [PubMed: 11408620] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) OF 130-434.
[13]	"2.1 A crystal structure of human PXR in complex with the St. John's wort compound hyperforin." Watkins R.E., Maglich J.M., Moore L.B., Wisely G.B., Noble S.M., Davis-Searles P.R., Lambert M.H., Kliewer S.A., Redinbo M.R. Biochemistry 42:1430-1438(2003) [PubMed: 12578355] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 130-434 IN COMPLEX WITH HYPERFORIN, FUNCTION, INTERACTION WITH NCOA1.
[14]	"Coactivator binding promotes the specific interaction between ligand and the pregnane X receptor." Watkins R.E., Davis-Searles P.R., Lambert M.H., Redinbo M.R. J. Mol. Biol. 331:815-828(2003) [PubMed: 12909012] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 130-434 IN COMPLEX WITH THE CHOLESTEROL-LOWERING COMPOUND SR12813 AND NCOA1.
[15]	"Structural disorder in the complex of human pregnane X receptor and the macrolide antibiotic rifampicin." Chrencik J.E., Orans J., Moore L.B., Xue Y., Peng L., Collins J.L., Wisely G.B., Lambert M.H., Kliewer S.A., Redinbo M.R. Mol. Endocrinol. 19:1125-1134(2005) [PubMed: 15705662] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 130-431 IN COMPLEX WITH RIFAMPICIN.
[16]	"Crystal structure of the PXR-T1317 complex provides a scaffold to examine the potential for receptor antagonism." Xue Y., Chao E., Zuercher W.J., Willson T.M., Collins J.L., Redinbo M.R. Bioorg. Med. Chem. 15:2156-2166(2007) [PubMed: 17215127] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 142-434 IN COMPLEX WITH T0901317 AND NCOA1, INTERACTION WITH NCOA1.
[17]	"Structural basis of human pregnane X receptor activation by the hops constituent colupulone." Teotico D.G., Bischof J.J., Peng L., Kliewer S.A., Redinbo M.R. Mol. Pharmacol. 74:1512-1520(2008) [PubMed: 18768384] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 130-434 IN COMPLEX WITH COLUPULONE, FUNCTION.
[18]	"Eleven novel single nucleotide polymorphisms in the NR1I2 (PXR) gene, four of which induce non-synonymous amino acid alterations." Koyano S., Kurose K., Ozawa S., Saeki M., Nakajima Y., Hasegawa R., Komamura K., Ueno K., Kamakura S., Nakajima T., Saito H., Kimura H., Goto Y., Saitoh O., Katoh M., Ohnuma T., Kawai M., Sugai K. , Ohtsuki T., Suzuki C., Minami N., Saito Y., Sawada J. Drug Metab. Pharmacokinet. 17:561-565(2002) [PubMed: 15618712] [Abstract] Cited for: VARIANTS CYS-98; GLN-148; TRP-381 AND VAL-403.
+	Additional computationally mapped references.

Web resources

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY091855 mRNA. Translation: AAM26736.1.
AF061056 mRNA. Translation: AAD05436.1.
AF084644 mRNA. Translation: AAC64557.1.
AF084645 mRNA. Translation: AAC64558.1.
AF364606 Genomic DNA. Translation: AAK38720.1.
AF364606 Genomic DNA. Translation: AAK38721.1.
AF364606 Genomic DNA. Translation: AAK38722.1.
AJ009936 mRNA. Translation: CAB55489.1.
AJ009936 mRNA. Translation: CAB55490.1.
AJ009936 mRNA. Translation: CAB55491.1.
AJ009937 mRNA. Translation: CAB55492.1.
AJ009937 mRNA. Translation: CAB55493.1.
AJ009937 mRNA. Translation: CAB55494.1.
DQ911122 Genomic DNA. Translation: ABJ52965.1.
DQ923326 Genomic DNA. Translation: ABJ52966.1.
EF614253 Genomic DNA. Translation: ABR09276.1.
BC017304 mRNA. Translation: AAH17304.2.

IPI

IPI00004364.
IPI00220084.
IPI00220085.
IPI00220086.
IPI00334983.
IPI00783954.
IPI00852956.

RefSeq

NP_003880.3. NM_003889.3.
NP_071285.1. NM_022002.2.
NP_148934.1. NM_033013.2.

UniGene

Hs.7303.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ILG	X-ray	2.52	A	130-434	[»]
1ILH	X-ray	2.76	A	130-434	[»]
1M13	X-ray	2.15	A	130-434	[»]
1NRL	X-ray	2.00	A/B	130-434	[»]
1SKX	X-ray	2.80	A	130-431	[»]
2O9I	X-ray	2.80	A/B	142-434	[»]
2QNV	X-ray	2.80	A	130-434	[»]
3CTB	X-ray	2.00	A/B	130-433	[»]
3HVL	X-ray	2.10	A/B	130-434	[»]
3R8D	X-ray	2.80	A	130-434	[»]

ProteinModelPortal

O75469.

SMR

O75469. Positions 39-124, 142-433.

DisProt

DP00323.

ModBase

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Protein-protein interaction databases

IntAct

O75469. 6 interactions.

STRING

O75469.

PTM databases

PhosphoSite

O75469.

Proteomic databases

PRIDE

O75469.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000337940; ENSP00000336528; ENSG00000144852.
ENST00000393716; ENSP00000377319; ENSG00000144852.
ENST00000393719; ENSP00000377321; ENSG00000144852.

GeneID

8856.

KEGG

hsa:8856.

UCSC

uc003edi.1. human.
uc003edj.1. human.
uc003edk.1. human.
uc003edl.1. human.

Organism-specific databases

CTD

8856.

GeneCards

GC03P119499.

HGNC

HGNC:7968. NR1I2.

MIM

603065. gene.

neXtProt

NX_O75469.

PharmGKB

PA378.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG09718.

GeneTree

ENSGT00570000079102.

HOVERGEN

HBG108655.

InParanoid

O75469.

OMA

GGKEIFS.

OrthoDB

EOG4QVCBX.

Enzyme and pathway databases

Reactome

REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

O75469.

Bgee

O75469.

Genevestigator

O75469.

GermOnline

ENSG00000144852. Homo sapiens.

Family and domain databases

InterPro

IPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR001723. Str_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]

Gene3D

G3DSA:1.10.565.10. Nucl_hrmn_rcpt_lig_bd. 2 hits.
G3DSA:3.30.50.10. Znf_NHR/GATA. 1 hit.

KO

K08540.

Pfam

PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]

PRINTS

PR00398. STRDHORMONER.
PR00047. STROIDFINGER.

SMART

SM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]

SUPFAM

SSF48508. Str_ncl_receptor. 1 hit.

PROSITE

PS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00783. Estradiol.
DB00977. Ethinyl Estradiol.
DB01045. Rifampin.
DB00163. Vitamin E.

NextBio

33249.

SOURCE

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Entry information

Entry name

NR1I2_HUMAN

Accession

Primary (citable) accession number: O75469
Secondary accession number(s): Q006P5 , Q008C8, Q96AC7, Q9UJ22, Q9UJ23, Q9UJ24, Q9UJ25, Q9UJ26, Q9UJ27, Q9UNW4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	November 1, 1998
Last modified:	January 25, 2012
This is version 138 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.