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Protein

Bile acid receptor

Gene

NR1H4

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

Functioni

Ligand-activated transcription factor. Receptor for bile acids such as chenodeoxycholic acid, lithocholic acid and deoxycholic acid. Represses the transcription of the cholesterol 7-alpha-hydroxylase gene (CYP7A1) through the induction of NR0B2 or FGF19 expression, via two distinct mechanisms. Activates the intestinal bile acid-binding protein (IBABP). Activates the transcription of bile salt export pump ABCB11 by directly recruiting histone methyltransferase CARM1 to this locus.8 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei375 – 3751AgonistBy similarity
Binding sitei383 – 3831AgonistBy similarity
Binding sitei461 – 4611AgonistBy similarity
Binding sitei483 – 4831AgonistBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi134 – 20976Nuclear receptorPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri137 – 15721NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri173 – 19725NR C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • bile acid and bile salt transport Source: Reactome
  • bile acid metabolic process Source: Reactome
  • cellular response to bile acid Source: BHF-UCL
  • cellular response to organonitrogen compound Source: BHF-UCL
  • digestive tract development Source: Ensembl
  • gene expression Source: Reactome
  • intracellular bile acid receptor signaling pathway Source: UniProtKB
  • intracellular receptor signaling pathway Source: BHF-UCL
  • negative regulation of bile acid biosynthetic process Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • nitrogen catabolite activation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • positive regulation of ammonia assimilation cycle Source: Ensembl
  • positive regulation of glutamate metabolic process Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • regulation of bile acid biosynthetic process Source: BHF-UCL
  • regulation of carbohydrate metabolic process Source: Ensembl
  • regulation of cholesterol metabolic process Source: BHF-UCL
  • regulation of urea metabolic process Source: BHF-UCL
  • response to glucose Source: Ensembl
  • response to lipopolysaccharide Source: Ensembl
  • signal transduction Source: ProtInc
  • small molecule metabolic process Source: Reactome
  • transcription initiation from RNA polymerase II promoter Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Activator, Receptor, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_11042. Recycling of bile acids and salts.
REACT_11048. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
REACT_11054. Synthesis of bile acids and bile salts.
REACT_116145. PPARA activates gene expression.
REACT_13812. Endogenous sterols.
REACT_15525. Nuclear Receptor transcription pathway.
SignaLinkiQ96RI1.

Names & Taxonomyi

Protein namesi
Recommended name:
Bile acid receptor
Alternative name(s):
Farnesoid X-activated receptor
Farnesol receptor HRR-1
Nuclear receptor subfamily 1 group H member 4
Retinoid X receptor-interacting protein 14
Short name:
RXR-interacting protein 14
Gene namesi
Name:NR1H4
Synonyms:BAR, FXR, HRR1, RIP14
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:7967. NR1H4.

Subcellular locationi

GO - Cellular componenti

  • nuclear euchromatin Source: BHF-UCL
  • nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

Orphaneti69665. Intrahepatic cholestasis of pregnancy.
PharmGKBiPA31752.

Chemistry

DrugBankiDB06777. Chenodeoxycholic acid.

Polymorphism and mutation databases

BioMutaiNR1H4.
DMDMi46577705.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 486486Bile acid receptorPRO_0000053538Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei220 – 2201N6-methyllysine; by SETD71 Publication

Post-translational modificationi

Methylation may increase transactivation of target genes.1 Publication

Keywords - PTMi

Methylation

Proteomic databases

PaxDbiQ96RI1.
PRIDEiQ96RI1.

PTM databases

PhosphoSiteiQ96RI1.

Expressioni

Gene expression databases

BgeeiQ96RI1.
CleanExiHS_NR1H4.
ExpressionAtlasiQ96RI1. baseline and differential.
GenevisibleiQ96RI1. HS.

Organism-specific databases

HPAiHPA047699.

Interactioni

Subunit structurei

Heterodimer of NR1H4 and RXR. After activation by agonist binding, interacts with a coactivator, NCOA1 or NCOA2 (By similarity). Interacts with CARM1 and SMARD1.By similarity9 Publications

Protein-protein interaction databases

BioGridi115296. 27 interactions.
DIPiDIP-39370N.
IntActiQ96RI1. 5 interactions.
STRINGi9606.ENSP00000447149.

Structurei

Secondary structure

1
486
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi261 – 27414Combined sources
Helixi281 – 2899Combined sources
Helixi294 – 31825Combined sources
Helixi322 – 3243Combined sources
Helixi327 – 35226Combined sources
Turni354 – 3563Combined sources
Helixi361 – 3677Combined sources
Turni368 – 3703Combined sources
Helixi373 – 38715Combined sources
Turni388 – 3903Combined sources
Helixi393 – 40412Combined sources
Beta strandi407 – 4115Combined sources
Helixi415 – 43622Combined sources
Helixi443 – 45614Combined sources
Helixi460 – 4656Combined sources
Beta strandi468 – 4725Combined sources
Helixi478 – 4803Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OSHX-ray1.80A258-486[»]
1OSKmodel-A258-486[»]
3BEJX-ray1.90A/B249-486[»]
3DCTX-ray2.50A252-486[»]
3DCUX-ray2.95A252-486[»]
3FLIX-ray2.00A258-486[»]
3FXVX-ray2.26A258-486[»]
3GD2X-ray3.20A260-486[»]
3HC5X-ray2.60A257-486[»]
3HC6X-ray3.20A257-486[»]
3L1BX-ray1.90A258-486[»]
3OKHX-ray2.50A258-486[»]
3OKIX-ray2.00A/C258-486[»]
3OLFX-ray1.90A/C258-486[»]
3OMKX-ray1.90A/C258-486[»]
3OMMX-ray2.10A/C258-486[»]
3OOFX-ray2.29A/C258-486[»]
3OOKX-ray2.29A/C258-486[»]
3P88X-ray2.95A258-486[»]
3P89X-ray2.30A258-486[»]
3RUTX-ray3.00A258-486[»]
3RUUX-ray2.50A258-486[»]
3RVFX-ray3.10A257-486[»]
4OIVX-ray1.70A/B258-483[»]
4WVDX-ray2.90A/B258-468[»]
ProteinModelPortaliQ96RI1.
SMRiQ96RI1. Positions 128-485.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96RI1.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni256 – 474219Ligand-bindingAdd
BLAST
Regioni342 – 3509Agonist bindingBy similarity

Sequence similaritiesi

Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri137 – 15721NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri173 – 19725NR C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG302915.
GeneTreeiENSGT00780000121834.
HOVERGENiHBG108655.
InParanoidiQ96RI1.
KOiK08537.
OMAiMKPAKGV.
OrthoDBiEOG7DC25S.
PhylomeDBiQ96RI1.
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.
IPR001728. ThyrH_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.
PR00546. THYROIDHORMR.
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 (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96RI1-3) [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
MVMQFQGLEN PIQISPHCSC TPSGFFMEMM SMKPAKGVLT EQVAGPLGQN
60 70 80 90 100
LEVEPYSQYS NVQFPQVQPQ ISSSSYYSNL GFYPQQPEEW YSPGIYELRR
110 120 130 140 150
MPAETLYQGE TEVAEMPVTK KPRMGASAGR IKGDELCVVC GDRASGYHYN
160 170 180 190 200
ALTCEGCKGF FRRSITKNAV YKCKNGGNCV MDMYMRRKCQ ECRLRKCKEM
210 220 230 240 250
GMLAECMYTG LLTEIQCKSK RLRKNVKQHA DQTVNEDSEG RDLRQVTSTT
260 270 280 290 300
KSCREKTELT PDQQTLLHFI MDSYNKQRMP QEITNKILKE EFSAEENFLI
310 320 330 340 350
LTEMATNHVQ VLVEFTKKLP GFQTLDHEDQ IALLKGSAVE AMFLRSAEIF
360 370 380 390 400
NKKLPSGHSD LLEERIRNSG ISDEYITPMF SFYKSIGELK MTQEEYALLT
410 420 430 440 450
AIVILSPDRQ YIKDREAVEK LQEPLLDVLQ KLCKIHQPEN PQHFACLLGR
460 470 480
LTELRTFNHH HAEMLMSWRV NDHKFTPLLC EIWDVQ
Length:486
Mass (Da):55,914
Last modified:April 26, 2004 - v2
Checksum:iC23283576A8CF76B
GO
Isoform 2 (identifier: Q96RI1-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     207-210: Missing.

Show »
Length:482
Mass (Da):55,462
Checksum:i2B9B563B0999C91D
GO
Isoform 3 (identifier: Q96RI1-1) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MVMQFQGLENPIQISPHCSCTPSGFFMEMMSMKPAK → MGSKMNLIEHSHLPTTDEFSFSENLF

Show »
Length:476
Mass (Da):54,862
Checksum:i37FB0351FB447544
GO
Isoform 4 (identifier: Q96RI1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MVMQFQGLENPIQISPHCSCTPSGFFMEMMSMKPAK → MGSKMNLIEHSHLPTTDEFSFSENLF
     207-210: Missing.

Show »
Length:472
Mass (Da):54,409
Checksum:i0A53D414B9049C4C
GO
Isoform 5 (identifier: Q96RI1-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MVMQFQGLENPIQISPHCSCTPSGFFMEMMSMKPAK → MGSKMNLIEHSHLPTTDEFSFSENLF
     159-209: Missing.

Note: No experimental confirmation available.
Show »
Length:425
Mass (Da):48,795
Checksum:iF29FB6B5C5FA2257
GO

Sequence cautioni

The sequence BC144183 differs from that shown. Reason: Frameshift at position 156. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti198 – 1981K → R in AAI44185 (PubMed:15489334).Curated
Sequence conflicti217 – 2171C → V in BC144183 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3636MVMQF…MKPAK → MGSKMNLIEHSHLPTTDEFS FSENLF in isoform 3, isoform 4 and isoform 5. 3 PublicationsVSP_010135Add
BLAST
Alternative sequencei159 – 20951Missing in isoform 5. 1 PublicationVSP_044547Add
BLAST
Alternative sequencei207 – 2104Missing in isoform 2 and isoform 4. 2 PublicationsVSP_003665

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U68233 mRNA. Translation: AAB08107.1.
AF384555 mRNA. Translation: AAK60271.1.
AF478445 mRNA. Translation: AAM53550.1.
AF478446 mRNA. Translation: AAM53551.1.
AK296612 mRNA. Translation: BAH12398.1.
AC010200 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97639.1.
BC144183 mRNA. No translation available.
BC144184 mRNA. Translation: AAI44185.1.
BC130573 mRNA. Translation: AAI30574.1.
CCDSiCCDS55873.1. [Q96RI1-1]
CCDS55874.1. [Q96RI1-5]
CCDS55875.1. [Q96RI1-4]
CCDS55876.1. [Q96RI1-3]
CCDS9078.1. [Q96RI1-2]
RefSeqiNP_001193906.1. NM_001206977.1. [Q96RI1-1]
NP_001193907.1. NM_001206978.1. [Q96RI1-5]
NP_001193908.1. NM_001206979.1. [Q96RI1-1]
NP_001193921.1. NM_001206992.1. [Q96RI1-4]
NP_001193922.1. NM_001206993.1. [Q96RI1-3]
NP_005114.1. NM_005123.3. [Q96RI1-2]
UniGeneiHs.282735.
Hs.732506.

Genome annotation databases

EnsembliENST00000188403; ENSP00000188403; ENSG00000012504. [Q96RI1-4]
ENST00000392986; ENSP00000376712; ENSG00000012504. [Q96RI1-1]
ENST00000548884; ENSP00000448506; ENSG00000012504. [Q96RI1-2]
ENST00000549996; ENSP00000448978; ENSG00000012504. [Q96RI1-5]
ENST00000551379; ENSP00000447149; ENSG00000012504. [Q96RI1-3]
GeneIDi9971.
KEGGihsa:9971.
UCSCiuc001ths.2. human. [Q96RI1-4]
uc001tht.2. human. [Q96RI1-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Wikipedia

Farnesoid X receptor entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U68233 mRNA. Translation: AAB08107.1.
AF384555 mRNA. Translation: AAK60271.1.
AF478445 mRNA. Translation: AAM53550.1.
AF478446 mRNA. Translation: AAM53551.1.
AK296612 mRNA. Translation: BAH12398.1.
AC010200 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97639.1.
BC144183 mRNA. No translation available.
BC144184 mRNA. Translation: AAI44185.1.
BC130573 mRNA. Translation: AAI30574.1.
CCDSiCCDS55873.1. [Q96RI1-1]
CCDS55874.1. [Q96RI1-5]
CCDS55875.1. [Q96RI1-4]
CCDS55876.1. [Q96RI1-3]
CCDS9078.1. [Q96RI1-2]
RefSeqiNP_001193906.1. NM_001206977.1. [Q96RI1-1]
NP_001193907.1. NM_001206978.1. [Q96RI1-5]
NP_001193908.1. NM_001206979.1. [Q96RI1-1]
NP_001193921.1. NM_001206992.1. [Q96RI1-4]
NP_001193922.1. NM_001206993.1. [Q96RI1-3]
NP_005114.1. NM_005123.3. [Q96RI1-2]
UniGeneiHs.282735.
Hs.732506.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OSHX-ray1.80A258-486[»]
1OSKmodel-A258-486[»]
3BEJX-ray1.90A/B249-486[»]
3DCTX-ray2.50A252-486[»]
3DCUX-ray2.95A252-486[»]
3FLIX-ray2.00A258-486[»]
3FXVX-ray2.26A258-486[»]
3GD2X-ray3.20A260-486[»]
3HC5X-ray2.60A257-486[»]
3HC6X-ray3.20A257-486[»]
3L1BX-ray1.90A258-486[»]
3OKHX-ray2.50A258-486[»]
3OKIX-ray2.00A/C258-486[»]
3OLFX-ray1.90A/C258-486[»]
3OMKX-ray1.90A/C258-486[»]
3OMMX-ray2.10A/C258-486[»]
3OOFX-ray2.29A/C258-486[»]
3OOKX-ray2.29A/C258-486[»]
3P88X-ray2.95A258-486[»]
3P89X-ray2.30A258-486[»]
3RUTX-ray3.00A258-486[»]
3RUUX-ray2.50A258-486[»]
3RVFX-ray3.10A257-486[»]
4OIVX-ray1.70A/B258-483[»]
4WVDX-ray2.90A/B258-468[»]
ProteinModelPortaliQ96RI1.
SMRiQ96RI1. Positions 128-485.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115296. 27 interactions.
DIPiDIP-39370N.
IntActiQ96RI1. 5 interactions.
STRINGi9606.ENSP00000447149.

Chemistry

BindingDBiQ96RI1.
ChEMBLiCHEMBL2047.
DrugBankiDB06777. Chenodeoxycholic acid.
GuidetoPHARMACOLOGYi603.

PTM databases

PhosphoSiteiQ96RI1.

Polymorphism and mutation databases

BioMutaiNR1H4.
DMDMi46577705.

Proteomic databases

PaxDbiQ96RI1.
PRIDEiQ96RI1.

Protocols and materials databases

DNASUi9971.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000188403; ENSP00000188403; ENSG00000012504. [Q96RI1-4]
ENST00000392986; ENSP00000376712; ENSG00000012504. [Q96RI1-1]
ENST00000548884; ENSP00000448506; ENSG00000012504. [Q96RI1-2]
ENST00000549996; ENSP00000448978; ENSG00000012504. [Q96RI1-5]
ENST00000551379; ENSP00000447149; ENSG00000012504. [Q96RI1-3]
GeneIDi9971.
KEGGihsa:9971.
UCSCiuc001ths.2. human. [Q96RI1-4]
uc001tht.2. human. [Q96RI1-3]

Organism-specific databases

CTDi9971.
GeneCardsiGC12P100867.
HGNCiHGNC:7967. NR1H4.
HPAiHPA047699.
MIMi603826. gene.
neXtProtiNX_Q96RI1.
Orphaneti69665. Intrahepatic cholestasis of pregnancy.
PharmGKBiPA31752.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG302915.
GeneTreeiENSGT00780000121834.
HOVERGENiHBG108655.
InParanoidiQ96RI1.
KOiK08537.
OMAiMKPAKGV.
OrthoDBiEOG7DC25S.
PhylomeDBiQ96RI1.
TreeFamiTF316304.

Enzyme and pathway databases

ReactomeiREACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_11042. Recycling of bile acids and salts.
REACT_11048. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
REACT_11054. Synthesis of bile acids and bile salts.
REACT_116145. PPARA activates gene expression.
REACT_13812. Endogenous sterols.
REACT_15525. Nuclear Receptor transcription pathway.
SignaLinkiQ96RI1.

Miscellaneous databases

EvolutionaryTraceiQ96RI1.
GeneWikiiFarnesoid_X_receptor.
GenomeRNAii9971.
NextBioi37658.
PROiQ96RI1.
SOURCEiSearch...

Gene expression databases

BgeeiQ96RI1.
CleanExiHS_NR1H4.
ExpressionAtlasiQ96RI1. baseline and differential.
GenevisibleiQ96RI1. 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.
IPR001728. ThyrH_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.
PR00546. THYROIDHORMR.
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. "The identification of the cDNA coding for HRR-1, a novel human farnesol receptor."
    Papetti M., Wood N., Lohmar P.D., Bowman M.R.
    Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  2. "Functional analysis of human farnesol receptor (NR1H4) splicing variant."
    Han J.-I., Bok S.-H., Jeong T.-S.
    Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
  3. "Generation of multiple farnesoid-X-receptor isoforms through the use of alternative promoters."
    Huber R.M., Murphy K., Miao B., Link J.R., Cunningham M.R., Rupar M.J., Gunyuzlu P.L., Haws T.F. Jr., Kassam A., Powell F., Hollis G.F., Young P.R., Mukherjee R., Burn T.C.
    Gene 290:35-43(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
  4. "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).
    Tissue: Colon.
  5. "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].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORMS 3 AND 5).
  8. Cited for: FUNCTION.
  9. Cited for: FUNCTION.
  10. "Definition of a novel growth factor-dependent signal cascade for the suppression of bile acid biosynthesis."
    Holt J.A., Luo G., Billin A.N., Bisi J., McNeill Y.Y., Kozarsky K.F., Donahee M., Wang D.Y., Mansfield T.A., Kliewer S.A., Goodwin B., Jones S.A.
    Genes Dev. 17:1581-1591(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "BAF60a mediates critical interactions between nuclear receptors and the BRG1 chromatin-remodeling complex for transactivation."
    Hsiao P.W., Fryer C.J., Trotter K.W., Wang W., Archer T.K.
    Mol. Cell. Biol. 23:6210-6220(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SMARD1.
  12. "Ligand-dependent activation of the farnesoid X-receptor directs arginine methylation of histone H3 by CARM1."
    Ananthanarayanan M., Li S., Balasubramaniyan N., Suchy F.J., Walsh M.J.
    J. Biol. Chem. 279:54348-54357(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CARM1.
  13. "Direct methylation of FXR by Set7/9, a lysine methyltransferase, regulates the expression of FXR target genes."
    Balasubramaniyan N., Ananthanarayanan M., Suchy F.J.
    Am. J. Physiol. 302:G937-G947(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT LYS-220 BY SETD7.
  14. Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 258-476 IN COMPLEX WITH SYNTHETIC AGONIST FEXARAMINE, FUNCTION, INTERACTION WITH NCOA1.
  15. "Structural basis for bile acid binding and activation of the nuclear receptor FXR."
    Mi L.Z., Devarakonda S., Harp J.M., Han Q., Pellicciari R., Willson T.M., Khorasanizadeh S., Rastinejad F.
    Mol. Cell 11:1093-1100(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 241-469 IN COMPLEXES WITH CHENODEOXYCHOLIC ACID ANALOGS AND NCOA2 COACTIVATOR PEPTIDE.
  16. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 252-486 IN COMPLEX WITH SYNTHETIC AGONIST, FUNCTION, INTERACTION WITH NCOA1.
  17. "Identification of a potent synthetic FXR agonist with an unexpected mode of binding and activation."
    Soisson S.M., Parthasarathy G., Adams A.D., Sahoo S., Sitlani A., Sparrow C., Cui J., Becker J.W.
    Proc. Natl. Acad. Sci. U.S.A. 105:5337-5342(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 249-486 IN COMPLEX WITH STEROID ANALOG MFA-1 AND NCOA1 PEPTIDE, INTERACTION WITH NCOA1, DOMAIN.
  18. Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 260-486 IN COMPLEX WITH SYNTHETIC AGONIST, FUNCTION, INTERACTION WITH NCOA1.
  19. Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 257-486 IN COMPLEX WITH SYNTHETIC AGONIST, FUNCTION, INTERACTION WITH NCOA1.
  20. "Discovery of XL335 (WAY-362450), a highly potent, selective, and orally active agonist of the farnesoid X receptor (FXR)."
    Flatt B., Martin R., Wang T.L., Mahaney P., Murphy B., Gu X.H., Foster P., Li J., Pircher P., Petrowski M., Schulman I., Westin S., Wrobel J., Yan G., Bischoff E., Daige C., Mohan R.
    J. Med. Chem. 52:904-907(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 258-486 IN COMPLEX WITH SYNTHETIC AGONIST.
  21. "Improvement of physiochemical properties of the tetrahydroazepinoindole series of farnesoid X receptor (FXR) agonists: beneficial modulation of lipids in primates."
    Lundquist J.T., Harnish D.C., Kim C.Y., Mehlmann J.F., Unwalla R.J., Phipps K.M., Crawley M.L., Commons T., Green D.M., Xu W., Hum W.T., Eta J.E., Feingold I., Patel V., Evans M.J., Lai K., Borges-Marcucci L., Mahaney P.E., Wrobel J.E.
    J. Med. Chem. 53:1774-1787(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 248-476 IN COMPLEX WITH SYNTHETIC AGONIST.

Entry informationi

Entry nameiNR1H4_HUMAN
AccessioniPrimary (citable) accession number: Q96RI1
Secondary accession number(s): A1L4K5
, B7Z412, B7ZM06, F8VYG8, Q8NFP5, Q8NFP6, Q92943
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: April 26, 2004
Last modified: June 24, 2015
This is version 152 of the entry and version 2 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

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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.