Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q96RI1 (NR1H4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:NR1H4
Synonyms:BAR, FXR, HRR1, RIP14
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length486 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.9 Ref.10 Ref.12 Ref.14 Ref.16 Ref.18 Ref.19

Subunit structure

Heterodimer of NR1H4 and RXR. After activation by agonist binding, interacts with a coactivator, NCOA1 or NCOA2 By similarity. Interacts with CARM1 and SMARD1. Ref.11 Ref.12 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19

Subcellular location

Nucleus Probable.

Post-translational modification

Methylation may increase transactivation of target genes. Ref.13

Sequence similarities

Belongs to the nuclear hormone receptor family. NR1 subfamily.

Contains 1 nuclear receptor DNA-binding domain.

Sequence caution

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

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
Receptor
Repressor
   PTMMethylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbile acid metabolic process

Inferred from electronic annotation. Source: Ensembl

cellular response to acid

Inferred from direct assay PubMed 21757002. Source: BHF-UCL

digestive tract development

Inferred from electronic annotation. Source: Ensembl

intracellular bile acid receptor signaling pathway

Inferred from direct assay Ref.8. Source: UniProtKB

negative regulation of bile acid biosynthetic process

Inferred from direct assay Ref.8. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity PubMed 21757002. Source: BHF-UCL

nitrogen catabolite activation of transcription from RNA polymerase II promoter

Inferred by curator PubMed 21757002. Source: BHF-UCL

positive regulation of ammonia assimilation cycle

Inferred from electronic annotation. Source: Ensembl

positive regulation of glutamate metabolic process

Inferred from sequence or structural similarity PubMed 21757002. Source: BHF-UCL

regulation of carbohydrate metabolic process

Inferred from electronic annotation. Source: Ensembl

regulation of cholesterol metabolic process

Traceable author statement PubMed 21757002. Source: BHF-UCL

regulation of urea metabolic process

Inferred from sequence or structural similarity PubMed 21757002. Source: BHF-UCL

response to glucose

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

   Cellular_componentnuclear euchromatin

Inferred from direct assay PubMed 21757002. Source: BHF-UCL

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionRNA polymerase II distal enhancer sequence-specific DNA binding

Inferred from direct assay PubMed 21757002. Source: BHF-UCL

RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 21757002. Source: BHF-UCL

RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription

Inferred from direct assay PubMed 21757002. Source: BHF-UCL

bile acid receptor activity

Inferred from direct assay Ref.8. Source: UniProtKB

chenodeoxycholic acid binding

Inferred from direct assay Ref.8. Source: UniProtKB

ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from sequence or structural similarity PubMed 21757002. Source: BHF-UCL

ligand-dependent nuclear receptor binding

Traceable author statement PubMed 21757002. Source: BHF-UCL

peptide binding

Inferred from electronic annotation. Source: Ensembl

steroid hormone receptor activity

Inferred from electronic annotation. Source: Ensembl

thyroid hormone receptor activity

Inferred from electronic annotation. Source: InterPro

transcription coactivator activity

Traceable author statement Ref.8. Source: ProtInc

transcription corepressor activity

Traceable author statement Ref.8. Source: ProtInc

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96RI1-3)

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 2 (identifier: Q96RI1-4)

The sequence of this isoform differs from the canonical sequence as follows:
     207-210: Missing.
Isoform 3 (identifier: Q96RI1-1)

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MVMQFQGLENPIQISPHCSCTPSGFFMEMMSMKPAK → MGSKMNLIEHSHLPTTDEFSFSENLF
Isoform 4 (identifier: Q96RI1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MVMQFQGLENPIQISPHCSCTPSGFFMEMMSMKPAK → MGSKMNLIEHSHLPTTDEFSFSENLF
     207-210: Missing.
Isoform 5 (identifier: Q96RI1-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MVMQFQGLENPIQISPHCSCTPSGFFMEMMSMKPAK → MGSKMNLIEHSHLPTTDEFSFSENLF
     159-209: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 486486Bile acid receptor
PRO_0000053538

Regions

DNA binding134 – 20976Nuclear receptor
Zinc finger137 – 15721NR C4-type
Zinc finger173 – 19725NR C4-type
Region256 – 474219Ligand-binding
Region342 – 3509Agonist binding By similarity

Sites

Binding site3751Agonist By similarity
Binding site3831Agonist By similarity
Binding site4611Agonist By similarity
Binding site4831Agonist By similarity

Amino acid modifications

Modified residue2201N6-methyllysine; by SETD7 Ref.13

Natural variations

Alternative sequence1 – 3636MVMQF…MKPAK → MGSKMNLIEHSHLPTTDEFS FSENLF in isoform 3, isoform 4 and isoform 5.
VSP_010135
Alternative sequence159 – 20951Missing in isoform 5.
VSP_044547
Alternative sequence207 – 2104Missing in isoform 2 and isoform 4.
VSP_003665

Experimental info

Sequence conflict1981K → R in AAI44185. Ref.7
Sequence conflict2171C → V in BC144183. Ref.7

Secondary structure

.............................. 486
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 26, 2004. Version 2.
Checksum: C23283576A8CF76B

FASTA48655,914
        10         20         30         40         50         60 
MVMQFQGLEN PIQISPHCSC TPSGFFMEMM SMKPAKGVLT EQVAGPLGQN LEVEPYSQYS 

        70         80         90        100        110        120 
NVQFPQVQPQ ISSSSYYSNL GFYPQQPEEW YSPGIYELRR MPAETLYQGE TEVAEMPVTK 

       130        140        150        160        170        180 
KPRMGASAGR IKGDELCVVC GDRASGYHYN ALTCEGCKGF FRRSITKNAV YKCKNGGNCV 

       190        200        210        220        230        240 
MDMYMRRKCQ ECRLRKCKEM GMLAECMYTG LLTEIQCKSK RLRKNVKQHA DQTVNEDSEG 

       250        260        270        280        290        300 
RDLRQVTSTT KSCREKTELT PDQQTLLHFI MDSYNKQRMP QEITNKILKE EFSAEENFLI 

       310        320        330        340        350        360 
LTEMATNHVQ VLVEFTKKLP GFQTLDHEDQ IALLKGSAVE AMFLRSAEIF NKKLPSGHSD 

       370        380        390        400        410        420 
LLEERIRNSG ISDEYITPMF SFYKSIGELK MTQEEYALLT AIVILSPDRQ YIKDREAVEK 

       430        440        450        460        470        480 
LQEPLLDVLQ KLCKIHQPEN PQHFACLLGR LTELRTFNHH HAEMLMSWRV NDHKFTPLLC 


EIWDVQ 

« Hide

Isoform 2 [UniParc].

Checksum: 2B9B563B0999C91D
Show »

FASTA48255,462
Isoform 3 [UniParc].

Checksum: 37FB0351FB447544
Show »

FASTA47654,862
Isoform 4 [UniParc].

Checksum: 0A53D414B9049C4C
Show »

FASTA47254,409
Isoform 5 [UniParc].

Checksum: F29FB6B5C5FA2257
Show »

FASTA42548,795

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Identification of a nuclear receptor for bile acids."
Makishima M., Okamoto A.Y., Repa J.J., Tu H., Learned R.M., Luk A., Hull M.V., Lustig K.D., Mangelsdorf D.J., Shan B.
Science 284:1362-1365(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Bile acids: natural ligands for an orphan nuclear receptor."
Parks D.J., Blanchard S.G., Bledsoe R.K., Chandra G., Consler T.G., Kliewer S.A., Stimmel J.B., Willson T.M., Zavacki A.M., Moore D.D., Lehmann J.M.
Science 284:1365-1368(1999) [PubMed] [Europe PMC] [Abstract]
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]"A chemical, genetic, and structural analysis of the nuclear bile acid receptor FXR."
Downes M., Verdecia M.A., Roecker A.J., Hughes R., Hogenesch J.B., Kast-Woelbern H.R., Bowman M.E., Ferrer J.L., Anisfeld A.M., Edwards P.A., Rosenfeld J.M., Alvarez J.G., Noel J.P., Nicolaou K.C., Evans R.M.
Mol. Cell 11:1079-1092(2003) [PubMed] [Europe PMC] [Abstract]
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]"Conformationally constrained farnesoid X receptor (FXR) agonists: Naphthoic acid-based analogs of GW 4064."
Akwabi-Ameyaw A., Bass J.Y., Caldwell R.D., Caravella J.A., Chen L., Creech K.L., Deaton D.N., Jones S.A., Kaldor I., Liu Y., Madauss K.P., Marr H.B., McFadyen R.B., Miller A.B., Iii F.N., Parks D.J., Spearing P.K., Todd D., Williams S.P., Wisely G.B.
Bioorg. Med. Chem. Lett. 18:4339-4343(2008) [PubMed] [Europe PMC] [Abstract]
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]"Substituted isoxazole analogs of farnesoid X receptor (FXR) agonist GW4064."
Bass J.Y., Caldwell R.D., Caravella J.A., Chen L., Creech K.L., Deaton D.N., Madauss K.P., Marr H.B., McFadyen R.B., Miller A.B., Parks D.J., Todd D., Williams S.P., Wisely G.B.
Bioorg. Med. Chem. Lett. 19:2969-2973(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 260-486 IN COMPLEX WITH SYNTHETIC AGONIST, FUNCTION, INTERACTION WITH NCOA1.
[19]"FXR agonist activity of conformationally constrained analogs of GW 4064."
Akwabi-Ameyaw A., Bass J.Y., Caldwell R.D., Caravella J.A., Chen L., Creech K.L., Deaton D.N., Madauss K.P., Marr H.B., McFadyen R.B., Miller A.B., Navas F. III, Parks D.J., Spearing P.K., Todd D., Williams S.P., Bruce Wisely G.
Bioorg. Med. Chem. Lett. 19:4733-4739(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Wikipedia

Farnesoid X receptor entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001193906.1. NM_001206977.1.
NP_001193907.1. NM_001206978.1.
NP_001193908.1. NM_001206979.1.
NP_001193921.1. NM_001206992.1.
NP_001193922.1. NM_001206993.1.
NP_005114.1. NM_005123.3.
UniGeneHs.282735.
Hs.732506.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OSHX-ray1.80A258-476[»]
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[»]
4II6X-ray2.90A/B258-473[»]
ProteinModelPortalQ96RI1.
SMRQ96RI1. Positions 134-485.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115296. 26 interactions.
DIPDIP-39370N.
IntActQ96RI1. 4 interactions.
STRING9606.ENSP00000315442.

Chemistry

BindingDBQ96RI1.
ChEMBLCHEMBL2047.
GuidetoPHARMACOLOGY603.

PTM databases

PhosphoSiteQ96RI1.

Polymorphism databases

DMDM46577705.

Proteomic databases

PaxDbQ96RI1.
PRIDEQ96RI1.

Protocols and materials databases

DNASU9971.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000188403; ENSP00000188403; ENSG00000012504. [Q96RI1-4]
ENST00000392986; ENSP00000376712; ENSG00000012504. [Q96RI1-1]
ENST00000548884; ENSP00000448506; ENSG00000012504. [Q96RI1-2]
ENST00000549996; ENSP00000448978; ENSG00000012504. [Q96RI1-5]
ENST00000551379; ENSP00000447149; ENSG00000012504. [Q96RI1-3]
GeneID9971.
KEGGhsa:9971.
UCSCuc001ths.2. human. [Q96RI1-4]
uc001tht.2. human. [Q96RI1-3]

Organism-specific databases

CTD9971.
GeneCardsGC12P100867.
HGNCHGNC:7967. NR1H4.
HPAHPA047699.
MIM603826. gene.
neXtProtNX_Q96RI1.
Orphanet69665. Intrahepatic cholestasis of pregnancy.
PharmGKBPA31752.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG302915.
HOVERGENHBG108655.
InParanoidQ96RI1.
KOK08537.
OMAMKPAKGV.
OrthoDBEOG7DC25S.
PhylomeDBQ96RI1.
TreeFamTF316304.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.
SignaLinkQ96RI1.

Gene expression databases

ArrayExpressQ96RI1.
BgeeQ96RI1.
CleanExHS_NR1H4.
GenevestigatorQ96RI1.

Family and domain databases

Gene3D1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProIPR008946. 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]
PfamPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSPR00398. STRDHORMONER.
PR00047. STROIDFINGER.
PR00546. THYROIDHORMR.
SMARTSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMSSF48508. SSF48508. 1 hit.
PROSITEPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ96RI1.
GeneWikiFarnesoid_X_receptor.
GenomeRNAi9971.
NextBio37658.
PROQ96RI1.
SOURCESearch...

Entry information

Entry nameNR1H4_HUMAN
AccessionPrimary (citable) accession number: Q96RI1
Secondary accession number(s): A1L4K5 expand/collapse secondary AC list , B7Z412, B7ZM06, F8VYG8, Q8NFP5, Q8NFP6, Q92943
Entry history
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: April 26, 2004
Last modified: March 19, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM