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Q96RI1

- NR1H4_HUMAN

UniProt

Q96RI1 - NR1H4_HUMAN

Protein

Bile acid receptor

Gene

NR1H4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 2 (26 Apr 2004)
      Previous versions | rss
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    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

    1. bile acid binding Source: BHF-UCL
    2. bile acid receptor activity Source: UniProtKB
    3. chenodeoxycholic acid binding Source: UniProtKB
    4. ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: BHF-UCL
    5. ligand-dependent nuclear receptor binding Source: BHF-UCL
    6. peptide binding Source: Ensembl
    7. protein binding Source: UniProtKB
    8. RNA polymerase II distal enhancer sequence-specific DNA binding Source: BHF-UCL
    9. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    10. RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription Source: BHF-UCL
    11. sequence-specific DNA binding Source: UniProtKB
    12. sequence-specific DNA binding transcription factor activity Source: ProtInc
    13. steroid hormone receptor activity Source: Ensembl
    14. thyroid hormone receptor activity Source: InterPro
    15. transcription coactivator activity Source: ProtInc
    16. transcription corepressor activity Source: ProtInc
    17. zinc ion binding Source: InterPro

    GO - Biological processi

    1. bile acid metabolic process Source: Ensembl
    2. cellular response to acid chemical Source: BHF-UCL
    3. cellular response to organonitrogen compound Source: BHF-UCL
    4. digestive tract development Source: Ensembl
    5. gene expression Source: Reactome
    6. intracellular bile acid receptor signaling pathway Source: UniProtKB
    7. intracellular receptor signaling pathway Source: BHF-UCL
    8. negative regulation of bile acid biosynthetic process Source: UniProtKB
    9. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    10. nitrogen catabolite activation of transcription from RNA polymerase II promoter Source: BHF-UCL
    11. positive regulation of ammonia assimilation cycle Source: Ensembl
    12. positive regulation of glutamate metabolic process Source: BHF-UCL
    13. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    14. regulation of bile acid biosynthetic process Source: BHF-UCL
    15. regulation of carbohydrate metabolic process Source: Ensembl
    16. regulation of cholesterol metabolic process Source: BHF-UCL
    17. regulation of urea metabolic process Source: BHF-UCL
    18. response to glucose Source: Ensembl
    19. response to lipopolysaccharide Source: Ensembl
    20. signal transduction Source: ProtInc
    21. transcription initiation from RNA polymerase II promoter Source: Reactome

    Keywords - Molecular functioni

    Activator, Receptor, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_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: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:7967. NR1H4.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. nuclear euchromatin Source: BHF-UCL
    2. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti69665. Intrahepatic cholestasis of pregnancy.
    PharmGKBiPA31752.

    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

    ArrayExpressiQ96RI1.
    BgeeiQ96RI1.
    CleanExiHS_NR1H4.
    GenevestigatoriQ96RI1.

    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. 26 interactions.
    DIPiDIP-39370N.
    IntActiQ96RI1. 5 interactions.
    STRINGi9606.ENSP00000315442.

    Structurei

    Secondary structure

    1
    486
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi261 – 27414
    Helixi281 – 2899
    Helixi297 – 31721
    Helixi322 – 3243
    Helixi327 – 35226
    Helixi356 – 36712
    Turni368 – 3703
    Turni373 – 3753
    Helixi376 – 38712
    Turni388 – 3903
    Helixi393 – 40412
    Beta strandi407 – 4115
    Helixi415 – 43622
    Helixi443 – 45513
    Helixi457 – 47014
    Helixi477 – 4837

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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[»]
    4II6X-ray2.90A/B258-473[»]
    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.
    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. Align

    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

    MVMQFQGLEN PIQISPHCSC TPSGFFMEMM SMKPAKGVLT EQVAGPLGQN    50
    LEVEPYSQYS NVQFPQVQPQ ISSSSYYSNL GFYPQQPEEW YSPGIYELRR 100
    MPAETLYQGE TEVAEMPVTK KPRMGASAGR IKGDELCVVC GDRASGYHYN 150
    ALTCEGCKGF FRRSITKNAV YKCKNGGNCV MDMYMRRKCQ ECRLRKCKEM 200
    GMLAECMYTG LLTEIQCKSK RLRKNVKQHA DQTVNEDSEG RDLRQVTSTT 250
    KSCREKTELT PDQQTLLHFI MDSYNKQRMP QEITNKILKE EFSAEENFLI 300
    LTEMATNHVQ VLVEFTKKLP GFQTLDHEDQ IALLKGSAVE AMFLRSAEIF 350
    NKKLPSGHSD LLEERIRNSG ISDEYITPMF SFYKSIGELK MTQEEYALLT 400
    AIVILSPDRQ YIKDREAVEK LQEPLLDVLQ KLCKIHQPEN PQHFACLLGR 450
    LTELRTFNHH HAEMLMSWRV NDHKFTPLLC EIWDVQ 486
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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]

    Polymorphism databases

    DMDMi46577705.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Farnesoid X receptor entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS55873.1. [Q96RI1-1 ]
    CCDS55874.1. [Q96RI1-5 ]
    CCDS55875.1. [Q96RI1-4 ]
    CCDS55876.1. [Q96RI1-3 ]
    CCDS9078.1. [Q96RI1-2 ]
    RefSeqi NP_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 ]
    UniGenei Hs.282735.
    Hs.732506.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1OSH X-ray 1.80 A 258-486 [» ]
    1OSK model - A 258-486 [» ]
    3BEJ X-ray 1.90 A/B 249-486 [» ]
    3DCT X-ray 2.50 A 252-486 [» ]
    3DCU X-ray 2.95 A 252-486 [» ]
    3FLI X-ray 2.00 A 258-486 [» ]
    3FXV X-ray 2.26 A 258-486 [» ]
    3GD2 X-ray 3.20 A 260-486 [» ]
    3HC5 X-ray 2.60 A 257-486 [» ]
    3HC6 X-ray 3.20 A 257-486 [» ]
    3L1B X-ray 1.90 A 258-486 [» ]
    3OKH X-ray 2.50 A 258-486 [» ]
    3OKI X-ray 2.00 A/C 258-486 [» ]
    3OLF X-ray 1.90 A/C 258-486 [» ]
    3OMK X-ray 1.90 A/C 258-486 [» ]
    3OMM X-ray 2.10 A/C 258-486 [» ]
    3OOF X-ray 2.29 A/C 258-486 [» ]
    3OOK X-ray 2.29 A/C 258-486 [» ]
    3P88 X-ray 2.95 A 258-486 [» ]
    3P89 X-ray 2.30 A 258-486 [» ]
    3RUT X-ray 3.00 A 258-486 [» ]
    3RUU X-ray 2.50 A 258-486 [» ]
    3RVF X-ray 3.10 A 257-486 [» ]
    4II6 X-ray 2.90 A/B 258-473 [» ]
    ProteinModelPortali Q96RI1.
    SMRi Q96RI1. Positions 128-485.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115296. 26 interactions.
    DIPi DIP-39370N.
    IntActi Q96RI1. 5 interactions.
    STRINGi 9606.ENSP00000315442.

    Chemistry

    BindingDBi Q96RI1.
    ChEMBLi CHEMBL2047.
    GuidetoPHARMACOLOGYi 603.

    PTM databases

    PhosphoSitei Q96RI1.

    Polymorphism databases

    DMDMi 46577705.

    Proteomic databases

    PaxDbi Q96RI1.
    PRIDEi Q96RI1.

    Protocols and materials databases

    DNASUi 9971.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000188403 ; ENSP00000188403 ; ENSG00000012504 . [Q96RI1-4 ]
    ENST00000392986 ; ENSP00000376712 ; ENSG00000012504 . [Q96RI1-1 ]
    ENST00000548884 ; ENSP00000448506 ; ENSG00000012504 . [Q96RI1-2 ]
    ENST00000549996 ; ENSP00000448978 ; ENSG00000012504 . [Q96RI1-5 ]
    ENST00000551379 ; ENSP00000447149 ; ENSG00000012504 . [Q96RI1-3 ]
    GeneIDi 9971.
    KEGGi hsa:9971.
    UCSCi uc001ths.2. human. [Q96RI1-4 ]
    uc001tht.2. human. [Q96RI1-3 ]

    Organism-specific databases

    CTDi 9971.
    GeneCardsi GC12P100867.
    HGNCi HGNC:7967. NR1H4.
    HPAi HPA047699.
    MIMi 603826. gene.
    neXtProti NX_Q96RI1.
    Orphaneti 69665. Intrahepatic cholestasis of pregnancy.
    PharmGKBi PA31752.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG302915.
    HOVERGENi HBG108655.
    InParanoidi Q96RI1.
    KOi K08537.
    OMAi MKPAKGV.
    OrthoDBi EOG7DC25S.
    PhylomeDBi Q96RI1.
    TreeFami TF316304.

    Enzyme and pathway databases

    Reactomei REACT_15525. Nuclear Receptor transcription pathway.
    SignaLinki Q96RI1.

    Miscellaneous databases

    EvolutionaryTracei Q96RI1.
    GeneWikii Farnesoid_X_receptor.
    GenomeRNAii 9971.
    NextBioi 37658.
    PROi Q96RI1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96RI1.
    Bgeei Q96RI1.
    CleanExi HS_NR1H4.
    Genevestigatori Q96RI1.

    Family and domain databases

    Gene3Di 1.10.565.10. 2 hits.
    3.30.50.10. 1 hit.
    InterProi IPR008946. 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 ]
    Pfami PF00104. Hormone_recep. 1 hit.
    PF00105. zf-C4. 1 hit.
    [Graphical view ]
    PRINTSi PR00398. STRDHORMONER.
    PR00047. STROIDFINGER.
    PR00546. THYROIDHORMR.
    SMARTi SM00430. HOLI. 1 hit.
    SM00399. ZnF_C4. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48508. SSF48508. 1 hit.
    PROSITEi PS00031. NUCLEAR_REC_DBD_1. 1 hit.
    PS51030. NUCLEAR_REC_DBD_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 144 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