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P28702

- RXRB_HUMAN

UniProt

P28702 - RXRB_HUMAN

Protein

Retinoic acid receptor RXR-beta

Gene

RXRB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 167 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 By similarity. Specifically binds 9-cis retinoic acid (9C-RA).By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi205 – 27066Nuclear receptorPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri205 – 22521NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri241 – 26525NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. 9-cis retinoic acid receptor activity Source: ProtInc
    2. ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: BHF-UCL
    3. protein binding Source: IntAct
    4. RNA polymerase II regulatory region sequence-specific DNA binding Source: NTNU_SB
    5. RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
    6. sequence-specific DNA binding transcription factor activity Source: ProtInc
    7. steroid hormone receptor activity Source: InterPro
    8. transcription coactivator activity Source: ProtInc
    9. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cardiac muscle cell proliferation Source: Ensembl
    2. cellular response to retinoic acid Source: Ensembl
    3. gene expression Source: Reactome
    4. in utero embryonic development Source: Ensembl
    5. maternal placenta development Source: Ensembl
    6. positive regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
    7. transcription initiation from RNA polymerase II promoter Source: Reactome
    8. ventricular cardiac muscle cell differentiation Source: Ensembl

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_15525. Nuclear Receptor transcription pathway.
    SignaLinkiP28702.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Retinoic acid receptor RXR-beta
    Alternative name(s):
    Nuclear receptor subfamily 2 group B member 2
    Retinoid X receptor beta
    Gene namesi
    Name:RXRB
    Synonyms:NR2B2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:10478. RXRB.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome
    2. nucleus Source: HGNC

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34891.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 533533Retinoic acid receptor RXR-betaPRO_0000053572Add
    BLAST

    Proteomic databases

    MaxQBiP28702.
    PaxDbiP28702.
    PRIDEiP28702.

    PTM databases

    PhosphoSiteiP28702.

    Expressioni

    Tissue specificityi

    Expressed in a variety of tumor cell lines.1 Publication

    Gene expression databases

    ArrayExpressiP28702.
    BgeeiP28702.
    CleanExiHS_RXRB.
    GenevestigatoriP28702.

    Organism-specific databases

    HPAiCAB002003.

    Interactioni

    Subunit structurei

    Homodimer By similarity. Heterodimer with a RAR molecule. Binds DNA preferentially as a RAR/RXR heterodimer.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CACNA1BQ009753EBI-748576,EBI-1055161

    Protein-protein interaction databases

    BioGridi112169. 29 interactions.
    IntActiP28702. 31 interactions.
    MINTiMINT-1365658.
    STRINGi9606.ENSP00000363812.

    Structurei

    Secondary structure

    1
    533
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi301 – 3099
    Helixi336 – 34712
    Helixi350 – 3556
    Helixi360 – 3623
    Helixi365 – 38723
    Turni388 – 3903
    Beta strandi394 – 3963
    Beta strandi402 – 4043
    Helixi405 – 4117
    Helixi414 – 42310
    Helixi425 – 4317
    Helixi435 – 44612
    Helixi457 – 47822
    Helixi485 – 4906
    Helixi493 – 51321
    Helixi517 – 5215

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1H9UX-ray2.70A/B/C/D299-522[»]
    1UHLX-ray2.90A298-533[»]
    ProteinModelPortaliP28702.
    SMRiP28702. Positions 202-532.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP28702.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 204204ModulatingBy similarityAdd
    BLAST
    Regioni271 – 33060HingeAdd
    BLAST
    Regioni331 – 533203Ligand-bindingBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi61 – 198138Pro-richAdd
    BLAST

    Domaini

    Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri205 – 22521NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri241 – 26525NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG327099.
    HOGENOMiHOG000260821.
    HOVERGENiHBG005606.
    KOiK08525.
    OMAiFLPERHA.
    PhylomeDBiP28702.
    TreeFamiTF352097.

    Family and domain databases

    Gene3Di1.10.565.10. 1 hit.
    3.30.50.10. 1 hit.
    InterProiIPR008946. Nucl_hormone_rcpt_ligand-bd.
    IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
    IPR000003. Retinoid-X_rcpt/HNF4.
    IPR001723. Str_hrmn_rcpt.
    IPR001628. Znf_hrmn_rcpt.
    IPR013088. Znf_NHR/GATA.
    [Graphical view]
    PfamiPF00104. Hormone_recep. 1 hit.
    PF00105. zf-C4. 1 hit.
    [Graphical view]
    PRINTSiPR00545. RETINOIDXR.
    PR00398. STRDHORMONER.
    PR00047. STROIDFINGER.
    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 (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P28702-1) [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

    MSWAARPPFL PQRHAAGQCG PVGVRKEMHC GVASRWRRRR PWLDPAAAAA    50
    AAVAGGEQQT PEPEPGEAGR DGMGDSGRDS RSPDSSSPNP LPQGVPPPSP 100
    PGPPLPPSTA PSLGGSGAPP PPPMPPPPLG SPFPVISSSM GSPGLPPPAP 150
    PGFSGPVSSP QINSTVSLPG GGSGPPEDVK PPVLGVRGLH CPPPPGGPGA 200
    GKRLCAICGD RSSGKHYGVY SCEGCKGFFK RTIRKDLTYS CRDNKDCTVD 250
    KRQRNRCQYC RYQKCLATGM KREAVQEERQ RGKDKDGDGE GAGGAPEEMP 300
    VDRILEAELA VEQKSDQGVE GPGGTGGSGS SPNDPVTNIC QAADKQLFTL 350
    VEWAKRIPHF SSLPLDDQVI LLRAGWNELL IASFSHRSID VRDGILLATG 400
    LHVHRNSAHS AGVGAIFDRV LTELVSKMRD MRMDKTELGC LRAIILFNPD 450
    AKGLSNPSEV EVLREKVYAS LETYCKQKYP EQQGRFAKLL LRLPALRSIG 500
    LKCLEHLFFF KLIGDTPIDT FLMEMLEAPH QLA 533
    Length:533
    Mass (Da):56,922
    Last modified:February 1, 1996 - v2
    Checksum:iD0069FE93AC16A04
    GO
    Isoform 2 (identifier: P28702-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         418-418: D → DRSLS

    Show »
    Length:537
    Mass (Da):57,365
    Checksum:iE6789FB00428DA2C
    GO

    Sequence cautioni

    The sequence BAD92481.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti112 – 1121S → T in AAA60293. (PubMed:1310259)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei418 – 4181D → DRSLS in isoform 2. 2 PublicationsVSP_045587

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M84820 mRNA. Translation: AAA60293.1.
    X63522 mRNA. Translation: CAA45087.1.
    AF065396 Genomic DNA. Translation: AAC18599.1.
    AF120161 Genomic DNA. Translation: AAD13794.1.
    HQ709179 mRNA. Translation: ADZ17386.1.
    AB209244 mRNA. Translation: BAD92481.1. Different initiation.
    AL031228 Genomic DNA. Translation: CAA20239.1.
    AL844527 Genomic DNA. Translation: CAI41836.2.
    CR936877 Genomic DNA. Translation: CAQ09065.1.
    CR759733 Genomic DNA. Translation: CAQ10299.1.
    CR354565 Genomic DNA. Translation: CAQ11083.1.
    AL645940 Genomic DNA. No translation available.
    AL662824 Genomic DNA. No translation available.
    BC001167 mRNA. Translation: AAH01167.1.
    X66424 mRNA. No translation available.
    CCDSiCCDS4768.1. [P28702-1]
    CCDS59007.1. [P28702-3]
    PIRiS37781.
    RefSeqiNP_001257330.1. NM_001270401.1. [P28702-3]
    NP_068811.1. NM_021976.4. [P28702-1]
    UniGeneiHs.388034.

    Genome annotation databases

    EnsembliENST00000374680; ENSP00000363812; ENSG00000204231. [P28702-1]
    ENST00000374685; ENSP00000363817; ENSG00000204231. [P28702-3]
    ENST00000383216; ENSP00000372703; ENSG00000206289. [P28702-3]
    ENST00000383217; ENSP00000372704; ENSG00000206289. [P28702-1]
    ENST00000415157; ENSP00000402506; ENSG00000228333. [P28702-1]
    ENST00000415909; ENSP00000410468; ENSG00000235712. [P28702-1]
    ENST00000431161; ENSP00000393286; ENSG00000235712. [P28702-3]
    ENST00000431820; ENSP00000411238; ENSG00000231321. [P28702-1]
    ENST00000436753; ENSP00000415199; ENSG00000227322. [P28702-1]
    ENST00000443603; ENSP00000402590; ENSG00000227322. [P28702-3]
    ENST00000455462; ENSP00000400104; ENSG00000228333. [P28702-3]
    ENST00000456244; ENSP00000393870; ENSG00000231321. [P28702-3]
    GeneIDi6257.
    KEGGihsa:6257.
    UCSCiuc003odb.4. human. [P28702-1]
    uc003odc.4. human.

    Polymorphism databases

    DMDMi1350911.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M84820 mRNA. Translation: AAA60293.1 .
    X63522 mRNA. Translation: CAA45087.1 .
    AF065396 Genomic DNA. Translation: AAC18599.1 .
    AF120161 Genomic DNA. Translation: AAD13794.1 .
    HQ709179 mRNA. Translation: ADZ17386.1 .
    AB209244 mRNA. Translation: BAD92481.1 . Different initiation.
    AL031228 Genomic DNA. Translation: CAA20239.1 .
    AL844527 Genomic DNA. Translation: CAI41836.2 .
    CR936877 Genomic DNA. Translation: CAQ09065.1 .
    CR759733 Genomic DNA. Translation: CAQ10299.1 .
    CR354565 Genomic DNA. Translation: CAQ11083.1 .
    AL645940 Genomic DNA. No translation available.
    AL662824 Genomic DNA. No translation available.
    BC001167 mRNA. Translation: AAH01167.1 .
    X66424 mRNA. No translation available.
    CCDSi CCDS4768.1. [P28702-1 ]
    CCDS59007.1. [P28702-3 ]
    PIRi S37781.
    RefSeqi NP_001257330.1. NM_001270401.1. [P28702-3 ]
    NP_068811.1. NM_021976.4. [P28702-1 ]
    UniGenei Hs.388034.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1H9U X-ray 2.70 A/B/C/D 299-522 [» ]
    1UHL X-ray 2.90 A 298-533 [» ]
    ProteinModelPortali P28702.
    SMRi P28702. Positions 202-532.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112169. 29 interactions.
    IntActi P28702. 31 interactions.
    MINTi MINT-1365658.
    STRINGi 9606.ENSP00000363812.

    Chemistry

    BindingDBi P28702.
    ChEMBLi CHEMBL1870.
    DrugBanki DB00459. Acitretin.
    DB00210. Adapalene.
    DB00523. Alitretinoin.
    DB00307. Bexarotene.
    DB00926. Etretinate.
    DB00799. Tazarotene.
    DB00755. Tretinoin.
    GuidetoPHARMACOLOGYi 611.

    PTM databases

    PhosphoSitei P28702.

    Polymorphism databases

    DMDMi 1350911.

    Proteomic databases

    MaxQBi P28702.
    PaxDbi P28702.
    PRIDEi P28702.

    Protocols and materials databases

    DNASUi 6257.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000374680 ; ENSP00000363812 ; ENSG00000204231 . [P28702-1 ]
    ENST00000374685 ; ENSP00000363817 ; ENSG00000204231 . [P28702-3 ]
    ENST00000383216 ; ENSP00000372703 ; ENSG00000206289 . [P28702-3 ]
    ENST00000383217 ; ENSP00000372704 ; ENSG00000206289 . [P28702-1 ]
    ENST00000415157 ; ENSP00000402506 ; ENSG00000228333 . [P28702-1 ]
    ENST00000415909 ; ENSP00000410468 ; ENSG00000235712 . [P28702-1 ]
    ENST00000431161 ; ENSP00000393286 ; ENSG00000235712 . [P28702-3 ]
    ENST00000431820 ; ENSP00000411238 ; ENSG00000231321 . [P28702-1 ]
    ENST00000436753 ; ENSP00000415199 ; ENSG00000227322 . [P28702-1 ]
    ENST00000443603 ; ENSP00000402590 ; ENSG00000227322 . [P28702-3 ]
    ENST00000455462 ; ENSP00000400104 ; ENSG00000228333 . [P28702-3 ]
    ENST00000456244 ; ENSP00000393870 ; ENSG00000231321 . [P28702-3 ]
    GeneIDi 6257.
    KEGGi hsa:6257.
    UCSCi uc003odb.4. human. [P28702-1 ]
    uc003odc.4. human.

    Organism-specific databases

    CTDi 6257.
    GeneCardsi GC06M033161.
    GC06Mj33082.
    GC06Mk33139.
    GC06Ml33315.
    GC06Mm33331.
    GC06Mn33090.
    HGNCi HGNC:10478. RXRB.
    HPAi CAB002003.
    MIMi 180246. gene.
    neXtProti NX_P28702.
    PharmGKBi PA34891.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG327099.
    HOGENOMi HOG000260821.
    HOVERGENi HBG005606.
    KOi K08525.
    OMAi FLPERHA.
    PhylomeDBi P28702.
    TreeFami TF352097.

    Enzyme and pathway databases

    Reactomei REACT_15525. Nuclear Receptor transcription pathway.
    SignaLinki P28702.

    Miscellaneous databases

    ChiTaRSi RXRB. human.
    EvolutionaryTracei P28702.
    GeneWikii Retinoid_X_receptor_beta.
    GenomeRNAii 6257.
    NextBioi 24299.
    PROi P28702.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P28702.
    Bgeei P28702.
    CleanExi HS_RXRB.
    Genevestigatori P28702.

    Family and domain databases

    Gene3Di 1.10.565.10. 1 hit.
    3.30.50.10. 1 hit.
    InterProi IPR008946. Nucl_hormone_rcpt_ligand-bd.
    IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
    IPR000003. Retinoid-X_rcpt/HNF4.
    IPR001723. Str_hrmn_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 PR00545. RETINOIDXR.
    PR00398. STRDHORMONER.
    PR00047. STROIDFINGER.
    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. "Purification, cloning, and RXR identity of the HeLa cell factor with which RAR or TR heterodimerizes to bind target sequences efficiently."
      Leid M., Kastner P., Lyons R., Nakshatri H., Saunders M., Zacharewsi T., Chen J.Y., Staub A., Garnier J.-M., Mader S., Chambon P.
      Cell 68:377-395(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), HETERODIMERIZATION.
      Tissue: Mammary carcinoma.
    2. Cited for: SEQUENCE REVISION.
    3. "Isolation of a full-length cDNA clone encoding a N-terminally variant form of the human retinoid X receptor beta."
      Fleischhauer K., Park J.H., Disanto J.P., Marks M.S., Ozato K., Yang S.Y.
      Nucleic Acids Res. 20:1801-1801(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. Numasawa T., Koga H., Ueyama K., Maeda S., Sakou T., Harata S., Leppert M., Inoue I.
      Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Isolation of cDNA coding for putatively new variants of multiple human nuclear receptors."
      Kaighin V.A., Martin A.L., Aronstam R.S.
      Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Liver.
    6. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    7. "Molecular cloning and characterization of the human HRXRB gene and 5' flanking region."
      Corella A., Vergara A., Paez G., de Miguel C., Encio I.
      Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    8. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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] (ISOFORM 1).
      Tissue: Brain.
    10. "Cloning and chromosome mapping of human retinoid X receptor beta: selective amino acid sequence conservation of a nuclear hormone receptor in mammals."
      Fleischhauer K., McBride O.W., DiSanto J.P., Ozato K., Yang S.Y.
      Hum. Genet. 90:505-510(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 161-331 (ISOFORM 1), TISSUE SPECIFICITY.
    11. "The structural basis for the specificity of retinoid-X receptor-selective agonists: new insights into the role of helix H12."
      Love J.D., Gooch J.T., Benko S., Li C., Nagy L., Chatterjee V.K., Evans R.M., Schwabe J.W.
      J. Biol. Chem. 277:11385-11391(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 299-522 IN COMPLEX WITH THE RXR-SPECIFIC AGONIST LG100268.
    12. "Crystal structure of the heterodimeric complex of LXRalpha and RXRbeta ligand-binding domains in a fully agonistic conformation."
      Svensson S., Ostberg T., Jacobsson M., Norstrom C., Stefansson K., Hallen D., Johansson I.C., Zachrisson K., Ogg D., Jendeberg L.
      EMBO J. 22:4625-4633(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 298-533 IN COMPLEX WITH NR1H3.

    Entry informationi

    Entry nameiRXRB_HUMAN
    AccessioniPrimary (citable) accession number: P28702
    Secondary accession number(s): P28703
    , Q59G65, Q5JP92, Q5STQ1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 167 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 6
      Human chromosome 6: 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