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P10826

- RARB_HUMAN

UniProt

P10826 - RARB_HUMAN

Protein

Retinoic acid receptor beta

Gene

RARB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 182 (01 Oct 2014)
      Sequence version 2 (16 Nov 2001)
      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 RXR/RAR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. In the absence or presence of hormone ligand, acts mainly as an activator of gene expression due to weak binding to corepressors. In concert with RARG, required for skeletal growth, matrix homeostasis and growth plate function.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi88 – 15366Nuclear receptorPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri88 – 10821NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri124 – 14825NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: ProtInc
    2. drug binding Source: Ensembl
    3. protein binding Source: IntAct
    4. retinoic acid receptor activity Source: ProtInc
    5. sequence-specific DNA binding Source: Ensembl
    6. steroid hormone receptor activity Source: InterPro
    7. zinc ion binding Source: InterPro

    GO - Biological processi

    1. embryonic digestive tract development Source: DFLAT
    2. embryonic eye morphogenesis Source: Ensembl
    3. embryonic hindlimb morphogenesis Source: Ensembl
    4. gene expression Source: Reactome
    5. growth plate cartilage development Source: Ensembl
    6. multicellular organism growth Source: Ensembl
    7. negative regulation of cartilage development Source: Ensembl
    8. negative regulation of cell proliferation Source: Ensembl
    9. negative regulation of chondrocyte differentiation Source: Ensembl
    10. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    11. positive regulation of apoptotic process Source: Ensembl
    12. positive regulation of neuron differentiation Source: Ensembl
    13. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    14. regulation of myelination Source: Ensembl
    15. signal transduction Source: ProtInc
    16. striatum development Source: Ensembl
    17. transcription initiation from RNA polymerase II promoter Source: Reactome
    18. ureteric bud development Source: Ensembl
    19. 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.
    SignaLinkiP10826.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Retinoic acid receptor beta
    Short name:
    RAR-beta
    Alternative name(s):
    HBV-activated protein
    Nuclear receptor subfamily 1 group B member 2
    RAR-epsilon
    Gene namesi
    Name:RARB
    Synonyms:HAP, NR1B2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:9865. RARB.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleoplasm Source: Reactome
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Microphthalmia, syndromic, 12 (MCOPS12) [MIM:615524]: A form of microphthalmia, a disorder of eye formation, ranging from small size of a single eye to complete bilateral absence of ocular tissues (anophthalmia). In many cases, microphthalmia/anophthalmia occurs in association with syndromes that include non-ocular abnormalities. MCOPS12 patients manifest variable features, including diaphragmatic hernia, pulmonary hypoplasia, and cardiac abnormalities.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti394 – 3941R → C in MCOPS12; increases transcriptional response to retinoic acid. 1 Publication
    VAR_070780
    Natural varianti394 – 3941R → S in MCOPS12; increases transcriptional response to retinoic acid. 1 Publication
    VAR_070781

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi188 – 1881T → I: No effect on transcriptional activation in the absence of hormone. 1 Publication
    Mutagenesisi191 – 1911I → V: No effect on transcriptional activation in the absence of hormone. 1 Publication
    Mutagenesisi222 – 2221L → I: Reduced transcriptional activation in the absence of hormone. Even greater reduction in transcriptional activation in the absence of hormone; when associated with D-223 or S-232. Great reduction in transcriptional activation in the absence of hormone; when associated with D-223 and S-232. 1 Publication
    Mutagenesisi223 – 2231G → D: Greatly reduced transcriptional activation in the absence of hormone. Even greater reduction in transcriptional activation in the absence of hormone; when associated with I-222 or S-232. Great reduction in transcriptional activation in the absence of hormone; when associated with I-222 and S-232. 1 Publication
    Mutagenesisi232 – 2321A → S: Reduced transcriptional activation in the absence of hormone. Some further reduction of transcriptional activity in the absence of hormone; when associated with I-222 or D-223. Great reduction in transcriptional activation in the absence of hormone; when associated with I-222 and D-223. 1 Publication

    Keywords - Diseasei

    Disease mutation, Microphthalmia, Proto-oncogene

    Organism-specific databases

    MIMi615524. phenotype.
    Orphaneti2470. Matthew-Wood syndrome.
    PharmGKBiPA34226.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 455455Retinoic acid receptor betaPRO_0000053467Add
    BLAST

    Proteomic databases

    MaxQBiP10826.
    PaxDbiP10826.
    PRIDEiP10826.

    Expressioni

    Gene expression databases

    ArrayExpressiP10826.
    BgeeiP10826.
    CleanExiHS_RARB.
    GenevestigatoriP10826.

    Organism-specific databases

    HPAiCAB002617.
    HPA004174.

    Interactioni

    Subunit structurei

    Homodimer By similarity. Heterodimer; with a RXR molecule. Binds DNA preferentially as a RAR/RXR heterodimer By similarity. Interacts weakly with NCOR2.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P032552EBI-8583223,EBI-2603114From a different organism.

    Protein-protein interaction databases

    BioGridi111850. 19 interactions.
    IntActiP10826. 9 interactions.
    MINTiMINT-1180428.
    STRINGi9606.ENSP00000332296.

    Structurei

    Secondary structure

    1
    455
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi87 – 915
    Beta strandi100 – 1023
    Helixi107 – 11812
    Beta strandi133 – 1353
    Helixi141 – 1488
    Helixi149 – 1513
    Helixi182 – 19817
    Beta strandi202 – 2054
    Helixi222 – 24423
    Helixi249 – 2513
    Helixi254 – 27421
    Beta strandi276 – 2783
    Turni279 – 2824
    Beta strandi283 – 2853
    Beta strandi289 – 2935
    Helixi294 – 3007
    Helixi303 – 3053
    Helixi306 – 31611
    Helixi317 – 3193
    Helixi323 – 33412
    Helixi345 – 36622
    Beta strandi368 – 3703
    Helixi373 – 40129
    Beta strandi402 – 4043
    Helixi408 – 4147

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HRANMR-A82-160[»]
    1XAPX-ray2.10A176-421[»]
    4DM6X-ray1.90A/B176-421[»]
    4DM8X-ray2.30A/B176-421[»]
    4JYGX-ray2.35A/B176-421[»]
    4JYHX-ray2.60A/B176-421[»]
    4JYIX-ray1.90A/B176-421[»]
    ProteinModelPortaliP10826.
    SMRiP10826. Positions 82-415.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10826.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 8787ModulatingAdd
    BLAST
    Regioni154 – 19946HingeAdd
    BLAST
    Regioni200 – 419220Ligand-bindingAdd
    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 fingeri88 – 10821NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri124 – 14825NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG297448.
    HOGENOMiHOG000010312.
    HOVERGENiHBG005606.
    KOiK08528.
    OMAiCINIPHC.
    PhylomeDBiP10826.
    TreeFamiTF328382.

    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.
    IPR003078. Retinoic_acid_rcpt.
    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]
    PRINTSiPR01292. RETNOICACIDR.
    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 (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform Beta-1 (identifier: P10826-1) [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

    MTTSGHACPV PAVNGHMTHY PATPYPLLFP PVIGGLSLPP LHGLHGHPPP    50
    SGCSTPSPAT IETQSTSSEE LVPSPPSPLP PPRVYKPCFV CQDKSSGYHY 100
    GVSACEGCKG FFRRSIQKNM IYTCHRDKNC VINKVTRNRC QYCRLQKCFE 150
    VGMSKESVRN DRNKKKKETS KQECTESYEM TAELDDLTEK IRKAHQETFP 200
    SLCQLGKYTT NSSADHRVRL DLGLWDKFSE LATKCIIKIV EFAKRLPGFT 250
    GLTIADQITL LKAACLDILI LRICTRYTPE QDTMTFSDGL TLNRTQMHNA 300
    GFGPLTDLVF TFANQLLPLE MDDTETGLLS AICLICGDRQ DLEEPTKVDK 350
    LQEPLLEALK IYIRKRRPSK PHMFPKILMK ITDLRSISAK GAERVITLKM 400
    EIPGSMPPLI QEMLENSEGH EPLTPSSSGN TAEHSPSISP SSVENSGVSQ 450
    SPLVQ 455
    Length:455
    Mass (Da):50,489
    Last modified:November 16, 2001 - v2
    Checksum:i8813263AD0495D5A
    GO
    Isoform Beta-2 (identifier: P10826-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-60: MTTSGHACPV...SGCSTPSPAT → MFDCMDVLSV...EWQHRHTAQS

    Show »
    Length:448
    Mass (Da):50,344
    Checksum:i844A298AD32F46A8
    GO
    Isoform Beta-3 (identifier: P10826-4)

    Sequence is not available
    Length:
    Mass (Da):
    Isoform Beta-4 (identifier: P10826-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-119: Missing.

    Show »
    Length:336
    Mass (Da):37,932
    Checksum:iD248E5CAB87DA44E
    GO

    Sequence cautioni

    The sequence CAA27637.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti206 – 2061G → A in CAA68398. (PubMed:2825037)Curated
    Sequence conflicti317 – 3171L → Q in CAA30262. (PubMed:2836738)Curated
    Sequence conflicti414 – 4141L → M in CAA68398. (PubMed:2825037)Curated
    Sequence conflicti454 – 4541V → L in CAA30262. (PubMed:2836738)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti90 – 901V → I in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036060
    Natural varianti394 – 3941R → C in MCOPS12; increases transcriptional response to retinoic acid. 1 Publication
    VAR_070780
    Natural varianti394 – 3941R → S in MCOPS12; increases transcriptional response to retinoic acid. 1 Publication
    VAR_070781

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 119119Missing in isoform Beta-4. 1 PublicationVSP_003635Add
    BLAST
    Alternative sequencei1 – 6060MTTSG…PSPAT → MFDCMDVLSVSPGQILDFYT ASPSSCMLQEKALKACFSGL TQTEWQHRHTAQS in isoform Beta-2. 3 PublicationsVSP_003634Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07282 mRNA. Translation: CAA30262.1.
    Y00291 mRNA. Translation: CAA68398.1.
    AF157483 mRNA. Translation: AAD45688.1.
    BC060794 mRNA. Translation: AAH60794.1.
    X56849 Genomic DNA. No translation available.
    X77664 Genomic DNA. Translation: CAA54740.1.
    X04014 Genomic DNA. Translation: CAA27637.1. Sequence problems.
    M57445 Genomic DNA. Translation: AAA58728.1.
    CCDSiCCDS2642.1. [P10826-2]
    CCDS46775.1. [P10826-3]
    PIRiS02827.
    S49021.
    RefSeqiNP_000956.2. NM_000965.4. [P10826-2]
    NP_001277145.1. NM_001290216.1. [P10826-1]
    NP_001277146.1. NM_001290217.1. [P10826-3]
    NP_001277195.1. NM_001290266.1.
    NP_001277205.1. NM_001290276.1. [P10826-3]
    NP_057236.1. NM_016152.3. [P10826-3]
    UniGeneiHs.654490.
    Hs.733004.

    Genome annotation databases

    EnsembliENST00000330688; ENSP00000332296; ENSG00000077092. [P10826-2]
    ENST00000437042; ENSP00000398840; ENSG00000077092. [P10826-3]
    ENST00000458646; ENSP00000391391; ENSG00000077092. [P10826-3]
    GeneIDi5915.
    KEGGihsa:5915.
    UCSCiuc003cdi.2. human. [P10826-1]

    Polymorphism databases

    DMDMi17380507.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07282 mRNA. Translation: CAA30262.1 .
    Y00291 mRNA. Translation: CAA68398.1 .
    AF157483 mRNA. Translation: AAD45688.1 .
    BC060794 mRNA. Translation: AAH60794.1 .
    X56849 Genomic DNA. No translation available.
    X77664 Genomic DNA. Translation: CAA54740.1 .
    X04014 Genomic DNA. Translation: CAA27637.1 . Sequence problems.
    M57445 Genomic DNA. Translation: AAA58728.1 .
    CCDSi CCDS2642.1. [P10826-2 ]
    CCDS46775.1. [P10826-3 ]
    PIRi S02827.
    S49021.
    RefSeqi NP_000956.2. NM_000965.4. [P10826-2 ]
    NP_001277145.1. NM_001290216.1. [P10826-1 ]
    NP_001277146.1. NM_001290217.1. [P10826-3 ]
    NP_001277195.1. NM_001290266.1.
    NP_001277205.1. NM_001290276.1. [P10826-3 ]
    NP_057236.1. NM_016152.3. [P10826-3 ]
    UniGenei Hs.654490.
    Hs.733004.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HRA NMR - A 82-160 [» ]
    1XAP X-ray 2.10 A 176-421 [» ]
    4DM6 X-ray 1.90 A/B 176-421 [» ]
    4DM8 X-ray 2.30 A/B 176-421 [» ]
    4JYG X-ray 2.35 A/B 176-421 [» ]
    4JYH X-ray 2.60 A/B 176-421 [» ]
    4JYI X-ray 1.90 A/B 176-421 [» ]
    ProteinModelPortali P10826.
    SMRi P10826. Positions 82-415.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111850. 19 interactions.
    IntActi P10826. 9 interactions.
    MINTi MINT-1180428.
    STRINGi 9606.ENSP00000332296.

    Chemistry

    BindingDBi P10826.
    ChEMBLi CHEMBL2008.
    DrugBanki DB00459. Acitretin.
    DB00210. Adapalene.
    DB00523. Alitretinoin.
    DB00926. Etretinate.
    DB04942. Tamibarotene.
    DB00799. Tazarotene.
    GuidetoPHARMACOLOGYi 591.

    Polymorphism databases

    DMDMi 17380507.

    Proteomic databases

    MaxQBi P10826.
    PaxDbi P10826.
    PRIDEi P10826.

    Protocols and materials databases

    DNASUi 5915.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000330688 ; ENSP00000332296 ; ENSG00000077092 . [P10826-2 ]
    ENST00000437042 ; ENSP00000398840 ; ENSG00000077092 . [P10826-3 ]
    ENST00000458646 ; ENSP00000391391 ; ENSG00000077092 . [P10826-3 ]
    GeneIDi 5915.
    KEGGi hsa:5915.
    UCSCi uc003cdi.2. human. [P10826-1 ]

    Organism-specific databases

    CTDi 5915.
    GeneCardsi GC03P025194.
    HGNCi HGNC:9865. RARB.
    HPAi CAB002617.
    HPA004174.
    MIMi 180220. gene.
    615524. phenotype.
    neXtProti NX_P10826.
    Orphaneti 2470. Matthew-Wood syndrome.
    PharmGKBi PA34226.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG297448.
    HOGENOMi HOG000010312.
    HOVERGENi HBG005606.
    KOi K08528.
    OMAi CINIPHC.
    PhylomeDBi P10826.
    TreeFami TF328382.

    Enzyme and pathway databases

    Reactomei REACT_15525. Nuclear Receptor transcription pathway.
    SignaLinki P10826.

    Miscellaneous databases

    EvolutionaryTracei P10826.
    GeneWikii Retinoic_acid_receptor_beta.
    GenomeRNAii 5915.
    NextBioi 23024.
    PROi P10826.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P10826.
    Bgeei P10826.
    CleanExi HS_RARB.
    Genevestigatori P10826.

    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.
    IPR003078. Retinoic_acid_rcpt.
    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 PR01292. RETNOICACIDR.
    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. "A new retinoic acid receptor identified from a hepatocellular carcinoma."
      Benbrook D., Lernherdt E., Pfahl M.
      Nature 333:669-672(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-2).
      Tissue: Placenta.
    2. "A novel steroid thyroid hormone receptor-related gene inappropriately expressed in human hepatocellular carcinoma."
      de The H., Marchio A., Tiollais P., Dejean A.
      Nature 330:667-670(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-2).
    3. "Elevated retinoic acid receptor beta(4) protein in human breast tumor cells with nuclear and cytoplasmic localization."
      Sommer K.M., Chen L.I., Treuting P.M., Smith L.T., Swisshelm K.
      Proc. Natl. Acad. Sci. U.S.A. 96:8651-8656(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-4).
      Tissue: Mammary tumor.
    4. "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 BETA-2).
      Tissue: Placenta.
    5. "Mouse and human retinoic acid receptor beta 2 promoters: sequence comparison and localization of retinoic acid responsiveness."
      Shen S., Kruyt F.A., den Hertog J., van der Saag P.T., Kruijer W.
      DNA Seq. 2:111-119(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52 (ISOFORM BETA-2).
    6. "Fetal isoform of human retinoic acid receptor beta expressed in small cell lung cancer lines."
      Houle B., Pelletier M., Wu J., Goodyer C., Bradley W.E.
      Cancer Res. 54:365-369(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72 (ISOFORM BETA-1).
    7. "Hepatitis B virus DNA integration in a sequence homologous to v-erb-A and steroid receptor genes in a hepatocellular carcinoma."
      Dejean A., Bougueleret L., Grzeschik K.-H., Tiollais P.
      Nature 322:70-72(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 61-109.
    8. "Hepatitis B virus as an insertional mutagene in a human hepatocellular carcinoma."
      Dejean A., de The H.
      Mol. Biol. Med. 7:213-222(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 61-109.
      Tissue: Liver.
    9. Cited for: IDENTIFICATION OF LIGAND.
    10. "Retinoic acid receptors beta and gamma do not repress, but instead activate target gene transcription in both the absence and presence of hormone ligand."
      Hauksdottir H., Farboud B., Privalsky M.L.
      Mol. Endocrinol. 17:373-385(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, HETERODIMERIZATION, INTERACTION WITH NCOR2, MUTAGENESIS OF THR-188; ILE-191; LEU-222; GLY-223 AND ALA-232.
    11. "Homo- and heteronuclear NMR studies of the human retinoic acid receptor beta DNA-binding domain: sequential assignments and identification of secondary structure elements."
      Kathira M., Knegtel R.M.A., Boelens R., Eib D., Schilthuis J.G., van der Saag P.T., Kaptein R.
      Biochemistry 31:6474-6480(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 82-160.
    12. "The solution structure of the human retinoic acid receptor-beta DNA-binding domain."
      Knegtel R.M.A., Katahira M., Schilthuis J.G., Bonvin A.M., Boelens R., Eib D., van der Saag P.T., Kaptein R.
      J. Biomol. NMR 3:1-17(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 82-160.
    13. Cited for: VARIANT [LARGE SCALE ANALYSIS] ILE-90.
    14. "Recessive and dominant mutations in retinoic acid receptor beta in cases with microphthalmia and diaphragmatic hernia."
      Srour M., Chitayat D., Caron V., Chassaing N., Bitoun P., Patry L., Cordier M.P., Capo-Chichi J.M., Francannet C., Calvas P., Ragge N., Dobrzeniecka S., Hamdan F.F., Rouleau G.A., Tremblay A., Michaud J.L.
      Am. J. Hum. Genet. 93:765-772(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MCOPS12 SER-394 AND CYS-394, CHARACTERIZATION OF VARIANTS MCOPS12 SER-394 AND CYS-394.

    Entry informationi

    Entry nameiRARB_HUMAN
    AccessioniPrimary (citable) accession number: P10826
    Secondary accession number(s): P12891
    , Q00989, Q15298, Q9UN48
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: November 16, 2001
    Last modified: October 1, 2014
    This is version 182 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 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3