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P48443

- RXRG_HUMAN

UniProt

P48443 - RXRG_HUMAN

Protein

Retinoic acid receptor RXR-gamma

Gene

RXRG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 1 (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. The high affinity ligand for RXRs is 9-cis retinoic acid By similarity.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi136 – 21176Nuclear receptorPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri139 – 15921NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri175 – 19925NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. 9-cis retinoic acid receptor activity Source: ProtInc
    2. protein binding Source: IntAct
    3. sequence-specific DNA binding Source: Ensembl
    4. steroid hormone receptor activity Source: InterPro
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. gene expression Source: Reactome
    2. heart development Source: Ensembl
    3. neuron differentiation Source: Ensembl
    4. peripheral nervous system development Source: Ensembl
    5. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    6. regulation of myelination Source: Ensembl
    7. response to retinoic acid Source: Ensembl
    8. skeletal muscle tissue development Source: Ensembl
    9. transcription initiation from RNA polymerase II promoter Source: Reactome

    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.
    SignaLinkiP48443.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Retinoic acid receptor RXR-gamma
    Alternative name(s):
    Nuclear receptor subfamily 2 group B member 3
    Retinoid X receptor gamma
    Gene namesi
    Name:RXRG
    Synonyms:NR2B3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:10479. RXRG.

    Subcellular locationi

    Nucleus PROSITE-ProRule annotation

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34892.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 463463Retinoic acid receptor RXR-gammaPRO_0000053576Add
    BLAST

    Proteomic databases

    MaxQBiP48443.
    PaxDbiP48443.
    PRIDEiP48443.

    PTM databases

    PhosphoSiteiP48443.

    Expressioni

    Gene expression databases

    ArrayExpressiP48443.
    BgeeiP48443.
    CleanExiHS_RXRG.
    GenevestigatoriP48443.

    Organism-specific databases

    HPAiCAB002615.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RARAP102763EBI-712405,EBI-413374

    Protein-protein interaction databases

    BioGridi112170. 26 interactions.
    DIPiDIP-56220N.
    IntActiP48443. 9 interactions.
    MINTiMINT-1378806.
    STRINGi9606.ENSP00000352900.

    Structurei

    Secondary structure

    1
    463
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi236 – 24611
    Helixi279 – 2857
    Helixi290 – 2923
    Helixi295 – 31723
    Beta strandi320 – 3267
    Beta strandi332 – 3343
    Helixi335 – 3406
    Helixi344 – 35310
    Helixi355 – 3617
    Helixi365 – 37612
    Helixi387 – 40822
    Helixi415 – 4206
    Helixi423 – 43412

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2GL8X-ray2.40A/B/C/D227-463[»]
    ProteinModelPortaliP48443.
    SMRiP48443. Positions 132-459.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP48443.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 138138ModulatingBy similarityAdd
    BLAST
    Regioni205 – 26056HingeAdd
    BLAST
    Regioni261 – 463203Ligand-bindingBy similarityAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri139 – 15921NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri175 – 19925NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG327099.
    HOGENOMiHOG000260821.
    HOVERGENiHBG005606.
    InParanoidiP48443.
    KOiK08526.
    OMAiFIKFPAG.
    OrthoDBiEOG72RMZ5.
    PhylomeDBiP48443.
    TreeFamiTF352097.

    Family and domain databases

    Gene3Di1.10.565.10. 1 hit.
    3.30.50.10. 1 hit.
    InterProiIPR021780. Nuc_recep-AF1.
    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]
    PfamiPF00104. Hormone_recep. 1 hit.
    PF11825. Nuc_recep-AF1. 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]

    Sequencei

    Sequence statusi: Complete.

    P48443-1 [UniParc]FASTAAdd to Basket

    « Hide

    MYGNYSHFMK FPAGYGGSPG HTGSTSMSPS AALSTGKPMD SHPSYTDTPV    50
    SAPRTLSAVG TPLNALGSPY RVITSAMGPP SGALAAPPGI NLVAPPSSQL 100
    NVVNSVSSSE DIKPLPGLPG IGNMNYPSTS PGSLVKHICA ICGDRSSGKH 150
    YGVYSCEGCK GFFKRTIRKD LIYTCRDNKD CLIDKRQRNR CQYCRYQKCL 200
    VMGMKREAVQ EERQRSRERA ESEAECATSG HEDMPVERIL EAELAVEPKT 250
    ESYGDMNMEN STNDPVTNIC HAADKQLFTL VEWAKRIPHF SDLTLEDQVI 300
    LLRAGWNELL IASFSHRSVS VQDGILLATG LHVHRSSAHS AGVGSIFDRV 350
    LTELVSKMKD MQMDKSELGC LRAIVLFNPD AKGLSNPSEV ETLREKVYAT 400
    LEAYTKQKYP EQPGRFAKLL LRLPALRSIG LKCLEHLFFF KLIGDTPIDT 450
    FLMEMLETPL QIT 463
    Length:463
    Mass (Da):50,871
    Last modified:February 1, 1996 - v1
    Checksum:iAED5C94BB62A3157
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U38480 mRNA. Translation: AAA80681.1.
    CR456705 mRNA. Translation: CAG32986.1.
    AL160058 Genomic DNA. Translation: CAC00596.1.
    CH471067 Genomic DNA. Translation: EAW90745.1.
    BC012063 mRNA. Translation: AAH12063.1.
    CCDSiCCDS1248.1.
    RefSeqiNP_001243500.1. NM_001256571.1.
    NP_008848.1. NM_006917.4.
    UniGeneiHs.26550.

    Genome annotation databases

    EnsembliENST00000359842; ENSP00000352900; ENSG00000143171.
    GeneIDi6258.
    KEGGihsa:6258.
    UCSCiuc001gda.3. human.

    Polymorphism databases

    DMDMi1350913.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U38480 mRNA. Translation: AAA80681.1 .
    CR456705 mRNA. Translation: CAG32986.1 .
    AL160058 Genomic DNA. Translation: CAC00596.1 .
    CH471067 Genomic DNA. Translation: EAW90745.1 .
    BC012063 mRNA. Translation: AAH12063.1 .
    CCDSi CCDS1248.1.
    RefSeqi NP_001243500.1. NM_001256571.1.
    NP_008848.1. NM_006917.4.
    UniGenei Hs.26550.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2GL8 X-ray 2.40 A/B/C/D 227-463 [» ]
    ProteinModelPortali P48443.
    SMRi P48443. Positions 132-459.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112170. 26 interactions.
    DIPi DIP-56220N.
    IntActi P48443. 9 interactions.
    MINTi MINT-1378806.
    STRINGi 9606.ENSP00000352900.

    Chemistry

    BindingDBi P48443.
    ChEMBLi CHEMBL2363070.
    DrugBanki DB00459. Acitretin.
    DB00210. Adapalene.
    DB00523. Alitretinoin.
    DB00926. Etretinate.
    DB00755. Tretinoin.
    GuidetoPHARMACOLOGYi 612.

    PTM databases

    PhosphoSitei P48443.

    Polymorphism databases

    DMDMi 1350913.

    Proteomic databases

    MaxQBi P48443.
    PaxDbi P48443.
    PRIDEi P48443.

    Protocols and materials databases

    DNASUi 6258.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000359842 ; ENSP00000352900 ; ENSG00000143171 .
    GeneIDi 6258.
    KEGGi hsa:6258.
    UCSCi uc001gda.3. human.

    Organism-specific databases

    CTDi 6258.
    GeneCardsi GC01M165370.
    HGNCi HGNC:10479. RXRG.
    HPAi CAB002615.
    MIMi 180247. gene.
    neXtProti NX_P48443.
    PharmGKBi PA34892.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG327099.
    HOGENOMi HOG000260821.
    HOVERGENi HBG005606.
    InParanoidi P48443.
    KOi K08526.
    OMAi FIKFPAG.
    OrthoDBi EOG72RMZ5.
    PhylomeDBi P48443.
    TreeFami TF352097.

    Enzyme and pathway databases

    Reactomei REACT_15525. Nuclear Receptor transcription pathway.
    SignaLinki P48443.

    Miscellaneous databases

    EvolutionaryTracei P48443.
    GeneWikii Retinoid_X_receptor_gamma.
    GenomeRNAii 6258.
    NextBioi 24303.
    PROi P48443.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P48443.
    Bgeei P48443.
    CleanExi HS_RXRG.
    Genevestigatori P48443.

    Family and domain databases

    Gene3Di 1.10.565.10. 1 hit.
    3.30.50.10. 1 hit.
    InterProi IPR021780. Nuc_recep-AF1.
    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.
    PF11825. Nuc_recep-AF1. 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. Cooke T.A., Allegretto E.A., Heyman R.A., Lamph W.W.
      Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Heart.
    2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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].
      Tissue: Eye.
    6. "Human retinoic acid receptor Rxr-gamma ligand-binding domain."
      Structural genomics consortium (SGC)
      Submitted (APR-2006) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 227-463.

    Entry informationi

    Entry nameiRXRG_HUMAN
    AccessioniPrimary (citable) accession number: P48443
    Secondary accession number(s): A6NIP1, Q6IBU7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 150 of the entry and version 1 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 1
      Human chromosome 1: 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