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Protein

Retinoic acid receptor RXR-beta

Gene

RXRB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

GO - Biological processi

Complete GO annotation...

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.
REACT_267785. Signaling by Retinoic Acid.
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 Componentsi: Chromosome 6, Unplaced

Organism-specific databases

HGNCiHGNC:10478. RXRB.

Subcellular locationi

GO - Cellular componenti

  • nucleoplasm Source: Reactome
  • nucleus Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34891.

Chemistry

DrugBankiDB00459. Acitretin.
DB00210. Adapalene.
DB00523. Alitretinoin.
DB00307. Bexarotene.
DB00799. Tazarotene.
DB00755. Tretinoin.

Polymorphism and mutation databases

BioMutaiRXRB.
DMDMi1350911.

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

BgeeiP28702.
CleanExiHS_RXRB.
ExpressionAtlasiP28702. baseline and differential.
GenevisibleiP28702. HS.

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
RARAP102764EBI-748576,EBI-413374

Protein-protein interaction databases

BioGridi112169. 31 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 – 3099Combined sources
Helixi336 – 34712Combined sources
Helixi350 – 3556Combined sources
Helixi360 – 3623Combined sources
Helixi365 – 38723Combined sources
Turni388 – 3903Combined sources
Beta strandi394 – 3963Combined sources
Beta strandi402 – 4043Combined sources
Helixi405 – 4117Combined sources
Helixi414 – 42310Combined sources
Helixi425 – 4317Combined sources
Helixi435 – 44612Combined sources
Helixi457 – 47822Combined sources
Helixi485 – 4906Combined sources
Helixi493 – 51321Combined sources
Helixi517 – 5215Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H9UX-ray2.70A/B/C/D299-522[»]
1UHLX-ray2.90A298-533[»]
ProteinModelPortaliP28702.
SMRiP28702. Positions 202-530.
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.
GeneTreeiENSGT00760000118948.
HOGENOMiHOG000260821.
HOVERGENiHBG005606.
InParanoidiP28702.
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. AlignAdd to basket

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

        10         20         30         40         50
MSWAARPPFL PQRHAAGQCG PVGVRKEMHC GVASRWRRRR PWLDPAAAAA
60 70 80 90 100
AAVAGGEQQT PEPEPGEAGR DGMGDSGRDS RSPDSSSPNP LPQGVPPPSP
110 120 130 140 150
PGPPLPPSTA PSLGGSGAPP PPPMPPPPLG SPFPVISSSM GSPGLPPPAP
160 170 180 190 200
PGFSGPVSSP QINSTVSLPG GGSGPPEDVK PPVLGVRGLH CPPPPGGPGA
210 220 230 240 250
GKRLCAICGD RSSGKHYGVY SCEGCKGFFK RTIRKDLTYS CRDNKDCTVD
260 270 280 290 300
KRQRNRCQYC RYQKCLATGM KREAVQEERQ RGKDKDGDGE GAGGAPEEMP
310 320 330 340 350
VDRILEAELA VEQKSDQGVE GPGGTGGSGS SPNDPVTNIC QAADKQLFTL
360 370 380 390 400
VEWAKRIPHF SSLPLDDQVI LLRAGWNELL IASFSHRSID VRDGILLATG
410 420 430 440 450
LHVHRNSAHS AGVGAIFDRV LTELVSKMRD MRMDKTELGC LRAIILFNPD
460 470 480 490 500
AKGLSNPSEV EVLREKVYAS LETYCKQKYP EQQGRFAKLL LRLPALRSIG
510 520 530
LKCLEHLFFF KLIGDTPIDT FLMEMLEAPH QLA
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.Curated

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:
EMBLi
GenBanki
DDBJi
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.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H9UX-ray2.70A/B/C/D299-522[»]
1UHLX-ray2.90A298-533[»]
ProteinModelPortaliP28702.
SMRiP28702. Positions 202-530.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

BindingDBiP28702.
ChEMBLiCHEMBL2363071.
DrugBankiDB00459. Acitretin.
DB00210. Adapalene.
DB00523. Alitretinoin.
DB00307. Bexarotene.
DB00799. Tazarotene.
DB00755. Tretinoin.
GuidetoPHARMACOLOGYi611.

PTM databases

PhosphoSiteiP28702.

Polymorphism and mutation databases

BioMutaiRXRB.
DMDMi1350911.

Proteomic databases

MaxQBiP28702.
PaxDbiP28702.
PRIDEiP28702.

Protocols and materials databases

DNASUi6257.
Structural Biology KnowledgebaseSearch...

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.

Organism-specific databases

CTDi6257.
GeneCardsiGC06M033161.
GC06Mj33082.
GC06Mk33139.
GC06Ml33315.
GC06Mm33331.
GC06Mn33090.
HGNCiHGNC:10478. RXRB.
HPAiCAB002003.
MIMi180246. gene.
neXtProtiNX_P28702.
PharmGKBiPA34891.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG327099.
GeneTreeiENSGT00760000118948.
HOGENOMiHOG000260821.
HOVERGENiHBG005606.
InParanoidiP28702.
KOiK08525.
OMAiFLPERHA.
PhylomeDBiP28702.
TreeFamiTF352097.

Enzyme and pathway databases

ReactomeiREACT_15525. Nuclear Receptor transcription pathway.
REACT_267785. Signaling by Retinoic Acid.
SignaLinkiP28702.

Miscellaneous databases

ChiTaRSiRXRB. human.
EvolutionaryTraceiP28702.
GeneWikiiRetinoid_X_receptor_beta.
GenomeRNAii6257.
NextBioi24299.
PROiP28702.
SOURCEiSearch...

Gene expression databases

BgeeiP28702.
CleanExiHS_RXRB.
ExpressionAtlasiP28702. baseline and differential.
GenevisibleiP28702. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "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.
  13. "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: June 24, 2015
This is version 175 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.