Rxra | ENSMUSG00000015846 | NCBI 20181

Details for: Rxra

Gene ID: 20181

Symbol: Rxra

Ensembl ID: ENSMUSG00000015846

Description: retinoid X receptor alpha

Associated with

Bile acid and bile salt metabolism
(R-MMU-194068)
Biological oxidations
(R-MMU-211859)
Carnitine metabolism
(R-MMU-200425)
Cellular responses to stimuli
(R-MMU-8953897)
Cellular responses to stress
(R-MMU-2262752)
Cellular response to chemical stress
(R-MMU-9711123)
Cytochrome p450 - arranged by substrate type
(R-MMU-211897)
Cytoprotection by hmox1
(R-MMU-9707564)
Developmental biology
(R-MMU-1266738)
Endogenous sterols
(R-MMU-211976)
Fatty acid metabolism
(R-MMU-8978868)
Gene expression (transcription)
(R-MMU-74160)
Generic transcription pathway
(R-MMU-212436)
Metabolism
(R-MMU-1430728)
Metabolism of lipids
(R-MMU-556833)
Metabolism of proteins
(R-MMU-392499)
Metabolism of steroids
(R-MMU-8957322)
Nr1h2 & nr1h3 regulate gene expression to control bile acid homeostasis
(R-MMU-9623433)
Nr1h2 and nr1h3-mediated signaling
(R-MMU-9024446)
Nr1h3 & nr1h2 regulate gene expression linked to cholesterol transport and efflux
(R-MMU-9029569)
Nuclear receptor transcription pathway
(R-MMU-383280)
Phase i - functionalization of compounds
(R-MMU-211945)
Post-translational protein modification
(R-MMU-597592)
Pyruvate metabolism
(R-MMU-70268)
Pyruvate metabolism and citric acid (tca) cycle
(R-MMU-71406)
Recycling of bile acids and salts
(R-MMU-159418)
Regulation of lipid metabolism by pparalpha
(R-MMU-400206)
Regulation of pyruvate dehydrogenase (pdh) complex
(R-MMU-204174)
Rna polymerase ii transcription
(R-MMU-73857)
Signaling by nuclear receptors
(R-MMU-9006931)
Signaling by retinoic acid
(R-MMU-5362517)
Signal transduction
(R-MMU-162582)
Sumo e3 ligases sumoylate target proteins
(R-MMU-3108232)
Sumoylation
(R-MMU-2990846)
Sumoylation of intracellular receptors
(R-MMU-4090294)
Synthesis of bile acids and bile salts
(R-MMU-192105)
Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol
(R-MMU-193368)
Synthesis of bile acids and bile salts via 27-hydroxycholesterol
(R-MMU-193807)
The citric acid (tca) cycle and respiratory electron transport
(R-MMU-1428517)
Transcriptional regulation of granulopoiesis
(R-MMU-9616222)
Transcriptional regulation of white adipocyte differentiation
(R-MMU-381340)
Cell differentiation
(GO:0030154)
Chromatin dna binding
(GO:0031490)
Dna-binding transcription factor activity
(GO:0003700)
Dna binding
(GO:0003677)
Dna binding domain binding
(GO:0050692)
Double-stranded dna binding
(GO:0003690)
Embryo implantation
(GO:0007566)
Enzyme binding
(GO:0019899)
Gene expression
(GO:0010467)
Heart development
(GO:0007507)
Heart morphogenesis
(GO:0003007)
Hormone-mediated signaling pathway
(GO:0009755)
Identical protein binding
(GO:0042802)
In utero embryonic development
(GO:0001701)
Ion binding
(GO:0043167)
Lbd domain binding
(GO:0050693)
Maternal placenta development
(GO:0001893)
Metal ion binding
(GO:0046872)
Negative regulation of cell population proliferation
(GO:0008285)
Negative regulation of gene expression
(GO:0010629)
Negative regulation of transcription by rna polymerase ii
(GO:0000122)
Nuclear receptor activity
(GO:0004879)
Nuclear receptor binding
(GO:0016922)
Nuclear retinoic acid receptor binding
(GO:0042974)
Nuclear steroid receptor activity
(GO:0003707)
Nuclear thyroid hormone receptor binding
(GO:0046966)
Nuclear vitamin d receptor binding
(GO:0042809)
Peptide binding
(GO:0042277)
Placenta development
(GO:0001890)
Positive regulation of bone mineralization
(GO:0030501)
Positive regulation of thyroid hormone mediated signaling pathway
(GO:0002157)
Protein-containing complex binding
(GO:0044877)
Protein binding
(GO:0005515)
Protein domain specific binding
(GO:0019904)
Regulation of dna-templated transcription
(GO:0006355)
Regulation of transcription by rna polymerase ii
(GO:0006357)
Retinoic acid-responsive element binding
(GO:0044323)
Retinoic acid binding
(GO:0001972)
Rna polymerase ii cis-regulatory region sequence-specific dna binding
(GO:0000978)
Rna polymerase ii intronic transcription regulatory region sequence-specific dna binding
(GO:0001162)
Rna polymerase ii transcription regulatory region sequence-specific dna binding
(GO:0000977)
Sequence-specific dna binding
(GO:0043565)
Sequence-specific double-stranded dna binding
(GO:1990837)
Transcription cis-regulatory region binding
(GO:0000976)
Transcription coactivator binding
(GO:0001223)
Transcription coregulator binding
(GO:0001221)
Vitamin d response element binding
(GO:0070644)
Zinc ion binding
(GO:0008270)

Other Information

Proteins

Genular Protein ID: 414158001

Symbol: RXRA_MOUSE

Name: Retinoic acid receptor RXR-alpha

UniProtKB Accession Codes:

P28700

Database IDs:

Citations:

PubMed ID: 1310259

Title: Purification, cloning, and RXR identity of the HeLa cell factor with which RAR or TR heterodimerizes to bind target sequences efficiently.

PubMed ID: 1310259

DOI: 10.1016/0092-8674(92)90478-u

PubMed ID: 1312497

Title: Characterization of three RXR genes that mediate the action of 9-cis retinoic acid.

PubMed ID: 1312497

DOI: 10.1101/gad.6.3.329

PubMed ID: 7838715

Title: Adipocyte-specific transcription factor ARF6 is a heterodimeric complex of two nuclear hormone receptors, PPAR gamma and RXR alpha.

PubMed ID: 7838715

DOI: 10.1093/nar/22.25.5628

PubMed ID: 10383391

Title: Hyperphosphorylation of the retinoid X receptor alpha by activated c-Jun NH2-terminal kinases.

PubMed ID: 10383391

DOI: 10.1074/jbc.274.27.18932

PubMed ID: 10788465

Title: Isolation and characterization of peroxisome proliferator-activated receptor (PPAR) interacting protein (PRIP) as a coactivator for PPAR.

PubMed ID: 10788465

DOI: 10.1074/jbc.275.18.13510

PubMed ID: 12032153

Title: The phosphorylation site located in the A region of retinoic X receptor alpha is required for the antiproliferative effect of retinoic acid (RA) and the activation of RA target genes in F9 cells.

PubMed ID: 12032153

DOI: 10.1074/jbc.m203623200

PubMed ID: 16606617

Title: Additional sex comb-like 1 (ASXL1), in cooperation with SRC-1, acts as a ligand-dependent coactivator for retinoic acid receptor.

PubMed ID: 16606617

DOI: 10.1074/jbc.m512616200

PubMed ID: 17595322

Title: Constitutive coactivator of peroxisome proliferator-activated receptor (PPARgamma), a novel coactivator of PPARgamma that promotes adipogenesis.

PubMed ID: 17595322

DOI: 10.1210/me.2006-0520

PubMed ID: 20078863

Title: The transforming acidic coiled coil (TACC1) protein modulates the transcriptional activity of the nuclear receptors TR and RAR.

PubMed ID: 20078863

DOI: 10.1186/1471-2199-11-3

PubMed ID: 21183079

Title: A tissue-specific atlas of mouse protein phosphorylation and expression.

PubMed ID: 21183079

DOI: 10.1016/j.cell.2010.12.001

PubMed ID: 10882070

Title: Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains.

PubMed ID: 10882070

DOI: 10.1016/s1097-2765(00)80424-4

PubMed ID: 15528208

Title: Characterization of the interaction between retinoic acid receptor/retinoid X receptor (RAR/RXR) heterodimers and transcriptional coactivators through structural and fluorescence anisotropy studies.

PubMed ID: 15528208

DOI: 10.1074/jbc.m409302200

PubMed ID: 25417649

Title: Retinoid X receptor alpha attenuates host antiviral response by suppressing type I interferon.

PubMed ID: 25417649

DOI: 10.1038/ncomms6494

PubMed ID: 26463675

Title: Retinoid X receptor activation reverses age-related deficiencies in myelin debris phagocytosis and remyelination.

PubMed ID: 26463675

DOI: 10.1093/brain/awv289

Sequence Information:

Length: 467
Mass: 51217
Checksum: 0AF62396BCDC87DB
Sequence:

MDTKHFLPLD FSTQVNSSSL NSPTGRGSMA VPSLHPSLGP GIGSPLGSPG QLHSPISTLS 
SPINGMGPPF SVISSPMGPH SMSVPTTPTL GFGTGSPQLN SPMNPVSSTE DIKPPLGLNG 
VLKVPAHPSG NMASFTKHIC AICGDRSSGK HYGVYSCEGC KGFFKRTVRK DLTYTCRDNK 
DCLIDKRQRN RCQYCRYQKC LAMGMKREAV QEERQRGKDR NENEVESTSS ANEDMPVEKI 
LEAELAVEPK TETYVEANMG LNPSSPNDPV TNICQAADKQ LFTLVEWAKR IPHFSELPLD 
DQVILLRAGW NELLIASFSH RSIAVKDGIL LATGLHVHRN SAHSAGVGAI FDRVLTELVS 
KMRDMQMDKT ELGCLRAIVL FNPDSKGLSN PAEVEALREK VYASLEAYCK HKYPEQPGRF 
AKLLLRLPAL RSIGLKCLEH LFFFKLIGDT PIDTFLMEML EAPHQAT

Genular Protein ID: 2202473710

Symbol: Q3UMU4_MOUSE

Name: N/A

UniProtKB Accession Codes:

Q3UMU4

Database IDs:

Citations:

PubMed ID: 10349636

Title: High-efficiency full-length cDNA cloning.

PubMed ID: 10349636

DOI: 10.1016/S0076-6879(99)03004-9

PubMed ID: 11042159

Title: Normalization and subtraction of cap-trapper-selected cDNAs to prepare full-length cDNA libraries for rapid discovery of new genes.

PubMed ID: 11042159

DOI: 10.1101/gr.145100

PubMed ID: 11076861

Title: RIKEN integrated sequence analysis (RISA) system--384-format sequencing pipeline with 384 multicapillary sequencer.

PubMed ID: 11076861

DOI: 10.1101/gr.152600

PubMed ID: 11217851

Title: Functional annotation of a full-length mouse cDNA collection.

PubMed ID: 11217851

DOI: 10.1038/35055500

PubMed ID: 12466851

Title: Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs.

PubMed ID: 12466851

DOI: 10.1038/nature01266

PubMed ID: 16141073

Title: Antisense Transcription in the Mammalian Transcriptome.

PubMed ID: 16141073

DOI: 10.1126/science.1112009

Sequence Information:

Length: 467
Mass: 51259
Checksum: 083F5826B8C9887E
Sequence:

MDTKHFLPLD FSTQVNSSSL NSPTGRGSMA VPSLHPSLGP GIGSPLGSPG QLHSPISTLS 
SPINGMGPPF SVISSPMGPH SMSVPTTPTL VFGTGSPQLN SPMNPVSSTE DIKPPLGLNG 
VLKVPAHPSG NMASFTKHIC AICGDRSSGK HYGVYSCEGC KGFFKRTVRK DLTYTCRDNK 
DCLIDKRQRN RCQYCRYQKC LAMGMKREAV QEERQRGKDR NENEVESTSS ANEDMPVEKI 
LEAELAVEPK TETYVEANMG LNPSSPNDPV TNICQAADKQ LFTLVEWAKR IPHFSELPLD 
DQVILLRAGW NELLIASFSH RSIAVKDGIL LATGLHVHRN SAHSAGVGAI FDRVLTELVS 
KMRDMQMDKT ELGCLRAIVL FNPDSKGLSN PAEVEALREK VYASLEAYCK HKYPEQPGRF 
AKLLLRLPAL RSIGLKCLEH LFFFKLIGDT PIDTFLMEML EAPHQAT

Genular Protein ID: 793167567

Symbol: Q6LC96_MOUSE

Name: N/A

UniProtKB Accession Codes:

Q6LC96

Database IDs:

Citations:

PubMed ID: 19468303

Title: Lineage-specific biology revealed by a finished genome assembly of the mouse.

PubMed ID: 19468303

DOI: 10.1371/journal.pbio.1000112

Sequence Information:

Length: 439
Mass: 48210
Checksum: 866DF102CB4ECBE5
Sequence:

MAVPSLHPSL GPGIGSPLGS PGQLHSPIST LSSPINGMGP PFSVISSPMG PHSMSVPTTP 
TLGFGTGSPQ LNSPMNPVSS TEDIKPPLGL NGVLKVPAHP SGNMASFTKH ICAICGDRSS 
GKHYGVYSCE GCKGFFKRTV RKDLTYTCRD NKDCLIDKRQ RNRCQYCRYQ KCLAMGMKRE 
AVQEERQRGK DRNENEVEST SSANEDMPVE KILEAELAVE PKTETYVEAN MGLNPSSPND 
PVTNICQAAD KQLFTLVEWA KRIPHFSELP LDDQVILLRA GWNELLIASF SHRSIAVKDG 
ILLATGLHVH RNSAHSAGVG AIFDRVLTEL VSKMRDMQMD KTELGCLRAI VLFNPDSKGL 
SNPAEVEALR EKVYASLEAY CKHKYPEQPG RFAKLLLRLP ALRSIGLKCL EHLFFFKLIG 
DTPIDTFLME MLEAPHQAT

The gene details are incomplete or unavailable at the moment.

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: Rxra

Associated with

Other Information

Purification, cloning, and RXR identity of the HeLa cell factor with which RAR or TR heterodimerizes to bind target sequences efficiently. PubMed ID: 1310259

Characterization of three RXR genes that mediate the action of 9-cis retinoic acid. PubMed ID: 1312497

Adipocyte-specific transcription factor ARF6 is a heterodimeric complex of two nuclear hormone receptors, PPAR gamma and RXR alpha. PubMed ID: 7838715

Hyperphosphorylation of the retinoid X receptor alpha by activated c-Jun NH2-terminal kinases. PubMed ID: 10383391

Isolation and characterization of peroxisome proliferator-activated receptor (PPAR) interacting protein (PRIP) as a coactivator for PPAR. PubMed ID: 10788465

The phosphorylation site located in the A region of retinoic X receptor alpha is required for the antiproliferative effect of retinoic acid (RA) and the activation of RA target genes in F9 cells. PubMed ID: 12032153

Additional sex comb-like 1 (ASXL1), in cooperation with SRC-1, acts as a ligand-dependent coactivator for retinoic acid receptor. PubMed ID: 16606617

Constitutive coactivator of peroxisome proliferator-activated receptor (PPARgamma), a novel coactivator of PPARgamma that promotes adipogenesis. PubMed ID: 17595322

The transforming acidic coiled coil (TACC1) protein modulates the transcriptional activity of the nuclear receptors TR and RAR. PubMed ID: 20078863

A tissue-specific atlas of mouse protein phosphorylation and expression. PubMed ID: 21183079

Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains. PubMed ID: 10882070

Characterization of the interaction between retinoic acid receptor/retinoid X receptor (RAR/RXR) heterodimers and transcriptional coactivators through structural and fluorescence anisotropy studies. PubMed ID: 15528208

Retinoid X receptor alpha attenuates host antiviral response by suppressing type I interferon. PubMed ID: 25417649

Retinoid X receptor activation reverses age-related deficiencies in myelin debris phagocytosis and remyelination. PubMed ID: 26463675

High-efficiency full-length cDNA cloning. PubMed ID: 10349636

Normalization and subtraction of cap-trapper-selected cDNAs to prepare full-length cDNA libraries for rapid discovery of new genes. PubMed ID: 11042159

RIKEN integrated sequence analysis (RISA) system--384-format sequencing pipeline with 384 multicapillary sequencer. PubMed ID: 11076861

Functional annotation of a full-length mouse cDNA collection. PubMed ID: 11217851

Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs. PubMed ID: 12466851

Antisense Transcription in the Mammalian Transcriptome. PubMed ID: 16141073

Lineage-specific biology revealed by a finished genome assembly of the mouse. PubMed ID: 19468303

Database document:

PubMed ID: 1310259

PubMed ID: 1312497

PubMed ID: 7838715

PubMed ID: 10383391

PubMed ID: 10788465

PubMed ID: 12032153

PubMed ID: 16606617

PubMed ID: 17595322

PubMed ID: 20078863

PubMed ID: 21183079

PubMed ID: 10882070

PubMed ID: 15528208

PubMed ID: 25417649

PubMed ID: 26463675

PubMed ID: 10349636

PubMed ID: 11042159

PubMed ID: 11076861

PubMed ID: 11217851

PubMed ID: 12466851

PubMed ID: 16141073

PubMed ID: 19468303