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P11416

- RARA_MOUSE

UniProt

P11416 - RARA_MOUSE

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Protein

Retinoic acid receptor alpha

Gene

Rara

Organism
Mus musculus (Mouse)
Status
Reviewed - 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 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 of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone acetylation, chromatin condensation and transcriptional suppression. On ligand binding, the corepressors dissociate from the receptors and associate with the coactivators leading to transcriptional activation. Regulates expression of target genes in a ligand-dependent manner by recruiting chromatin complexes containing KMT2E/MLL5. Mediates retinoic acid-induced granulopoiesis. RARA plays an essential role in the regulation of retinoic acid-induced germ cell development during spermatogenesis. Has a role in the survival of early spermatocytes at the beginning prophase of meiosis. In Sertoli cells, may promote the survival and development of early meiotic prophase spermatocytes. In concert with RARG, required for skeletal growth, matrix homeostasis and growth plate function.7 Publications

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. chromatin DNA binding Source: Ensembl
  2. DNA binding Source: MGI
  3. drug binding Source: Ensembl
  4. ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: MGI
  5. mRNA 5'-UTR binding Source: Ensembl
  6. phosphatidylinositol 3-kinase regulator activity Source: Ensembl
  7. retinoic acid binding Source: Ensembl
  8. retinoic acid receptor activity Source: MGI
  9. retinoic acid-responsive element binding Source: Ensembl
  10. RNA polymerase II regulatory region DNA binding Source: MGI
  11. RNA polymerase II regulatory region sequence-specific DNA binding Source: MGI
  12. sequence-specific DNA binding Source: MGI
  13. sequence-specific DNA binding transcription factor activity Source: MGI
  14. steroid hormone receptor activity Source: InterPro
  15. transcription coactivator activity Source: Ensembl
  16. transcription corepressor activity Source: Ensembl
  17. transcription factor binding Source: UniProtKB
  18. transcription regulatory region DNA binding Source: UniProtKB
  19. translation repressor activity, nucleic acid binding Source: Ensembl
  20. zinc ion binding Source: InterPro

GO - Biological processi

  1. apoptotic cell clearance Source: Ensembl
  2. bone development Source: MGI
  3. cellular response to estrogen stimulus Source: Ensembl
  4. cellular response to lipopolysaccharide Source: UniProtKB
  5. cellular response to retinoic acid Source: Ensembl
  6. chondroblast differentiation Source: MGI
  7. embryonic camera-type eye development Source: MGI
  8. face development Source: MGI
  9. female pregnancy Source: Ensembl
  10. germ cell development Source: UniProtKB
  11. glandular epithelial cell development Source: MGI
  12. growth plate cartilage development Source: MGI
  13. intracellular estrogen receptor signaling pathway Source: Ensembl
  14. limb development Source: MGI
  15. liver development Source: Ensembl
  16. multicellular organism growth Source: MGI
  17. negative regulation of apoptotic process Source: MGI
  18. negative regulation of cartilage development Source: MGI
  19. negative regulation of cell differentiation Source: MGI
  20. negative regulation of cell proliferation Source: Ensembl
  21. negative regulation of gene expression Source: MGI
  22. negative regulation of granulocyte differentiation Source: Ensembl
  23. negative regulation of interferon-gamma production Source: Ensembl
  24. negative regulation of transcription, DNA-templated Source: MGI
  25. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  26. negative regulation of translational initiation Source: MGI
  27. negative regulation of tumor necrosis factor production Source: Ensembl
  28. neural tube closure Source: MGI
  29. outflow tract septum morphogenesis Source: MGI
  30. positive regulation of binding Source: Ensembl
  31. positive regulation of cell cycle Source: Ensembl
  32. positive regulation of cell proliferation Source: MGI
  33. positive regulation of ERK1 and ERK2 cascade Source: Ensembl
  34. positive regulation of gene expression Source: UniProtKB
  35. positive regulation of interleukin-13 production Source: Ensembl
  36. positive regulation of interleukin-4 production Source: Ensembl
  37. positive regulation of interleukin-5 production Source: Ensembl
  38. positive regulation of neuron differentiation Source: Ensembl
  39. positive regulation of phosphatidylinositol 3-kinase signaling Source: Ensembl
  40. positive regulation of protein kinase B signaling Source: Ensembl
  41. positive regulation of T-helper 2 cell differentiation Source: Ensembl
  42. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  43. prostate gland development Source: Ensembl
  44. protein phosphorylation Source: Ensembl
  45. regulation of granulocyte differentiation Source: MGI
  46. regulation of myelination Source: Ensembl
  47. regulation of synaptic plasticity Source: Ensembl
  48. regulation of transcription, DNA-templated Source: MGI
  49. response to cytokine Source: Ensembl
  50. response to estradiol Source: Ensembl
  51. response to ethanol Source: Ensembl
  52. response to retinoic acid Source: MGI
  53. response to vitamin A Source: Ensembl
  54. Sertoli cell fate commitment Source: UniProtKB
  55. spermatogenesis Source: MGI
  56. trachea cartilage development Source: MGI
  57. ureteric bud development Source: MGI
  58. ventricular cardiac muscle cell differentiation Source: MGI
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_234105. Nuclear Receptor transcription pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Retinoic acid receptor alpha
Short name:
RAR-alpha
Alternative name(s):
Nuclear receptor subfamily 1 group B member 1
Gene namesi
Name:Rara
Synonyms:Nr1b1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:97856. Rara.

Subcellular locationi

Nucleus. Cytoplasm
Note: Nuclear localization depends on ligand binding, phosphorylation and sumoylation. Transloaction to the nucleus is dependent on activation of PKC and the downstream MAPK phosphorylation.

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. dendrite Source: MGI
  3. neuronal cell body Source: MGI
  4. nuclear chromatin Source: Ensembl
  5. nucleus Source: UniProtKB
  6. perinuclear region of cytoplasm Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Seminiferous tubules of 6 month-old animals display varying degrees of testicular degeneration, with moderate to severe levels of germ-cell degeneration. Epithelial cells in the epididymis show general disorganization. Sperm count is reduced to about 1.7% of wild-type and sperm mobility reduced by half. Rara and Rarg, but not Rara and Rarb, double knockout mice exhibit growth retardation after 3 weeks. Defects are found in the growth plates with deficiency in cartilage. Growth retardation was noticable in limb sketal elements such as femurs. Early lethality and male sterility due to squamous metaplasia of the seminal vesicles and prostate are also observed.3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi74 – 741S → A: No effect on phosphorylation, no effect on transcriptional activity. 1 Publication
Mutagenesisi77 – 771S → A: Decreases phosphorylation and no effect on interaction with CDK7. Strongly reduces transcriptional activity. 2 Publications
Mutagenesisi347 – 3471K → A or Q: Greatly reduced interaction with RXRA and NCOR1 and transcriptional activation. 1 Publication
Mutagenesisi347 – 3471K → F: Reduced methylation levels. Little effect on interaction with RXRA or NCOR1. Small loss in transcriptional activation. 1 Publication
Mutagenesisi369 – 3691S → A: Abolishes phosphorylation and prevents phosphorylation of S-77. 1 Publication
Mutagenesisi449 – 4491S → A: No change in phosphorylation levels and no effect on transcriptional activity. 1 Publication
Mutagenesisi456 – 4561S → A: No change in phosphorylation levels and no effect on transcriptional activity. 1 Publication
Mutagenesisi461 – 4611S → A: No change in phosphorylation levels and no effect on transcriptional activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 462462Retinoic acid receptor alphaPRO_0000053462Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei77 – 771Phosphoserine; by CDK72 Publications
Modified residuei96 – 961Phosphoserine; by PKB/AKT1By similarity
Cross-linki166 – 166Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki171 – 171Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei219 – 2191Phosphoserine; by PKABy similarity
Modified residuei347 – 3471N6,N6,N6-trimethyllysine1 Publication
Modified residuei369 – 3691Phosphoserine; by PKA and RPS6KA51 Publication
Cross-linki399 – 399Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

Post-translational modificationi

Phosphorylated on serine and threonine residues. Phosphorylation does not change during cell cycle. Phosphorylation on Ser-77 is crucial for the N-terminal AF1 transcriptional activity. Under stress conditions, MAPK8 enhances phosphorylation on Thr-181, Ser-445 and Ser-461 leading to RARA ubiquitination and degradation. Phosphorylation by AKT1 inhibits the transactivation activity. On retinoic acid stimulation, phosphorylation on Ser-369 by RPS6KA5 promotes interaction with GTF2H3 and the CDK7-mediated phosphorylation of Ser-77.3 Publications
Sumoylated with SUMO2, mainly on Lys-399 which is also required for SENP6 binding. On all-trans retinoic acid (ATRA) binding, a confromational change may occur that allows sumoylation on two additional site, Lys-166 and Lys-171. Probably desumoylated by SENP6. Sumoylation levels determine nuclear localization and regulate ATRA-mediated transcriptional activity (By similarity).By similarity

Keywords - PTMi

Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP11416.

PTM databases

PhosphoSiteiP11416.

Expressioni

Tissue specificityi

Expressed in Sertoli cells and germ cells.1 Publication

Inductioni

By retinoic acid.1 Publication

Gene expression databases

BgeeiP11416.
CleanExiMM_RARA.
ExpressionAtlasiP11416. baseline and differential.
GenevestigatoriP11416.

Interactioni

Subunit structurei

Interacts with PRMT2 (By similarity). Interacts with LRIF1 (By similarity). Interacts with NCOA7 in a ligand-inducible manner. Interacts with KMT2E/MLL5. Interacts (via the ligand-binding domain) with PRAME; interaction is direct and ligand (retinoic acid)-dependent. Interacts with PRKAR1A; the interaction negatively. regulates RARA transcriptional activity. Interacts with NCOR1 and NCOR2; the interaction occurs in the absence of ligand and represses transciptional activity. Interacts with NCOA3 and NCOA6 coactivators, leading to a strong increase of transcription of target genes. Interacts with CDK7; the interaction is enhanced by interaction with GTF2H3. Interacts with GTF2H3; the interaction requires prior phosphorylation on Ser-369 which then enhances interaction with CDK7. Interacts with ASXL1 and NCOA1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Rps6ka5Q8C0502EBI-346736,EBI-8391218

Protein-protein interaction databases

BioGridi202586. 70 interactions.
DIPiDIP-31480N.
IntActiP11416. 11 interactions.
MINTiMINT-5210296.

Structurei

3D structure databases

ProteinModelPortaliP11416.
SMRiP11416. Positions 87-415.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 8787ModulatingAdd
BLAST
Regioni154 – 19946HingeAdd
BLAST
Regioni200 – 419220Ligand-bindingAdd
BLAST
Regioni404 – 41916Required for binding corepressor NCOR1Add
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.
GeneTreeiENSGT00760000118837.
HOGENOMiHOG000010312.
HOVERGENiHBG005606.
InParanoidiP11416.
KOiK08527.
OMAiNNSSDQR.
OrthoDBiEOG738053.
PhylomeDBiP11416.
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. 2 hits.
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 Alpha-1 (identifier: P11416-1) [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
MASNSSSCPT PGGGHLNGYP VPPYAFFFPP MLGGLSPPGA LTSLQHQLPV
60 70 80 90 100
SGYSTPSPAT IETQSSSSEE IVPSPPSPPP LPRIYKPCFV CQDKSSGYHY
110 120 130 140 150
GVSACEGCKG FFRRSIQKNM VYTCHRDKNC IINKVTRNRC QYCRLQKCFD
160 170 180 190 200
VGMSKESVRN DRNKKKKEAP KPECSESYTL TPEVGELIEK VRKAHQETFP
210 220 230 240 250
ALCQLGKYTT NNSSEQRVSL DIDLWDKFSE LSTKCIIKTV EFAKQLPGFT
260 270 280 290 300
TLTIADQITL LKAACLDILI LRICTRYTPE QDTMTFSDGL TLNRTQMHNA
310 320 330 340 350
GFGPLTDLVF AFANQLLPLE MDDAETGLLS AICLICGDRQ DLEQPDKVDM
360 370 380 390 400
LQEPLLEALK VYVRKRRPSR PHMFPKMLMK ITDLRSISAK GAERVITLKM
410 420 430 440 450
EIPGSMPPLI QEMLENSEGL DTLSGQSGGG TRDGGGLAPP PGSCSPSLSP
460
SSHRSSPATQ SP
Length:462
Mass (Da):50,735
Last modified:October 1, 1989 - v1
Checksum:i726F7799633A85AD
GO
Isoform Alpha-2 (identifier: P11416-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: MASNSSSCPT...SGYSTPSPAT → MYESVEVGGL...TPLWNGSNHS

Show »
Length:459
Mass (Da):50,935
Checksum:i15096242FF09896E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti163 – 1631N → K in AAA40031. (PubMed:2174108)Curated
Sequence conflicti179 – 1791T → S in AAA40031. (PubMed:2174108)Curated
Sequence conflicti284 – 2841M → L in AAA40031. (PubMed:2174108)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti391 – 3911G → A in embryonal carcinoma cell line RAC65.
Natural varianti392 – 46271Missing in embryonal carcinoma cell line RAC65.
Add
BLAST

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6060MASNS…PSPAT → MYESVEVGGLTPAPNPFLVV DFYNQNRACLLQEKGLPAPG PYSTPLRTPLWNGSNHS in isoform Alpha-2. 1 PublicationVSP_003630Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56572 mRNA. Translation: CAA39919.1.
X56565 mRNA. Translation: CAA39917.1.
S56656 mRNA. Translation: AAB25783.1.
X57528 mRNA. Translation: CAA40749.1.
M60909 mRNA. Translation: AAA40031.1.
BC010216 mRNA. Translation: AAH10216.1.
CCDSiCCDS36304.1. [P11416-1]
CCDS48905.1. [P11416-2]
PIRiS05050.
RefSeqiNP_001169999.1. NM_001176528.1. [P11416-2]
NP_001170773.1. NM_001177302.1. [P11416-1]
NP_001170774.1. NM_001177303.1. [P11416-1]
NP_033050.2. NM_009024.2. [P11416-1]
XP_006532654.1. XM_006532591.1. [P11416-1]
XP_006532655.1. XM_006532592.1. [P11416-1]
XP_006532656.1. XM_006532593.1. [P11416-1]
XP_006532657.1. XM_006532594.1. [P11416-1]
UniGeneiMm.439744.

Genome annotation databases

EnsembliENSMUST00000068133; ENSMUSP00000069744; ENSMUSG00000037992. [P11416-1]
ENSMUST00000107473; ENSMUSP00000103097; ENSMUSG00000037992. [P11416-2]
ENSMUST00000107474; ENSMUSP00000103098; ENSMUSG00000037992. [P11416-1]
ENSMUST00000107475; ENSMUSP00000103099; ENSMUSG00000037992. [P11416-1]
ENSMUST00000164748; ENSMUSP00000129791; ENSMUSG00000037992. [P11416-1]
GeneIDi19401.
KEGGimmu:19401.
UCSCiuc007lhx.1. mouse. [P11416-1]
uc007lhz.2. mouse. [P11416-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56572 mRNA. Translation: CAA39919.1 .
X56565 mRNA. Translation: CAA39917.1 .
S56656 mRNA. Translation: AAB25783.1 .
X57528 mRNA. Translation: CAA40749.1 .
M60909 mRNA. Translation: AAA40031.1 .
BC010216 mRNA. Translation: AAH10216.1 .
CCDSi CCDS36304.1. [P11416-1 ]
CCDS48905.1. [P11416-2 ]
PIRi S05050.
RefSeqi NP_001169999.1. NM_001176528.1. [P11416-2 ]
NP_001170773.1. NM_001177302.1. [P11416-1 ]
NP_001170774.1. NM_001177303.1. [P11416-1 ]
NP_033050.2. NM_009024.2. [P11416-1 ]
XP_006532654.1. XM_006532591.1. [P11416-1 ]
XP_006532655.1. XM_006532592.1. [P11416-1 ]
XP_006532656.1. XM_006532593.1. [P11416-1 ]
XP_006532657.1. XM_006532594.1. [P11416-1 ]
UniGenei Mm.439744.

3D structure databases

ProteinModelPortali P11416.
SMRi P11416. Positions 87-415.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202586. 70 interactions.
DIPi DIP-31480N.
IntActi P11416. 11 interactions.
MINTi MINT-5210296.

Chemistry

BindingDBi P11416.
ChEMBLi CHEMBL2792.
GuidetoPHARMACOLOGYi 590.

PTM databases

PhosphoSitei P11416.

Proteomic databases

PRIDEi P11416.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000068133 ; ENSMUSP00000069744 ; ENSMUSG00000037992 . [P11416-1 ]
ENSMUST00000107473 ; ENSMUSP00000103097 ; ENSMUSG00000037992 . [P11416-2 ]
ENSMUST00000107474 ; ENSMUSP00000103098 ; ENSMUSG00000037992 . [P11416-1 ]
ENSMUST00000107475 ; ENSMUSP00000103099 ; ENSMUSG00000037992 . [P11416-1 ]
ENSMUST00000164748 ; ENSMUSP00000129791 ; ENSMUSG00000037992 . [P11416-1 ]
GeneIDi 19401.
KEGGi mmu:19401.
UCSCi uc007lhx.1. mouse. [P11416-1 ]
uc007lhz.2. mouse. [P11416-2 ]

Organism-specific databases

CTDi 5914.
MGIi MGI:97856. Rara.

Phylogenomic databases

eggNOGi NOG297448.
GeneTreei ENSGT00760000118837.
HOGENOMi HOG000010312.
HOVERGENi HBG005606.
InParanoidi P11416.
KOi K08527.
OMAi NNSSDQR.
OrthoDBi EOG738053.
PhylomeDBi P11416.
TreeFami TF328382.

Enzyme and pathway databases

Reactomei REACT_234105. Nuclear Receptor transcription pathway.

Miscellaneous databases

NextBioi 296513.
PROi P11416.
SOURCEi Search...

Gene expression databases

Bgeei P11416.
CleanExi MM_RARA.
ExpressionAtlasi P11416. baseline and differential.
Genevestigatori P11416.

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. 2 hits.
PROSITEi PS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of murine alpha and beta retinoic acid receptors and a novel receptor gamma predominantly expressed in skin."
    Zelent A., Krust A., Petkovich M., Kastner P., Chambon P.
    Nature 339:714-717(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-1).
  2. "Cloning of several genes coding for retinoic acid nuclear receptors in the mouse embryonal carcinoma cell line PCC7-MZ1."
    Heiermann R., Rentrop M., Lang E., Maelicke A.
    J. Recept. Res. 13:693-709(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-1).
  3. "Multiple isoforms of the mouse retinoic acid receptor alpha are generated by alternative splicing and differential induction by retinoic acid."
    Leroy P., Krust A., Zelent A., Mendelsohn C., Garnier J.-M., Kastner P., Dierich A., Chambon P.
    EMBO J. 10:59-69(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA-1 AND ALPHA-2).
  4. "Retinoic acid resistance of the variant embryonal carcinoma cell line RAC65 is caused by expression of a truncated RAR alpha."
    Kruyt F.A.E., van der Veer L., Mader S., van den Brink C.E., Feijen A., Jonk L.J., Kruijer W., van der Saag P.T.
    Differentiation 49:27-37(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (VARIANT IN EMBRYONAL CARCINOMA CELL LINE RAC65).
  5. "A dominant negative mutation of the alpha retinoic acid receptor gene in a retinoic acid-nonresponsive embryonal carcinoma cell."
    Pratt M.A.C., Kralova J., McBurney M.W.
    Mol. Cell. Biol. 10:6445-6453(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (VARIANT IN EMBRYONAL CARCINOMA CELL LINE RAC65).
  6. "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 ALPHA-1).
    Strain: FVB/N.
    Tissue: Mammary gland.
  7. "Lysine trimethylation of retinoic acid receptor-alpha: a novel means to regulate receptor function."
    Huq M.D., Tsai N.-P., Khan S.A., Wei L.-N.
    Mol. Cell. Proteomics 6:677-688(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 340-359, METHYLATION AT LYS-347, FUNCTION, INTERACTION WITH RXRA AND NCOR1, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF LYS-347.
  8. "Stimulation of RAR alpha activation function AF-1 through binding to the general transcription factor TFIIH and phosphorylation by CDK7."
    Rochette-Egly C., Adam S., Rossignol M., Egly J.-M., Chambon P.
    Cell 90:97-107(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDK7 AND GTF2H3, PHOSPHORYLATION AT SER-77, FUNCTION, MUTAGENESIS OF SER-74; SER-77; SER-449; SER-456 AND SER-461.
  9. "The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function."
    Torchia J., Rose D.W., Inostroza J., Kamei Y., Westin S., Glass C.K., Rosenfeld M.G.
    Nature 387:677-684(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NCOA3.
  10. "Follicle-stimulating hormone inhibits all-trans-retinoic acid-induced retinoic acid receptor alpha nuclear localization and transcriptional activation in mouse Sertoli cell lines."
    Braun K.W., Tribley W.A., Griswold M.D., Kim K.H.
    J. Biol. Chem. 275:4145-4151(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  11. "Isolation and characterization of peroxisome proliferator-activated receptor (PPAR) interacting protein (PRIP) as a coactivator for PPAR."
    Zhu Y.-J., Kan L., Qi C., Kanwar Y.S., Yeldandi A.V., Rao M.S., Reddy J.K.
    J. Biol. Chem. 275:13510-13516(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NCOA6.
  12. "Positive regulation of retinoic acid receptor alpha by protein kinase C and mitogen-activated protein kinase in sertoli cells."
    Braun K.W., Vo M.N., Kim K.H.
    Biol. Reprod. 67:29-37(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, SUBCELLULAR LOCATION.
  13. "Male sterility in mice lacking retinoic acid receptor alpha involves specific abnormalities in spermiogenesis."
    Chung S.S., Wang X., Wolgemuth D.J.
    Differentiation 73:188-198(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  14. "Potential functions of retinoic acid receptor A in Sertoli cells and germ cells during spermatogenesis."
    Doyle T.J., Braun K.W., McLean D.J., Wright R.W., Griswold M.D., Kim K.H.
    Ann. N. Y. Acad. Sci. 1120:114-130(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, INDUCTION.
  15. "Retinoic acid receptors are required for skeletal growth, matrix homeostasis and growth plate function in postnatal mouse."
    Williams J.A., Kondo N., Okabe T., Takeshita N., Pilchak D.M., Koyama E., Ochiai T., Jensen D., Chu M.L., Kane M.A., Napoli J.L., Enomoto-Iwamoto M., Ghyselinck N., Chambon P., Pacifici M., Iwamoto M.
    Dev. Biol. 328:315-327(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  16. "A coordinated phosphorylation cascade initiated by p38MAPK/MSK1 directs RARalpha to target promoters."
    Bruck N., Vitoux D., Ferry C., Duong V., Bauer A., de The H., Rochette-Egly C.
    EMBO J. 28:34-47(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-77 AND SER-369, FUNCTION, INTERACTION WITH GTF2H3, MUTAGENESIS OF SER-77 AND SER-369.

Entry informationi

Entry nameiRARA_MOUSE
AccessioniPrimary (citable) accession number: P11416
Secondary accession number(s): P22603
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: November 26, 2014
This is version 168 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3