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P11416

- RARA_MOUSE

UniProt

P11416 - RARA_MOUSE

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Protein
Retinoic acid receptor alpha
Gene
Rara, Nr1b1
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 receptor
Add
BLAST
Zinc fingeri88 – 10821NR C4-type
Add
BLAST
Zinc fingeri124 – 14825NR C4-type
Add
BLAST

GO - Molecular functioni

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

GO - Biological processi

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

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.2 Publications

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 alpha
PRO_0000053462Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei77 – 771Phosphoserine; by CDK72 Publications
Modified residuei96 – 961Phosphoserine; by PKB/AKT1 By 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 PKA By 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.

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

ArrayExpressiP11416.
BgeeiP11416.
CleanExiMM_RARA.
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.5 Publications

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.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 8787Modulating
Add
BLAST
Regioni154 – 19946Hinge
Add
BLAST
Regioni200 – 419220Ligand-binding
Add
BLAST
Regioni404 – 41916Required for binding corepressor NCOR1
Add
BLAST

Domaini

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

Sequence similaritiesi

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG297448.
GeneTreeiENSGT00740000114969.
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

MASNSSSCPT PGGGHLNGYP VPPYAFFFPP MLGGLSPPGA LTSLQHQLPV    50
SGYSTPSPAT IETQSSSSEE IVPSPPSPPP LPRIYKPCFV CQDKSSGYHY 100
GVSACEGCKG FFRRSIQKNM VYTCHRDKNC IINKVTRNRC QYCRLQKCFD 150
VGMSKESVRN DRNKKKKEAP KPECSESYTL TPEVGELIEK VRKAHQETFP 200
ALCQLGKYTT NNSSEQRVSL DIDLWDKFSE LSTKCIIKTV EFAKQLPGFT 250
TLTIADQITL LKAACLDILI LRICTRYTPE QDTMTFSDGL TLNRTQMHNA 300
GFGPLTDLVF AFANQLLPLE MDDAETGLLS AICLICGDRQ DLEQPDKVDM 350
LQEPLLEALK VYVRKRRPSR PHMFPKMLMK ITDLRSISAK GAERVITLKM 400
EIPGSMPPLI QEMLENSEGL DTLSGQSGGG TRDGGGLAPP PGSCSPSLSP 450
SSHRSSPATQ SP 462
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

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.
VSP_003630Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti163 – 1631N → K in AAA40031. 1 Publication
Sequence conflicti179 – 1791T → S in AAA40031. 1 Publication
Sequence conflicti284 – 2841M → L in AAA40031. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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...

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 ENSGT00740000114969.
HOGENOMi HOG000010312.
HOVERGENi HBG005606.
InParanoidi P11416.
KOi K08527.
OMAi NNSSDQR.
OrthoDBi EOG738053.
PhylomeDBi P11416.
TreeFami TF328382.

Miscellaneous databases

NextBioi 296513.
PROi P11416.
SOURCEi Search...

Gene expression databases

ArrayExpressi P11416.
Bgeei P11416.
CleanExi MM_RARA.
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: September 3, 2014
This is version 165 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

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