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P11416 (RARA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 164. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Retinoic acid receptor alpha

Short name=RAR-alpha
Alternative name(s):
Nuclear receptor subfamily 1 group B member 1
Gene names
Name:Rara
Synonyms:Nr1b1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length462 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7 Ref.8 Ref.10 Ref.13 Ref.14 Ref.15 Ref.16

Subunit structure

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. Ref.7 Ref.8 Ref.9 Ref.11 Ref.16

Subcellular location

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. Ref.10 Ref.12

Tissue specificity

Expressed in Sertoli cells and germ cells. Ref.14

Induction

By retinoic acid. Ref.14

Domain

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

Post-translational modification

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. Ref.8 Ref.12 Ref.16

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.

Disruption phenotype

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. Ref.13 Ref.14 Ref.15

Sequence similarities

Belongs to the nuclear hormone receptor family. NR1 subfamily.

Contains 1 nuclear receptor DNA-binding domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionReceptor
   PTMIsopeptide bond
Methylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processSertoli cell fate commitment

Inferred from mutant phenotype Ref.14. Source: UniProtKB

apoptotic cell clearance

Inferred from electronic annotation. Source: Ensembl

cellular response to estrogen stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to lipopolysaccharide

Inferred from direct assay PubMed 19752193. Source: UniProtKB

cellular response to retinoic acid

Inferred from electronic annotation. Source: Ensembl

chondroblast differentiation

Inferred from mutant phenotype PubMed 10684250. Source: MGI

female pregnancy

Inferred from electronic annotation. Source: Ensembl

germ cell development

Inferred from mutant phenotype Ref.13. Source: UniProtKB

growth plate cartilage development

Inferred from genetic interaction Ref.15. Source: MGI

intracellular estrogen receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

liver development

Inferred from electronic annotation. Source: Ensembl

multicellular organism growth

Inferred from genetic interaction Ref.15. Source: MGI

negative regulation of cartilage development

Inferred from mutant phenotype PubMed 10684250. Source: MGI

negative regulation of cell differentiation

Inferred from mutant phenotype PubMed 10684250. Source: MGI

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of gene expression

Inferred from genetic interaction PubMed 18026104. Source: MGI

negative regulation of granulocyte differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of interferon-gamma production

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 8152920. Source: MGI

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 11641275. Source: MGI

negative regulation of translational initiation

Inferred from direct assay PubMed 18495661. Source: MGI

negative regulation of tumor necrosis factor production

Inferred from electronic annotation. Source: Ensembl

positive regulation of ERK1 and ERK2 cascade

Inferred from electronic annotation. Source: Ensembl

positive regulation of T-helper 2 cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of binding

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell cycle

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from genetic interaction PubMed 18026104. Source: MGI

positive regulation of gene expression

Inferred from mutant phenotype PubMed 19752193. Source: UniProtKB

positive regulation of interleukin-13 production

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-4 production

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-5 production

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuron differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein kinase B signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from genetic interaction. Source: MGI

prostate gland development

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

regulation of granulocyte differentiation

Inferred from mutant phenotype PubMed 11222375. Source: MGI

regulation of myelination

Inferred from electronic annotation. Source: Ensembl

regulation of synaptic plasticity

Inferred from electronic annotation. Source: Ensembl

regulation of transcription, DNA-templated

Inferred from direct assay Ref.12PubMed 12101409PubMed 15322135. Source: MGI

response to cytokine

Inferred from electronic annotation. Source: Ensembl

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to retinoic acid

Inferred from mutant phenotype PubMed 11222375. Source: MGI

response to vitamin A

Inferred from electronic annotation. Source: Ensembl

spermatogenesis

Inferred from mutant phenotype PubMed 8394014. Source: MGI

ureteric bud development

Inferred from mutant phenotype PubMed 12195422. Source: MGI

ventricular cardiac muscle cell differentiation

Inferred from mutant phenotype PubMed 9428411. Source: MGI

   Cellular_componentcytoplasm

Inferred from direct assay Ref.12. Source: MGI

dendrite

Inferred from direct assay PubMed 18495661. Source: MGI

neuronal cell body

Inferred from direct assay PubMed 18495661. Source: MGI

nuclear chromatin

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 19752193. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionDNA binding

Inferred from direct assay PubMed 14980219PubMed 15528198. Source: MGI

chromatin DNA binding

Inferred from electronic annotation. Source: Ensembl

drug binding

Inferred from electronic annotation. Source: Ensembl

ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from direct assay PubMed 15322135. Source: MGI

mRNA 5'-UTR binding

Inferred from electronic annotation. Source: Ensembl

phosphatidylinositol 3-kinase regulator activity

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 10531331PubMed 16723356PubMed 17641689PubMed 19752193PubMed 8978696. Source: UniProtKB

retinoic acid binding

Inferred from electronic annotation. Source: Ensembl

retinoic acid receptor activity

Inferred from direct assay PubMed 15528198. Source: MGI

retinoic acid-responsive element binding

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding

Inferred from direct assay PubMed 17928865. Source: MGI

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 15528198PubMed 8152920. Source: MGI

steroid hormone receptor activity

Inferred from electronic annotation. Source: InterPro

transcription coactivator activity

Inferred from electronic annotation. Source: Ensembl

transcription corepressor activity

Inferred from electronic annotation. Source: Ensembl

transcription factor binding

Inferred from physical interaction PubMed 17641689. Source: UniProtKB

transcription regulatory region DNA binding

Inferred from mutant phenotype PubMed 19752193. Source: UniProtKB

translation repressor activity, nucleic acid binding

Inferred from electronic annotation. Source: Ensembl

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Rps6ka5Q8C0502EBI-346736,EBI-8391218

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Alpha-1 (identifier: P11416-1)

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.
Isoform Alpha-2 (identifier: P11416-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 462462Retinoic acid receptor alpha
PRO_0000053462

Regions

DNA binding88 – 15366Nuclear receptor
Zinc finger88 – 10821NR C4-type
Zinc finger124 – 14825NR C4-type
Region1 – 8787Modulating
Region154 – 19946Hinge
Region200 – 419220Ligand-binding
Region404 – 41916Required for binding corepressor NCOR1

Amino acid modifications

Modified residue771Phosphoserine; by CDK7 Ref.8 Ref.16
Modified residue961Phosphoserine; by PKB/AKT1 By similarity
Modified residue2191Phosphoserine; by PKA By similarity
Modified residue3471N6,N6,N6-trimethyllysine Ref.7
Modified residue3691Phosphoserine; by PKA and RPS6KA5 Ref.16
Cross-link166Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link171Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link399Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence1 – 6060MASNS…PSPAT → MYESVEVGGLTPAPNPFLVV DFYNQNRACLLQEKGLPAPG PYSTPLRTPLWNGSNHS in isoform Alpha-2.
VSP_003630
Natural variant3911G → A in embryonal carcinoma cell line RAC65.
Natural variant392 – 46271Missing in embryonal carcinoma cell line RAC65.

Experimental info

Mutagenesis741S → A: No effect on phosphorylation, no effect on transcriptional activity. Ref.8
Mutagenesis771S → A: Decreases phosphorylation and no effect on interaction with CDK7. Strongly reduces transcriptional activity. Ref.8 Ref.16
Mutagenesis3471K → A or Q: Greatly reduced interaction with RXRA and NCOR1 and transcriptional activation. Ref.7
Mutagenesis3471K → F: Reduced methylation levels. Little effect on interaction with RXRA or NCOR1. Small loss in transcriptional activation. Ref.7
Mutagenesis3691S → A: Abolishes phosphorylation and prevents phosphorylation of S-77. Ref.16
Mutagenesis4491S → A: No change in phosphorylation levels and no effect on transcriptional activity. Ref.8
Mutagenesis4561S → A: No change in phosphorylation levels and no effect on transcriptional activity. Ref.8
Mutagenesis4611S → A: No change in phosphorylation levels and no effect on transcriptional activity. Ref.8
Sequence conflict1631N → K in AAA40031. Ref.5
Sequence conflict1791T → S in AAA40031. Ref.5
Sequence conflict2841M → L in AAA40031. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform Alpha-1 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: 726F7799633A85AD

FASTA46250,735
        10         20         30         40         50         60 
MASNSSSCPT PGGGHLNGYP VPPYAFFFPP MLGGLSPPGA LTSLQHQLPV SGYSTPSPAT 

        70         80         90        100        110        120 
IETQSSSSEE IVPSPPSPPP LPRIYKPCFV CQDKSSGYHY GVSACEGCKG FFRRSIQKNM 

       130        140        150        160        170        180 
VYTCHRDKNC IINKVTRNRC QYCRLQKCFD VGMSKESVRN DRNKKKKEAP KPECSESYTL 

       190        200        210        220        230        240 
TPEVGELIEK VRKAHQETFP ALCQLGKYTT NNSSEQRVSL DIDLWDKFSE LSTKCIIKTV 

       250        260        270        280        290        300 
EFAKQLPGFT TLTIADQITL LKAACLDILI LRICTRYTPE QDTMTFSDGL TLNRTQMHNA 

       310        320        330        340        350        360 
GFGPLTDLVF AFANQLLPLE MDDAETGLLS AICLICGDRQ DLEQPDKVDM LQEPLLEALK 

       370        380        390        400        410        420 
VYVRKRRPSR PHMFPKMLMK ITDLRSISAK GAERVITLKM EIPGSMPPLI QEMLENSEGL 

       430        440        450        460 
DTLSGQSGGG TRDGGGLAPP PGSCSPSLSP SSHRSSPATQ SP 

« Hide

Isoform Alpha-2 [UniParc].

Checksum: 15096242FF09896E
Show »

FASTA45950,935

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS36304.1. [P11416-1]
CCDS48905.1. [P11416-2]
PIRS05050.
RefSeqNP_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]
UniGeneMm.439744.

3D structure databases

ProteinModelPortalP11416.
SMRP11416. Positions 87-415.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202586. 70 interactions.
DIPDIP-31480N.
IntActP11416. 11 interactions.
MINTMINT-5210296.

Chemistry

BindingDBP11416.
ChEMBLCHEMBL2792.
GuidetoPHARMACOLOGY590.

PTM databases

PhosphoSiteP11416.

Proteomic databases

PRIDEP11416.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000068133; ENSMUSP00000069744; ENSMUSG00000037992. [P11416-1]
ENSMUST00000107473; ENSMUSP00000103097; ENSMUSG00000037992. [P11416-2]
ENSMUST00000107474; ENSMUSP00000103098; ENSMUSG00000037992. [P11416-1]
ENSMUST00000107475; ENSMUSP00000103099; ENSMUSG00000037992. [P11416-1]
ENSMUST00000164748; ENSMUSP00000129791; ENSMUSG00000037992. [P11416-1]
GeneID19401.
KEGGmmu:19401.
UCSCuc007lhx.1. mouse. [P11416-1]
uc007lhz.2. mouse. [P11416-2]

Organism-specific databases

CTD5914.
MGIMGI:97856. Rara.

Phylogenomic databases

eggNOGNOG297448.
GeneTreeENSGT00740000114969.
HOGENOMHOG000010312.
HOVERGENHBG005606.
InParanoidP11416.
KOK08527.
OMANNSSDQR.
OrthoDBEOG738053.
PhylomeDBP11416.
TreeFamTF328382.

Gene expression databases

ArrayExpressP11416.
BgeeP11416.
CleanExMM_RARA.
GenevestigatorP11416.

Family and domain databases

Gene3D1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProIPR008946. 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]
PfamPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSPR01292. RETNOICACIDR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMSSF48508. SSF48508. 2 hits.
PROSITEPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio296513.
PROP11416.
SOURCESearch...

Entry information

Entry nameRARA_MOUSE
AccessionPrimary (citable) accession number: P11416
Secondary accession number(s): P22603
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: July 9, 2014
This is version 164 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot