UniProtKB - P11416 (RARA_MOUSE)
Retinoic acid receptor alpha
Rara
Functioni
Receptor for retinoic acid (PubMed:17205979).
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 (PubMed:17205979).
The RXR/RAR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 (PubMed:17205979).
In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone deacetylation, chromatin condensation and transcriptional suppression (By similarity).
On ligand binding, the corepressors dissociate from the receptors and associate with the coactivators leading to transcriptional activation (PubMed:17205979, PubMed:9230306, PubMed:19078967).
Formation of heterocomplex with histone deacetylases might lead to inhibition of RARE DNA element binding and to transcriptional repression (By similarity).
Transcriptional activation and RARE DNA element binding might be supported by the transcription factor KLF2 (By similarity).
RARA plays an essential role in the regulation of retinoic acid-induced germ cell development during spermatogenesis (PubMed:15901285).
Has a role in the survival of early spermatocytes at the beginning prophase of meiosis (PubMed:15901285, PubMed:17905941).
In Sertoli cells, may promote the survival and development of early meiotic prophase spermatocytes (PubMed:10660575, PubMed:17905941).
In concert with RARG, required for skeletal growth, matrix homeostasis and growth plate function (PubMed:19389355).
Together with RXRA, positively regulates microRNA-10a expression, thereby inhibiting the GATA6/VCAM1 signaling response to pulsatile shear stress in vascular endothelial cells (By similarity).
In association with HDAC3, HDAC5 and HDAC7 corepressors, plays a role in the repression of microRNA-10a and thereby promotes the inflammatory response (By similarity).
By similarity7 PublicationsRegions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
DNA bindingi | 88 – 153 | Nuclear receptorPROSITE-ProRule annotationAdd BLAST | 66 | |
Zinc fingeri | 88 – 108 | NR C4-typePROSITE-ProRule annotationAdd BLAST | 21 | |
Zinc fingeri | 124 – 148 | NR C4-typePROSITE-ProRule annotationAdd BLAST | 25 |
GO - Molecular functioni
- alpha-actinin binding Source: MGI
- chromatin binding Source: MGI
- chromatin DNA binding Source: MGI
- DNA binding Source: MGI
- DNA-binding transcription factor activity Source: MGI
- DNA-binding transcription repressor activity Source: Ensembl
- enzyme binding Source: MGI
- heterocyclic compound binding Source: MGI
- histone deacetylase binding Source: MGI
- mRNA 5'-UTR binding Source: MGI
- nuclear receptor activity Source: MGI
- phosphatidylinositol 3-kinase regulator activity Source: MGI
- protein domain specific binding Source: MGI
- protein kinase A binding Source: MGI
- protein kinase B binding Source: MGI
- retinoic acid binding Source: MGI
- retinoic acid-responsive element binding Source: MGI
- RNA polymerase II cis-regulatory region sequence-specific DNA binding Source: MGI
- RNA polymerase II transcription regulatory region sequence-specific DNA binding Source: MGI
- sequence-specific DNA binding Source: MGI
- sequence-specific double-stranded DNA binding Source: MGI
- signaling receptor binding Source: MGI
- transcription cis-regulatory region binding Source: MGI
- transcription coactivator binding Source: UniProtKB
- translation repressor activity, mRNA regulatory element binding Source: MGI
- zinc ion binding Source: InterPro
GO - Biological processi
- apoptotic cell clearance Source: MGI
- bone development Source: MGI
- cell differentiation Source: GO_Central
- cellular response to estrogen stimulus Source: MGI
- cellular response to lipopolysaccharide Source: UniProtKB
- cellular response to retinoic acid Source: Ensembl
- chondroblast differentiation Source: MGI
- embryonic camera-type eye development Source: MGI
- face development Source: MGI
- female pregnancy Source: Ensembl
- germ cell development Source: UniProtKB
- glandular epithelial cell development Source: MGI
- growth plate cartilage development Source: MGI
- hippocampus development Source: Ensembl
- hormone-mediated signaling pathway Source: GO_Central
- limb development Source: MGI
- liver development Source: Ensembl
- male gonad development Source: MGI
- mRNA transcription by RNA polymerase II Source: Ensembl
- multicellular organism growth Source: MGI
- negative regulation of cartilage development Source: MGI
- negative regulation of cell differentiation Source: MGI
- negative regulation of cell population proliferation Source: MGI
- negative regulation of gene expression Source: MGI
- negative regulation of granulocyte differentiation Source: MGI
- negative regulation of interferon-gamma production Source: MGI
- negative regulation of pri-miRNA transcription by RNA polymerase II Source: Ensembl
- negative regulation of transcription, DNA-templated Source: MGI
- negative regulation of transcription by RNA polymerase II Source: MGI
- negative regulation of translation Source: MGI
- negative regulation of tumor necrosis factor production Source: MGI
- neural tube closure Source: MGI
- positive regulation of binding Source: MGI
- positive regulation of cell cycle Source: MGI
- positive regulation of cell population proliferation Source: MGI
- positive regulation of ERK1 and ERK2 cascade Source: MGI
- positive regulation of gene expression Source: UniProtKB
- positive regulation of interleukin-13 production Source: MGI
- positive regulation of interleukin-4 production Source: MGI
- positive regulation of interleukin-5 production Source: MGI
- positive regulation of neuron differentiation Source: MGI
- positive regulation of phosphatidylinositol 3-kinase signaling Source: MGI
- positive regulation of protein kinase B signaling Source: MGI
- positive regulation of T-helper 2 cell differentiation Source: MGI
- positive regulation of transcription, DNA-templated Source: MGI
- positive regulation of transcription by RNA polymerase II Source: MGI
- prostate gland development Source: Ensembl
- protein phosphorylation Source: MGI
- regulation of apoptotic process Source: MGI
- regulation of granulocyte differentiation Source: MGI
- regulation of myelination Source: MGI
- regulation of synaptic plasticity Source: MGI
- regulation of transcription, DNA-templated Source: MGI
- response to cytokine Source: Ensembl
- response to estradiol Source: Ensembl
- response to ethanol Source: MGI
- response to retinoic acid Source: MGI
- response to vitamin A Source: Ensembl
- retinoic acid receptor signaling pathway Source: MGI
- Sertoli cell fate commitment Source: UniProtKB
- signal transduction Source: MGI
- trachea cartilage development Source: MGI
- ureteric bud development Source: MGI
- ventricular cardiac muscle cell differentiation Source: MGI
Keywordsi
Molecular function | DNA-binding, Receptor |
Biological process | Transcription, Transcription regulation |
Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
Reactomei | R-MMU-383280, Nuclear Receptor transcription pathway R-MMU-4090294, SUMOylation of intracellular receptors R-MMU-5362517, Signaling by Retinoic Acid R-MMU-9616222, Transcriptional regulation of granulopoiesis |
Names & Taxonomyi
Protein namesi | Recommended name: Retinoic acid receptor alphaShort name: RAR-alpha Alternative name(s): Nuclear receptor subfamily 1 group B member 1 |
Gene namesi | Name:Rara Synonyms:Nr1b1 |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:97856, Rara |
VEuPathDBi | HostDB:ENSMUSG00000037992 |
Subcellular locationi
Nucleus
- Nucleus 2 Publications
Cytoplasm and Cytosol
- Cytoplasm 2 Publications
Note: Nuclear localization depends on ligand binding, phosphorylation and sumoylation (PubMed:10660575, PubMed:12079996). Translocation to the nucleus is dependent on activation of PKC and the downstream MAPK phosphorylation (PubMed:10660575, PubMed:12079996). Increased nuclear localization upon pulsatile shear stress (By similarity).By similarity2 Publications
Cytoskeleton
- actin cytoskeleton Source: MGI
Cytosol
- cytosol Source: MGI
Nucleus
- nucleolus Source: MGI
- nucleoplasm Source: MGI
- nucleus Source: UniProtKB
- RNA polymerase II transcription regulator complex Source: Ensembl
Other locations
- chromatin Source: MGI
- cytoplasm Source: MGI
- dendrite Source: MGI
- neuron projection Source: MGI
- perinuclear region of cytoplasm Source: MGI
- protein-containing complex Source: MGI
- transcription regulator complex Source: ComplexPortal
Keywords - Cellular componenti
Cytoplasm, NucleusPathology & Biotechi
Disruption phenotypei
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 74 | S → A: No effect on phosphorylation, no effect on transcriptional activity. 1 Publication | 1 | |
Mutagenesisi | 77 | S → A: Decreases phosphorylation and no effect on interaction with CDK7. Strongly reduces transcriptional activity. 2 Publications | 1 | |
Mutagenesisi | 347 | K → A or Q: Greatly reduced interaction with RXRA and NCOR1 and transcriptional activation. 1 Publication | 1 | |
Mutagenesisi | 347 | K → F: Reduced methylation levels. Little effect on interaction with RXRA or NCOR1. Small loss in transcriptional activation. 1 Publication | 1 | |
Mutagenesisi | 369 | S → A: Abolishes phosphorylation and prevents phosphorylation of S-77. 1 Publication | 1 | |
Mutagenesisi | 449 | S → A: No change in phosphorylation levels and no effect on transcriptional activity. 1 Publication | 1 | |
Mutagenesisi | 456 | S → A: No change in phosphorylation levels and no effect on transcriptional activity. 1 Publication | 1 | |
Mutagenesisi | 461 | S → A: No change in phosphorylation levels and no effect on transcriptional activity. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL2792 |
DrugCentrali | P11416 |
GuidetoPHARMACOLOGYi | 590 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000053462 | 1 – 462 | Retinoic acid receptor alphaAdd BLAST | 462 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 77 | Phosphoserine; by CDK72 Publications | 1 | |
Modified residuei | 96 | Phosphoserine; by PKB/AKT1By similarity | 1 | |
Cross-linki | 166 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity | ||
Cross-linki | 171 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity | ||
Modified residuei | 219 | Phosphoserine; by PKABy similarity | 1 | |
Modified residuei | 347 | N6,N6,N6-trimethyllysine1 Publication | 1 | |
Modified residuei | 369 | Phosphoserine; by PKA and RPS6KA51 Publication | 1 | |
Cross-linki | 399 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity |
Post-translational modificationi
Keywords - PTMi
Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugationProteomic databases
MaxQBi | P11416 |
PaxDbi | P11416 |
PRIDEi | P11416 |
ProteomicsDBi | 300233 [P11416-1] 300234 [P11416-2] |
PTM databases
iPTMneti | P11416 |
PhosphoSitePlusi | P11416 |
Expressioni
Tissue specificityi
Inductioni
Gene expression databases
Bgeei | ENSMUSG00000037992, Expressed in granulocyte and 240 other tissues |
ExpressionAtlasi | P11416, baseline and differential |
Genevisiblei | P11416, MM |
Interactioni
Subunit structurei
Heterodimer; with RXRA (PubMed:17205979). Binds DNA preferentially as a heterodimer (By similarity). RXRA serves as enhancer to induce RARA binding to RARE (By similarity).
Interacts with RXRG (By similarity).
Interacts with NCOA3 and NCOA6 coactivators, leading to a strong increase of transcription of target genes (PubMed:10788465, PubMed:9192892).
Interacts with NCOA7; the interaction requires ligand-binding (By similarity).
Interacts (via the ligand-binding domain) with PRAME; interaction is direct and ligand (retinoic acid)-dependent (By similarity).
Interacts with PRKAR1A; the interaction negatively regulates RARA transcriptional activity (By similarity).
Interacts with NCOR1; the interaction occurs in the absence of ligand and represses transcriptional activity (PubMed:17205979).
Interacts with NCOR2 (By similarity).
Interacts with PRMT2 (By similarity).
Interacts with LRIF1 (By similarity).
Interacts with ASXL1 and NCOA1 (By similarity).
Interacts with ACTN4 (By similarity).
Interacts with CDK7; the interaction is enhanced by interaction with GTF2H3 (PubMed:9230306).
Interacts with GTF2H3; the interaction requires prior phosphorylation on Ser-369 which then enhances interaction with CDK7 (PubMed:19078967). In a complex with HDAC3, HDAC5 and HDAC7; the HDACs serve as corepressors of RARA, causing its deacetylation and inhibition of RARE DNA element binding; association with HDAC3, HDAC5 and HDAC7 is increased upon oscillatory shear stress (By similarity). In the absence of hormonal ligand, interacts with TACC1 (PubMed:20078863).
By similarity6 PublicationsBinary interactionsi
P11416
With | #Exp. | IntAct |
---|---|---|
Rps6ka5 [Q8C050] | 2 | EBI-346736,EBI-8391218 |
NFE2L2 [Q16236] from Homo sapiens. | 2 | EBI-346736,EBI-2007911 |
GO - Molecular functioni
- alpha-actinin binding Source: MGI
- enzyme binding Source: MGI
- histone deacetylase binding Source: MGI
- protein domain specific binding Source: MGI
- protein kinase A binding Source: MGI
- protein kinase B binding Source: MGI
- signaling receptor binding Source: MGI
- transcription coactivator binding Source: UniProtKB
Protein-protein interaction databases
BioGRIDi | 202586, 74 interactors |
ComplexPortali | CPX-584, RXRalpha-RARalpha retinoic acid receptor complex CPX-667, RARalpha-NCOA1 activated retinoic acid receptor complex CPX-668, RARalpha-NCOA2 activated retinoic acid receptor complex CPX-818, RXRalpha-RARalpha-NCOA2 retinoic acid receptor complex |
DIPi | DIP-31480N |
IntActi | P11416, 15 interactors |
MINTi | P11416 |
STRINGi | 10090.ENSMUSP00000069744 |
Chemistry databases
BindingDBi | P11416 |
Miscellaneous databases
RNActi | P11416, protein |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 183 – 417 | NR LBDPROSITE-ProRule annotationAdd BLAST | 235 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 87 | ModulatingAdd BLAST | 87 | |
Regioni | 52 – 77 | DisorderedSequence analysisAdd BLAST | 26 | |
Regioni | 154 – 182 | HingeAdd BLAST | 29 | |
Regioni | 404 – 419 | Required for binding corepressor NCOR1Add BLAST | 16 | |
Regioni | 420 – 462 | DisorderedSequence analysisAdd BLAST | 43 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 408 – 416 | 9aaTADBy similarity | 9 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 52 – 71 | Polar residuesSequence analysisAdd BLAST | 20 | |
Compositional biasi | 447 – 462 | Polar residuesSequence analysisAdd BLAST | 16 |
Domaini
Sequence similaritiesi
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 88 – 108 | NR C4-typePROSITE-ProRule annotationAdd BLAST | 21 | |
Zinc fingeri | 124 – 148 | NR C4-typePROSITE-ProRule annotationAdd BLAST | 25 |
Keywords - Domaini
Zinc-fingerPhylogenomic databases
eggNOGi | KOG3575, Eukaryota |
GeneTreei | ENSGT00940000159997 |
HOGENOMi | CLU_007368_18_2_1 |
InParanoidi | P11416 |
OMAi | PPYSYFF |
OrthoDBi | 1466354at2759 |
PhylomeDBi | P11416 |
TreeFami | TF328382 |
Family and domain databases
Gene3Di | 1.10.565.10, 1 hit 3.30.50.10, 1 hit |
InterProi | View protein in InterPro IPR035500, NHR-like_dom_sf IPR000536, Nucl_hrmn_rcpt_lig-bd IPR001723, Nuclear_hrmn_rcpt IPR003078, Retinoic_acid_rcpt IPR001628, Znf_hrmn_rcpt IPR013088, Znf_NHR/GATA |
Pfami | View protein in Pfam PF00104, Hormone_recep, 1 hit PF00105, zf-C4, 1 hit |
PRINTSi | PR01292, RETNOICACIDR PR00398, STRDHORMONER PR00047, STROIDFINGER |
SMARTi | View protein in SMART SM00430, HOLI, 1 hit SM00399, ZnF_C4, 1 hit |
SUPFAMi | SSF48508, SSF48508, 1 hit |
PROSITEi | View protein in PROSITE PS51843, NR_LBD, 1 hit PS00031, NUCLEAR_REC_DBD_1, 1 hit PS51030, NUCLEAR_REC_DBD_2, 1 hit |
s (2)i Sequence
Sequence statusi: Complete.
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
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
The sequence of this isoform differs from the canonical sequence as follows:
1-60: MASNSSSCPT...SGYSTPSPAT → MYESVEVGGL...TPLWNGSNHS
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 163 | N → K in AAA40031 (PubMed:2174108).Curated | 1 | |
Sequence conflicti | 179 | T → S in AAA40031 (PubMed:2174108).Curated | 1 | |
Sequence conflicti | 284 | M → L in AAA40031 (PubMed:2174108).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 391 | G → A in embryonal carcinoma cell line RAC65. | 1 | |
Natural varianti | 392 – 462 | Missing in embryonal carcinoma cell line RAC65. Add BLAST | 71 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_003630 | 1 – 60 | MASNS…PSPAT → MYESVEVGGLTPAPNPFLVV DFYNQNRACLLQEKGLPAPG PYSTPLRTPLWNGSNHS in isoform Alpha-2. 1 PublicationAdd BLAST | 60 |
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_006532655.1, XM_006532592.3 [P11416-1] XP_006532656.1, XM_006532593.2 [P11416-1] XP_017169842.1, XM_017314353.1 |
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] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
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_006532655.1, XM_006532592.3 [P11416-1] XP_006532656.1, XM_006532593.2 [P11416-1] XP_017169842.1, XM_017314353.1 |
3D structure databases
SASBDBi | P11416 |
SMRi | P11416 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 202586, 74 interactors |
ComplexPortali | CPX-584, RXRalpha-RARalpha retinoic acid receptor complex CPX-667, RARalpha-NCOA1 activated retinoic acid receptor complex CPX-668, RARalpha-NCOA2 activated retinoic acid receptor complex CPX-818, RXRalpha-RARalpha-NCOA2 retinoic acid receptor complex |
DIPi | DIP-31480N |
IntActi | P11416, 15 interactors |
MINTi | P11416 |
STRINGi | 10090.ENSMUSP00000069744 |
Chemistry databases
BindingDBi | P11416 |
ChEMBLi | CHEMBL2792 |
DrugCentrali | P11416 |
GuidetoPHARMACOLOGYi | 590 |
PTM databases
iPTMneti | P11416 |
PhosphoSitePlusi | P11416 |
Proteomic databases
MaxQBi | P11416 |
PaxDbi | P11416 |
PRIDEi | P11416 |
ProteomicsDBi | 300233 [P11416-1] 300234 [P11416-2] |
Protocols and materials databases
Antibodypediai | 16473, 803 antibodies from 47 providers |
DNASUi | 19401 |
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 |
VEuPathDBi | HostDB:ENSMUSG00000037992 |
Phylogenomic databases
eggNOGi | KOG3575, Eukaryota |
GeneTreei | ENSGT00940000159997 |
HOGENOMi | CLU_007368_18_2_1 |
InParanoidi | P11416 |
OMAi | PPYSYFF |
OrthoDBi | 1466354at2759 |
PhylomeDBi | P11416 |
TreeFami | TF328382 |
Enzyme and pathway databases
Reactomei | R-MMU-383280, Nuclear Receptor transcription pathway R-MMU-4090294, SUMOylation of intracellular receptors R-MMU-5362517, Signaling by Retinoic Acid R-MMU-9616222, Transcriptional regulation of granulopoiesis |
Miscellaneous databases
BioGRID-ORCSi | 19401, 2 hits in 66 CRISPR screens |
ChiTaRSi | Rara, mouse |
PROi | PR:P11416 |
RNActi | P11416, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000037992, Expressed in granulocyte and 240 other tissues |
ExpressionAtlasi | P11416, baseline and differential |
Genevisiblei | P11416, MM |
Family and domain databases
Gene3Di | 1.10.565.10, 1 hit 3.30.50.10, 1 hit |
InterProi | View protein in InterPro IPR035500, NHR-like_dom_sf IPR000536, Nucl_hrmn_rcpt_lig-bd IPR001723, Nuclear_hrmn_rcpt IPR003078, Retinoic_acid_rcpt IPR001628, Znf_hrmn_rcpt IPR013088, Znf_NHR/GATA |
Pfami | View protein in Pfam PF00104, Hormone_recep, 1 hit PF00105, zf-C4, 1 hit |
PRINTSi | PR01292, RETNOICACIDR PR00398, STRDHORMONER PR00047, STROIDFINGER |
SMARTi | View protein in SMART SM00430, HOLI, 1 hit SM00399, ZnF_C4, 1 hit |
SUPFAMi | SSF48508, SSF48508, 1 hit |
PROSITEi | View protein in PROSITE PS51843, NR_LBD, 1 hit PS00031, NUCLEAR_REC_DBD_1, 1 hit PS51030, NUCLEAR_REC_DBD_2, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | RARA_MOUSE | |
Accessioni | P11416Primary (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: | February 23, 2022 | |
This is version 227 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencing, Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - SIMILARITY comments
Index of protein domains and families