RARB
entrez
5915
canonical
uniprot
P10826
canonical
ensembl
ENSG00000077092
resolver
ensp
ENSP00000332296
resolver
ensp
ENSP00000391391
resolver
ensp
ENSP00000398840
resolver
ensp
ENSP00000510520
resolver
ensp
ENSP00000510650
resolver
enst
ENST00000691912
resolver
genesymbol
NR1B2
resolver
genesymbol
RARB
resolver
genesymbol_syn
HAP
resolver
genesymbol_syn
NR1B2
resolver
genesymbol_syn
RARB
resolver
hgnc
HGNC:9865
resolver
uniprot
A0A8I5KWP3
resolver
uniprot
F1D8S6
resolver
uniprot
P12891
resolver
uniprot
Q00989
resolver
uniprot
Q15298
resolver
uniprot
Q3SB16
resolver
uniprot
Q5QHG3
resolver
uniprot
Q86UC5
resolver
uniprot
Q9UN48
resolver
uniprot_entry
A0A8I5KWP3_HUMAN
resolver
uniprot_entry
F1D8S6_HUMAN
resolver
uniprot_entry
Q3SB16_HUMAN
resolver
uniprot_entry
Q5QHG3_HUMAN
resolver
uniprot_entry
Q86UC5_HUMAN
resolver
uniprot_entry
RARB_HUMAN
resolver
uniprot_sec
P12891
resolver
uniprot_sec
Q00989
resolver
uniprot_sec
Q15298
resolver
uniprot_sec
Q9UN48
resolver
amino_acid_sequence
MTTSGHACPVPAVNGHMTHYPATPYPLLFPPVIGGLSLPPLHGLHGHPPPSGCSTPSPATIETQSTSSEELVPSPPSPLPPPRVYKPCFVCQDKSSGYHYGVSACEGCKGFFRRSIQKNMIYTCHRDKNCVINKVTRNRCQYCRLQKCFEVGMSKESVRNDRNKKKKETSKQECTESYEMTAELDDLTEKIRKAHQETFPSLCQLGKYTTNSSADHRVRLDLGLWDKFSELATKCIIKIVEFAKRLPGFTGLTIADQITLLKAACLDILILRICTRYTPEQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFTFANQLLPLEMDDTETGLLSAICLICGDRQDLEEPTKVDKLQEPLLEALKIYIRKRRPSKPHMFPKILMKITDLRSISAKGAERVITLKMEIPGSMPPLIQEMLENSEGHEPLTPSSSGNTAEHSPSISPSSVENSGVSQSPLVQ
uniprot
proteins
disease_involvement
DISEASE: Microphthalmia, syndromic, 12 (MCOPS12) [MIM:615524]: A form of microphthalmia, a disorder of eye formation, ranging from small size of a single eye to complete bilateral absence of ocular tissues (anophthalmia). In many cases, microphthalmia/anophthalmia occurs in association with syndromes that include non-ocular abnormalities. MCOPS12 patients manifest variable features, including diaphragmatic hernia, pulmonary hypoplasia, and cardiac abnormalities. {ECO:0000269|PubMed:24075189, ECO:0000269|PubMed:27120018}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
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 or presence of hormone ligand, acts mainly as an activator of gene expression due to weak binding to corepressors (PubMed:12554770). The RXRA/RARB heterodimer can act as a repressor on the DR1 element and as an activator on the DR5 element (PubMed:29021580). In concert with RARG, required for skeletal growth, matrix homeostasis and growth plate function (By similarity). {ECO:0000250|UniProtKB:P22605, ECO:0000269|PubMed:12554770, ECO:0000269|PubMed:29021580}.
uniprot
proteins
mass_dalton
50489
uniprot
proteins
mutagenesis
MUTAGEN 106; /note="E->A: As a heterodimer with RXRA, abolishes transcriptional repression on DR1, reduces transcriptional activation on DR5 and binding affinity for DR1 and DR5 DNA elements."; /evidence="ECO:0000269|PubMed:29021580"; MUTAGEN 113; /note="R->A: As a heterodimer with RXRA, abolishes transcriptional repression on DR1 and reduces transcriptional activation on DR5."; /evidence="ECO:0000269|PubMed:29021580"; MUTAGEN 120; /note="M->E: As a heterodimer with RXRA, reduces transcriptional repression on DR1 and reduces transcriptional activation on DR5. Reduces binding affinity for DR1 and DR5 DNA elements; when associated with E-366."; /evidence="ECO:0000269|PubMed:29021580"; MUTAGEN 123; /note="T->V: Reduces transcriptional repression on DR1 and reduces transcriptional activation on DR5; when associated with E-369 and E-370."; MUTAGEN 188; /note="T->I: No effect on transcriptional activation in the absence of hormone."; /evidence="ECO:0000269|PubMed:12554770"; MUTAGEN 191; /note="I->V: No effect on transcriptional activation in the absence of hormone."; /evidence="ECO:0000269|PubMed:12554770"; MUTAGEN 222; /note="L->I: Reduced transcriptional activation in the absence of hormone. Even greater reduction in transcriptional activation in the absence of hormone; when associated with D-223 or S-232. Great reduction in transcriptional activation in the absence of hormone; when associated with D-223 and S-232."; /evidence="ECO:0000269|PubMed:12554770"; MUTAGEN 223; /note="G->D: Greatly reduced transcriptional activation in the absence of hormone. Even greater reduction in transcriptional activation in the absence of hormone; when associated with I-222 or S-232. Great reduction in transcriptional activation in the absence of hormone; when associated with I-222 and S-232."; /evidence="ECO:0000269|PubMed:12554770"; MUTAGEN 232; /note="A->S: Reduced transcriptional activation in the absence of hormone. Some further reduction of transcriptional activity in the absence of hormone; when associated with I-222 or D-223. Great reduction in transcriptional activation in the absence of hormone; when associated with I-222 and D-223."; /evidence="ECO:0000269|PubMed:12554770"; MUTAGEN 365; /note="K->E: As a heterodimer with RXRA, reduces transcriptional repression on DR1 and reduces transcriptional activation on DR5. Reduces transcriptional repression on DR1 and reduces transcriptional activation on DR5; when associated with E-366 and E-367."; /evidence="ECO:0000269|PubMed:29021580"; MUTAGEN 366; /note="R->E: As a heterodimer with RXRA, reduces binding affinity for DR5 DNA element and no change in binding to DR1. Reduces transcriptional repression on DR1 and reduces transcriptional activation on DR5; when associated with E-365 and E-367. Reduces binding affinity for DR1 and DR5 DNA elements; when associated with E-120."; /evidence="ECO:0000269|PubMed:29021580"; MUTAGEN 367; /note="R->E: As a heterodimer with RXRA, reduces transcriptional repression on DR1 and reduces transcriptional activation on DR5. Reduces transcriptional repression on DR1 and reduces transcriptional activation on DR5; when associated with E-365 and E-366."; /evidence="ECO:0000269|PubMed:29021580"; MUTAGEN 369; /note="S->E: Reduces transcriptional repression on DR1 and reduces transcriptional activation on DR5; when associated with V-123 and E-370."; MUTAGEN 370; /note="K->E: Reduces transcriptional repression on DR1 and reduced transcriptional activation on DR5; when associated with V-123 and E-369.
uniprot
proteins
protein_family
NR1 subfamily
uniprot
proteins
protein_family
Nuclear hormone receptor family
uniprot
proteins
pubmed
10411930
uniprot
proteins
pubmed
12554770
uniprot
proteins
pubmed
1321662
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1663808
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
2170809
uniprot
proteins
pubmed
24075189
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
27120018
uniprot
proteins
pubmed
28167758
uniprot
proteins
pubmed
2825037
uniprot
proteins
pubmed
2833708
uniprot
proteins
pubmed
2836738
uniprot
proteins
pubmed
29021580
uniprot
proteins
pubmed
3014347
uniprot
proteins
pubmed
8275470
uniprot
proteins
pubmed
8383553
uniprot
proteins
sequence_length
455
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28167758}. Cytoplasm {ECO:0000269|PubMed:28167758}.; SUBCELLULAR LOCATION: [Isoform Beta-1]: Nucleus.; SUBCELLULAR LOCATION: [Isoform Beta-2]: Nucleus.; SUBCELLULAR LOCATION: [Isoform Beta-4]: Cytoplasm.
uniprot
proteins