UniProtKB - P10826 (RARB_HUMAN)
Protein
Retinoic acid receptor beta
Gene
RARB
Organism
Homo sapiens (Human)
Status
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 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).By similarity2 Publications
Regions
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
- DNA binding Source: ProtInc
- DNA-binding transcription factor activity, RNA polymerase II-specific Source: NTNU_SB
- drug binding Source: Ensembl
- nuclear receptor activity Source: GO_Central
- protein-containing complex binding Source: Ensembl
- retinoid X receptor binding Source: Ensembl
- RNA polymerase II cis-regulatory region sequence-specific DNA binding Source: GO_Central
- sequence-specific double-stranded DNA binding Source: ARUK-UCL
- zinc ion binding Source: InterPro
GO - Biological processi
- cell differentiation Source: GO_Central
- embryonic digestive tract development Source: DFLAT
- embryonic eye morphogenesis Source: Ensembl
- embryonic hindlimb morphogenesis Source: Ensembl
- glandular epithelial cell development Source: Ensembl
- growth plate cartilage development Source: Ensembl
- hormone-mediated signaling pathway Source: GO_Central
- multicellular organism growth Source: Ensembl
- negative regulation of apoptotic process Source: Ensembl
- negative regulation of cell population proliferation Source: Ensembl
- negative regulation of chondrocyte differentiation Source: Ensembl
- negative regulation of transcription by RNA polymerase II Source: GO_Central
- outflow tract septum morphogenesis Source: Ensembl
- positive regulation of apoptotic process Source: Ensembl
- positive regulation of neuron differentiation Source: Ensembl
- positive regulation of transcription by RNA polymerase II Source: GO_Central
- regulation of myelination Source: Ensembl
- retinoic acid receptor signaling pathway Source: GO_Central
- signal transduction Source: ProtInc
- striatum development Source: Ensembl
- transcription initiation from RNA polymerase II promoter Source: Reactome
- ureteric bud development Source: Ensembl
- ventricular cardiac muscle cell differentiation Source: Ensembl
Keywordsi
Molecular function | DNA-binding, Receptor |
Biological process | Transcription, Transcription regulation |
Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
PathwayCommonsi | P10826 |
Reactomei | R-HSA-383280, Nuclear Receptor transcription pathway R-HSA-5362517, Signaling by Retinoic Acid R-HSA-5617472, Activation of anterior HOX genes in hindbrain development during early embryogenesis |
SignaLinki | P10826 |
SIGNORi | P10826 |
Names & Taxonomyi
Protein namesi | Recommended name: Retinoic acid receptor betaShort name: RAR-beta Alternative name(s): HBV-activated protein Nuclear receptor subfamily 1 group B member 2 RAR-epsilon |
Gene namesi | Name:RARB Synonyms:HAP, NR1B2 |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
EuPathDBi | HostDB:ENSG00000077092.18 |
HGNCi | HGNC:9865, RARB |
MIMi | 180220, gene |
neXtProti | NX_P10826 |
Subcellular locationi
Nucleus
Nucleus
Other locations
Nucleus
- nuclear chromatin Source: NTNU_SB
- nucleoplasm Source: HPA
- nucleus Source: UniProtKB
Other locations
- cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
Cytoplasm, NucleusPathology & Biotechi
Involvement in diseasei
Microphthalmia, syndromic, 12 (MCOPS12)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
Related information in OMIMFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_077141 | 220 | L → P in MCOPS12; increased transcriptional response to retinoic acid ligands. 1 Publication | 1 | |
Natural variantiVAR_077142 | 303 | G → A in MCOPS12; increased transcriptional response to retinoic acid ligands. 1 Publication | 1 | |
Natural variantiVAR_070780 | 394 | R → C in MCOPS12; increased transcriptional response to retinoic acid ligands. 2 Publications | 1 | |
Natural variantiVAR_070781 | 394 | R → S in MCOPS12; increases transcriptional response to retinoic acid. 1 Publication | 1 |
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 106 | 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. 1 Publication | 1 | |
Mutagenesisi | 113 | R → A: As a heterodimer with RXRA, abolishes transcriptional repression on DR1 and reduces transcriptional activation on DR5. 1 Publication | 1 | |
Mutagenesisi | 120 | 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. 1 Publication | 1 | |
Mutagenesisi | 123 | T → V: Reduces transcriptional repression on DR1 and reduces transcriptional activation on DR5; when associated with E-369 and E-370. | 1 | |
Mutagenesisi | 188 | T → I: No effect on transcriptional activation in the absence of hormone. 1 Publication | 1 | |
Mutagenesisi | 191 | I → V: No effect on transcriptional activation in the absence of hormone. 1 Publication | 1 | |
Mutagenesisi | 222 | 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. 1 Publication | 1 | |
Mutagenesisi | 223 | 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. 1 Publication | 1 | |
Mutagenesisi | 232 | 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. 1 Publication | 1 | |
Mutagenesisi | 365 | 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. 1 Publication | 1 | |
Mutagenesisi | 366 | 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. 1 Publication | 1 | |
Mutagenesisi | 367 | 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. 1 Publication | 1 | |
Mutagenesisi | 369 | S → E: Reduces transcriptional repression on DR1 and reduces transcriptional activation on DR5; when associated with V-123 and E-370. | 1 | |
Mutagenesisi | 370 | K → E: Reduces transcriptional repression on DR1 and reduced transcriptional activation on DR5; when associated with V-123 and E-369. | 1 |
Keywords - Diseasei
Disease mutation, Microphthalmia, Proto-oncogeneOrganism-specific databases
DisGeNETi | 5915 |
GeneReviewsi | RARB |
MalaCardsi | RARB |
MIMi | 615524, phenotype |
OpenTargetsi | ENSG00000077092 |
Orphaneti | 2470, Matthew-Wood syndrome |
PharmGKBi | PA34226 |
Miscellaneous databases
Pharosi | P10826, Tclin |
Chemistry databases
ChEMBLi | CHEMBL2008 |
DrugBanki | DB00459, Acitretin DB00210, Adapalene DB00523, Alitretinoin DB02877, Arotinoid acid DB00926, Etretinate DB05785, LGD-1550 DB04942, Tamibarotene DB00799, Tazarotene DB00755, Tretinoin DB12808, Trifarotene |
DrugCentrali | P10826 |
GuidetoPHARMACOLOGYi | 591 |
Polymorphism and mutation databases
BioMutai | RARB |
DMDMi | 17380507 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000053467 | 1 – 455 | Retinoic acid receptor betaAdd BLAST | 455 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 77 | PhosphoserineCombined sources | 1 |
Keywords - PTMi
PhosphoproteinProteomic databases
jPOSTi | P10826 |
MassIVEi | P10826 |
PaxDbi | P10826 |
PeptideAtlasi | P10826 |
PRIDEi | P10826 |
ProteomicsDBi | 52654 [P10826-1] 52655 [P10826-2] 52656 [P10826-3] |
PTM databases
GlyGeni | P10826, 1 site, 1 O-linked glycan (1 site) |
iPTMneti | P10826 |
PhosphoSitePlusi | P10826 |
Expressioni
Tissue specificityi
Expressed in aortic endothelial cells (at protein level).1 Publication
Gene expression databases
Bgeei | ENSG00000077092, Expressed in forebrain and 170 other tissues |
ExpressionAtlasi | P10826, baseline and differential |
Genevisiblei | P10826, HS |
Organism-specific databases
HPAi | ENSG00000077092, Tissue enhanced (retina) |
Interactioni
Subunit structurei
Binary interactionsi
Hide detailsIsoform Beta-2 [P10826-2]
GO - Molecular functioni
- retinoid X receptor binding Source: Ensembl
Protein-protein interaction databases
BioGRIDi | 111850, 25 interactors |
IntActi | P10826, 20 interactors |
MINTi | P10826 |
STRINGi | 9606.ENSP00000332296 |
Chemistry databases
BindingDBi | P10826 |
Miscellaneous databases
RNActi | P10826, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P10826 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P10826 |
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 | 154 – 182 | HingeAdd BLAST | 29 |
Domaini
Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.
The DNA-binding nuclear receptor domain and the NR LBD domain are required for binding of the RARB/RXRA heterodimer to both DR1 and DR5 DNA elements.1 Publication
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 | ENSGT00940000156196 |
HOGENOMi | CLU_007368_18_0_1 |
InParanoidi | P10826 |
OMAi | FTENYEM |
OrthoDBi | 1165737at2759 |
PhylomeDBi | P10826 |
TreeFami | TF328382 |
Family and domain databases
Gene3Di | 1.10.565.10, 1 hit 3.30.50.10, 1 hit |
IDEALi | IID00439 |
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 (4+)i Sequence
Sequence statusi: Complete.
This entry describes 4 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 4 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All
Isoform Beta-1 (identifier: P10826-1) [UniParc]FASTAAdd to basket
This 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
MTTSGHACPV PAVNGHMTHY PATPYPLLFP PVIGGLSLPP LHGLHGHPPP
60 70 80 90 100
SGCSTPSPAT IETQSTSSEE LVPSPPSPLP PPRVYKPCFV CQDKSSGYHY
110 120 130 140 150
GVSACEGCKG FFRRSIQKNM IYTCHRDKNC VINKVTRNRC QYCRLQKCFE
160 170 180 190 200
VGMSKESVRN DRNKKKKETS KQECTESYEM TAELDDLTEK IRKAHQETFP
210 220 230 240 250
SLCQLGKYTT NSSADHRVRL DLGLWDKFSE LATKCIIKIV EFAKRLPGFT
260 270 280 290 300
GLTIADQITL LKAACLDILI LRICTRYTPE QDTMTFSDGL TLNRTQMHNA
310 320 330 340 350
GFGPLTDLVF TFANQLLPLE MDDTETGLLS AICLICGDRQ DLEEPTKVDK
360 370 380 390 400
LQEPLLEALK IYIRKRRPSK PHMFPKILMK ITDLRSISAK GAERVITLKM
410 420 430 440 450
EIPGSMPPLI QEMLENSEGH EPLTPSSSGN TAEHSPSISP SSVENSGVSQ
SPLVQ
Isoform Beta-2 (identifier: P10826-2) [UniParc]FASTAAdd to basket
The sequence of this isoform differs from the canonical sequence as follows:
1-60: MTTSGHACPV...SGCSTPSPAT → MFDCMDVLSV...EWQHRHTAQS
Isoform Beta-3 (identifier: P10826-4)
Sequence is not available
Length:–
Mass (Da):–
Isoform Beta-4 (identifier: P10826-3) [UniParc]FASTAAdd to basket
The sequence of this isoform differs from the canonical sequence as follows:
1-119: Missing.
Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basketD6RBI3 | D6RBI3_HUMAN | Retinoic acid receptor beta | RARB | 402 | Annotation score: |
Sequence cautioni
The sequence CAA27637 differs from that shown. Reason: Erroneous gene model prediction.Curated
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 206 | G → A in CAA68398 (PubMed:2825037).Curated | 1 | |
Sequence conflicti | 317 | L → Q in CAA30262 (PubMed:2836738).Curated | 1 | |
Sequence conflicti | 414 | L → M in CAA68398 (PubMed:2825037).Curated | 1 | |
Sequence conflicti | 454 | V → L in CAA30262 (PubMed:2836738).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_036060 | 90 | V → I in a colorectal cancer sample; somatic mutation. 1 Publication | 1 | |
Natural variantiVAR_077141 | 220 | L → P in MCOPS12; increased transcriptional response to retinoic acid ligands. 1 Publication | 1 | |
Natural variantiVAR_077142 | 303 | G → A in MCOPS12; increased transcriptional response to retinoic acid ligands. 1 Publication | 1 | |
Natural variantiVAR_070780 | 394 | R → C in MCOPS12; increased transcriptional response to retinoic acid ligands. 2 Publications | 1 | |
Natural variantiVAR_070781 | 394 | R → S in MCOPS12; increases transcriptional response to retinoic acid. 1 Publication | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_003635 | 1 – 119 | Missing in isoform Beta-4. 1 PublicationAdd BLAST | 119 | |
Alternative sequenceiVSP_003634 | 1 – 60 | MTTSG…PSPAT → MFDCMDVLSVSPGQILDFYT ASPSSCMLQEKALKACFSGL TQTEWQHRHTAQS in isoform Beta-2. 3 PublicationsAdd BLAST | 60 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X07282 mRNA Translation: CAA30262.1 Y00291 mRNA Translation: CAA68398.1 AF157483 mRNA Translation: AAD45688.1 BC060794 mRNA Translation: AAH60794.1 X56849 Genomic DNA No translation available. X77664 Genomic DNA Translation: CAA54740.1 X04014 Genomic DNA Translation: CAA27637.1 Sequence problems. M57445 Genomic DNA Translation: AAA58728.1 |
CCDSi | CCDS2642.1 [P10826-2] CCDS46775.1 [P10826-3] |
PIRi | S02827 S49021 |
RefSeqi | NP_000956.2, NM_000965.4 [P10826-2] NP_001277145.1, NM_001290216.2 [P10826-1] NP_001277146.1, NM_001290217.1 [P10826-3] NP_001277195.1, NM_001290266.1 NP_001277205.1, NM_001290276.1 [P10826-3] NP_057236.1, NM_016152.3 [P10826-3] |
Genome annotation databases
Ensembli | ENST00000330688; ENSP00000332296; ENSG00000077092 [P10826-2] ENST00000437042; ENSP00000398840; ENSG00000077092 [P10826-3] ENST00000458646; ENSP00000391391; ENSG00000077092 [P10826-3] |
GeneIDi | 5915 |
KEGGi | hsa:5915 |
UCSCi | uc003cdh.4, human [P10826-1] |
Keywords - Coding sequence diversityi
Alternative splicing, PolymorphismSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X07282 mRNA Translation: CAA30262.1 Y00291 mRNA Translation: CAA68398.1 AF157483 mRNA Translation: AAD45688.1 BC060794 mRNA Translation: AAH60794.1 X56849 Genomic DNA No translation available. X77664 Genomic DNA Translation: CAA54740.1 X04014 Genomic DNA Translation: CAA27637.1 Sequence problems. M57445 Genomic DNA Translation: AAA58728.1 |
CCDSi | CCDS2642.1 [P10826-2] CCDS46775.1 [P10826-3] |
PIRi | S02827 S49021 |
RefSeqi | NP_000956.2, NM_000965.4 [P10826-2] NP_001277145.1, NM_001290216.2 [P10826-1] NP_001277146.1, NM_001290217.1 [P10826-3] NP_001277195.1, NM_001290266.1 NP_001277205.1, NM_001290276.1 [P10826-3] NP_057236.1, NM_016152.3 [P10826-3] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1HRA | NMR | - | A | 82-160 | [»] | |
1XAP | X-ray | 2.10 | A | 176-421 | [»] | |
4DM6 | X-ray | 1.90 | A/B | 176-421 | [»] | |
4DM8 | X-ray | 2.30 | A/B | 176-421 | [»] | |
4JYG | X-ray | 2.35 | A/B | 176-421 | [»] | |
4JYH | X-ray | 2.60 | A/B | 176-421 | [»] | |
4JYI | X-ray | 1.90 | A/B | 176-421 | [»] | |
5UAN | X-ray | 3.51 | B | 80-455 | [»] | |
6SSQ | X-ray | 2.30 | A/B | 176-421 | [»] | |
SMRi | P10826 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 111850, 25 interactors |
IntActi | P10826, 20 interactors |
MINTi | P10826 |
STRINGi | 9606.ENSP00000332296 |
Chemistry databases
BindingDBi | P10826 |
ChEMBLi | CHEMBL2008 |
DrugBanki | DB00459, Acitretin DB00210, Adapalene DB00523, Alitretinoin DB02877, Arotinoid acid DB00926, Etretinate DB05785, LGD-1550 DB04942, Tamibarotene DB00799, Tazarotene DB00755, Tretinoin DB12808, Trifarotene |
DrugCentrali | P10826 |
GuidetoPHARMACOLOGYi | 591 |
PTM databases
GlyGeni | P10826, 1 site, 1 O-linked glycan (1 site) |
iPTMneti | P10826 |
PhosphoSitePlusi | P10826 |
Polymorphism and mutation databases
BioMutai | RARB |
DMDMi | 17380507 |
Proteomic databases
jPOSTi | P10826 |
MassIVEi | P10826 |
PaxDbi | P10826 |
PeptideAtlasi | P10826 |
PRIDEi | P10826 |
ProteomicsDBi | 52654 [P10826-1] 52655 [P10826-2] 52656 [P10826-3] |
Protocols and materials databases
Antibodypediai | 934, 504 antibodies |
DNASUi | 5915 |
Genome annotation databases
Ensembli | ENST00000330688; ENSP00000332296; ENSG00000077092 [P10826-2] ENST00000437042; ENSP00000398840; ENSG00000077092 [P10826-3] ENST00000458646; ENSP00000391391; ENSG00000077092 [P10826-3] |
GeneIDi | 5915 |
KEGGi | hsa:5915 |
UCSCi | uc003cdh.4, human [P10826-1] |
Organism-specific databases
CTDi | 5915 |
DisGeNETi | 5915 |
EuPathDBi | HostDB:ENSG00000077092.18 |
GeneCardsi | RARB |
GeneReviewsi | RARB |
HGNCi | HGNC:9865, RARB |
HPAi | ENSG00000077092, Tissue enhanced (retina) |
MalaCardsi | RARB |
MIMi | 180220, gene 615524, phenotype |
neXtProti | NX_P10826 |
OpenTargetsi | ENSG00000077092 |
Orphaneti | 2470, Matthew-Wood syndrome |
PharmGKBi | PA34226 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG3575, Eukaryota |
GeneTreei | ENSGT00940000156196 |
HOGENOMi | CLU_007368_18_0_1 |
InParanoidi | P10826 |
OMAi | FTENYEM |
OrthoDBi | 1165737at2759 |
PhylomeDBi | P10826 |
TreeFami | TF328382 |
Enzyme and pathway databases
PathwayCommonsi | P10826 |
Reactomei | R-HSA-383280, Nuclear Receptor transcription pathway R-HSA-5362517, Signaling by Retinoic Acid R-HSA-5617472, Activation of anterior HOX genes in hindbrain development during early embryogenesis |
SignaLinki | P10826 |
SIGNORi | P10826 |
Miscellaneous databases
BioGRID-ORCSi | 5915, 7 hits in 871 CRISPR screens |
ChiTaRSi | RARB, human |
EvolutionaryTracei | P10826 |
GeneWikii | Retinoic_acid_receptor_beta |
GenomeRNAii | 5915 |
Pharosi | P10826, Tclin |
PROi | PR:P10826 |
RNActi | P10826, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000077092, Expressed in forebrain and 170 other tissues |
ExpressionAtlasi | P10826, baseline and differential |
Genevisiblei | P10826, HS |
Family and domain databases
Gene3Di | 1.10.565.10, 1 hit 3.30.50.10, 1 hit |
IDEALi | IID00439 |
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 |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | RARB_HUMAN | |
Accessioni | P10826Primary (citable) accession number: P10826 Secondary accession number(s): P12891 Q9UN48 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1989 |
Last sequence update: | November 16, 2001 | |
Last modified: | December 2, 2020 | |
This is version 240 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- Human chromosome 3
Human chromosome 3: entries, gene names and cross-references to MIM - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations