RARB

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. In concert with RARG, required for skeletal growth, matrix homeostasis and growth plate function.1 Publication

Regions

Feature key	Position(s)	DescriptionActions	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
Traceable author statementⁱ
- 2153268
DNA-binding transcription factor activity, RNA polymerase II-specific Source: NTNU_SB
drug binding Source: Ensembl
nuclear receptor transcription coactivator activity
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
protein-containing complex binding Source: Ensembl
retinoic acid receptor activity
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
retinoid X receptor binding Source: Ensembl
RNA polymerase II regulatory region sequence-specific DNA binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
signaling receptor activity
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
steroid hormone receptor activity Source: InterPro
transcription factor binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
transcription regulatory region sequence-specific DNA binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
zinc ion binding Source: InterPro

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

bone morphogenesis
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
cell differentiation
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
cellular response to retinoic acid
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
embryonic digestive tract development
Source: DFLAT
Inferred from mutant phenotypeⁱ
- 19443732
embryonic eye morphogenesis Source: Ensembl
embryonic hindlimb morphogenesis Source: Ensembl
epithelium development
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
gland development
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
glandular epithelial cell development Source: Ensembl
growth plate cartilage development Source: Ensembl
hormone-mediated signaling pathway
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
liver development
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
multicellular organism development
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
multicellular organism growth Source: Ensembl
negative regulation of apoptotic process Source: Ensembl
negative regulation of cell proliferation Source: Ensembl
negative regulation of chondrocyte differentiation Source: Ensembl
negative regulation of transcription by RNA polymerase II
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
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
Inferred from biological aspect of ancestorⁱ
- 21873635
regulation of myelination Source: Ensembl
response to lipid
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
response to retinoic acid
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
retinoic acid receptor signaling pathway
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
signal transduction
Source: ProtInc
Traceable author statementⁱ
- 2833708
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

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	DNA-binding, Receptor
Biological process	Transcription, Transcription regulation
Ligand	Metal-binding, Zinc

Enzyme and pathway databases

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 beta Short 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	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 3

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000077092.18
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:9865 RARB
MIMⁱ	180220 gene
neXtProtⁱ	NX_P10826

Keywords - Cellular componentⁱ

Cytoplasm, Nucleus

Pathology & 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.

Feature key	Position(s)	DescriptionActions	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	Length
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

Keywords - Diseaseⁱ

Disease mutation, Microphthalmia, Proto-oncogene

Organism-specific databases

DisGeNET More...DisGeNETⁱ	5915
MalaCards human disease database More...MalaCardsⁱ	RARB
MIMⁱ	615524 phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000077092
Orphanetⁱ	2470 Matthew-Wood syndrome
PharmGKBⁱ	PA34226

Chemistry databases

ChEMBLⁱ	CHEMBL2008
Drug and drug target database More...DrugBankⁱ	DB00459 Acitretin DB00210 Adapalene DB00523 Alitretinoin DB00926 Etretinate DB05785 LGD-1550 DB04942 Tamibarotene DB00799 Tazarotene DB02877 TTNPB
IUPHAR/BPS Guide to PHARMACOLOGY More...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

Phosphoprotein

Proteomic databases

PaxDbⁱ	P10826
PeptideAtlas More...PeptideAtlasⁱ	P10826
PRIDEⁱ	P10826
ProteomicsDBⁱ	52654 52655 [P10826-2] 52656 [P10826-3]

PTM databases

iPTMnetⁱ	P10826
PhosphoSitePlusⁱ	P10826

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000077092 Expressed in 153 organ(s), highest expression level in forebrain
CleanExⁱ	HS_RARB
ExpressionAtlasⁱ	P10826 baseline and differential
Genevisibleⁱ	P10826 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB002617 HPA004174

HPAⁱ

CAB002617
HPA004174

Interactionⁱ

Subunit structureⁱ

Homodimer (By similarity). Heterodimer; with a RXR molecule. Binds DNA preferentially as a RAR/RXR heterodimer (By similarity). Interacts weakly with NCOR2.By similarity1 Publication

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
	P03255	2	EBI-8583223,EBI-2603114	From Human adenovirus C serotype 5.
MEOX2	P50222	3	EBI-8583223,EBI-748397
RXRB	P28702	11	EBI-8583223,EBI-748576
RXRB	P28702-3	3	EBI-8583223,EBI-16429492
RXRG	P48443	5	EBI-8583223,EBI-712405

GO - Molecular functionⁱ

retinoid X receptor binding Source: Ensembl
transcription factor binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	111850, 22 interactors
IntActⁱ	P10826, 17 interactors
Molecular INTeraction database More...MINTⁱ	P10826
STRINGⁱ	9606.ENSP00000332296

Chemistry databases

BindingDBⁱ

P10826

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	87 – 91	Combined sources	5
Beta strandⁱ	100 – 102	Combined sources	3
Helixⁱ	107 – 118	Combined sources	12
Beta strandⁱ	133 – 135	Combined sources	3
Helixⁱ	141 – 148	Combined sources	8
Helixⁱ	149 – 151	Combined sources	3
Helixⁱ	182 – 198	Combined sources	17
Beta strandⁱ	202 – 205	Combined sources	4
Helixⁱ	222 – 244	Combined sources	23
Helixⁱ	249 – 251	Combined sources	3
Helixⁱ	254 – 274	Combined sources	21
Beta strandⁱ	276 – 278	Combined sources	3
Turnⁱ	279 – 282	Combined sources	4
Beta strandⁱ	283 – 285	Combined sources	3
Beta strandⁱ	289 – 293	Combined sources	5
Helixⁱ	294 – 300	Combined sources	7
Helixⁱ	303 – 305	Combined sources	3
Helixⁱ	306 – 316	Combined sources	11
Helixⁱ	317 – 319	Combined sources	3
Helixⁱ	323 – 334	Combined sources	12
Helixⁱ	345 – 366	Combined sources	22
Beta strandⁱ	368 – 370	Combined sources	3
Helixⁱ	373 – 401	Combined sources	29
Beta strandⁱ	402 – 404	Combined sources	3
Helixⁱ	408 – 414	Combined sources	7

Show more details

3D structure databases

ProteinModelPortalⁱ	P10826
SMRⁱ	P10826
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P10826

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.

Sequence similaritiesⁱ

Belongs to the nuclear hormone receptor family. NR1 subfamily.Curated

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-finger

Phylogenomic databases

eggNOGⁱ	KOG3575 Eukaryota ENOG410XRZC LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00870000136372
HOGENOMⁱ	HOG000010312
HOVERGENⁱ	HBG005606
InParanoidⁱ	P10826
KEGG Orthology (KO) More...KOⁱ	K08528
OMAⁱ	SVPGFKM
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0XCQ
PhylomeDBⁱ	P10826
TreeFamⁱ	TF328382

Family and domain databases

Gene3Dⁱ	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
Pfam protein domain database More...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

Sequences (4+)ⁱ

Sequence statusⁱ: Complete.

This entry describes 4 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 4 described isoforms and 1 potential isoform that is computationally mapped.Show all Align All

Isoform Beta-1 (identifier: P10826-1) [UniParc]FASTA Add 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

        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

Length:455

Mass (Da):50,489

Last modified:November 16, 2001 - v2

Checksum:ⁱ8813263AD0495D5A

GO

Isoform Beta-2 (identifier: P10826-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-60: MTTSGHACPV...SGCSTPSPAT → MFDCMDVLSV...EWQHRHTAQS

« Hide

        10         20         30         40         50
MFDCMDVLSV SPGQILDFYT ASPSSCMLQE KALKACFSGL TQTEWQHRHT 
        60         70         80         90        100
AQSIETQSTS SEELVPSPPS PLPPPRVYKP CFVCQDKSSG YHYGVSACEG 
       110        120        130        140        150
CKGFFRRSIQ KNMIYTCHRD KNCVINKVTR NRCQYCRLQK CFEVGMSKES 
       160        170        180        190        200
VRNDRNKKKK ETSKQECTES YEMTAELDDL TEKIRKAHQE TFPSLCQLGK 
       210        220        230        240        250
YTTNSSADHR VRLDLGLWDK FSELATKCII KIVEFAKRLP GFTGLTIADQ 
       260        270        280        290        300
ITLLKAACLD ILILRICTRY TPEQDTMTFS DGLTLNRTQM HNAGFGPLTD 
       310        320        330        340        350
LVFTFANQLL PLEMDDTETG LLSAICLICG DRQDLEEPTK VDKLQEPLLE 
       360        370        380        390        400
ALKIYIRKRR PSKPHMFPKI LMKITDLRSI SAKGAERVIT LKMEIPGSMP 
       410        420        430        440 
PLIQEMLENS EGHEPLTPSS SGNTAEHSPS ISPSSVENSG VSQSPLVQ

Show »

Length:448

Mass (Da):50,344

Checksum:ⁱ844A298AD32F46A8

GO

Isoform Beta-3 (identifier: P10826-4)

Sequence is not available

Length:–

Mass (Da):–

Isoform Beta-4 (identifier: P10826-3) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-119: Missing.

« Hide

        10         20         30         40         50
MIYTCHRDKN CVINKVTRNR CQYCRLQKCF EVGMSKESVR NDRNKKKKET 
        60         70         80         90        100
SKQECTESYE MTAELDDLTE KIRKAHQETF PSLCQLGKYT TNSSADHRVR 
       110        120        130        140        150
LDLGLWDKFS ELATKCIIKI VEFAKRLPGF TGLTIADQIT LLKAACLDIL 
       160        170        180        190        200
ILRICTRYTP EQDTMTFSDG LTLNRTQMHN AGFGPLTDLV FTFANQLLPL 
       210        220        230        240        250
EMDDTETGLL SAICLICGDR QDLEEPTKVD KLQEPLLEAL KIYIRKRRPS 
       260        270        280        290        300
KPHMFPKILM KITDLRSISA KGAERVITLK MEIPGSMPPL IQEMLENSEG 
       310        320        330 
HEPLTPSSSG NTAEHSPSIS PSSVENSGVS QSPLVQ

Show »

Length:336

Mass (Da):37,932

Checksum:ⁱD248E5CAB87DA44E

GO

Computationally mapped potential isoform sequencesⁱ

There is 1 potential isoform mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name		Protein names	Gene names	Length	Annotation

	D6RBI3	D6RBI3_HUMAN		Retinoic acid receptor beta 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	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	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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS2642.1 [P10826-2] CCDS46775.1 [P10826-3]
PIRⁱ	S02827 S49021
NCBI Reference Sequences More...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]
UniGeneⁱ	Hs.543218 Hs.581530 Hs.654490 Hs.733004

Genome annotation databases

Ensemblⁱ	ENST00000330688; ENSP00000332296; ENSG00000077092 [P10826-2] ENST00000437042; ENSP00000398840; ENSG00000077092 [P10826-3] ENST00000458646; ENSP00000391391; ENSG00000077092 [P10826-3]
GeneIDⁱ	5915
KEGGⁱ	hsa:5915
UCSC genome browser More...UCSCⁱ	uc003cdh.4 human [P10826-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P10826	Retinoic acid receptor beta (Fragment)		HUMAN		402	UniRef100_P10826
RARB isoform 1 (Fragment)		PANTR		402
P10826-2	Retinoic acid receptor beta variant 1		HUMAN		448	UniRef100_F1D8S6
RARB isoform 3		PANTR		448
Uncharacterized protein		MACMU		448
Uncharacterized protein		COLAP		448
RARB isoform 2		PONAB		448
+10
P10826-3	Retinoic acid receptor beta 5		HUMAN		336	UniRef100_Q5QHG3
RARB isoform 2		PANTR		336
RARB isoform 1		PONAB		336
Retinoic acid receptor beta isoform 2		MACMU		336
Uncharacterized protein		COLAP		336
+5

Protein	Similar proteins		Species	Score	Length	Source
P10826	Isoform Beta-1 of Retinoic acid receptor beta		MOUSE		455	UniRef90_P22605-2
Retinoic acid receptor beta		CHICK		455
Retinoic acid receptor beta		COTJA		455
retinoic acid receptor beta isoform X1		LIPVE		458
retinoic acid receptor beta isoform X1		MESAU		455
+124
P10826-2	Retinoic acid receptor, beta		RAT		448	UniRef90_D3ZFD9
Retinoic acid receptor beta		PONAB		526
Beta-retinoic acid receptor (Fragment)		Mus sp.		28
Retinoic acid receptor beta isoform 1 (Fragment)		MACMU		22
Retinoic acid receptor beta		HORSE		523
+161
P10826-3	Retinoic acid receptor beta	)	MOUSE		482	UniRef90_P22605
Retinoic acid receptor beta		Bengalese finch		483
retinoic acid receptor beta isoform X1		ODORO		482
retinoic acid receptor beta isoform X1		ERIEU		482
retinoic acid receptor beta isoform X1		NEOSC		482
+112

Protein	Similar proteins		Species	Score	Length	Source
P10826	Isoform Alpha-2 of Retinoic acid receptor alpha		MOUSE		459	UniRef50_P11416-2
Retinoic acid receptor alpha		CHICK		460
Retinoic acid receptor beta		COTJA		455
Retinoic acid receptor gamma		XENLA		476
Retinoic acid receptor gamma		NOTVI		505
+599
P10826-2	Retinoic acid receptor alpha		MOUSE		462	UniRef50_P11416
Retinoic acid receptor alpha		CANLF		462
Retinoic acid receptor alpha-A		DANRE		444
Retinoic acid receptor gamma	)	HUMAN		454
retinoic acid receptor alpha		URSMA		527
+618

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]
UniGeneⁱ	Hs.543218 Hs.581530 Hs.654490 Hs.733004

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...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	[»]
ProteinModelPortalⁱ	P10826
SMRⁱ	P10826
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	111850, 22 interactors
IntActⁱ	P10826, 17 interactors
MINTⁱ	P10826
STRINGⁱ	9606.ENSP00000332296

Chemistry databases

BindingDBⁱ	P10826
ChEMBLⁱ	CHEMBL2008
DrugBankⁱ	DB00459 Acitretin DB00210 Adapalene DB00523 Alitretinoin DB00926 Etretinate DB05785 LGD-1550 DB04942 Tamibarotene DB00799 Tazarotene DB02877 TTNPB
GuidetoPHARMACOLOGYⁱ	591

PTM databases

iPTMnetⁱ	P10826
PhosphoSitePlusⁱ	P10826

Polymorphism and mutation databases

BioMutaⁱ	RARB
DMDMⁱ	17380507

Proteomic databases

PaxDbⁱ	P10826
PeptideAtlasⁱ	P10826
PRIDEⁱ	P10826
ProteomicsDBⁱ	52654 52655 [P10826-2] 52656 [P10826-3]

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	5915
Structural Biology Knowledgebase	Search...

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
HGNCⁱ	HGNC:9865 RARB
HPAⁱ	CAB002617 HPA004174
MalaCardsⁱ	RARB
MIMⁱ	180220 gene 615524 phenotype
neXtProtⁱ	NX_P10826
OpenTargetsⁱ	ENSG00000077092
Orphanetⁱ	2470 Matthew-Wood syndrome
PharmGKBⁱ	PA34226
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG3575 Eukaryota ENOG410XRZC LUCA
GeneTreeⁱ	ENSGT00870000136372
HOGENOMⁱ	HOG000010312
HOVERGENⁱ	HBG005606
InParanoidⁱ	P10826
KOⁱ	K08528
OMAⁱ	SVPGFKM
OrthoDBⁱ	EOG091G0XCQ
PhylomeDBⁱ	P10826
TreeFamⁱ	TF328382

Enzyme and pathway databases

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

ChiTaRSⁱ	RARB human
EvolutionaryTraceⁱ	P10826
GeneWikiⁱ	Retinoic_acid_receptor_beta
GenomeRNAiⁱ	5915
Protein Ontology More...PROⁱ	PR:P10826
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000077092 Expressed in 153 organ(s), highest expression level in forebrain
CleanExⁱ	HS_RARB
ExpressionAtlasⁱ	P10826 baseline and differential
Genevisibleⁱ	P10826 HS

Family and domain databases

Gene3Dⁱ	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
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	RARB_HUMAN
Accessionⁱ	P10826Primary (citable) accession number: P10826 Secondary accession number(s): P12891 , Q00989, Q15298, Q9UN48
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
	Last sequence update:	November 16, 2001
	Last modified:	November 7, 2018
	This is version 225 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, Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
Human chromosome 3
Human chromosome 3: entries, gene names and cross-references to MIM
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
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

UniProtKB

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UniProtKB - P10826 (RARB_HUMAN)

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Retinoic acid receptor beta

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Regions

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GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

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Nucleus

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Keywords - Cellular componenti

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Keywords - Diseasei

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

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<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Zinc finger

Keywords - Domaini

Phylogenomic databases

Family and domain databases

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ