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P10826

- RARB_HUMAN

UniProt

P10826 - RARB_HUMAN

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Protein

Retinoic acid receptor beta

Gene

RARB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi88 – 15366Nuclear receptorPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri88 – 10821NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri124 – 14825NR C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: ProtInc
  2. drug binding Source: Ensembl
  3. retinoic acid receptor activity Source: ProtInc
  4. RNA polymerase II regulatory region sequence-specific DNA binding Source: Ensembl
  5. steroid hormone receptor activity Source: InterPro
  6. zinc ion binding Source: InterPro

GO - Biological processi

  1. embryonic digestive tract development Source: DFLAT
  2. embryonic eye morphogenesis Source: Ensembl
  3. embryonic hindlimb morphogenesis Source: Ensembl
  4. gene expression Source: Reactome
  5. glandular epithelial cell development Source: Ensembl
  6. growth plate cartilage development Source: Ensembl
  7. multicellular organism growth Source: Ensembl
  8. negative regulation of apoptotic process Source: Ensembl
  9. negative regulation of cartilage development Source: Ensembl
  10. negative regulation of cell proliferation Source: Ensembl
  11. negative regulation of chondrocyte differentiation Source: Ensembl
  12. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  13. outflow tract septum morphogenesis Source: Ensembl
  14. positive regulation of apoptotic process Source: Ensembl
  15. positive regulation of cell proliferation Source: Ensembl
  16. positive regulation of neuron differentiation Source: Ensembl
  17. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  18. regulation of myelination Source: Ensembl
  19. retinal pigment epithelium development Source: Ensembl
  20. signal transduction Source: ProtInc
  21. striatum development Source: Ensembl
  22. transcription initiation from RNA polymerase II promoter Source: Reactome
  23. ureteric bud development Source: Ensembl
  24. ventricular cardiac muscle cell differentiation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_15525. Nuclear Receptor transcription pathway.
SignaLinkiP10826.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:9865. RARB.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleoplasm Source: Reactome
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti394 – 3941R → C in MCOPS12; increases transcriptional response to retinoic acid. 1 Publication
VAR_070780
Natural varianti394 – 3941R → S in MCOPS12; increases transcriptional response to retinoic acid. 1 Publication
VAR_070781

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi188 – 1881T → I: No effect on transcriptional activation in the absence of hormone. 1 Publication
Mutagenesisi191 – 1911I → V: No effect on transcriptional activation in the absence of hormone. 1 Publication
Mutagenesisi222 – 2221L → 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
Mutagenesisi223 – 2231G → 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
Mutagenesisi232 – 2321A → 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

Keywords - Diseasei

Disease mutation, Microphthalmia, Proto-oncogene

Organism-specific databases

MIMi615524. phenotype.
Orphaneti2470. Matthew-Wood syndrome.
PharmGKBiPA34226.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 455455Retinoic acid receptor betaPRO_0000053467Add
BLAST

Proteomic databases

MaxQBiP10826.
PaxDbiP10826.
PRIDEiP10826.

Expressioni

Gene expression databases

BgeeiP10826.
CleanExiHS_RARB.
ExpressionAtlasiP10826. baseline and differential.
GenevestigatoriP10826.

Organism-specific databases

HPAiCAB002617.
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

WithEntry#Exp.IntActNotes
P032552EBI-8583223,EBI-2603114From a different organism.

Protein-protein interaction databases

BioGridi111850. 20 interactions.
IntActiP10826. 9 interactions.
MINTiMINT-1180428.
STRINGi9606.ENSP00000332296.

Structurei

Secondary structure

1
455
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi87 – 915
Beta strandi100 – 1023
Helixi107 – 11812
Beta strandi133 – 1353
Helixi141 – 1488
Helixi149 – 1513
Helixi182 – 19817
Beta strandi202 – 2054
Helixi222 – 24423
Helixi249 – 2513
Helixi254 – 27421
Beta strandi276 – 2783
Turni279 – 2824
Beta strandi283 – 2853
Beta strandi289 – 2935
Helixi294 – 3007
Helixi303 – 3053
Helixi306 – 31611
Helixi317 – 3193
Helixi323 – 33412
Helixi345 – 36622
Beta strandi368 – 3703
Helixi373 – 40129
Beta strandi402 – 4043
Helixi408 – 4147

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HRANMR-A82-160[»]
1XAPX-ray2.10A176-421[»]
4DM6X-ray1.90A/B176-421[»]
4DM8X-ray2.30A/B176-421[»]
4JYGX-ray2.35A/B176-421[»]
4JYHX-ray2.60A/B176-421[»]
4JYIX-ray1.90A/B176-421[»]
ProteinModelPortaliP10826.
SMRiP10826. Positions 82-415.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10826.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 8787ModulatingAdd
BLAST
Regioni154 – 19946HingeAdd
BLAST
Regioni200 – 419220Ligand-bindingAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri88 – 10821NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri124 – 14825NR C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG297448.
GeneTreeiENSGT00760000118837.
HOGENOMiHOG000010312.
HOVERGENiHBG005606.
InParanoidiP10826.
KOiK08528.
OMAiCINIPHC.
PhylomeDBiP10826.
TreeFamiTF328382.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR008946. 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]
PfamiPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR01292. RETNOICACIDR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 1 hit.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform Beta-1 (identifier: P10826-1) [UniParc]FASTAAdd 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]FASTAAdd to Basket

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

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]FASTAAdd to Basket

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

Show »
Length:336
Mass (Da):37,932
Checksum:iD248E5CAB87DA44E
GO

Sequence cautioni

The sequence CAA27637.1 differs from that shown. Reason: Erroneous gene model prediction.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti206 – 2061G → A in CAA68398. (PubMed:2825037)Curated
Sequence conflicti317 – 3171L → Q in CAA30262. (PubMed:2836738)Curated
Sequence conflicti414 – 4141L → M in CAA68398. (PubMed:2825037)Curated
Sequence conflicti454 – 4541V → L in CAA30262. (PubMed:2836738)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti90 – 901V → I in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036060
Natural varianti394 – 3941R → C in MCOPS12; increases transcriptional response to retinoic acid. 1 Publication
VAR_070780
Natural varianti394 – 3941R → S in MCOPS12; increases transcriptional response to retinoic acid. 1 Publication
VAR_070781

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 119119Missing in isoform Beta-4. 1 PublicationVSP_003635Add
BLAST
Alternative sequencei1 – 6060MTTSG…PSPAT → MFDCMDVLSVSPGQILDFYT ASPSSCMLQEKALKACFSGL TQTEWQHRHTAQS in isoform Beta-2. 3 PublicationsVSP_003634Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
CCDSiCCDS2642.1. [P10826-2]
CCDS46775.1. [P10826-3]
PIRiS02827.
S49021.
RefSeqiNP_000956.2. NM_000965.4. [P10826-2]
NP_001277145.1. NM_001290216.1. [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]
UniGeneiHs.654490.
Hs.733004.

Genome annotation databases

EnsembliENST00000330688; ENSP00000332296; ENSG00000077092. [P10826-2]
ENST00000437042; ENSP00000398840; ENSG00000077092. [P10826-3]
ENST00000458646; ENSP00000391391; ENSG00000077092. [P10826-3]
GeneIDi5915.
KEGGihsa:5915.
UCSCiuc003cdi.2. human. [P10826-1]

Polymorphism databases

DMDMi17380507.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_001290216.1. [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.654490.
Hs.733004.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P10826.
SMRi P10826. Positions 82-415.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111850. 20 interactions.
IntActi P10826. 9 interactions.
MINTi MINT-1180428.
STRINGi 9606.ENSP00000332296.

Chemistry

BindingDBi P10826.
ChEMBLi CHEMBL2008.
DrugBanki DB00459. Acitretin.
DB00210. Adapalene.
DB00523. Alitretinoin.
DB04942. Tamibarotene.
DB00799. Tazarotene.
GuidetoPHARMACOLOGYi 591.

Polymorphism databases

DMDMi 17380507.

Proteomic databases

MaxQBi P10826.
PaxDbi P10826.
PRIDEi P10826.

Protocols and materials databases

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 uc003cdi.2. human. [P10826-1 ]

Organism-specific databases

CTDi 5915.
GeneCardsi GC03P025194.
HGNCi HGNC:9865. RARB.
HPAi CAB002617.
HPA004174.
MIMi 180220. gene.
615524. phenotype.
neXtProti NX_P10826.
Orphaneti 2470. Matthew-Wood syndrome.
PharmGKBi PA34226.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG297448.
GeneTreei ENSGT00760000118837.
HOGENOMi HOG000010312.
HOVERGENi HBG005606.
InParanoidi P10826.
KOi K08528.
OMAi CINIPHC.
PhylomeDBi P10826.
TreeFami TF328382.

Enzyme and pathway databases

Reactomei REACT_15525. Nuclear Receptor transcription pathway.
SignaLinki P10826.

Miscellaneous databases

EvolutionaryTracei P10826.
GeneWikii Retinoic_acid_receptor_beta.
GenomeRNAii 5915.
NextBioi 23024.
PROi P10826.
SOURCEi Search...

Gene expression databases

Bgeei P10826.
CleanExi HS_RARB.
ExpressionAtlasi P10826. baseline and differential.
Genevestigatori P10826.

Family and domain databases

Gene3Di 1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProi IPR008946. 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 ]
Pfami PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view ]
PRINTSi PR01292. RETNOICACIDR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTi SM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view ]
SUPFAMi SSF48508. SSF48508. 1 hit.
PROSITEi PS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A new retinoic acid receptor identified from a hepatocellular carcinoma."
    Benbrook D., Lernherdt E., Pfahl M.
    Nature 333:669-672(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-2).
    Tissue: Placenta.
  2. "A novel steroid thyroid hormone receptor-related gene inappropriately expressed in human hepatocellular carcinoma."
    de The H., Marchio A., Tiollais P., Dejean A.
    Nature 330:667-670(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-2).
  3. "Elevated retinoic acid receptor beta(4) protein in human breast tumor cells with nuclear and cytoplasmic localization."
    Sommer K.M., Chen L.I., Treuting P.M., Smith L.T., Swisshelm K.
    Proc. Natl. Acad. Sci. U.S.A. 96:8651-8656(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-4).
    Tissue: Mammary tumor.
  4. "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 BETA-2).
    Tissue: Placenta.
  5. "Mouse and human retinoic acid receptor beta 2 promoters: sequence comparison and localization of retinoic acid responsiveness."
    Shen S., Kruyt F.A., den Hertog J., van der Saag P.T., Kruijer W.
    DNA Seq. 2:111-119(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52 (ISOFORM BETA-2).
  6. "Fetal isoform of human retinoic acid receptor beta expressed in small cell lung cancer lines."
    Houle B., Pelletier M., Wu J., Goodyer C., Bradley W.E.
    Cancer Res. 54:365-369(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72 (ISOFORM BETA-1).
  7. "Hepatitis B virus DNA integration in a sequence homologous to v-erb-A and steroid receptor genes in a hepatocellular carcinoma."
    Dejean A., Bougueleret L., Grzeschik K.-H., Tiollais P.
    Nature 322:70-72(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 61-109.
  8. "Hepatitis B virus as an insertional mutagene in a human hepatocellular carcinoma."
    Dejean A., de The H.
    Mol. Biol. Med. 7:213-222(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 61-109.
    Tissue: Liver.
  9. Cited for: IDENTIFICATION OF LIGAND.
  10. "Retinoic acid receptors beta and gamma do not repress, but instead activate target gene transcription in both the absence and presence of hormone ligand."
    Hauksdottir H., Farboud B., Privalsky M.L.
    Mol. Endocrinol. 17:373-385(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, HETERODIMERIZATION, INTERACTION WITH NCOR2, MUTAGENESIS OF THR-188; ILE-191; LEU-222; GLY-223 AND ALA-232.
  11. "Homo- and heteronuclear NMR studies of the human retinoic acid receptor beta DNA-binding domain: sequential assignments and identification of secondary structure elements."
    Kathira M., Knegtel R.M.A., Boelens R., Eib D., Schilthuis J.G., van der Saag P.T., Kaptein R.
    Biochemistry 31:6474-6480(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 82-160.
  12. "The solution structure of the human retinoic acid receptor-beta DNA-binding domain."
    Knegtel R.M.A., Katahira M., Schilthuis J.G., Bonvin A.M., Boelens R., Eib D., van der Saag P.T., Kaptein R.
    J. Biomol. NMR 3:1-17(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 82-160.
  13. Cited for: VARIANT [LARGE SCALE ANALYSIS] ILE-90.
  14. "Recessive and dominant mutations in retinoic acid receptor beta in cases with microphthalmia and diaphragmatic hernia."
    Srour M., Chitayat D., Caron V., Chassaing N., Bitoun P., Patry L., Cordier M.P., Capo-Chichi J.M., Francannet C., Calvas P., Ragge N., Dobrzeniecka S., Hamdan F.F., Rouleau G.A., Tremblay A., Michaud J.L.
    Am. J. Hum. Genet. 93:765-772(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MCOPS12 SER-394 AND CYS-394, CHARACTERIZATION OF VARIANTS MCOPS12 SER-394 AND CYS-394.

Entry informationi

Entry nameiRARB_HUMAN
AccessioniPrimary (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: October 29, 2014
This is version 183 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3