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Protein

Retinoic acid receptor alpha

Gene

RARA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone acetylation, chromatin condensation and transcriptional suppression. On ligand binding, the corepressors dissociate from the receptors and associate with the coactivators leading to transcriptional activation. RARA plays an essential role in the regulation of retinoic acid-induced germ cell development during spermatogenesis. Has a role in the survival of early spermatocytes at the beginning prophase of meiosis. In Sertoli cells, may promote the survival and development of early meiotic prophase spermatocytes. In concert with RARG, required for skeletal growth, matrix homeostasis and growth plate function (By similarity). Regulates expression of target genes in a ligand-dependent manner by recruiting chromatin complexes containing KMT2E/MLL5. Mediates retinoic acid-induced granulopoiesis.By similarity4 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi88 – 153Nuclear receptorPROSITE-ProRule annotationAdd BLAST66
Zinc fingeri88 – 108NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri124 – 148NR C4-typePROSITE-ProRule annotationAdd BLAST25

GO - Molecular functioni

  • alpha-actinin binding Source: UniProtKB
  • chromatin DNA binding Source: UniProtKB
  • drug binding Source: Ensembl
  • enzyme binding Source: UniProtKB
  • mRNA 5'-UTR binding Source: Ensembl
  • protein domain specific binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein kinase A binding Source: UniProtKB
  • protein kinase B binding Source: UniProtKB
  • receptor binding Source: UniProtKB
  • retinoic acid binding Source: BHF-UCL
  • retinoic acid receptor activity Source: BHF-UCL
  • retinoic acid-responsive element binding Source: UniProtKB
  • RNA polymerase II regulatory region sequence-specific DNA binding Source: Ensembl
  • steroid hormone receptor activity Source: InterPro
  • transcription coactivator activity Source: UniProtKB
  • transcription corepressor activity Source: UniProtKB
  • transcription factor activity, sequence-specific DNA binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB
  • translation repressor activity, nucleic acid binding Source: Ensembl
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000131759-MONOMER.
ReactomeiR-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.
SignaLinkiP10276.
SIGNORiP10276.

Names & Taxonomyi

Protein namesi
Recommended name:
Retinoic acid receptor alpha
Short name:
RAR-alpha
Alternative name(s):
Nuclear receptor subfamily 1 group B member 1
Gene namesi
Name:RARA
Synonyms:NR1B1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:9864. RARA.

Subcellular locationi

  • Nucleus
  • Cytoplasm

  • Note: Nuclear localization depends on ligand binding, phosphorylation and sumoylation. Transloaction to the nucleus in the absence of ligand is dependent on activation of PKC and the downstream MAPK phosphorylation.

GO - Cellular componenti

  • actin cytoskeleton Source: HPA
  • cell surface Source: BHF-UCL
  • cytoplasm Source: UniProtKB
  • dendrite Source: Ensembl
  • neuronal cell body Source: Ensembl
  • nuclear chromatin Source: BHF-UCL
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Chromosomal aberrations involving RARA are commonly found in acute promyelocytic leukemia. Translocation t(11;17)(q32;q21) with ZBTB16/PLZF; translocation t(15;17)(q21;q21) with PML; translocation t(5;17)(q32;q11) with NPM. The PML-RARA oncoprotein requires both the PML ring structure and coiled-coil domain for both interaction with UBE2I, nuclear microspeckle location and sumoylation. In addition, the coiled-coil domain functions in blocking RA-mediated transactivation and cell differentiation.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi95S → A: No effect on PKB/AKT1-mediated phosphorylation. Repressed transactivation. 1 Publication1
Mutagenesisi96S → A: Abolishes PKB/AKT1-mediated phosphorylation. Repressed transactivation. 1 Publication1
Mutagenesisi147K → R: Abrogates sumoylation in the presence or absence of ATRA and primarily nuclear localization and enhanced ATRA-mediated transcriptional activity; when associated with R-166; R-171 and R-399. 1 Publication1
Mutagenesisi154S → A: No effect on PKB/AKT1-mediated phosphorylation. No repression of transactivation. 1 Publication1
Mutagenesisi157S → A: No effect on PKB/AKT1-mediated phosphorylation. Repressed transactivation. 1 Publication1
Mutagenesisi166K → R: Cytoplasmic in the absence of ATRA and reduced transcriptional activity in the presence of ATRA. Low sumoylation levels in the presence of ATRA; when associated with R-399. Nuclear localization and enhanced transcriptional activity; when associated with R-171 and R-399. Primarily nuclear localization and enhanced ATRA-mediated transcriptional activity; when associated with R-147; R-171 and R-399. 1 Publication1
Mutagenesisi171K → R: Cytoplasmic in the absence of ATRA and reduced transcriptional activity in the presence of ATRA. Low sumoylation levels in the presence of ATRA; when associated with R-399. Nuclear localization and enhanced transcriptional activity; when associated with R-166 and R-399. Primarily nuclear localization and enhanced ATRA-mediated transcriptional activity; when associated with R-147; R-166 and R-399. 1 Publication1
Mutagenesisi219S → A: No effect on heterodimerization with RARA. On ATRA treatment, localizes to the nucleus, and increased protein levels; when associated with A-369. 1 Publication1
Mutagenesisi219S → E: No effect on heterodimerization with RARA. On ATRA treatment, localizes to both nucleus and cytoplasm, no increase in protein levels, and decrease in RARA-mediated transcriptional activity; when associated with E-369. 1 Publication1
Mutagenesisi369S → A: No effect on heterodimerization with RARA. On ATRA treatment, localizes to the nucleus, and increased protein levels; when associated with A-219. 1 Publication1
Mutagenesisi369S → E: Some inhibition of heterodimerization with RARA. On ATRA treatment, localizes to both nucleus and cytoplasm, increase in protein levels, and decrease in RARA-mediated transcriptional activity; when associated with E-219. 1 Publication1
Mutagenesisi396I → E: Abrogates interaction with NCOR1 or NCOR2. Increased affinity for NCOR1 and NCOR2 in the presence of BMS493. Increased transcriptional activity in the presence of agonist and decreased activity in the presence of neutral antagonist. 1 Publication1
Mutagenesisi399K → R in the absence of ATRA, abolishes sumoylation and is mainly nuclear. In the presence of ATRA, some sumoylation, cytoplasmic location, reduced transcriptional activity and no SENP6 binding. Low sumoylation levels in the presence of ATRA and nuclear location in the absence of ATRA; when associated with R-166 or with R-171. Primarily nuclear localization and enhanced ATRA-mediated transcriptional activity; when associated with R-147; R-166 and R-171. 1 Publication1
Mutagenesisi409 – 410LI → AA: Abolishes interaction with ASXL1 and NCOA1. 1 Publication2
Mutagenesisi412E → Q: Impairs interaction with ASXL1 and NCOA1; when associated with Q-415. 1 Publication1
Mutagenesisi413 – 414ML → AA: Abolishes interaction with ASXL1 and NCOA1. 1 Publication2
Mutagenesisi415E → Q: Impairs interaction with ASXL1 and NCOA1; when associated with Q-412. 1 Publication1

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei60 – 61Breakpoint for translocation to form PLZF-RAR-alpha, RAR-alpha1-PLZF and PML-RAR-alpha oncogenes2

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNETi5914.
MalaCardsiRARA.
MIMi612376. phenotype.
OpenTargetsiENSG00000131759.
Orphaneti520. Acute promyelocytic leukemia.
PharmGKBiPA34225.

Chemistry databases

ChEMBLiCHEMBL2055.
DrugBankiDB00459. Acitretin.
DB00210. Adapalene.
DB00523. Alitretinoin.
DB00982. Isotretinoin.
DB04942. Tamibarotene.
DB00799. Tazarotene.
GuidetoPHARMACOLOGYi590.

Polymorphism and mutation databases

BioMutaiRARA.
DMDMi133483.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000534611 – 462Retinoic acid receptor alphaAdd BLAST462

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei77Phosphoserine; by CDK7By similarity1
Modified residuei96Phosphoserine; by PKB/AKT11 Publication1
Cross-linki166Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Cross-linki171Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei219Phosphoserine; by PKA1 Publication1
Modified residuei369Phosphoserine; by PKA1 Publication1
Cross-linki399Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication

Post-translational modificationi

Phosphorylated on serine and threonine residues. Phosphorylation does not change during cell cycle. Phosphorylation on Ser-77 is crucial for transcriptional activity (By similarity). Phosphorylation by AKT1 is required for the repressor activity but has no effect on DNA binding, protein stability nor subcellular localization. Phosphorylated by PKA in vitro. This phosphorylation on Ser-219 and Ser-369 is critical for ligand binding, nuclear localization and transcriptional activity in response to FSH signaling.By similarity2 Publications
Sumoylated with SUMO2, mainly on Lys-399 which is also required for SENP6 binding. On all-trans retinoic acid (ATRA) binding, a confromational change may occur that allows sumoylation on two additional site, Lys-166 and Lys-171. Probably desumoylated by SENP6. Sumoylation levels determine nuclear localization and regulate ATRA-mediated transcriptional activity.2 Publications
Trimethylation enhances heterodimerization with RXRA and positively modulates the transcriptional activation.
Ubiquitinated.

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP10276.
PeptideAtlasiP10276.
PRIDEiP10276.

PTM databases

iPTMnetiP10276.
PhosphoSitePlusiP10276.

Expressioni

Gene expression databases

BgeeiENSG00000131759.
CleanExiHS_RARA.
ExpressionAtlasiP10276. baseline and differential.
GenevisibleiP10276. HS.

Organism-specific databases

HPAiHPA058282.

Interactioni

Subunit structurei

Heterodimer; with RXRA. Binds DNA preferentially as a heterodimer. Interacts with CDK7 (By similarity). Interacts with coactivators NCOA3 and NCOA6. Interacts with NCOA7; the interaction requires ligand-binding. Interacts with KMT2E/MLL5. Interacts (via the ligand-binding domain) with PRAME; the interaction is ligand (retinoic acid)-dependent. Interacts with AKT1; the interaction phosphorylates RARA and represses transactivation. Interacts with PRKAR1A; the interaction negatively regulates RARA transcriptional activity. Interacts with NCOR1 and NCOR2. Interacts with PRMT2. Interacts with LRIF1. Interacts with ASXL1 and NCOA1. Interacts with ACTN4.By similarity15 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Asxl1P595984EBI-413374,EBI-5743705From a different organism.
EZH2Q159102EBI-413374,EBI-530054
GNAQP501484EBI-413374,EBI-3909604
ITGB1BP2Q9UKP32EBI-413374,EBI-5659717
MED1Q156483EBI-413374,EBI-394459
MED25Q71SY510EBI-413374,EBI-394558
NCOA1Q157883EBI-413374,EBI-455189
NCOA3Q9Y6Q92EBI-413374,EBI-81196
NCOR1O753763EBI-413374,EBI-347233
NRIP1P485524EBI-413374,EBI-746484
PHF8Q9UPP1-22EBI-413374,EBI-6601215
PRKDCP785273EBI-413374,EBI-352053
RXRAP197936EBI-413374,EBI-78598
RXRBP287028EBI-413374,EBI-748576
RXRGP4844314EBI-413374,EBI-712405
SIRT1Q96EB63EBI-413374,EBI-1802965
SUMO1P631655EBI-413374,EBI-80140
TEKT4Q8WW243EBI-10197061,EBI-750487
ZNF423Q2M1K92EBI-413374,EBI-950016

GO - Molecular functioni

  • alpha-actinin binding Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • protein domain specific binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein kinase A binding Source: UniProtKB
  • protein kinase B binding Source: UniProtKB
  • receptor binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111849. 115 interactors.
DIPiDIP-34N.
IntActiP10276. 54 interactors.
MINTiMINT-123081.
STRINGi9606.ENSP00000254066.

Chemistry databases

BindingDBiP10276.

Structurei

Secondary structure

1462
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni89 – 91Combined sources3
Beta strandi97 – 99Combined sources3
Helixi106 – 117Combined sources12
Turni134 – 136Combined sources3
Helixi137 – 139Combined sources3
Helixi141 – 150Combined sources10
Helixi155 – 157Combined sources3
Helixi183 – 196Combined sources14
Helixi202 – 204Combined sources3
Beta strandi214 – 216Combined sources3
Helixi222 – 244Combined sources23
Helixi249 – 251Combined sources3
Helixi254 – 275Combined sources22
Turni279 – 282Combined sources4
Beta strandi283 – 285Combined sources3
Beta strandi289 – 293Combined sources5
Helixi294 – 300Combined sources7
Helixi303 – 305Combined sources3
Helixi306 – 316Combined sources11
Helixi317 – 319Combined sources3
Helixi323 – 334Combined sources12
Helixi345 – 366Combined sources22
Helixi373 – 401Combined sources29
Beta strandi402 – 404Combined sources3
Helixi408 – 414Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DKFX-ray2.50B182-416[»]
1DSZX-ray1.70A82-167[»]
3A9EX-ray2.75B153-421[»]
3KMRX-ray1.80A176-421[»]
3KMZX-ray2.10A/B176-421[»]
4DQMX-ray2.75A/C182-415[»]
5K13X-ray1.85A181-426[»]
ProteinModelPortaliP10276.
SMRiP10276.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10276.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 87ModulatingAdd BLAST87
Regioni154 – 199HingeAdd BLAST46
Regioni200 – 419Ligand-bindingAdd BLAST220
Regioni404 – 419Required for binding corepressor NCOR1Add BLAST16

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)DescriptionActionsGraphical viewLength
Zinc fingeri88 – 108NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri124 – 148NR C4-typePROSITE-ProRule annotationAdd BLAST25

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
GeneTreeiENSGT00850000132242.
HOGENOMiHOG000010312.
HOVERGENiHBG005606.
InParanoidiP10276.
KOiK08527.
OMAiFLMVDYY.
PhylomeDBiP10276.
TreeFamiTF328382.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR000536. Nucl_hrmn_rcpt_lig-bd.
IPR001723. Nuclear_hrmn_rcpt.
IPR003078. Retinoic_acid_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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Alpha-1 (identifier: P10276-1) [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
MASNSSSCPT PGGGHLNGYP VPPYAFFFPP MLGGLSPPGA LTTLQHQLPV
60 70 80 90 100
SGYSTPSPAT IETQSSSSEE IVPSPPSPPP LPRIYKPCFV CQDKSSGYHY
110 120 130 140 150
GVSACEGCKG FFRRSIQKNM VYTCHRDKNC IINKVTRNRC QYCRLQKCFE
160 170 180 190 200
VGMSKESVRN DRNKKKKEVP 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 DLEQPDRVDM
360 370 380 390 400
LQEPLLEALK VYVRKRRPSR PHMFPKMLMK ITDLRSISAK GAERVITLKM
410 420 430 440 450
EIPGSMPPLI QEMLENSEGL DTLSGQPGGG GRDGGGLAPP PGSCSPSLSP
460
SSNRSSPATH SP
Length:462
Mass (Da):50,771
Last modified:October 1, 1989 - v2
Checksum:iE8D1CF9A1E57CB99
GO
Isoform Alpha-2 (identifier: P10276-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: MASNSSSCPT...SGYSTPSPAT → MYESVEVGGP...TPLWNGSNHS

Show »
Length:457
Mass (Da):50,742
Checksum:i1E328ED7945D1F95
GO
Isoform Alpha-1-deltaBC (identifier: P10276-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     61-157: Missing.

Note: Does not bind nor transactivate RARE on its own but may do so as a heterodimer with Alpha-1.
Show »
Length:365
Mass (Da):39,700
Checksum:iD24F282D50E9953E
GO

Sequence cautioni

The sequence AAB00112 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAB00113 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAB62809 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti241E → D in AAD05222 (PubMed:10337631).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0036291 – 60MASNS…PSPAT → MYESVEVGGPTPNPFLVVDF YNQNRACLLPEKGLPAPGPY STPLRTPLWNGSNHS in isoform Alpha-2. 1 PublicationAdd BLAST60
Alternative sequenceiVSP_04314361 – 157Missing in isoform Alpha-1-deltaBC. 1 PublicationAdd BLAST97

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06614 mRNA. Translation: CAA29829.1.
X06538 mRNA. Translation: CAA29787.1.
AF088895
, AF088889, AF088890, AF088891, AF088892, AF088893, AF088894 Genomic DNA. Translation: AAD05222.1.
FJ487576 mRNA. Translation: ACK86665.1.
AC080112 Genomic DNA. No translation available.
BC008727 mRNA. Translation: AAH08727.1.
BC071733 mRNA. Translation: AAH71733.1.
X56058, X58685 mRNA. Translation: CAA39533.1.
X58685 mRNA. Translation: CAA41532.1.
U41742 mRNA. Translation: AAB00112.1. Different initiation.
U41743 mRNA. Translation: AAB00113.1. Different initiation.
AF283809 Genomic DNA. Translation: AAF87249.1.
AB067754 mRNA. Translation: BAB62809.1. Different initiation.
CCDSiCCDS11366.1. [P10276-1]
CCDS42317.1. [P10276-2]
CCDS45671.1. [P10276-3]
PIRiA29491.
RefSeqiNP_000955.1. NM_000964.3. [P10276-1]
NP_001019980.1. NM_001024809.3. [P10276-2]
NP_001138773.1. NM_001145301.2.
NP_001138774.1. NM_001145302.2. [P10276-3]
XP_005257610.1. XM_005257553.1. [P10276-1]
XP_005257611.1. XM_005257554.1. [P10276-1]
XP_011523397.1. XM_011525095.1. [P10276-1]
UniGeneiHs.654583.

Genome annotation databases

EnsembliENST00000254066; ENSP00000254066; ENSG00000131759. [P10276-1]
ENST00000394081; ENSP00000377643; ENSG00000131759. [P10276-2]
ENST00000394089; ENSP00000377649; ENSG00000131759. [P10276-1]
ENST00000425707; ENSP00000389993; ENSG00000131759. [P10276-3]
GeneIDi5914.
KEGGihsa:5914.
UCSCiuc002hun.3. human. [P10276-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
Wikipedia

Retinoic acid receptor entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06614 mRNA. Translation: CAA29829.1.
X06538 mRNA. Translation: CAA29787.1.
AF088895
, AF088889, AF088890, AF088891, AF088892, AF088893, AF088894 Genomic DNA. Translation: AAD05222.1.
FJ487576 mRNA. Translation: ACK86665.1.
AC080112 Genomic DNA. No translation available.
BC008727 mRNA. Translation: AAH08727.1.
BC071733 mRNA. Translation: AAH71733.1.
X56058, X58685 mRNA. Translation: CAA39533.1.
X58685 mRNA. Translation: CAA41532.1.
U41742 mRNA. Translation: AAB00112.1. Different initiation.
U41743 mRNA. Translation: AAB00113.1. Different initiation.
AF283809 Genomic DNA. Translation: AAF87249.1.
AB067754 mRNA. Translation: BAB62809.1. Different initiation.
CCDSiCCDS11366.1. [P10276-1]
CCDS42317.1. [P10276-2]
CCDS45671.1. [P10276-3]
PIRiA29491.
RefSeqiNP_000955.1. NM_000964.3. [P10276-1]
NP_001019980.1. NM_001024809.3. [P10276-2]
NP_001138773.1. NM_001145301.2.
NP_001138774.1. NM_001145302.2. [P10276-3]
XP_005257610.1. XM_005257553.1. [P10276-1]
XP_005257611.1. XM_005257554.1. [P10276-1]
XP_011523397.1. XM_011525095.1. [P10276-1]
UniGeneiHs.654583.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DKFX-ray2.50B182-416[»]
1DSZX-ray1.70A82-167[»]
3A9EX-ray2.75B153-421[»]
3KMRX-ray1.80A176-421[»]
3KMZX-ray2.10A/B176-421[»]
4DQMX-ray2.75A/C182-415[»]
5K13X-ray1.85A181-426[»]
ProteinModelPortaliP10276.
SMRiP10276.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111849. 115 interactors.
DIPiDIP-34N.
IntActiP10276. 54 interactors.
MINTiMINT-123081.
STRINGi9606.ENSP00000254066.

Chemistry databases

BindingDBiP10276.
ChEMBLiCHEMBL2055.
DrugBankiDB00459. Acitretin.
DB00210. Adapalene.
DB00523. Alitretinoin.
DB00982. Isotretinoin.
DB04942. Tamibarotene.
DB00799. Tazarotene.
GuidetoPHARMACOLOGYi590.

PTM databases

iPTMnetiP10276.
PhosphoSitePlusiP10276.

Polymorphism and mutation databases

BioMutaiRARA.
DMDMi133483.

Proteomic databases

PaxDbiP10276.
PeptideAtlasiP10276.
PRIDEiP10276.

Protocols and materials databases

DNASUi5914.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000254066; ENSP00000254066; ENSG00000131759. [P10276-1]
ENST00000394081; ENSP00000377643; ENSG00000131759. [P10276-2]
ENST00000394089; ENSP00000377649; ENSG00000131759. [P10276-1]
ENST00000425707; ENSP00000389993; ENSG00000131759. [P10276-3]
GeneIDi5914.
KEGGihsa:5914.
UCSCiuc002hun.3. human. [P10276-1]

Organism-specific databases

CTDi5914.
DisGeNETi5914.
GeneCardsiRARA.
HGNCiHGNC:9864. RARA.
HPAiHPA058282.
MalaCardsiRARA.
MIMi180240. gene.
612376. phenotype.
neXtProtiNX_P10276.
OpenTargetsiENSG00000131759.
Orphaneti520. Acute promyelocytic leukemia.
PharmGKBiPA34225.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
GeneTreeiENSGT00850000132242.
HOGENOMiHOG000010312.
HOVERGENiHBG005606.
InParanoidiP10276.
KOiK08527.
OMAiFLMVDYY.
PhylomeDBiP10276.
TreeFamiTF328382.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000131759-MONOMER.
ReactomeiR-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.
SignaLinkiP10276.
SIGNORiP10276.

Miscellaneous databases

ChiTaRSiRARA. human.
EvolutionaryTraceiP10276.
GeneWikiiRetinoic_acid_receptor_alpha.
GenomeRNAii5914.
PROiP10276.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000131759.
CleanExiHS_RARA.
ExpressionAtlasiP10276. baseline and differential.
GenevisibleiP10276. HS.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR000536. Nucl_hrmn_rcpt_lig-bd.
IPR001723. Nuclear_hrmn_rcpt.
IPR003078. Retinoic_acid_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]
ProtoNetiSearch...

Entry informationi

Entry nameiRARA_HUMAN
AccessioniPrimary (citable) accession number: P10276
Secondary accession number(s): B8Y636
, P78456, Q13440, Q13441, Q96S41, Q9NQS0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 1, 1989
Last modified: November 30, 2016
This is version 214 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 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.