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Protein

Retinoic acid receptor alpha

Gene

RARA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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).By similarity3 Publications

Caution

Was originally thought to be part of the MLL5-L complex, at least composed of KMT2E, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT (PubMed:19377461). However, the corresponding article has been retracted (PubMed:24336203).2 Publications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

GO - Biological processi

Keywordsi

Molecular functionDNA-binding, Receptor
Biological processTranscription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-383280 Nuclear Receptor transcription pathway
R-HSA-4090294 SUMOylation of intracellular receptors
R-HSA-5362517 Signaling by Retinoic Acid
R-HSA-5617472 Activation of anterior HOX genes in hindbrain development during early embryogenesis
SignaLinkiP10276
SIGNORiP10276

Protein family/group databases

MoonDBiP10276 Predicted

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

EuPathDBiHostDB:ENSG00000131759.17
HGNCiHGNC:9864 RARA
MIMi180240 gene
neXtProtiNX_P10276

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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.3 Publications

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
DB00926 Etretinate
DB00982 Isotretinoin
DB05785 LGD-1550
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

EPDiP10276
PaxDbiP10276
PeptideAtlasiP10276
PRIDEiP10276
ProteomicsDBi52592
52593 [P10276-2]
52594 [P10276-3]

PTM databases

iPTMnetiP10276
PhosphoSitePlusiP10276
SwissPalmiP10276

Expressioni

Gene expression databases

BgeeiENSG00000131759 Expressed in 217 organ(s), highest expression level in nasal cavity epithelium
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 (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 similarity14 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi111849, 116 interactors
ComplexPortaliCPX-508 RXRalpha-RARalpha retinoic acid receptor complex
CPX-816 RXRalpha-RARalpha-NCOA2 retinoic acid receptor complex
CORUMiP10276
DIPiDIP-34N
IntActiP10276, 68 interactors
MINTiP10276
STRINGi9606.ENSP00000254066

Chemistry databases

BindingDBiP10276

Structurei

Secondary structure

1462
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP10276
SMRiP10276
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10276

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini183 – 417NR LBDPROSITE-ProRule annotationAdd BLAST235

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 87ModulatingAdd BLAST87
Regioni154 – 182HingeAdd BLAST29
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

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
GeneTreeiENSGT00870000136372
HOGENOMiHOG000010312
HOVERGENiHBG005606
InParanoidiP10276
KOiK08527
OMAiNNSSDQR
PhylomeDBiP10276
TreeFamiTF328382

Family and domain databases

Gene3Di3.30.50.10, 1 hit
InterProiView 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
PfamiView protein in Pfam
PF00104 Hormone_recep, 1 hit
PF00105 zf-C4, 1 hit
PRINTSiPR01292 RETNOICACIDR
PR00398 STRDHORMONER
PR00047 STROIDFINGER
SMARTiView protein in SMART
SM00430 HOLI, 1 hit
SM00399 ZnF_C4, 1 hit
SUPFAMiSSF48508 SSF48508, 1 hit
PROSITEiView protein in PROSITE
PS51843 NR_LBD, 1 hit
PS00031 NUCLEAR_REC_DBD_1, 1 hit
PS51030 NUCLEAR_REC_DBD_2, 1 hit

Sequences (3+)i

Sequence statusi: Complete.

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

This entry has 3 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A8MUP8A8MUP8_HUMAN
Retinoic acid receptor alpha
RARA hCG_2007196
478Annotation score:
J3KSJ4J3KSJ4_HUMAN
Retinoic acid receptor alpha
RARA
186Annotation score:
J3QRM2J3QRM2_HUMAN
Retinoic acid receptor alpha
RARA
66Annotation score:

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 [P10276-1]
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

Similar proteinsi

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 [P10276-1]
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, 116 interactors
ComplexPortaliCPX-508 RXRalpha-RARalpha retinoic acid receptor complex
CPX-816 RXRalpha-RARalpha-NCOA2 retinoic acid receptor complex
CORUMiP10276
DIPiDIP-34N
IntActiP10276, 68 interactors
MINTiP10276
STRINGi9606.ENSP00000254066

Chemistry databases

BindingDBiP10276
ChEMBLiCHEMBL2055
DrugBankiDB00459 Acitretin
DB00210 Adapalene
DB00523 Alitretinoin
DB00926 Etretinate
DB00982 Isotretinoin
DB05785 LGD-1550
DB04942 Tamibarotene
DB00799 Tazarotene
GuidetoPHARMACOLOGYi590

Protein family/group databases

MoonDBiP10276 Predicted

PTM databases

iPTMnetiP10276
PhosphoSitePlusiP10276
SwissPalmiP10276

Polymorphism and mutation databases

BioMutaiRARA
DMDMi133483

Proteomic databases

EPDiP10276
PaxDbiP10276
PeptideAtlasiP10276
PRIDEiP10276
ProteomicsDBi52592
52593 [P10276-2]
52594 [P10276-3]

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
EuPathDBiHostDB:ENSG00000131759.17
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
GeneTreeiENSGT00870000136372
HOGENOMiHOG000010312
HOVERGENiHBG005606
InParanoidiP10276
KOiK08527
OMAiNNSSDQR
PhylomeDBiP10276
TreeFamiTF328382

Enzyme and pathway databases

ReactomeiR-HSA-383280 Nuclear Receptor transcription pathway
R-HSA-4090294 SUMOylation of intracellular receptors
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
PROiPR:P10276
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000131759 Expressed in 217 organ(s), highest expression level in nasal cavity epithelium
CleanExiHS_RARA
ExpressionAtlasiP10276 baseline and differential
GenevisibleiP10276 HS

Family and domain databases

Gene3Di3.30.50.10, 1 hit
InterProiView 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
PfamiView protein in Pfam
PF00104 Hormone_recep, 1 hit
PF00105 zf-C4, 1 hit
PRINTSiPR01292 RETNOICACIDR
PR00398 STRDHORMONER
PR00047 STROIDFINGER
SMARTiView protein in SMART
SM00430 HOLI, 1 hit
SM00399 ZnF_C4, 1 hit
SUPFAMiSSF48508 SSF48508, 1 hit
PROSITEiView protein in PROSITE
PS51843 NR_LBD, 1 hit
PS00031 NUCLEAR_REC_DBD_1, 1 hit
PS51030 NUCLEAR_REC_DBD_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiRARA_HUMAN
AccessioniPrimary (citable) accession number: P10276
Secondary accession number(s): B8Y636
, P78456, Q13440, Q13441, Q96S41, Q9NQS0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 1, 1989
Last modified: November 7, 2018
This is version 233 of the entry and version 2 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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