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Retinoic acid receptor alpha (RAR-alpha) (Nuclear receptor subfamily 1 group B member 1)

 RARA_HUMAN              Reviewed;         462 AA.
P10276; B8Y636; P78456; Q13440; Q13441; Q96S41; Q9NQS0;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 2.
27-SEP-2017, entry version 221.
RecName: Full=Retinoic acid receptor alpha;
Short=RAR-alpha;
AltName: Full=Nuclear receptor subfamily 1 group B member 1;
Name=RARA; Synonyms=NR1B1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-1).
PubMed=2825036; DOI=10.1038/330624a0;
Giguere V., Ong E.S., Segui P., Evans R.M.;
"Identification of a receptor for the morphogen retinoic acid.";
Nature 330:624-629(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-1), AND CHROMOSOMAL
TRANSLOCATION WITH PML.
PubMed=8302850; DOI=10.1073/pnas.91.3.1178;
Chen Z., Guidez F., Rousselot P., Agadir A., Chen S.-J., Wang Z.-Y.,
Degos L., Zelent A., Waxman S., Chomienne C.;
"PLZF-RAR alpha fusion proteins generated from the variant
t(11;17)(q23;q21) translocation in acute promyelocytic leukemia
inhibit ligand-dependent transactivation of wild-type retinoic acid
receptors.";
Proc. Natl. Acad. Sci. U.S.A. 91:1178-1182(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM ALPHA-1).
PubMed=10337631; DOI=10.1007/s003359901036;
Hjalt T.A.H., Murray J.C.;
"Genomic structure of the human retinoic acid receptor-alpha1 gene.";
Mamm. Genome 10:528-529(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-1-DELTABC).
PubMed=11812818; DOI=10.1093/nar/29.24.4901;
Parrado A., Despouy G., Kraiba R., Le Pogam C., Dupas S.,
Choquette M., Robledo M., Larghero J., Bui H., Le Gall I.,
Rochette-Egly C., Chomienne C., Padua R.A.;
"Retinoic acid receptor alpha1 variants, RARalpha1DeltaB and
RARalpha1DeltaBC, define a new class of nuclear receptor isoforms.";
Nucleic Acids Res. 29:4901-4908(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS ALPHA-1 AND ALPHA-2).
TISSUE=Blood, and Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-80 (ISOFORM ALPHA-1).
PubMed=2175878; DOI=10.1093/nar/18.23.6799;
Brand N.J., Petkovich M., Chambon P.;
"Characterization of a functional promoter for the human retinoic acid
receptor-alpha (hRAR-alpha).";
Nucleic Acids Res. 18:6799-6806(1990).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 31-462.
PubMed=2825025; DOI=10.1038/330444a0;
Petkovich M., Brand N.J., Krust A., Chambon P.;
"A human retinoic acid receptor which belongs to the family of nuclear
receptors.";
Nature 330:444-450(1987).
[9]
SEQUENCE REVISION.
Chambon P.;
Submitted (DEC-1988) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 61-462, AND CHROMOSOMAL TRANSLOCATION
WITH NPM.
TISSUE=Bone marrow;
PubMed=8562957;
Redner R.L., Rush E.A., Faas S., Rudert W.A., Corey S.J.;
"The t(5;17) variant of acute promyelocytic leukemia expresses a
nucleophosmin-retinoic acid receptor fusion.";
Blood 87:882-886(1996).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-54 (ISOFORM ALPHA-2).
Chen A., Petrie K., Waxman S., Zelent A.;
"Homo sapiens retinoic acid receptor alpha (RAR-alpha) gene, promoter
and 5' region of RAR-alpha 2 isoform.";
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 61-68, AND CHROMOSOMAL TRANSLOCATION
WITH PML.
PubMed=12691149;
Fujita K., Oba R., Harada H., Mori H., Niikura H., Isoyama K.,
Omine M.;
"Cytogenetics, FISH and RT-PCR analysis of acute promyelocytic
leukemia: structure of the fusion point in a case lacking classic
t(15;17) translocation.";
Leuk. Lymphoma 44:111-115(2003).
[13]
INTERACTION WITH NCOA3.
PubMed=9267036; DOI=10.1016/S0092-8674(00)80516-4;
Chen H., Lin R.J., Schiltz R.L., Chakravarti D., Nash A., Nagy L.,
Privalsky M.L., Nakatani Y., Evans R.M.;
"Nuclear receptor coactivator ACTR is a novel histone
acetyltransferase and forms a multimeric activation complex with P/CAF
and CBP/p300.";
Cell 90:569-580(1997).
[14]
INTERACTION WITH NCOA6.
PubMed=10567404; DOI=10.1074/jbc.274.48.34283;
Lee S.-K., Anzick S.L., Choi J.-E., Bubendorf L., Guan X.-Y.,
Jung Y.-K., Kallioniemi O.-P., Kononen J., Trent J.M., Azorsa D.,
Jhun B.-H., Cheong J.H., Lee Y.C., Meltzer P.S., Lee J.W.;
"A nuclear factor ASC-2, as a cancer-amplified transcriptional
coactivator essential for ligand-dependent transactivation by nuclear
receptors in vivo.";
J. Biol. Chem. 274:34283-34293(1999).
[15]
INTERACTION WITH PRMT2.
PubMed=12039952; DOI=10.1074/jbc.M201053200;
Qi C., Chang J., Zhu Y., Yeldandi A.V., Rao S.M., Zhu Y.-J.;
"Identification of protein arginine methyltransferase 2 as a
coactivator for estrogen receptor alpha.";
J. Biol. Chem. 277:28624-28630(2002).
[16]
INTERACTION WITH NCOA7.
PubMed=11971969; DOI=10.1128/MCB.22.10.3358-3372.2002;
Shao W., Halachmi S., Brown M.;
"ERAP140, a conserved tissue-specific nuclear receptor coactivator.";
Mol. Cell. Biol. 22:3358-3372(2002).
[17]
INTERACTION OF THE PML-RARALPHA ONCOPROTEIN WITH UBE2I, SUMOYLATION,
AND SUBCELLULAR LOCATION.
PubMed=15809060; DOI=10.1016/j.bbrc.2005.03.052;
Kim Y.E., Kim D.Y., Lee J.M., Kim S.T., Han T.H., Ahn J.H.;
"Requirement of the coiled-coil domain of PML-RARalpha oncoprotein for
localization, sumoylation, and inhibition of monocyte
differentiation.";
Biochem. Biophys. Res. Commun. 330:746-754(2005).
[18]
INTERACTION WITH PRAME.
PubMed=16179254; DOI=10.1016/j.cell.2005.07.003;
Epping M.T., Wang L., Edel M.J., Carlee L., Hernandez M., Bernards R.;
"The human tumor antigen PRAME is a dominant repressor of retinoic
acid receptor signaling.";
Cell 122:835-847(2005).
[19]
PHOSPHORYLATION AT SER-96, FUNCTION, INTERACTION WITH AKT1, AND
MUTAGENESIS OF SER-95; SER-96; SER-154 AND SER-157.
PubMed=16417524; DOI=10.1042/BJ20051794;
Srinivas H., Xia D., Moore N.L., Uray I.P., Kim H., Ma L.,
Weigel N.L., Brown P.H., Kurie J.M.;
"Akt phosphorylates and suppresses the transactivation of retinoic
acid receptor alpha.";
Biochem. J. 395:653-662(2006).
[20]
INTERACTION WITH ASXL1 AND NCOA1, AND MUTAGENESIS OF 409-ILE-LEU-410;
GLU-412; 413-MET-LEU-414 AND GLU-415.
PubMed=16606617; DOI=10.1074/jbc.M512616200;
Cho Y.S., Kim E.J., Park U.H., Sin H.S., Um S.J.;
"Additional sex comb-like 1 (ASXL1), in cooperation with SRC-1, acts
as a ligand-dependent coactivator for retinoic acid receptor.";
J. Biol. Chem. 281:17588-17598(2006).
[21]
INTERACTION WITH LRIF1.
PubMed=17455211; DOI=10.1002/jcb.21340;
Li H.J., Haque Z.K., Chen A., Mendelsohn M.;
"RIF-1, a novel nuclear receptor corepressor that associates with the
nuclear matrix.";
J. Cell. Biochem. 102:1021-1035(2007).
[22]
SUMOYLATION AT LYS-166; LYS-171 AND LYS-399, FUNCTION, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF LYS-147; LYS-166; LYS-171 AND LYS-399.
PubMed=19850744; DOI=10.1210/en.2009-0868;
Zhu L., Santos N.C., Kim K.H.;
"Small ubiquitin-like modifier-2 modification of retinoic acid
receptor-alpha regulates its subcellular localization and
transcriptional activity.";
Endocrinology 150:5586-5595(2009).
[23]
FUNCTION, AND INTERACTION WITH KMT2E.
PubMed=19377461; DOI=10.1038/nature07954;
Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G.,
Kitagawa H., Kato S.;
"GlcNAcylation of a histone methyltransferase in retinoic-acid-induced
granulopoiesis.";
Nature 459:455-459(2009).
[24]
PHOSPHORYLATION AT SER-219 AND SER-369, INTERACTION WITH RXRA AND
PRKAR1A, FUNCTION, AND MUTAGENESIS OF SER-219 AND SER-369.
PubMed=20215566; DOI=10.1210/en.2009-1338;
Santos N.C., Kim K.H.;
"Activity of retinoic acid receptor-alpha is directly regulated at its
protein kinase A sites in response to follicle-stimulating hormone
signaling.";
Endocrinology 151:2361-2372(2010).
[25]
INTERACTION WITH ACTN4.
PubMed=22351778; DOI=10.1074/jbc.M112.345421;
Khurana S., Chakraborty S., Lam M., Liu Y., Su Y.T., Zhao X.,
Saleem M.A., Mathieson P.W., Bruggeman L.A., Kao H.Y.;
"Familial focal segmental glomerulosclerosis (FSGS)-linked alpha-
actinin 4 (ACTN4) protein mutants lose ability to activate
transcription by nuclear hormone receptors.";
J. Biol. Chem. 287:12027-12035(2012).
[26]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 82-167 IN COMPLEX WITH RXRA
AND DNA.
PubMed=10698945; DOI=10.1093/emboj/19.5.1045;
Rastinejad F., Wagner T., Zhao Q., Khorasanizadeh S.;
"Structure of the RXR-RAR DNA-binding complex on the retinoic acid
response element DR1.";
EMBO J. 19:1045-1054(2000).
[27]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 182-416 IN COMPLEX WITH
M.MUSCULUS RXRA.
PubMed=10882070; DOI=10.1016/S1097-2765(00)80424-4;
Bourguet W., Vivat V., Wurtz J.M., Chambon P., Gronemeyer H.,
Moras D.;
"Crystal structure of a heterodimeric complex of RAR and RXR ligand-
binding domains.";
Mol. Cell 5:289-298(2000).
[28]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 176-421 IN COMPLEXES WITH
AGONIST AM580 AND NCOA1 AND WITH INVERSE AGONIST BMS493 AND NCOR1,
INTERACTION WITH NCOR1 AND NCOR2, AND MUTAGENESIS OF ILE-396.
PubMed=20543827; DOI=10.1038/nsmb.1855;
le Maire A., Teyssier C., Erb C., Grimaldi M., Alvarez S.,
de Lera A.R., Balaguer P., Gronemeyer H., Royer C.A., Germain P.,
Bourguet W.;
"A unique secondary-structure switch controls constitutive gene
repression by retinoic acid receptor.";
Nat. Struct. Mol. Biol. 17:801-807(2010).
-!- FUNCTION: 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.
{ECO:0000250, ECO:0000269|PubMed:16417524,
ECO:0000269|PubMed:19377461, ECO:0000269|PubMed:19850744,
ECO:0000269|PubMed:20215566}.
-!- SUBUNIT: 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.
{ECO:0000250|UniProtKB:P11416, ECO:0000269|PubMed:10567404,
ECO:0000269|PubMed:10698945, ECO:0000269|PubMed:10882070,
ECO:0000269|PubMed:11971969, ECO:0000269|PubMed:12039952,
ECO:0000269|PubMed:15809060, ECO:0000269|PubMed:16179254,
ECO:0000269|PubMed:16417524, ECO:0000269|PubMed:16606617,
ECO:0000269|PubMed:17455211, ECO:0000269|PubMed:19377461,
ECO:0000269|PubMed:20215566, ECO:0000269|PubMed:20543827,
ECO:0000269|PubMed:22351778, ECO:0000269|PubMed:9267036}.
-!- INTERACTION:
P59598:Asxl1 (xeno); NbExp=4; IntAct=EBI-413374, EBI-5743705;
Q15910:EZH2; NbExp=2; IntAct=EBI-413374, EBI-530054;
P50148:GNAQ; NbExp=4; IntAct=EBI-413374, EBI-3909604;
Q9UKP3:ITGB1BP2; NbExp=2; IntAct=EBI-413374, EBI-5659717;
Q15648:MED1; NbExp=3; IntAct=EBI-413374, EBI-394459;
Q71SY5:MED25; NbExp=10; IntAct=EBI-413374, EBI-394558;
Q15788:NCOA1; NbExp=3; IntAct=EBI-413374, EBI-455189;
Q9Y6Q9:NCOA3; NbExp=2; IntAct=EBI-413374, EBI-81196;
O75376:NCOR1; NbExp=3; IntAct=EBI-413374, EBI-347233;
P48552:NRIP1; NbExp=4; IntAct=EBI-413374, EBI-746484;
Q9UPP1-2:PHF8; NbExp=2; IntAct=EBI-413374, EBI-6601215;
P78527:PRKDC; NbExp=3; IntAct=EBI-413374, EBI-352053;
P19793:RXRA; NbExp=7; IntAct=EBI-413374, EBI-78598;
P28702:RXRB; NbExp=10; IntAct=EBI-413374, EBI-748576;
P48443:RXRG; NbExp=14; IntAct=EBI-413374, EBI-712405;
Q96EB6:SIRT1; NbExp=3; IntAct=EBI-413374, EBI-1802965;
P63165:SUMO1; NbExp=5; IntAct=EBI-413374, EBI-80140;
Q8WW24:TEKT4; NbExp=3; IntAct=EBI-413374, EBI-750487;
Q2M1K9:ZNF423; NbExp=2; IntAct=EBI-413374, EBI-950016;
-!- SUBCELLULAR LOCATION: 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.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=Alpha-1;
IsoId=P10276-1; Sequence=Displayed;
Name=Alpha-2;
IsoId=P10276-2; Sequence=VSP_003629;
Name=Alpha-1-deltaBC;
IsoId=P10276-3; Sequence=VSP_043143;
Note=Does not bind nor transactivate RARE on its own but may do
so as a heterodimer with Alpha-1.;
-!- DOMAIN: Composed of three domains: a modulating N-terminal domain,
a DNA-binding domain and a C-terminal ligand-binding domain.
-!- PTM: 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. {ECO:0000250, ECO:0000269|PubMed:16417524,
ECO:0000269|PubMed:20215566}.
-!- PTM: 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.
{ECO:0000269|PubMed:15809060, ECO:0000269|PubMed:19850744}.
-!- PTM: Trimethylation enhances heterodimerization with RXRA and
positively modulates the transcriptional activation.
-!- PTM: Ubiquitinated.
-!- DISEASE: Note=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. {ECO:0000269|PubMed:12691149,
ECO:0000269|PubMed:8302850, ECO:0000269|PubMed:8562957}.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB00112.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAB00113.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAB62809.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/RARAID46.html";
-!- WEB RESOURCE: Name=Wikipedia; Note=Retinoic acid receptor entry;
URL="https://en.wikipedia.org/wiki/Retinoic_acid_receptor";
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EMBL; X06614; CAA29829.1; -; mRNA.
EMBL; X06538; CAA29787.1; -; mRNA.
EMBL; AF088895; AAD05222.1; -; Genomic_DNA.
EMBL; AF088889; AAD05222.1; JOINED; Genomic_DNA.
EMBL; AF088890; AAD05222.1; JOINED; Genomic_DNA.
EMBL; AF088891; AAD05222.1; JOINED; Genomic_DNA.
EMBL; AF088892; AAD05222.1; JOINED; Genomic_DNA.
EMBL; AF088893; AAD05222.1; JOINED; Genomic_DNA.
EMBL; AF088894; AAD05222.1; JOINED; Genomic_DNA.
EMBL; FJ487576; ACK86665.1; -; mRNA.
EMBL; AC080112; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC008727; AAH08727.1; -; mRNA.
EMBL; BC071733; AAH71733.1; -; mRNA.
EMBL; X56058; CAA39533.1; -; Genomic_DNA.
EMBL; X58685; CAA39533.1; JOINED; mRNA.
EMBL; X58685; CAA41532.1; -; mRNA.
EMBL; U41742; AAB00112.1; ALT_INIT; mRNA.
EMBL; U41743; AAB00113.1; ALT_INIT; mRNA.
EMBL; AF283809; AAF87249.1; -; Genomic_DNA.
EMBL; AB067754; BAB62809.1; ALT_INIT; mRNA.
CCDS; CCDS11366.1; -. [P10276-1]
CCDS; CCDS42317.1; -. [P10276-2]
CCDS; CCDS45671.1; -. [P10276-3]
PIR; A29491; A29491.
RefSeq; NP_000955.1; NM_000964.3. [P10276-1]
RefSeq; NP_001019980.1; NM_001024809.3. [P10276-2]
RefSeq; NP_001138773.1; NM_001145301.2.
RefSeq; NP_001138774.1; NM_001145302.2. [P10276-3]
RefSeq; XP_005257610.1; XM_005257553.1. [P10276-1]
RefSeq; XP_005257611.1; XM_005257554.1. [P10276-1]
RefSeq; XP_011523397.1; XM_011525095.1. [P10276-1]
UniGene; Hs.654583; -.
PDB; 1DKF; X-ray; 2.50 A; B=182-416.
PDB; 1DSZ; X-ray; 1.70 A; A=82-167.
PDB; 3A9E; X-ray; 2.75 A; B=153-421.
PDB; 3KMR; X-ray; 1.80 A; A=176-421.
PDB; 3KMZ; X-ray; 2.10 A; A/B=176-421.
PDB; 4DQM; X-ray; 2.75 A; A/C=182-415.
PDB; 5K13; X-ray; 1.85 A; A=181-426.
PDBsum; 1DKF; -.
PDBsum; 1DSZ; -.
PDBsum; 3A9E; -.
PDBsum; 3KMR; -.
PDBsum; 3KMZ; -.
PDBsum; 4DQM; -.
PDBsum; 5K13; -.
ProteinModelPortal; P10276; -.
SMR; P10276; -.
BioGrid; 111849; 116.
CORUM; P10276; -.
DIP; DIP-34N; -.
IntAct; P10276; 61.
MINT; MINT-123081; -.
STRING; 9606.ENSP00000254066; -.
BindingDB; P10276; -.
ChEMBL; CHEMBL2055; -.
DrugBank; DB00459; Acitretin.
DrugBank; DB00210; Adapalene.
DrugBank; DB00523; Alitretinoin.
DrugBank; DB00926; Etretinate.
DrugBank; DB00982; Isotretinoin.
DrugBank; DB05785; LGD-1550.
DrugBank; DB04942; Tamibarotene.
DrugBank; DB00799; Tazarotene.
GuidetoPHARMACOLOGY; 590; -.
iPTMnet; P10276; -.
PhosphoSitePlus; P10276; -.
BioMuta; RARA; -.
DMDM; 133483; -.
PaxDb; P10276; -.
PeptideAtlas; P10276; -.
PRIDE; P10276; -.
DNASU; 5914; -.
Ensembl; ENST00000254066; ENSP00000254066; ENSG00000131759. [P10276-1]
Ensembl; ENST00000394081; ENSP00000377643; ENSG00000131759. [P10276-2]
Ensembl; ENST00000394089; ENSP00000377649; ENSG00000131759. [P10276-1]
Ensembl; ENST00000425707; ENSP00000389993; ENSG00000131759. [P10276-3]
GeneID; 5914; -.
KEGG; hsa:5914; -.
UCSC; uc002hun.3; human. [P10276-1]
CTD; 5914; -.
DisGeNET; 5914; -.
EuPathDB; HostDB:ENSG00000131759.17; -.
GeneCards; RARA; -.
HGNC; HGNC:9864; RARA.
HPA; HPA058282; -.
MalaCards; RARA; -.
MIM; 180240; gene.
MIM; 612376; phenotype.
neXtProt; NX_P10276; -.
OpenTargets; ENSG00000131759; -.
Orphanet; 520; Acute promyelocytic leukemia.
PharmGKB; PA34225; -.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
GeneTree; ENSGT00870000136372; -.
HOGENOM; HOG000010312; -.
HOVERGEN; HBG005606; -.
InParanoid; P10276; -.
KO; K08527; -.
OMA; QECSESY; -.
PhylomeDB; P10276; -.
TreeFam; TF328382; -.
Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
Reactome; R-HSA-5362517; Signaling by Retinoic Acid.
Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
SignaLink; P10276; -.
SIGNOR; P10276; -.
ChiTaRS; RARA; human.
EvolutionaryTrace; P10276; -.
GeneWiki; Retinoic_acid_receptor_alpha; -.
GenomeRNAi; 5914; -.
PRO; PR:P10276; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000131759; -.
CleanEx; HS_RARA; -.
ExpressionAtlas; P10276; baseline and differential.
Genevisible; P10276; HS.
GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
GO; GO:0009986; C:cell surface; IC:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0051393; F:alpha-actinin binding; IPI:UniProtKB.
GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB.
GO; GO:0008144; F:drug binding; IEA:Ensembl.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
GO; GO:0048027; F:mRNA 5'-UTR binding; IEA:Ensembl.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0051018; F:protein kinase A binding; IDA:UniProtKB.
GO; GO:0043422; F:protein kinase B binding; IPI:UniProtKB.
GO; GO:0005102; F:receptor binding; IDA:UniProtKB.
GO; GO:0001972; F:retinoic acid binding; IDA:BHF-UCL.
GO; GO:0003708; F:retinoic acid receptor activity; IDA:BHF-UCL.
GO; GO:0044323; F:retinoic acid-responsive element binding; IDA:UniProtKB.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0003707; F:steroid hormone receptor activity; IEA:InterPro.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0000900; F:translation repressor activity, nucleic acid binding; IEA:Ensembl.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0043277; P:apoptotic cell clearance; IMP:UniProtKB.
GO; GO:0071391; P:cellular response to estrogen stimulus; IDA:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0071300; P:cellular response to retinoic acid; IDA:UniProtKB.
GO; GO:0060591; P:chondroblast differentiation; IEA:Ensembl.
GO; GO:0031076; P:embryonic camera-type eye development; IEA:Ensembl.
GO; GO:0060324; P:face development; IEA:Ensembl.
GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
GO; GO:0007281; P:germ cell development; IEA:Ensembl.
GO; GO:0002068; P:glandular epithelial cell development; IEA:Ensembl.
GO; GO:0003417; P:growth plate cartilage development; IEA:Ensembl.
GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
GO; GO:0060173; P:limb development; IEA:Ensembl.
GO; GO:0001889; P:liver development; IEA:Ensembl.
GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0061037; P:negative regulation of cartilage development; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:0030853; P:negative regulation of granulocyte differentiation; IDA:UniProtKB.
GO; GO:0032689; P:negative regulation of interferon-gamma production; IDA:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0045947; P:negative regulation of translational initiation; IEA:Ensembl.
GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IDA:BHF-UCL.
GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
GO; GO:0003148; P:outflow tract septum morphogenesis; IEA:Ensembl.
GO; GO:0051099; P:positive regulation of binding; IMP:UniProtKB.
GO; GO:0045787; P:positive regulation of cell cycle; IMP:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0032736; P:positive regulation of interleukin-13 production; IDA:BHF-UCL.
GO; GO:0032753; P:positive regulation of interleukin-4 production; IDA:BHF-UCL.
GO; GO:0032754; P:positive regulation of interleukin-5 production; IDA:BHF-UCL.
GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
GO; GO:0045630; P:positive regulation of T-helper 2 cell differentiation; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0030850; P:prostate gland development; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; IMP:UniProtKB.
GO; GO:0031641; P:regulation of myelination; IEA:Ensembl.
GO; GO:0048167; P:regulation of synaptic plasticity; IEA:Ensembl.
GO; GO:0034097; P:response to cytokine; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0032526; P:response to retinoic acid; IMP:BHF-UCL.
GO; GO:0033189; P:response to vitamin A; IEA:Ensembl.
GO; GO:0048384; P:retinoic acid receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0060010; P:Sertoli cell fate commitment; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; IDA:BHF-UCL.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:0060534; P:trachea cartilage development; IEA:Ensembl.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0001657; P:ureteric bud development; IEA:Ensembl.
GO; GO:0055012; P:ventricular cardiac muscle cell differentiation; IEA:Ensembl.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001723; Nuclear_hrmn_rcpt.
InterPro; IPR003078; Retinoic_acid_rcpt.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF00105; zf-C4; 1.
PRINTS; PR01292; RETNOICACIDR.
PRINTS; PR00398; STRDHORMONER.
PRINTS; PR00047; STROIDFINGER.
SMART; SM00430; HOLI; 1.
SMART; SM00399; ZnF_C4; 1.
SUPFAM; SSF48508; SSF48508; 1.
PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromosomal rearrangement;
Complete proteome; Cytoplasm; DNA-binding; Isopeptide bond;
Metal-binding; Nucleus; Phosphoprotein; Proto-oncogene; Receptor;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 462 Retinoic acid receptor alpha.
/FTId=PRO_0000053461.
DNA_BIND 88 153 Nuclear receptor. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 88 108 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 124 148 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
REGION 1 87 Modulating.
REGION 154 199 Hinge.
REGION 200 419 Ligand-binding.
REGION 404 419 Required for binding corepressor NCOR1.
SITE 60 61 Breakpoint for translocation to form
PLZF-RAR-alpha, RAR-alpha1-PLZF and PML-
RAR-alpha oncogenes.
MOD_RES 77 77 Phosphoserine; by CDK7.
{ECO:0000250|UniProtKB:P11416}.
MOD_RES 96 96 Phosphoserine; by PKB/AKT1.
{ECO:0000269|PubMed:16417524}.
MOD_RES 219 219 Phosphoserine; by PKA.
{ECO:0000269|PubMed:20215566}.
MOD_RES 369 369 Phosphoserine; by PKA.
{ECO:0000269|PubMed:20215566}.
CROSSLNK 166 166 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:19850744}.
CROSSLNK 171 171 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:19850744}.
CROSSLNK 399 399 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:19850744}.
VAR_SEQ 1 60 MASNSSSCPTPGGGHLNGYPVPPYAFFFPPMLGGLSPPGAL
TTLQHQLPVSGYSTPSPAT -> MYESVEVGGPTPNPFLVV
DFYNQNRACLLPEKGLPAPGPYSTPLRTPLWNGSNHS (in
isoform Alpha-2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_003629.
VAR_SEQ 61 157 Missing (in isoform Alpha-1-deltaBC).
{ECO:0000303|PubMed:11812818}.
/FTId=VSP_043143.
MUTAGEN 95 95 S->A: No effect on PKB/AKT1-mediated
phosphorylation. Repressed
transactivation.
{ECO:0000269|PubMed:16417524}.
MUTAGEN 96 96 S->A: Abolishes PKB/AKT1-mediated
phosphorylation. Repressed
transactivation.
{ECO:0000269|PubMed:16417524}.
MUTAGEN 147 147 K->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.
{ECO:0000269|PubMed:19850744}.
MUTAGEN 154 154 S->A: No effect on PKB/AKT1-mediated
phosphorylation. No repression of
transactivation.
{ECO:0000269|PubMed:16417524}.
MUTAGEN 157 157 S->A: No effect on PKB/AKT1-mediated
phosphorylation. Repressed
transactivation.
{ECO:0000269|PubMed:16417524}.
MUTAGEN 166 166 K->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.
{ECO:0000269|PubMed:19850744}.
MUTAGEN 171 171 K->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.
{ECO:0000269|PubMed:19850744}.
MUTAGEN 219 219 S->A: No effect on heterodimerization
with RARA. On ATRA treatment, localizes
to the nucleus, and increased protein
levels; when associated with A-369.
{ECO:0000269|PubMed:20215566}.
MUTAGEN 219 219 S->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.
{ECO:0000269|PubMed:20215566}.
MUTAGEN 369 369 S->A: No effect on heterodimerization
with RARA. On ATRA treatment, localizes
to the nucleus, and increased protein
levels; when associated with A-219.
{ECO:0000269|PubMed:20215566}.
MUTAGEN 369 369 S->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.
{ECO:0000269|PubMed:20215566}.
MUTAGEN 396 396 I->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.
{ECO:0000269|PubMed:20543827}.
MUTAGEN 399 399 K->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.
{ECO:0000269|PubMed:19850744}.
MUTAGEN 409 410 LI->AA: Abolishes interaction with ASXL1
and NCOA1. {ECO:0000269|PubMed:16606617}.
MUTAGEN 412 412 E->Q: Impairs interaction with ASXL1 and
NCOA1; when associated with Q-415.
{ECO:0000269|PubMed:16606617}.
MUTAGEN 413 414 ML->AA: Abolishes interaction with ASXL1
and NCOA1. {ECO:0000269|PubMed:16606617}.
MUTAGEN 415 415 E->Q: Impairs interaction with ASXL1 and
NCOA1; when associated with Q-412.
{ECO:0000269|PubMed:16606617}.
CONFLICT 241 241 E -> D (in Ref. 3; AAD05222).
{ECO:0000305}.
TURN 89 91 {ECO:0000244|PDB:1DSZ}.
STRAND 97 99 {ECO:0000244|PDB:1DSZ}.
HELIX 106 117 {ECO:0000244|PDB:1DSZ}.
TURN 134 136 {ECO:0000244|PDB:1DSZ}.
HELIX 137 139 {ECO:0000244|PDB:1DSZ}.
HELIX 141 150 {ECO:0000244|PDB:1DSZ}.
HELIX 155 157 {ECO:0000244|PDB:1DSZ}.
HELIX 183 196 {ECO:0000244|PDB:3KMR}.
HELIX 202 204 {ECO:0000244|PDB:3KMR}.
STRAND 214 216 {ECO:0000244|PDB:5K13}.
HELIX 222 244 {ECO:0000244|PDB:3KMR}.
HELIX 249 251 {ECO:0000244|PDB:3KMR}.
HELIX 254 275 {ECO:0000244|PDB:3KMR}.
TURN 279 282 {ECO:0000244|PDB:3KMR}.
STRAND 283 285 {ECO:0000244|PDB:3KMR}.
STRAND 289 293 {ECO:0000244|PDB:3KMR}.
HELIX 294 300 {ECO:0000244|PDB:3KMR}.
HELIX 303 305 {ECO:0000244|PDB:3KMR}.
HELIX 306 316 {ECO:0000244|PDB:3KMR}.
HELIX 317 319 {ECO:0000244|PDB:3KMR}.
HELIX 323 334 {ECO:0000244|PDB:3KMR}.
HELIX 345 366 {ECO:0000244|PDB:3KMR}.
HELIX 373 401 {ECO:0000244|PDB:3KMR}.
STRAND 402 404 {ECO:0000244|PDB:3KMR}.
HELIX 408 414 {ECO:0000244|PDB:3KMR}.
SEQUENCE 462 AA; 50771 MW; E8D1CF9A1E57CB99 CRC64;
MASNSSSCPT PGGGHLNGYP VPPYAFFFPP MLGGLSPPGA LTTLQHQLPV SGYSTPSPAT
IETQSSSSEE IVPSPPSPPP LPRIYKPCFV CQDKSSGYHY GVSACEGCKG FFRRSIQKNM
VYTCHRDKNC IINKVTRNRC QYCRLQKCFE VGMSKESVRN DRNKKKKEVP KPECSESYTL
TPEVGELIEK VRKAHQETFP ALCQLGKYTT NNSSEQRVSL DIDLWDKFSE LSTKCIIKTV
EFAKQLPGFT TLTIADQITL LKAACLDILI LRICTRYTPE QDTMTFSDGL TLNRTQMHNA
GFGPLTDLVF AFANQLLPLE MDDAETGLLS AICLICGDRQ DLEQPDRVDM LQEPLLEALK
VYVRKRRPSR PHMFPKMLMK ITDLRSISAK GAERVITLKM EIPGSMPPLI QEMLENSEGL
DTLSGQPGGG GRDGGGLAPP PGSCSPSLSP SSNRSSPATH SP


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