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Retinoic acid receptor RXR-alpha (Nuclear receptor subfamily 2 group B member 1) (Retinoid X receptor alpha)

 RXRA_MOUSE              Reviewed;         467 AA.
P28700;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
01-DEC-1992, sequence version 1.
27-SEP-2017, entry version 180.
RecName: Full=Retinoic acid receptor RXR-alpha;
AltName: Full=Nuclear receptor subfamily 2 group B member 1;
AltName: Full=Retinoid X receptor alpha;
Name=Rxra; Synonyms=Nr2b1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], HETERODIMERIZATION WITH RARA, AND
FUNCTION.
PubMed=1310259; DOI=10.1016/0092-8674(92)90478-U;
Leid M., Kastner P., Lyons R., Nakshatri H., Saunders M.,
Zacharewsi T., Chen J.Y., Staub A., Garnier J.-M., Mader S.,
Chambon P.;
"Purification, cloning, and RXR identity of the HeLa cell factor with
which RAR or TR heterodimerizes to bind target sequences
efficiently.";
Cell 68:377-395(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION OF LIGAND.
PubMed=1312497; DOI=10.1101/gad.6.3.329;
Mangelsdorf D.J., Borgmeyer U., Heyman R.A., Zhou J.Y., Ong E.S.,
Oro A.E., Kakizuka A., Evans R.M.;
"Characterization of three RXR genes that mediate the action of 9-cis
retinoic acid.";
Genes Dev. 6:329-344(1992).
[3]
PROTEIN SEQUENCE OF 5-16; 27-46; 291-307 AND 446-465, AND SUBUNIT.
TISSUE=Adipose tissue;
PubMed=7838715; DOI=10.1093/nar/22.25.5628;
Tontonoz P., Graves R.A., Budavari A.I., Erdjument-Bromage H., Lui M.,
Hu E., Tempst P., Spiegelman B.M.;
"Adipocyte-specific transcription factor ARF6 is a heterodimeric
complex of two nuclear hormone receptors, PPAR gamma and RXR alpha.";
Nucleic Acids Res. 22:5628-5634(1994).
[4]
PHOSPHORYLATION AT SER-22; SER-61; SER-75; THR-87 AND SER-265,
FUNCTION, AND MUTAGENESIS OF SER-22; SER-44; SER-48; SER-54; SER-61;
SER-75; THR-87; SER-96; SER-101 AND SER-265.
PubMed=10383391; DOI=10.1074/jbc.274.27.18932;
Adam-Stitah S., Penna L., Chambon P., Rochette-Egly C.;
"Hyperphosphorylation of the retinoid X receptor alpha by activated c-
Jun NH2-terminal kinases.";
J. Biol. Chem. 274:18932-18941(1999).
[5]
INTERACTION WITH NCOA6.
PubMed=10788465; DOI=10.1074/jbc.275.18.13510;
Zhu Y.-J., Kan L., Qi C., Kanwar Y.S., Yeldandi A.V., Rao M.S.,
Reddy J.K.;
"Isolation and characterization of peroxisome proliferator-activated
receptor (PPAR) interacting protein (PRIP) as a coactivator for
PPAR.";
J. Biol. Chem. 275:13510-13516(2000).
[6]
PHOSPHORYLATION AT SER-22, FUNCTION, AND MUTAGENESIS OF SER-22.
PubMed=12032153; DOI=10.1074/jbc.M203623200;
Bastien J., Adam-Stitah S., Plassat J.L., Chambon P.,
Rochette-Egly C.;
"The phosphorylation site located in the A region of retinoic X
receptor alpha is required for the antiproliferative effect of
retinoic acid (RA) and the activation of RA target genes in F9
cells.";
J. Biol. Chem. 277:28683-28689(2002).
[7]
INTERACTION WITH ASXL1 AND NCOA1, AND MUTAGENESIS OF 455-PHE-LEU-456
AND 459-MET-LEU-460.
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).
[8]
INTERACTION WITH FAM120B.
PubMed=17595322; DOI=10.1210/me.2006-0520;
Li D., Kang Q., Wang D.-M.;
"Constitutive coactivator of peroxisome proliferator-activated
receptor (PPARgamma), a novel coactivator of PPARgamma that promotes
adipogenesis.";
Mol. Endocrinol. 21:2320-2333(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, and Liver;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[10]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 230-462 OF MUTANT ALA-318 IN
COMPLEX WITH H.SAPIENS RARA.
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).
[11]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 230-467 IN COMPLEX WITH RARB
AND MED1.
PubMed=15528208; DOI=10.1074/jbc.M409302200;
Pogenberg V., Guichou J.F., Vivat-Hannah V., Kammerer S., Perez E.,
Germain P., de Lera A.R., Gronemeyer H., Royer C.A., Bourguet W.;
"Characterization of the interaction between retinoic acid
receptor/retinoid X receptor (RAR/RXR) heterodimers and
transcriptional coactivators through structural and fluorescence
anisotropy studies.";
J. Biol. Chem. 280:1625-1633(2005).
-!- 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 RAR/RXR
heterodimers bind to the retinoic acid response elements (RARE)
composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. The high
affinity ligand for RXRs is 9-cis retinoic acid. RXRA serves as a
common heterodimeric partner for a number of nuclear receptors. 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. The RXRA/PPARA heterodimer
is required for PPARA transcriptional activity on fatty acid
oxidation genes such as ACOX1 and the P450 system genes.
{ECO:0000269|PubMed:10383391, ECO:0000269|PubMed:12032153,
ECO:0000269|PubMed:1310259}.
-!- SUBUNIT: Homodimer (By similarity). Heterodimer with RARA;
required for ligand-dependent retinoic acid receptor
transcriptional activity. Heterodimer with PPARA (via the leucine-
like zipper in the LBD); the interaction is required for PPARA
transcriptional activity. Also heterodimerizes with PPARG (By
similarity). Interacts with coactivator NCOA3, PELP1, SENP6, SFPQ,
DNTTIP2 and RNF8. Interacts with PRMT2. Interacts with
BHLHE40/DEC1, BHLHE41/DEC2, NCOR1 and NCOR2. Interacts in a
ligand-dependent fashion with MED1 (By similarity). Interacts with
coactivator NCOA6, and FAM120B. Interacts with ASXL1. Interacts in
a ligand-dependent fashion with NCOA1. {ECO:0000250,
ECO:0000269|PubMed:10788465, ECO:0000269|PubMed:10882070,
ECO:0000269|PubMed:15528208, ECO:0000269|PubMed:16606617,
ECO:0000269|PubMed:17595322, ECO:0000269|PubMed:7838715}.
-!- INTERACTION:
Q8IXJ9:ASXL1 (xeno); NbExp=2; IntAct=EBI-346715, EBI-1646500;
P59598:Asxl1; NbExp=2; IntAct=EBI-346715, EBI-5743705;
Q71SY5:MED25 (xeno); NbExp=3; IntAct=EBI-346715, EBI-394558;
P23246-1:SFPQ (xeno); NbExp=3; IntAct=EBI-346715, EBI-355463;
Q13501:SQSTM1 (xeno); NbExp=3; IntAct=EBI-346715, EBI-307104;
Q64337:Sqstm1; NbExp=3; IntAct=EBI-346715, EBI-645025;
P11473:VDR (xeno); NbExp=3; IntAct=EBI-346715, EBI-286357;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- DOMAIN: Composed of three domains: a modulating N-terminal or AF1
domain, a DNA-binding domain and a C-terminal ligand-binding or
AF2 domain.
-!- PTM: Phosphorylated on serine and threonine residues mainly in the
N-terminal modulating domain. Phosphorylated on Ser-28, in vitro,
by PKA. This phosphorylation is required for repression of cAMP-
mediated transcriptional activity of RARA (By similarity).
Constiutively phosphorylated on Ser-22 in the presence or absence
of ligand. Under stress conditions, hyperphosphorylated by
activated JNK on Ser-61, Ser-75, Thr-87 and Ser-265. {ECO:0000250,
ECO:0000269|PubMed:10383391, ECO:0000269|PubMed:12032153}.
-!- PTM: Sumoylation negatively regulates transcriptional activity.
Desumoylated specifically by SENP6 (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
subfamily. {ECO:0000305}.
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EMBL; M84817; AAA40080.1; -; mRNA.
EMBL; X66223; CAA46962.1; -; mRNA.
CCDS; CCDS15830.1; -.
PIR; S26668; S26668.
RefSeq; NP_035435.1; NM_011305.3.
UniGene; Mm.24624; -.
PDB; 1DKF; X-ray; 2.50 A; A=230-462.
PDB; 1XDK; X-ray; 2.90 A; A/E=230-467.
PDB; 3A9E; X-ray; 2.75 A; A=228-467.
PDBsum; 1DKF; -.
PDBsum; 1XDK; -.
PDBsum; 3A9E; -.
ProteinModelPortal; P28700; -.
SMR; P28700; -.
BioGrid; 203038; 16.
IntAct; P28700; 19.
MINT; MINT-2775018; -.
STRING; 10090.ENSMUSP00000076491; -.
BindingDB; P28700; -.
ChEMBL; CHEMBL3084; -.
GuidetoPHARMACOLOGY; 610; -.
iPTMnet; P28700; -.
PhosphoSitePlus; P28700; -.
MaxQB; P28700; -.
PaxDb; P28700; -.
PRIDE; P28700; -.
Ensembl; ENSMUST00000077257; ENSMUSP00000076491; ENSMUSG00000015846.
Ensembl; ENSMUST00000166775; ENSMUSP00000133044; ENSMUSG00000015846.
GeneID; 20181; -.
KEGG; mmu:20181; -.
UCSC; uc008ixs.1; mouse.
CTD; 6256; -.
MGI; MGI:98214; Rxra.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
GeneTree; ENSGT00760000118948; -.
HOGENOM; HOG000260821; -.
HOVERGEN; HBG005606; -.
InParanoid; P28700; -.
KO; K08524; -.
OMA; LTCGMKR; -.
OrthoDB; EOG091G0YX6; -.
PhylomeDB; P28700; -.
TreeFam; TF352097; -.
Reactome; R-MMU-159418; Recycling of bile acids and salts.
Reactome; R-MMU-192105; Synthesis of bile acids and bile salts.
Reactome; R-MMU-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
Reactome; R-MMU-193807; Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
Reactome; R-MMU-200425; Import of palmitoyl-CoA into the mitochondrial matrix.
Reactome; R-MMU-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
Reactome; R-MMU-211976; Endogenous sterols.
Reactome; R-MMU-381340; Transcriptional regulation of white adipocyte differentiation.
Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
Reactome; R-MMU-400206; Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
Reactome; R-MMU-442533; Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.
Reactome; R-MMU-5362517; Signaling by Retinoic Acid.
Reactome; R-MMU-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
ChiTaRS; Rxra; mouse.
EvolutionaryTrace; P28700; -.
PRO; PR:P28700; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000015846; -.
CleanEx; MM_RXRA; -.
ExpressionAtlas; P28700; baseline and differential.
Genevisible; P28700; MM.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0043235; C:receptor complex; ISO:MGI.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; IDA:BHF-UCL.
GO; GO:0004886; F:9-cis retinoic acid receptor activity; IDA:MGI.
GO; GO:0031490; F:chromatin DNA binding; IDA:MGI.
GO; GO:0050692; F:DBD domain binding; ISO:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0050693; F:LBD domain binding; ISO:MGI.
GO; GO:0016922; F:ligand-dependent nuclear receptor binding; ISO:MGI.
GO; GO:0042277; F:peptide binding; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; IPI:MGI.
GO; GO:0001972; F:retinoic acid binding; ISO:MGI.
GO; GO:0044323; F:retinoic acid-responsive element binding; ISO:MGI.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0004879; F:RNA polymerase II transcription factor activity, ligand-activated sequence-specific DNA binding; IDA:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; IGI:MGI.
GO; GO:0003707; F:steroid hormone receptor activity; IEA:InterPro.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IGI:MGI.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0042809; F:vitamin D receptor binding; ISO:MGI.
GO; GO:0070644; F:vitamin D response element binding; IEA:Ensembl.
GO; GO:0008270; F:zinc ion binding; ISO:MGI.
GO; GO:0060978; P:angiogenesis involved in coronary vascular morphogenesis; TAS:DFLAT.
GO; GO:0043010; P:camera-type eye development; IGI:MGI.
GO; GO:0055007; P:cardiac muscle cell differentiation; TAS:DFLAT.
GO; GO:0060038; P:cardiac muscle cell proliferation; IMP:MGI.
GO; GO:0007566; P:embryo implantation; IGI:MGI.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0003007; P:heart morphogenesis; TAS:DFLAT.
GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
GO; GO:0001893; P:maternal placenta development; IGI:MGI.
GO; GO:0060485; P:mesenchyme development; TAS:DFLAT.
GO; GO:0019048; P:modulation by virus of host morphology or physiology; ISO:MGI.
GO; GO:0010629; P:negative regulation of gene expression; TAS:DFLAT.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IGI:MGI.
GO; GO:0035357; P:peroxisome proliferator activated receptor signaling pathway; ISO:MGI.
GO; GO:0001890; P:placenta development; IMP:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:1901522; P:positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus; IDA:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IGI:MGI.
GO; GO:0045994; P:positive regulation of translational initiation by iron; IGI:MGI.
GO; GO:0051289; P:protein homotetramerization; ISO:MGI.
GO; GO:0060687; P:regulation of branching involved in prostate gland morphogenesis; IMP:MGI.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IGI:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0032526; P:response to retinoic acid; ISO:MGI.
GO; GO:0048384; P:retinoic acid receptor signaling pathway; IDA:MGI.
GO; GO:0060528; P:secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development; IMP:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0055012; P:ventricular cardiac muscle cell differentiation; IMP:MGI.
GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IMP:MGI.
GO; GO:0061032; P:visceral serous pericardium development; TAS:DFLAT.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR021780; Nuc_recep-AF1.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001723; Nuclear_hrmn_rcpt.
InterPro; IPR000003; Retinoid-X_rcpt/HNF4.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF11825; Nuc_recep-AF1; 1.
Pfam; PF00105; zf-C4; 1.
PRINTS; PR00545; RETINOIDXR.
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; Complete proteome; Direct protein sequencing;
DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
Receptor; Reference proteome; Transcription; Transcription regulation;
Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 467 Retinoic acid receptor RXR-alpha.
/FTId=PRO_0000053567.
DNA_BIND 140 205 Nuclear receptor. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 140 160 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 176 200 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
REGION 1 139 Modulating domain. {ECO:0000250}.
REGION 206 229 Hinge.
REGION 230 467 Ligand-binding domain.
MOD_RES 22 22 Phosphoserine.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:10383391,
ECO:0000269|PubMed:12032153}.
MOD_RES 28 28 Phosphoserine.
{ECO:0000250|UniProtKB:P19793}.
MOD_RES 61 61 Phosphoserine; by MAPK8 and MAPK9.
{ECO:0000269|PubMed:10383391}.
MOD_RES 75 75 Phosphoserine; by MAPK8 and MAPK9.
{ECO:0000269|PubMed:10383391}.
MOD_RES 87 87 Phosphothreonine; by MAPK8 and MAPK9.
{ECO:0000269|PubMed:10383391}.
MOD_RES 134 134 Phosphoserine.
{ECO:0000250|UniProtKB:P19793}.
MOD_RES 264 264 Phosphoserine.
{ECO:0000250|UniProtKB:P19793}.
MOD_RES 265 265 Phosphoserine; by MAPK8 and MAPK9.
{ECO:0000269|PubMed:10383391}.
CROSSLNK 4 4 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P19793}.
CROSSLNK 113 113 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
MUTAGEN 22 22 S->A: Loss of constituitive
phosphorylation. No effect on RXRA
transcriptional activity.
{ECO:0000269|PubMed:10383391,
ECO:0000269|PubMed:12032153}.
MUTAGEN 44 44 S->A: No effect on constituitive
phosphorylation.
{ECO:0000269|PubMed:10383391}.
MUTAGEN 48 48 S->A: No effect on constituitive
phosphorylation.
{ECO:0000269|PubMed:10383391}.
MUTAGEN 54 54 S->A: No effect on constituitive
phosphorylation.
{ECO:0000269|PubMed:10383391}.
MUTAGEN 61 61 S->A: No effect on constituitive
phosphorylation, decreased stress-induced
phosphorylation but no effect on RXRA
transcriptional activity. Abolishes
stress-induced phosphorylation but no
effect on RXRA transcriptional activity;
when associated with A-75 and A-87. No
effect on RXRA transcriptional activity.
{ECO:0000269|PubMed:10383391}.
MUTAGEN 75 75 S->A: No effect on constituitive
phosphorylation, decreased stress-induced
phosphorylation but no effect on RXRA
transcriptional activity. Abolishes
stress-induced phosphorylation but no
effect on RXRA transcriptional activity;
when associated with A-61 and A-87.
{ECO:0000269|PubMed:10383391}.
MUTAGEN 87 87 T->A: No effect on constituitive
phosphorylation, decreased stress-induced
phosphorylation but no effect on RXRA
transcriptional activity. Abolishes
stress-induced phosphorylation but no
effect on RXRA transcriptional activity;
when associated with A-61 and A-75.
phosphorylation. No effect on RXRA
transcriptional activity.
{ECO:0000269|PubMed:10383391}.
MUTAGEN 96 96 S->A: No effect on constituitive
phosphorylation.
{ECO:0000269|PubMed:10383391}.
MUTAGEN 101 101 S->A: No effect on constituitive
phosphorylation.
{ECO:0000269|PubMed:10383391}.
MUTAGEN 265 265 S->A: No effect on constiuitive
phosphorylation but loss of stress-
induced phosphorylation. No effect on
RXRA transcriptional activity.
{ECO:0000269|PubMed:10383391}.
MUTAGEN 455 456 FL->AA: Abolishes interaction with ASXL1
and NCOA1. {ECO:0000269|PubMed:16606617}.
MUTAGEN 459 460 ML->AA: Abolishes interaction with ASXL1
and NCOA1. {ECO:0000269|PubMed:16606617}.
HELIX 231 234 {ECO:0000244|PDB:1DKF}.
HELIX 237 246 {ECO:0000244|PDB:1DKF}.
HELIX 269 282 {ECO:0000244|PDB:1DKF}.
HELIX 284 289 {ECO:0000244|PDB:1DKF}.
TURN 292 296 {ECO:0000244|PDB:1DKF}.
HELIX 299 321 {ECO:0000244|PDB:1DKF}.
STRAND 323 330 {ECO:0000244|PDB:1DKF}.
STRAND 336 338 {ECO:0000244|PDB:1DKF}.
HELIX 339 344 {ECO:0000244|PDB:1DKF}.
HELIX 348 357 {ECO:0000244|PDB:1DKF}.
HELIX 359 364 {ECO:0000244|PDB:1DKF}.
HELIX 369 380 {ECO:0000244|PDB:1DKF}.
HELIX 391 412 {ECO:0000244|PDB:1DKF}.
HELIX 419 424 {ECO:0000244|PDB:1DKF}.
HELIX 426 438 {ECO:0000244|PDB:1DKF}.
TURN 439 443 {ECO:0000244|PDB:1DKF}.
HELIX 447 449 {ECO:0000244|PDB:1DKF}.
HELIX 452 461 {ECO:0000244|PDB:1DKF}.
SEQUENCE 467 AA; 51217 MW; 0AF62396BCDC87DB CRC64;
MDTKHFLPLD FSTQVNSSSL NSPTGRGSMA VPSLHPSLGP GIGSPLGSPG QLHSPISTLS
SPINGMGPPF SVISSPMGPH SMSVPTTPTL GFGTGSPQLN SPMNPVSSTE DIKPPLGLNG
VLKVPAHPSG NMASFTKHIC AICGDRSSGK HYGVYSCEGC KGFFKRTVRK DLTYTCRDNK
DCLIDKRQRN RCQYCRYQKC LAMGMKREAV QEERQRGKDR NENEVESTSS ANEDMPVEKI
LEAELAVEPK TETYVEANMG LNPSSPNDPV TNICQAADKQ LFTLVEWAKR IPHFSELPLD
DQVILLRAGW NELLIASFSH RSIAVKDGIL LATGLHVHRN SAHSAGVGAI FDRVLTELVS
KMRDMQMDKT ELGCLRAIVL FNPDSKGLSN PAEVEALREK VYASLEAYCK HKYPEQPGRF
AKLLLRLPAL RSIGLKCLEH LFFFKLIGDT PIDTFLMEML EAPHQAT


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