ESR1_RAT
ID ESR1_RAT Reviewed; 600 AA.
AC P06211;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=Estrogen receptor;
DE Short=ER;
DE AltName: Full=ER-alpha;
DE AltName: Full=Estradiol receptor;
DE AltName: Full=Nuclear receptor subfamily 3 group A member 1;
GN Name=Esr1; Synonyms=Esr, Estr, Nr3a1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar;
RA Muramatsu M.;
RL Submitted (MAR-1987) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3031601; DOI=10.1093/nar/15.6.2499;
RA Koike S., Sakai M.;
RT "Molecular cloning and characterization of rat estrogen receptor cDNA.";
RL Nucleic Acids Res. 15:2499-2513(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Uterus;
RA Maggi A.M.A.;
RL Submitted (JUN-1991) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INTERACTION WITH UBE1C.
RX PubMed=11818503; DOI=10.1210/mend.16.2.0778;
RA Fan M., Long X., Bailey J.A., Reed C.A., Osborne E., Gize E.A., Kirk E.A.,
RA Bigsby R.M., Nephew K.P.;
RT "The activating enzyme of NEDD8 inhibits steroid receptor function.";
RL Mol. Endocrinol. 16:315-330(2002).
RN [5]
RP INTERACTION WITH MAP1S.
RX PubMed=17658481; DOI=10.1016/j.bbrc.2007.06.179;
RA Eriksson M., Samuelsson H., Samuelsson E.-B., Liu L., McKeehan W.L.,
RA Benedikz E., Sundstroem E.;
RT "The NMDAR subunit NR3A interacts with microtubule-associated protein 1S in
RT the brain.";
RL Biochem. Biophys. Res. Commun. 361:127-132(2007).
RN [6]
RP INTERACTION WITH DNAAF4.
RX PubMed=19423554; DOI=10.1093/hmg/ddp215;
RA Massinen S., Tammimies K., Tapia-Paez I., Matsson H., Hokkanen M.E.,
RA Soederberg O., Landegren U., Castren E., Gustafsson J.A., Treuter E.,
RA Kere J.;
RT "Functional interaction of DYX1C1 with estrogen receptors suggests
RT involvement of hormonal pathways in dyslexia.";
RL Hum. Mol. Genet. 18:2802-2812(2009).
CC -!- FUNCTION: Nuclear hormone receptor. The steroid hormones and their
CC receptors are involved in the regulation of eukaryotic gene expression
CC and affect cellular proliferation and differentiation in target
CC tissues. Ligand-dependent nuclear transactivation involves either
CC direct homodimer binding to a palindromic estrogen response element
CC (ERE) sequence or association with other DNA-binding transcription
CC factors, such as AP-1/c-Jun, c-Fos, ATF-2, Sp1 and Sp3, to mediate ERE-
CC independent signaling. Ligand binding induces a conformational change
CC allowing subsequent or combinatorial association with multiprotein
CC coactivator complexes through LXXLL motifs of their respective
CC components. Mutual transrepression occurs between the estrogen receptor
CC (ER) and NF-kappa-B in a cell-type specific manner. Decreases NF-kappa-
CC B DNA-binding activity and inhibits NF-kappa-B-mediated transcription
CC from the IL6 promoter and displace RELA/p65 and associated coregulators
CC from the promoter. Recruited to the NF-kappa-B response element of the
CC CCL2 and IL8 promoters and can displace CREBBP. Present with NF-kappa-B
CC components RELA/p65 and NFKB1/p50 on ERE sequences. Can also act
CC synergistically with NF-kappa-B to activate transcription involving
CC respective recruitment adjacent response elements; the function
CC involves CREBBP. Can activate the transcriptional activity of TFF1.
CC Also mediates membrane-initiated estrogen signaling involving various
CC kinase cascades. Essential for MTA1-mediated transcriptional regulation
CC of BRCA1 and BCAS3 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with BCAS3. Binds DNA as a homodimer (By
CC similarity). Can form a heterodimer with ESR2 (By similarity).
CC Interacts with coactivator NCOA5. Interacts with PELP1, the interaction
CC is enhanced by 17-beta-estradiol; the interaction increases ESR1
CC transcriptional activity (By similarity). Interacts with NCOA7; the
CC interaction is ligand-inducible. Interacts with AKAP13, CUEDC2, HEXIM1,
CC KDM5A, MAP1S, SMARD1, and UBE1C. Interacts with MUC1; the interaction
CC is stimulated by 7 beta-estradiol (E2) and enhances ESR1-mediated
CC transcription. Interacts with DNTTIP2, and UIMC1. Interacts with
CC KMT2D/MLL2. Interacts with ATAD2; the interaction is enhanced by
CC estradiol. Interacts with KIF18A and LDB1. Interacts with RLIM (via its
CC C-terminus). Interacts with MACROD1. Interacts with SH2D4A and PLCG.
CC Interacts with SH2D4A; the interaction blocks binding to PLCG and
CC inhibits estrogen-induced cell proliferation. Interacts with DYNLL1.
CC Interacts with CCDC62; the interaction requires estradiol and appears
CC to enhance the transcription of target genes. Interacts with NR2C1; the
CC interaction prevents homodimerization of ESR1 and suppresses its
CC transcriptional activity and cell growth. Interacts with DNAAF4.
CC Interacts with PRMT2. Interacts with RBFOX2. Interacts with EP300; the
CC interaction is estrogen-dependent and enhanced by CITED1. Interacts
CC with CITED1; the interaction is estrogen-dependent (By similarity).
CC Interacts with FAM120B, FOXL2, PHB2 and SLC30A9. Interacts with
CC coactivators NCOA3 and NCOA6. Interacts with STK3/MST2 only in the
CC presence of SAV1 and vice-versa. Binds to CSNK1D. Interacts with NCOA2;
CC NCOA2 can interact with ESR1 AF-1 and AF-2 domains simultaneously and
CC mediate their transcriptional synergy. Interacts with DDX5. Interacts
CC with NCOA1; the interaction seems to require a self-association of N-
CC terminal and C-terminal regions. Interacts with ZNF366, DDX17, NFKB1,
CC RELA, SP1 and SP3. Interacts with NRIP1 (By similarity). Interacts with
CC GPER1; the interaction occurs in an estrogen-dependent manner (By
CC similarity). Interacts with TRIP4 (ufmylated); estrogen dependent (By
CC similarity). Interacts with LMTK3; the interaction phosphorylates ESR1
CC (in vitro) and protects it against proteasomal degradation. Interacts
CC with CCAR2 (via N-terminus) in a ligand-independent manner. Interacts
CC with ZFHX3 (By similarity). Interacts with SFR1 in a ligand-dependent
CC and -independent manner (By similarity). Interacts with DCAF13, LATS1
CC and DCAF1; regulates ESR1 ubiquitination and ubiquitin-mediated
CC proteasomal degradation. Interacts (via DNA-binding domain) with POU4F2
CC (C-terminus); this interaction increases the estrogen receptor ESR1
CC transcriptional activity in a DNA- and ligand 17-beta-estradiol-
CC independent manner (By similarity). Interacts with ESRRB isoform 1 (By
CC similarity). Interacts with UBE3A and WBP2 (By similarity). Interacts
CC with GTF2B (By similarity). Interacts with RBM39 (By similarity). In
CC the absence of hormonal ligand, interacts with TACC1 (By similarity).
CC Interacts with PI3KR1 or PI3KR2 and PTK2/FAK1 (By similarity).
CC Interacts with SRC (By similarity). {ECO:0000250|UniProtKB:P03372,
CC ECO:0000250|UniProtKB:P19785, ECO:0000269|PubMed:17658481,
CC ECO:0000269|PubMed:19423554}.
CC -!- INTERACTION:
CC P06211; P50503: St13; NbExp=4; IntAct=EBI-7983651, EBI-917694;
CC P06211; P62989: Ubb; NbExp=5; IntAct=EBI-7983651, EBI-7038538;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
CC Cytoplasm {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cell membrane
CC {ECO:0000250}. Note=Colocalizes with ZDHHC7 and ZDHHC21 in the Golgi
CC apparatus where most probably palmitoylation occurs. Associated with
CC the plasma membrane when palmitoylated. {ECO:0000250}.
CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC DNA-binding domain and a C-terminal ligand-binding domain. The
CC modulating domain, also known as A/B or AF-1 domain has a ligand-
CC independent transactivation function. The C-terminus contains a ligand-
CC dependent transactivation domain, also known as E/F or AF-2 domain
CC which overlaps with the ligand binding domain. AF-1 and AF-2 activate
CC transcription independently and synergistically and act in a
CC promoter- and cell-specific manner (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated by cyclin A/CDK2 and CK1. Phosphorylation probably
CC enhances transcriptional activity. Dephosphorylation at Ser-123 by
CC PPP5C inhibits its transactivation activity (By similarity).
CC Phosphorylated by LMTK3 (in vitro) (By similarity).
CC {ECO:0000250|UniProtKB:P03372}.
CC -!- PTM: Ubiquitinated; regulated by LATS1 via DCAF1 it leads to ESR1
CC proteasomal degradation. Deubiquitinated by OTUB1.
CC {ECO:0000250|UniProtKB:P03372}.
CC -!- PTM: Palmitoylated at Cys-452 by ZDHHC7 and ZDHHC21. This modification
CC is required for plasma membrane targeting and for rapid intracellular
CC signaling via ERK and AKT kinases and cAMP generation, but not for
CC signaling mediated by the nuclear hormone receptor (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Dimethylated by PRMT1 at Arg-265. The methylation may favor
CC cytoplasmic localization. Demethylated by JMJD6 at Arg-265.
CC {ECO:0000250|UniProtKB:P03372}.
CC -!- MISCELLANEOUS: In the absence of ligand, steroid hormone receptors are
CC thought to be weakly associated with nuclear components; hormone
CC binding greatly increases receptor affinity. The hormone-receptor
CC complex appears to recognize discrete DNA sequences upstream of
CC transcriptional start sites.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y00102; CAA68287.1; -; mRNA.
DR EMBL; X61098; CAA43411.1; -; mRNA.
DR PIR; S07379; QRRTE.
DR RefSeq; NP_036821.1; NM_012689.1.
DR AlphaFoldDB; P06211; -.
DR SMR; P06211; -.
DR BioGRID; 247000; 11.
DR CORUM; P06211; -.
DR DIP; DIP-41279N; -.
DR IntAct; P06211; 6.
DR MINT; P06211; -.
DR STRING; 10116.ENSRNOP00000026350; -.
DR BindingDB; P06211; -.
DR ChEMBL; CHEMBL2724; -.
DR DrugCentral; P06211; -.
DR GuidetoPHARMACOLOGY; 620; -.
DR GlyGen; P06211; 2 sites.
DR iPTMnet; P06211; -.
DR PhosphoSitePlus; P06211; -.
DR SwissPalm; P06211; -.
DR PaxDb; P06211; -.
DR GeneID; 24890; -.
DR KEGG; rno:24890; -.
DR UCSC; RGD:2581; rat.
DR CTD; 2099; -.
DR RGD; 2581; Esr1.
DR eggNOG; KOG3575; Eukaryota.
DR InParanoid; P06211; -.
DR PhylomeDB; P06211; -.
DR Reactome; R-RNO-1251985; Nuclear signaling by ERBB4.
DR Reactome; R-RNO-1257604; PIP3 activates AKT signaling.
DR Reactome; R-RNO-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-RNO-4090294; SUMOylation of intracellular receptors.
DR Reactome; R-RNO-5689896; Ovarian tumor domain proteases.
DR Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-RNO-8866910; TFAP2 (AP-2) family regulates transcription of growth factors and their receptors.
DR Reactome; R-RNO-8931987; RUNX1 regulates estrogen receptor mediated transcription.
DR Reactome; R-RNO-8939211; ESR-mediated signaling.
DR Reactome; R-RNO-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-RNO-9018519; Estrogen-dependent gene expression.
DR PRO; PR:P06211; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0000791; C:euchromatin; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0030315; C:T-tubule; IDA:RGD.
DR GO; GO:0043195; C:terminal bouton; IDA:RGD.
DR GO; GO:0097550; C:transcription preinitiation complex; ISO:RGD.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0051117; F:ATPase binding; ISO:RGD.
DR GO; GO:0008013; F:beta-catenin binding; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IMP:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; IPI:RGD.
DR GO; GO:0034056; F:estrogen response element binding; ISO:RGD.
DR GO; GO:0042562; F:hormone binding; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0030284; F:nuclear estrogen receptor activity; IDA:RGD.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISO:RGD.
DR GO; GO:0004879; F:nuclear receptor activity; ISO:RGD.
DR GO; GO:0003707; F:nuclear steroid receptor activity; IDA:RGD.
DR GO; GO:0036312; F:phosphatidylinositol 3-kinase regulatory subunit binding; IPI:RGD.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0005496; F:steroid binding; IDA:UniProtKB.
DR GO; GO:0017025; F:TBP-class protein binding; ISO:RGD.
DR GO; GO:0001093; F:TFIIB-class transcription factor binding; ISO:RGD.
DR GO; GO:0001223; F:transcription coactivator binding; IPI:RGD.
DR GO; GO:0001221; F:transcription coregulator binding; ISO:RGD.
DR GO; GO:0001222; F:transcription corepressor binding; ISO:RGD.
DR GO; GO:0031798; F:type 1 metabotropic glutamate receptor binding; IPI:RGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0008209; P:androgen metabolic process; ISO:RGD.
DR GO; GO:0001547; P:antral ovarian follicle growth; ISO:RGD.
DR GO; GO:1990375; P:baculum development; IEP:RGD.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IDA:UniProtKB.
DR GO; GO:0071391; P:cellular response to estrogen stimulus; ISO:RGD.
DR GO; GO:0046697; P:decidualization; IEP:RGD.
DR GO; GO:0002064; P:epithelial cell development; ISO:RGD.
DR GO; GO:0060750; P:epithelial cell proliferation involved in mammary gland duct elongation; ISO:RGD.
DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; ISO:RGD.
DR GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0008584; P:male gonad development; IEP:RGD.
DR GO; GO:0060749; P:mammary gland alveolus development; ISO:RGD.
DR GO; GO:0060745; P:mammary gland branching involved in pregnancy; ISO:RGD.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0046325; P:negative regulation of glucose import; IDA:RGD.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:1903799; P:negative regulation of miRNA maturation; ISO:RGD.
DR GO; GO:1901215; P:negative regulation of neuron death; IDA:RGD.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IMP:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0090209; P:negative regulation of triglyceride metabolic process; IDA:RGD.
DR GO; GO:0002076; P:osteoblast development; IEP:RGD.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:UniProtKB.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IMP:RGD.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:RGD.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:RGD.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; ISS:UniProtKB.
DR GO; GO:0010863; P:positive regulation of phospholipase C activity; IDA:UniProtKB.
DR GO; GO:0045899; P:positive regulation of RNA polymerase II transcription preinitiation complex assembly; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0060527; P:prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis; ISO:RGD.
DR GO; GO:0060523; P:prostate epithelial cord elongation; ISO:RGD.
DR GO; GO:0071168; P:protein localization to chromatin; ISO:RGD.
DR GO; GO:0042981; P:regulation of apoptotic process; ISO:RGD.
DR GO; GO:0060687; P:regulation of branching involved in prostate gland morphogenesis; ISO:RGD.
DR GO; GO:0050727; P:regulation of inflammatory response; ISO:RGD.
DR GO; GO:0043523; P:regulation of neuron apoptotic process; IDA:RGD.
DR GO; GO:0034121; P:regulation of toll-like receptor signaling pathway; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0043627; P:response to estrogen; ISO:RGD.
DR GO; GO:0060009; P:Sertoli cell development; IEP:RGD.
DR GO; GO:0060011; P:Sertoli cell proliferation; IMP:RGD.
DR GO; GO:0048863; P:stem cell differentiation; ISO:RGD.
DR GO; GO:0060065; P:uterus development; ISO:RGD.
DR GO; GO:0060068; P:vagina development; ISO:RGD.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR024178; Est_rcpt/est-rel_rcp.
DR InterPro; IPR001292; Estr_rcpt.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR024736; Oestrogen-typ_rcpt_final_C_dom.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF12743; ESR1_C; 1.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF02159; Oest_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PIRSF; PIRSF500101; ER-a; 1.
DR PIRSF; PIRSF002527; ER-like_NR; 1.
DR PRINTS; PR00543; OESTROGENR.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 1: Evidence at protein level;
KW Activator; Cell membrane; Cytoplasm; DNA-binding; Glycoprotein;
KW Golgi apparatus; Lipid-binding; Lipoprotein; Membrane; Metal-binding;
KW Methylation; Nucleus; Palmitate; Phosphoprotein; Receptor;
KW Reference proteome; Steroid-binding; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..600
FT /note="Estrogen receptor"
FT /id="PRO_0000053623"
FT DOMAIN 316..552
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 190..255
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 190..210
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 226..250
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..189
FT /note="Modulating (transactivation AF-1); mediates
FT interaction with MACROD1"
FT /evidence="ECO:0000250"
FT REGION 35..179
FT /note="Interaction with DDX5; self-association"
FT /evidence="ECO:0000250"
FT REGION 35..47
FT /note="Required for interaction with NCOA1"
FT /evidence="ECO:0000250"
FT REGION 148..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..315
FT /note="Mediates interaction with DNTTIP2"
FT /evidence="ECO:0000250"
FT REGION 256..315
FT /note="Hinge"
FT REGION 267..600
FT /note="Interaction with AKAP13"
FT /evidence="ECO:0000250"
FT REGION 269..600
FT /note="Self-association"
FT /evidence="ECO:0000250"
FT REGION 316..600
FT /note="Transactivation AF-2"
FT /evidence="ECO:0000250"
FT REGION 558..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 109
FT /note="Phosphoserine; by CDK2"
FT /evidence="ECO:0000250|UniProtKB:P03372"
FT MOD_RES 111
FT /note="Phosphoserine; by CDK2"
FT /evidence="ECO:0000250|UniProtKB:P03372"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P03372"
FT MOD_RES 172
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:P03372"
FT MOD_RES 265
FT /note="Asymmetric dimethylarginine; by PRMT1"
FT /evidence="ECO:0000250|UniProtKB:P03372"
FT MOD_RES 542
FT /note="Phosphotyrosine; by Tyr-kinases"
FT /evidence="ECO:0000250|UniProtKB:P03372"
FT LIPID 452
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 10
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 576
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT CONFLICT 488
FT /note="N -> T (in Ref. 3; CAA43411)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 600 AA; 67030 MW; C9C7D8CACE0F57D8 CRC64;
MTMTLHTKAS GMALLHQIQG NELEPLNRPQ LKMPMERALG EVYVDNSKPA VFNYPEGAAY
EFNAAAAAAA AGASAPVYGQ SSITYGPGSE AAAFGANSLG AFPQLNSVSP SPLMLLHPPP
HVSPFLHPHG HQVPYYLENE PSAYAVRDTG PPAFYRSNSD NRRQNGRERL SSSSEKGNMI
MESAKETRYC AVCNDYASGY HYGVWSCEGC KAFFKRSIQG HNDYMCPATN QCTIDKNRRK
SCQACRLRKC YEVGMMKGGI RKDRRGGRML KHKRQRDDLE GRNEMGTSGD MRAANLWPSP
LVIKHTKKNS PALSLTADQM VSALLDAEPP LIYSEYDPSR PFSEASMMGL LTNLADRELV
HMINWAKRVP GFGDLNLHDQ VHLLECAWLE ILMIGLVWRS MEHPGKLLFA PNLLLDRNQG
KCVEGMVEIF DMLLATSSRF RMMNLQGEEF VCLKSIILLN SGVYTFLSST LKSLEEKDHI
HRVLDKINDT LIHLMAKAGL TLQQQHRRLA QLLLILSHIR HMSNKGMEHL YNMKCKNVVP
LYDLLLEMLD AHRLHAPASR MGVPPEEPSQ SQLTTTSSTS AHSLQTYYIP PEAEGFPNTI
