P19785 · ESR1_MOUSE
- ProteinEstrogen receptor
- GeneEsr1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids599 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Ligand-dependent nuclear transactivation involves either direct homodimer binding to a palindromic estrogen response element (ERE) sequence or association with other DNA-binding transcription factors, such as AP-1/c-Jun, c-Fos, ATF-2, Sp1 and Sp3, to mediate ERE-independent signaling. Ligand binding induces a conformational change allowing subsequent or combinatorial association with multiprotein coactivator complexes through LXXLL motifs of their respective components. Mutual transrepression occurs between the estrogen receptor (ER) and NF-kappa-B in a cell-type specific manner. Decreases NF-kappa-B DNA-binding activity and inhibits NF-kappa-B-mediated transcription from the IL6 promoter and displace RELA/p65 and associated coregulators from the promoter. Recruited to the NF-kappa-B response element of the CCL2 and IL8 promoters and can displace CREBBP. Present with NF-kappa-B components RELA/p65 and NFKB1/p50 on ERE sequences. Can also act synergistically with NF-kappa-B to activate transcription involving respective recruitment adjacent response elements; the function involves CREBBP. Can activate the transcriptional activity of TFF1. Also mediates membrane-initiated estrogen signaling involving various kinase cascades. Essential for MTA1-mediated transcriptional regulation of BRCA1 and BCAS3. Maintains neuronal survival in response to ischemic reperfusion injury when in the presence of circulating estradiol (17-beta-estradiol/E2) (By similarity).
Features
Showing features for dna binding, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
DNA binding | 189-254 | Nuclear receptor | ||||
Sequence: CAVCNDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQACRLRKCYEVGM | ||||||
Binding site | 357 | 17beta-estradiol (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 398 | 17beta-estradiol (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 528 | 17beta-estradiol (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameEstrogen receptor
- Short namesER
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP19785
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Colocalizes with ZDHHC7 and ZDHHC21 in the Golgi apparatus where most probably palmitoylation occurs. Associated with the plasma membrane when palmitoylated.
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 362 | No effect on transcriptional activity and estrogen-induced interaction with NCOA1. Abolishes estrogen-induced interaction with NCOA1; when associated with A-376 and A-380. | ||||
Sequence: I → A | ||||||
Mutagenesis | 362 | Abolishes transcriptional activity and estrogen-induced interaction with NCOA1. | ||||
Sequence: I → D | ||||||
Mutagenesis | 366 | Greatly reduces transcriptional activity and estrogen-induced interaction with NCOA1. | ||||
Sequence: K → A | ||||||
Mutagenesis | 366 | Abolishes transcriptional activity and estrogen-induced interaction with NCOA1. | ||||
Sequence: K → D | ||||||
Mutagenesis | 366 | Reduces transcriptional activity and estrogen-induced interaction with NCOA1. | ||||
Sequence: K → L | ||||||
Mutagenesis | 371 | Abolishes estrogen-dependent NF-kappa B transcriptional repression, impairs transcriptional activity, abolishes estrogen-induced interaction with NCOA1. | ||||
Sequence: F → A | ||||||
Mutagenesis | 376 | Reduces transcriptional activity, no effect on estrogen-induced interaction with NCOA1. Abolishes estrogen-induced interaction with NCOA1; when associated with A-362 and A-380. | ||||
Sequence: L → A | ||||||
Mutagenesis | 376 | Reduces transcriptional activity and estrogen-induced interaction with NCOA1. | ||||
Sequence: L → D | ||||||
Mutagenesis | 380 | No effect on transcriptional activity and estrogen-induced interaction with NCOA1. Abolishes estrogen-induced interaction with NCOA1; when associated with A-362 and A-376. | ||||
Sequence: V → A | ||||||
Mutagenesis | 380 | Abolishes transcriptional activity and estrogen-induced interaction with NCOA1. | ||||
Sequence: V → D | ||||||
Mutagenesis | 451 | Loss of ZDHHC7 and ZDHHC21 binding. Loss of palmitoylation. | ||||
Sequence: C → A | ||||||
Mutagenesis | 508 | Reduces DNA-binding, attenuates transcriptional activity, does not effect estrogen-dependent NF-kappa B transcriptional repression; when associated with E-512 and E-515. | ||||
Sequence: L → A | ||||||
Mutagenesis | 508 | Abolishes DNA-binding, abolishes transcriptional activity and estrogen-dependent NF-kappa B transcriptional repression; when associated with E-512 and E-515. | ||||
Sequence: L → E | ||||||
Mutagenesis | 509 | Reduces DNA-binding,, attenuates transcriptional activity, does not effect estrogen-dependent NF-kappa B transcriptional repression. | ||||
Sequence: A → E | ||||||
Mutagenesis | 512 | Reduces DNA-binding, attenuates transcriptional activity, does not effect estrogen-dependent NF-kappa B transcriptional repression; when associated with E-508 and E-515. | ||||
Sequence: L → A | ||||||
Mutagenesis | 512 | Abolishes DNA-binding, abolishes transcriptional activity and estrogen-dependent NF-kappa B transcriptional repression; when associated with E-508 and E-515. | ||||
Sequence: L → E | ||||||
Mutagenesis | 515 | Reduces DNA-binding, attenuates transcriptional activity, does not effect estrogen-dependent NF-kappa B transcriptional repression; when associated with E-508 and E-512. | ||||
Sequence: L → A | ||||||
Mutagenesis | 515 | Abolishes DNA-binding, abolishes transcriptional activity and estrogen-dependent NF-kappa B transcriptional repression; when associated with E-508 and E-512. | ||||
Sequence: L → E | ||||||
Mutagenesis | 525 | Abolishes estrogen binding; impairs repression of NF-kappa activity. | ||||
Sequence: G → R | ||||||
Mutagenesis | 542 | Abolishes estrogen-dependent NF-kappa B transcriptional repression, impairs transcriptional activity, impairs estrogen-induced interaction with NCOA1; when associated with Q-546 and N-548. | ||||
Sequence: D → N | ||||||
Mutagenesis | 543 | Abolishes estrogen-induced interaction with NCOA1. | ||||
Sequence: L → A | ||||||
Mutagenesis | 543-544 | Abolishes estrogen-dependent NF-kappa B transcriptional repression, abolishes estrogen-induced interaction with NCOA1. | ||||
Sequence: LL → AA | ||||||
Mutagenesis | 546 | Abolishes estrogen-dependent NF-kappa B transcriptional repression, impairs transcriptional activity, impairs estrogen-induced interaction with NCOA1; when associated with N-542 and N-548. | ||||
Sequence: E → Q | ||||||
Mutagenesis | 547-548 | No effect on estrogen-dependent NF-kappa B transcriptional repression, greatly impairs transcriptional activity, abolishes estrogen-induced interaction with NCOA1. | ||||
Sequence: ML → AA | ||||||
Mutagenesis | 549 | Abolishes estrogen-dependent NF-kappa B transcriptional repression, impairs transcriptional activity, impairs estrogen-induced interaction with NCOA1; when associated with N-542 and Q-546. | ||||
Sequence: D → N | ||||||
Natural variant | 591 | in strain: SJL/J | ||||
Sequence: E → Q |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 36 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for chain, glycosylation, modified residue, lipidation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000053621 | 1-599 | Estrogen receptor | |||
Sequence: MTMTLHTKASGMALLHQIQGNELEPLNRPQLKMPMERALGEVYVDNSKPTVFNYPEGAAYEFNAAAAAAAAASAPVYGQSGIAYGPGSEAAAFSANSLGAFPQLNSVSPSPLMLLHPPPQLSPFLHPHGQQVPYYLENEPSAYAVRDTGPPAFYRSNSDNRRQNGRERLSSSNEKGNMIMESAKETRYCAVCNDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQACRLRKCYEVGMMKGGIRKDRRGGRMLKHKRQRDDLEGRNEMGASGDMRAANLWPSPLVIKHTKKNSPALSLTADQMVSALLDAEPPMIYSEYDPSRPFSEASMMGLLTNLADRELVHMINWAKRVPGFGDLNLHDQVHLLECAWLEILMIGLVWRSMEHPGKLLFAPNLLLDRNQGKCVEGMVEIFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGVYTFLSSTLKSLEEKDHIHRVLDKITDTLIHLMAKAGLTLQQQHRRLAQLLLILSHIRHMSNKGMEHLYNMKCKNVVPLYDLLLEMLDAHRLHAPASRMGVPPEEPSQTQLATTSSTSAHSLQTYYIPPEAEGFPNTI | ||||||
Glycosylation | 10 | O-linked (GlcNAc) serine | ||||
Sequence: S | ||||||
Glycosylation | 50 | O-linked (GlcNAc) threonine | ||||
Sequence: T | ||||||
Modified residue | 108 | Phosphoserine; by CDK2 | ||||
Sequence: S | ||||||
Modified residue | 110 | Phosphoserine; by CDK2 | ||||
Sequence: S | ||||||
Modified residue | 122 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 171 | Phosphoserine; by CK2 | ||||
Sequence: S | ||||||
Modified residue | 264 | Asymmetric dimethylarginine; by PRMT1 | ||||
Sequence: R | ||||||
Lipidation | 451 | S-palmitoyl cysteine | ||||
Sequence: C | ||||||
Modified residue | 541 | Phosphotyrosine; by Tyr-kinases | ||||
Sequence: Y | ||||||
Glycosylation | CAR_000137 | 575 | O-linked (GlcNAc) threonine | |||
Sequence: T |
Post-translational modification
Phosphorylated by cyclin A/CDK2 and CK1. Phosphorylation probably enhances transcriptional activity. Dephosphorylation at Ser-122 by PPP5C inhibits its transactivation activity (By similarity).
Phosphorylated by LMTK3 (in vitro) (By similarity).
Phosphorylated by LMTK3 (in vitro) (By similarity).
Ubiquitinated. Deubiquitinated by OTUB1 (By similarity).
Palmitoylated at Cys-451 by ZDHHC7 and ZDHHC21. This modification is required for plasma membrane targeting and for rapid intracellular signaling via ERK and AKT kinases and cAMP generation, but not for signaling mediated by the nuclear hormone receptor.
Ubiquitinated; regulated by LATS1 via DCAF1 it leads to ESR1 proteasomal degradation. Deubiquitinated by OTUB1 (By similarity).
Ubiquitinated by STUB1/CHIP; in the CA1 hippocampal region following loss of endogenous circulating estradiol (17-beta-estradiol/E2) (By similarity).
Ubiquitinated by UBR5, leading to its degradation: UBR5 specifically recognizes and binds ligand-bound ESR1 when it is not associated with coactivators (NCOAs). In presence of NCOAs, the UBR5-degron is not accessible, preventing its ubiquitination and degradation (By similarity).
Ubiquitinated by STUB1/CHIP; in the CA1 hippocampal region following loss of endogenous circulating estradiol (17-beta-estradiol/E2) (By similarity).
Ubiquitinated by UBR5, leading to its degradation: UBR5 specifically recognizes and binds ligand-bound ESR1 when it is not associated with coactivators (NCOAs). In presence of NCOAs, the UBR5-degron is not accessible, preventing its ubiquitination and degradation (By similarity).
Dimethylated by PRMT1 at Arg-264. The methylation may favor cytoplasmic localization. Demethylated by JMJD6 at Arg-264.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Interacts with BCAS3. Binds DNA as a homodimer (By similarity).
Can form a heterodimer with ESR2 (By similarity).
Interacts with coactivator NCOA5. Interacts with PELP1, the interaction is enhanced by 17-beta-estradiol; the interaction increases ESR1 transcriptional activity (By similarity).
Interacts with NCOA7; the interaction is ligand-inducible. Interacts with AKAP13, CUEDC2, HEXIM1, KDM5A, MAP1S, SMARD1, and UBE1C. Interacts with MUC1; the interaction is stimulated by 7 beta-estradiol (E2) and enhances ESR1-mediated transcription. Interacts with DNTTIP2, and UIMC1. Interacts with KMT2D/MLL2. Interacts with ATAD2; the interaction is enhanced by estradiol. Interacts with KIF18A and LDB1. Interacts with RLIM (via its C-terminus). Interacts with MACROD1. Interacts with SH2D4A and PLCG. Interacts with SH2D4A; the interaction blocks binding to PLCG and inhibits estrogen-induced cell proliferation. Interacts with DYNLL1. Interacts with CCDC62; the interaction requires estradiol and appears to enhance the transcription of target genes. Interacts with NR2C1; the interaction prevents homodimerization of ESR1 and suppresses its transcriptional activity and cell growth. Interacts with DNAAF4. Interacts with PRMT2. Interacts with RBFOX2. Interacts with EP300; the interaction is estrogen-dependent and enhanced by CITED1. Interacts with CITED1; the interaction is estrogen-dependent (By similarity).
Interacts with FAM120B, FOXL2, PHB2 and SLC30A9. Interacts with coactivators NCOA3 and NCOA6. Interacts with STK3/MST2 only in the presence of SAV1 and vice-versa. Binds to CSNK1D. Interacts with NCOA2; NCOA2 can interact with ESR1 AF-1 and AF-2 domains simultaneously and mediate their transcriptional synergy. Interacts with DDX5. Interacts with NCOA1; the interaction seems to require a self-association of N-terminal and C-terminal regions. Interacts with ZNF366, DDX17, NFKB1, RELA, SP1 and SP3. Interacts with NRIP1 (By similarity).
Interacts with GPER1; the interaction occurs in an estrogen-dependent manner. Interacts with CLOCK and the interaction is stimulated by estrogen (By similarity).
Interacts with BCAS3. Interacts with TRIP4 (ufmylated); estrogen dependent (By similarity).
Interacts with LMTK3; the interaction phosphorylates ESR1 (in vitro) and protects it against proteasomal degradation. Interacts with CCAR2 (via N-terminus) in a ligand-independent manner. Interacts with ZFHX3 (By similarity).
Interacts with SFR1 in a ligand-dependent and -independent manner (By similarity).
Interacts with DCAF13, LATS1 and DCAF1; regulates ESR1 ubiquitination and ubiquitin-mediated proteasomal degradation (By similarity).
Interacts (via DNA-binding domain) with POU4F2 isoform 2 (C-terminus); this interaction increases the estrogen receptor ESR1 transcriptional activity in a DNA- and ligand 17-beta-estradiol-independent manner (PubMed:9448000).
Interacts with ESRRB isoform 1 (By similarity).
Interacts with UBE3A and WBP2 (By similarity).
Interacts with GTF2B (By similarity).
Interacts with RBM39 (PubMed:11704680).
In the absence of hormonal ligand, interacts with TACC1 (By similarity).
Interacts with PI3KR1 or PI3KR2 and PTK2/FAK1 (By similarity).
Interacts with SRC (By similarity).
Interacts with BAG1; the interaction is promoted in the absence of estradiol (17-beta-estradiol/E2) (By similarity).
Interacts with and ubiquitinated by STUB1; the interaction is promoted in the absence of estradiol (17-beta-estradiol/E2) (By similarity).
Interacts with NEDD8 (By similarity).
Can form a heterodimer with ESR2 (By similarity).
Interacts with coactivator NCOA5. Interacts with PELP1, the interaction is enhanced by 17-beta-estradiol; the interaction increases ESR1 transcriptional activity (By similarity).
Interacts with NCOA7; the interaction is ligand-inducible. Interacts with AKAP13, CUEDC2, HEXIM1, KDM5A, MAP1S, SMARD1, and UBE1C. Interacts with MUC1; the interaction is stimulated by 7 beta-estradiol (E2) and enhances ESR1-mediated transcription. Interacts with DNTTIP2, and UIMC1. Interacts with KMT2D/MLL2. Interacts with ATAD2; the interaction is enhanced by estradiol. Interacts with KIF18A and LDB1. Interacts with RLIM (via its C-terminus). Interacts with MACROD1. Interacts with SH2D4A and PLCG. Interacts with SH2D4A; the interaction blocks binding to PLCG and inhibits estrogen-induced cell proliferation. Interacts with DYNLL1. Interacts with CCDC62; the interaction requires estradiol and appears to enhance the transcription of target genes. Interacts with NR2C1; the interaction prevents homodimerization of ESR1 and suppresses its transcriptional activity and cell growth. Interacts with DNAAF4. Interacts with PRMT2. Interacts with RBFOX2. Interacts with EP300; the interaction is estrogen-dependent and enhanced by CITED1. Interacts with CITED1; the interaction is estrogen-dependent (By similarity).
Interacts with FAM120B, FOXL2, PHB2 and SLC30A9. Interacts with coactivators NCOA3 and NCOA6. Interacts with STK3/MST2 only in the presence of SAV1 and vice-versa. Binds to CSNK1D. Interacts with NCOA2; NCOA2 can interact with ESR1 AF-1 and AF-2 domains simultaneously and mediate their transcriptional synergy. Interacts with DDX5. Interacts with NCOA1; the interaction seems to require a self-association of N-terminal and C-terminal regions. Interacts with ZNF366, DDX17, NFKB1, RELA, SP1 and SP3. Interacts with NRIP1 (By similarity).
Interacts with GPER1; the interaction occurs in an estrogen-dependent manner. Interacts with CLOCK and the interaction is stimulated by estrogen (By similarity).
Interacts with BCAS3. Interacts with TRIP4 (ufmylated); estrogen dependent (By similarity).
Interacts with LMTK3; the interaction phosphorylates ESR1 (in vitro) and protects it against proteasomal degradation. Interacts with CCAR2 (via N-terminus) in a ligand-independent manner. Interacts with ZFHX3 (By similarity).
Interacts with SFR1 in a ligand-dependent and -independent manner (By similarity).
Interacts with DCAF13, LATS1 and DCAF1; regulates ESR1 ubiquitination and ubiquitin-mediated proteasomal degradation (By similarity).
Interacts (via DNA-binding domain) with POU4F2 isoform 2 (C-terminus); this interaction increases the estrogen receptor ESR1 transcriptional activity in a DNA- and ligand 17-beta-estradiol-independent manner (PubMed:9448000).
Interacts with ESRRB isoform 1 (By similarity).
Interacts with UBE3A and WBP2 (By similarity).
Interacts with GTF2B (By similarity).
Interacts with RBM39 (PubMed:11704680).
In the absence of hormonal ligand, interacts with TACC1 (By similarity).
Interacts with PI3KR1 or PI3KR2 and PTK2/FAK1 (By similarity).
Interacts with SRC (By similarity).
Interacts with BAG1; the interaction is promoted in the absence of estradiol (17-beta-estradiol/E2) (By similarity).
Interacts with and ubiquitinated by STUB1; the interaction is promoted in the absence of estradiol (17-beta-estradiol/E2) (By similarity).
Interacts with NEDD8 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | P19785 | NCOA1 Q15788 | 3 | EBI-346765, EBI-455189 | |
BINARY | P19785 | Pgr Q00175 | 5 | EBI-346765, EBI-346821 | |
XENO | P19785 | URI1 O94763 | 2 | EBI-346765, EBI-357067 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, zinc finger, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-188 | Modulating (transactivation AF-1); mediates interaction with MACROD1 | ||||
Sequence: MTMTLHTKASGMALLHQIQGNELEPLNRPQLKMPMERALGEVYVDNSKPTVFNYPEGAAYEFNAAAAAAAAASAPVYGQSGIAYGPGSEAAAFSANSLGAFPQLNSVSPSPLMLLHPPPQLSPFLHPHGQQVPYYLENEPSAYAVRDTGPPAFYRSNSDNRRQNGRERLSSSNEKGNMIMESAKETRY | ||||||
Region | 35-47 | Required for interaction with NCOA1 | ||||
Sequence: MERALGEVYVDNS | ||||||
Region | 35-178 | Interaction with DDX5; self-association | ||||
Sequence: MERALGEVYVDNSKPTVFNYPEGAAYEFNAAAAAAAAASAPVYGQSGIAYGPGSEAAAFSANSLGAFPQLNSVSPSPLMLLHPPPQLSPFLHPHGQQVPYYLENEPSAYAVRDTGPPAFYRSNSDNRRQNGRERLSSSNEKGNM | ||||||
Region | 147-175 | Disordered | ||||
Sequence: DTGPPAFYRSNSDNRRQNGRERLSSSNEK | ||||||
Zinc finger | 189-209 | NR C4-type | ||||
Sequence: CAVCNDYASGYHYGVWSCEGC | ||||||
Region | 189-314 | Mediates interaction with DNTTIP2 | ||||
Sequence: CAVCNDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQACRLRKCYEVGMMKGGIRKDRRGGRMLKHKRQRDDLEGRNEMGASGDMRAANLWPSPLVIKHTKKNSPALSL | ||||||
Zinc finger | 225-249 | NR C4-type | ||||
Sequence: CPATNQCTIDKNRRKSCQACRLRKC | ||||||
Region | 255-314 | Hinge | ||||
Sequence: MKGGIRKDRRGGRMLKHKRQRDDLEGRNEMGASGDMRAANLWPSPLVIKHTKKNSPALSL | ||||||
Region | 266-599 | Interaction with AKAP13 | ||||
Sequence: GRMLKHKRQRDDLEGRNEMGASGDMRAANLWPSPLVIKHTKKNSPALSLTADQMVSALLDAEPPMIYSEYDPSRPFSEASMMGLLTNLADRELVHMINWAKRVPGFGDLNLHDQVHLLECAWLEILMIGLVWRSMEHPGKLLFAPNLLLDRNQGKCVEGMVEIFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGVYTFLSSTLKSLEEKDHIHRVLDKITDTLIHLMAKAGLTLQQQHRRLAQLLLILSHIRHMSNKGMEHLYNMKCKNVVPLYDLLLEMLDAHRLHAPASRMGVPPEEPSQTQLATTSSTSAHSLQTYYIPPEAEGFPNTI | ||||||
Region | 268-599 | Self-association | ||||
Sequence: MLKHKRQRDDLEGRNEMGASGDMRAANLWPSPLVIKHTKKNSPALSLTADQMVSALLDAEPPMIYSEYDPSRPFSEASMMGLLTNLADRELVHMINWAKRVPGFGDLNLHDQVHLLECAWLEILMIGLVWRSMEHPGKLLFAPNLLLDRNQGKCVEGMVEIFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGVYTFLSSTLKSLEEKDHIHRVLDKITDTLIHLMAKAGLTLQQQHRRLAQLLLILSHIRHMSNKGMEHLYNMKCKNVVPLYDLLLEMLDAHRLHAPASRMGVPPEEPSQTQLATTSSTSAHSLQTYYIPPEAEGFPNTI | ||||||
Domain | 315-551 | NR LBD | ||||
Sequence: TADQMVSALLDAEPPMIYSEYDPSRPFSEASMMGLLTNLADRELVHMINWAKRVPGFGDLNLHDQVHLLECAWLEILMIGLVWRSMEHPGKLLFAPNLLLDRNQGKCVEGMVEIFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGVYTFLSSTLKSLEEKDHIHRVLDKITDTLIHLMAKAGLTLQQQHRRLAQLLLILSHIRHMSNKGMEHLYNMKCKNVVPLYDLLLEMLDAH | ||||||
Region | 315-599 | Transactivation AF-2 | ||||
Sequence: TADQMVSALLDAEPPMIYSEYDPSRPFSEASMMGLLTNLADRELVHMINWAKRVPGFGDLNLHDQVHLLECAWLEILMIGLVWRSMEHPGKLLFAPNLLLDRNQGKCVEGMVEIFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGVYTFLSSTLKSLEEKDHIHRVLDKITDTLIHLMAKAGLTLQQQHRRLAQLLLILSHIRHMSNKGMEHLYNMKCKNVVPLYDLLLEMLDAHRLHAPASRMGVPPEEPSQTQLATTSSTSAHSLQTYYIPPEAEGFPNTI | ||||||
Region | 557-581 | Disordered | ||||
Sequence: ASRMGVPPEEPSQTQLATTSSTSAH | ||||||
Compositional bias | 564-581 | Polar residues | ||||
Sequence: PEEPSQTQLATTSSTSAH |
Domain
Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain. The modulating domain, also known as A/B or AF-1 domain has a ligand-independent transactivation function. The C-terminus contains a ligand-dependent transactivation domain, also known as E/F or AF-2 domain which overlaps with the ligand binding domain. AF-1 and AF-2 activate transcription independently and synergistically and act in a promoter- and cell-specific manner (By similarity).
Sequence similarities
Belongs to the nuclear hormone receptor family. NR3 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length599
- Mass (Da)66,955
- Last updated1991-02-01 v1
- Checksum05F5E2FC21CC0A8B
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
D3Z6V3 | D3Z6V3_MOUSE | Esr1 | 499 |
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 269 | in Ref. 4; AAF22561 | ||||
Sequence: L → M | ||||||
Compositional bias | 564-581 | Polar residues | ||||
Sequence: PEEPSQTQLATTSSTSAH |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M38651 EMBL· GenBank· DDBJ | AAA37580.1 EMBL· GenBank· DDBJ | mRNA | ||
AK036627 EMBL· GenBank· DDBJ | BAC29510.1 EMBL· GenBank· DDBJ | mRNA | ||
AK041525 EMBL· GenBank· DDBJ | BAC30973.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ276597 EMBL· GenBank· DDBJ | CAB85618.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF128221 EMBL· GenBank· DDBJ | AAF22562.1 EMBL· GenBank· DDBJ | mRNA | ||
AF128220 EMBL· GenBank· DDBJ | AAF22561.1 EMBL· GenBank· DDBJ | mRNA |