HUMAN:ESR1

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	ESR1 (synonyms: ESR, NR3A1)
Protein Name(s)	Estrogen receptor ER ER-alpha Estradiol receptor Nuclear receptor subfamily 3 group A member 1
External Links
UniProt	P03372
EMBL	X03635 M12674 U47678 AY425004 BX640939 AL356311 AL049821 AL078582 AL590993 AL049821 AL078582 AL356311 AL590993 AL590993 AL049821 AL078582 AL356311 AL078582 AL356311 AL590993 CH471051 BC128573 BC128574 AH008151 X73067 Z75126
CCDS	CCDS5234.1
PIR	S64737
RefSeq	NP_000116.2 NP_001116212.1 NP_001116213.1 NP_001116214.1 NP_001278159.1 NP_001278170.1 XP_006715438.1
UniGene	Hs.208124 Hs.744830
PDB	1A52 1AKF 1ERE 1ERR 1G50 1GWQ 1GWR 1HCP 1HCQ 1L2I 1PCG 1QKT 1QKU 1R5K 1SJ0 1UOM 1X7E 1X7R 1XP1 1XP6 1XP9 1XPC 1XQC 1YIM 1YIN 1ZKY 2AYR 2B1V 2B1Z 2B23 2BJ4 2FAI 2G44 2G5O 2I0J 2IOG 2IOK 2JF9 2JFA 2LLO 2LLQ 2OCF 2OUZ 2P15 2POG 2Q6J 2Q70 2QA6 2QA8 2QAB 2QE4 2QGT 2QGW 2QH6 2QR9 2QSE 2QXM 2QXS 2QZO 2R6W 2R6Y 2YAT 2YJA 3CBM 3CBO 3CBP 3DT3 3ERD 3ERT 3HLV 3HM1 3L03 3OS8 3OS9 3OSA 3Q95 3Q97 3UU7 3UUA 3UUC 3UUD 4AA6 4DMA 4IU7 4IUI 4IV2 4IV4 4IVW 4IVY 4IW6 4IW8 4IWC 4IWF 4JC3 4JDD 4MG5 4MG6 4MG7 4MG8 4MG9 4MGA 4MGB 4MGC 4MGD 4O6F 4PP6 4PPP 4PPS
PDBsum	1A52 1AKF 1ERE 1ERR 1G50 1GWQ 1GWR 1HCP 1HCQ 1L2I 1PCG 1QKT 1QKU 1R5K 1SJ0 1UOM 1X7E 1X7R 1XP1 1XP6 1XP9 1XPC 1XQC 1YIM 1YIN 1ZKY 2AYR 2B1V 2B1Z 2B23 2BJ4 2FAI 2G44 2G5O 2I0J 2IOG 2IOK 2JF9 2JFA 2LLO 2LLQ 2OCF 2OUZ 2P15 2POG 2Q6J 2Q70 2QA6 2QA8 2QAB 2QE4 2QGT 2QGW 2QH6 2QR9 2QSE 2QXM 2QXS 2QZO 2R6W 2R6Y 2YAT 2YJA 3CBM 3CBO 3CBP 3DT3 3ERD 3ERT 3HLV 3HM1 3L03 3OS8 3OS9 3OSA 3Q95 3Q97 3UU7 3UUA 3UUC 3UUD 4AA6 4DMA 4IU7 4IUI 4IV2 4IV4 4IVW 4IVY 4IW6 4IW8 4IWC 4IWF 4JC3 4JDD 4MG5 4MG6 4MG7 4MG8 4MG9 4MGA 4MGB 4MGC 4MGD 4O6F 4PP6 4PPP 4PPS
DisProt	DP00074
ProteinModelPortal	P03372
SMR	P03372
BioGrid	108403
DIP	DIP-5965N
IntAct	P03372
MINT	MINT-129047
STRING	9606.ENSP00000206249
BindingDB	P03372
ChEMBL	CHEMBL2093866
DrugBank	DB01431 DB00882 DB00286 DB01406 DB00304 DB00890 DB00255 DB00783 DB01196 DB04573 DB00655 DB04574 DB00977 DB00823 DB00294 DB01185 DB00947 DB00367 DB00603 DB01065 DB01357 DB01183 DB00957 DB04938 DB00396 DB04575 DB00481 DB00675 DB00539 DB01108
GuidetoPHARMACOLOGY	620
PhosphoSite	P03372
UniCarbKB	P03372
DMDM	544257
PaxDb	P03372
PRIDE	P03372
DNASU	2099
Ensembl	ENST00000206249 ENST00000338799 ENST00000440973 ENST00000443427
GeneID	2099
KEGG	hsa:2099
UCSC	uc003qom.4
CTD	2099
GeneCards	GC06P151988
HGNC	HGNC:3467
HPA	CAB000037 CAB055099 HPA000449 HPA000450
MIM	133430 615363
neXtProt	NX_P03372
Orphanet	785
PharmGKB	PA156
eggNOG	NOG320746
GeneTree	ENSGT00760000118887
HOVERGEN	HBG108344
InParanoid	P03372
KO	K08550
OMA	AFYRPNS
OrthoDB	EOG7288S1
PhylomeDB	P03372
TreeFam	TF323751
Reactome	REACT_116022 REACT_15525
SignaLink	P03372
ChiTaRS	ESR1
EvolutionaryTrace	P03372
GeneWiki	Estrogen_receptor_alpha
GenomeRNAi	2099
NextBio	8491
PRO	PR:P03372
Proteomes	UP000005640
Bgee	P03372
CleanEx	HS_ESR1
ExpressionAtlas	P03372
Genevestigator	P03372
GO	GO:0005737 GO:0005794 GO:0016021 GO:0016020 GO:0005654 GO:0005634 GO:0005886 GO:0035327 GO:0008013 GO:0003682 GO:0001046 GO:0019899 GO:0030284 GO:0034056 GO:0038052 GO:0042802 GO:0030235 GO:0000978 GO:0001077 GO:0003700 GO:0005496 GO:0003707 GO:0008134 GO:0008270 GO:0008209 GO:0001547 GO:0071392 GO:0006338 GO:0002064 GO:0060750 GO:0010467 GO:0030520 GO:0030518 GO:0008584 GO:0060749 GO:0060745 GO:0010629 GO:0043124 GO:0043433 GO:0007200 GO:0007204 GO:0048146 GO:0045429 GO:0051000 GO:0010863 GO:0048386 GO:0051091 GO:0045944 GO:0060527 GO:0060523 GO:0042981 GO:0060687 GO:0006355 GO:0032355 GO:0043627 GO:0007165 GO:0006367 GO:0006351 GO:0060065 GO:0060068
Gene3D	1.10.565.10 3.30.50.10
InterPro	IPR008946 IPR000536 IPR024178 IPR001292 IPR024736 IPR001723 IPR001628 IPR013088
Pfam	PF12743 PF00104 PF02159 PF00105
PIRSF	PIRSF500101 PIRSF002527
PRINTS	PR00543 PR00398 PR00047
SMART	SM00430 SM00399
SUPFAM	SSF48508
PROSITE	PS00031 PS51030

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
enables	GO:0030284	estrogen receptor activity	PMID:15831516^[1]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0000981	DNA-binding transcription factor activity, RNA polymerase II-specific	PMID:19274049^[2]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0000981	DNA-binding transcription factor activity, RNA polymerase II-specific	PMID:19274049^[2]	ECO:0000255	match to sequence model evidence used in manual assertion	InterPro:IPR000324 InterPro:IPR001628 InterPro:IPR001723	F		Seeded From UniProt	complete
enables	GO:0000981	DNA-binding transcription factor activity, RNA polymerase II-specific	GO_REF:0000113	ECO:0005556	multiple sequence alignment evidence used in manual assertion	UniProtKB:Q00175	F		Seeded From UniProt	complete
enables	GO:0001223	transcription coactivator binding	PMID:21642474^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q969T9	F		Seeded From UniProt	complete
involved_in	GO:0045893	positive regulation of transcription, DNA-templated	PMID:9841876^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0030284	estrogen receptor activity	PMID:9841876^[4]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0030520	intracellular estrogen receptor signaling pathway	PMID:9841876^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0019901	protein kinase binding	PMID:28068668^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O95835	F		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:11595744^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0017025	TBP-class protein binding	PMID:11595744^[6]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P13393	F		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:18563714^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	occurs_in:(CL:0002622) regulates_transcription_of:(ENSEMBL:ENSG00000107562)	Seeded From UniProt	complete
involved_in	GO:0071168	protein localization to chromatin	PMID:20388878^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	part_of:(GO:0071391) has_input:(UniProtKB:Q9Y618)\|part_of(GO:0071391) has_input:(UniProtKB:O75376)	Seeded From UniProt	complete
involved_in	GO:0000122	negative regulation of transcription by RNA polymerase II	PMID:20388878^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	regulates_expression_of:(ENSEMBL:ENSG00000207870) regulates_expression_of:(ENSEMBL:ENSG00000207725) part_of:(GO:0071391)	Seeded From UniProt	complete
part_of	GO:0000790	nuclear chromatin	PMID:20388878^[8]	ECO:0000314	direct assay evidence used in manual assertion		C	coincident_with:(SO:0000167) coincident_with:(ENSEMBL:ENSG00000207870) coincident_with:(ENSEMBL:ENSG00000207725) part_of:(GO:0071391)	Seeded From UniProt	complete
involved_in	GO:1903799	negative regulation of production of miRNAs involved in gene silencing by miRNA	PMID:20388878^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	regulates_expression_of:(ENSEMBL:ENSG00000270069) regulates_expression_of:(ENSEMBL:ENSG00000207870) part_of:(GO:0071391)	Seeded From UniProt	complete
involved_in	GO:0045899	positive regulation of RNA polymerase II transcriptional preinitiation complex assembly	PMID:9841876^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0097550	transcriptional preinitiation complex	PMID:9841876^[4]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0000790	nuclear chromatin	PMID:15831516^[1]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0034056	estrogen response element binding	PMID:15831516^[1]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:15831516^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P10276) part_of:(GO:0071392)	Seeded From UniProt	complete
involved_in	GO:0071392	cellular response to estradiol stimulus	PMID:15831516^[1]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006366	transcription by RNA polymerase II	PMID:15831516^[1]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0004879	nuclear receptor activity	PMID:15831516^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	activated_by:(CHEBI:16469)	Seeded From UniProt	complete
involved_in	GO:0045893	positive regulation of transcription, DNA-templated	PMID:20074560^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:20074560^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0008134	transcription factor binding	PMID:17505058^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9H6U6	F		Seeded From UniProt	complete
enables	GO:0003682	chromatin binding	PMID:17505058^[10]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0035327	transcriptionally active chromatin	PMID:17505058^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:17505058^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:17505058^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:22853951^[11]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9Y2J8	F		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:9841876^[4]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0001093	TFIIB-class transcription factor binding	PMID:9841876^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P03372	F		Seeded From UniProt	complete
enables	GO:0034056	estrogen response element binding	PMID:9841876^[4]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0030331	estrogen receptor binding	PMID:9841876^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P03372	F		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:12047722^[12]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(NCBI_Gene:5020)	Seeded From UniProt	complete
enables	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific	PMID:12047722^[12]	ECO:0000314	direct assay evidence used in manual assertion		F	occurs_at:(SO:0001952)	Seeded From UniProt	complete
enables	GO:0000978	RNA polymerase II proximal promoter sequence-specific DNA binding	PMID:12047722^[12]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0032355	response to estradiol	PMID:15304487^[13]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008013	beta-catenin binding	PMID:15304487^[13]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P35222	F		Seeded From UniProt	complete
enables	GO:0003700	DNA-binding transcription factor activity	PMID:12552091^[14]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0071392	cellular response to estradiol stimulus	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P06211	P		Seeded From UniProt	complete
involved_in	GO:0051091	positive regulation of DNA-binding transcription factor activity	PMID:10681512^[15]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051091	positive regulation of DNA-binding transcription factor activity	PMID:9328340^[16]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:15345745^[17]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P24387)\|has_regulation_target:(UniProtKB:P24388)	Seeded From UniProt	complete
involved_in	GO:0043627	response to estrogen	PMID:11581164^[18]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043433	negative regulation of DNA-binding transcription factor activity	PMID:10816575^[19]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043124	negative regulation of I-kappaB kinase/NF-kappaB signaling	PMID:16043358^[20]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043124	negative regulation of I-kappaB kinase/NF-kappaB signaling	PMID:7651415^[21]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0034056	estrogen response element binding	PMID:15345745^[17]	ECO:0000314	direct assay evidence used in manual assertion		F	has_participant:(UniProtKB:P24387)	Seeded From UniProt	complete
enables	GO:0034056	estrogen response element binding	PMID:17975005^[22]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0030520	intracellular estrogen receptor signaling pathway	PMID:3753802^[23]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030518	intracellular steroid hormone receptor signaling pathway	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P06211	P		Seeded From UniProt	complete
enables	GO:0030284	estrogen receptor activity	PMID:3753802^[23]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0030235	nitric-oxide synthase regulator activity	PMID:12389206^[24]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:12039952^[25]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P55345	F		Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:11960618^[26]	ECO:0000303	author statement without traceable support used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0010863	positive regulation of phospholipase C activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P06211	P		Seeded From UniProt	complete
involved_in	GO:0010629	negative regulation of gene expression	PMID:21695196^[27]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:Q12794)	Seeded From UniProt	complete
involved_in	GO:0007204	positive regulation of cytosolic calcium ion concentration	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P06211	P		Seeded From UniProt	complete
involved_in	GO:0007200	phospholipase C-activating G protein-coupled receptor signaling pathway	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P06211	P		Seeded From UniProt	complete
involved_in	GO:0006355	regulation of transcription, DNA-templated	PMID:3753802^[23]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006338	chromatin remodeling	PMID:12351687^[28]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:15569929^[29]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:20080953^[30]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:15569929^[29]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0005496	steroid binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P06211	F		Seeded From UniProt	complete
enables	GO:0000978	RNA polymerase II proximal promoter sequence-specific DNA binding	PMID:15345745^[17]	ECO:0000314	direct assay evidence used in manual assertion		F	has_participant:(UniProtKB:P24387)	Seeded From UniProt	complete
enables	GO:0051117	ATPase binding	PMID:12058073^[31]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:11544182^[32]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0004879	nuclear receptor activity	PMID:18722177^[33]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q8IX12	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:23065768^[34]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P03372	F	occurs_in:(GO:0005737)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:21182205^[35]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P03372	F	occurs_in:(GO:0005737)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:11682626^[36]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P03372	F	occurs_in:(GO:0005737)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:11265755^[37]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P03372	F	occurs_in:(GO:0005737)	Seeded From UniProt	complete
involved_in	GO:0071392	cellular response to estradiol stimulus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19785 ensembl:ENSMUSP00000101215	P		Seeded From UniProt	complete
involved_in	GO:0071391	cellular response to estrogen stimulus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19785 ensembl:ENSMUSP00000101215	P		Seeded From UniProt	complete
involved_in	GO:0060750	epithelial cell proliferation involved in mammary gland duct elongation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19785 ensembl:ENSMUSP00000101215	P		Seeded From UniProt	complete
involved_in	GO:0060749	mammary gland alveolus development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19785 ensembl:ENSMUSP00000101215	P		Seeded From UniProt	complete
involved_in	GO:0060745	mammary gland branching involved in pregnancy	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19785 ensembl:ENSMUSP00000101215	P		Seeded From UniProt	complete
involved_in	GO:0060687	regulation of branching involved in prostate gland morphogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19785 ensembl:ENSMUSP00000101215	P		Seeded From UniProt	complete
involved_in	GO:0060527	prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19785 ensembl:ENSMUSP00000101215	P		Seeded From UniProt	complete
involved_in	GO:0060523	prostate epithelial cord elongation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19785 ensembl:ENSMUSP00000101215	P		Seeded From UniProt	complete
involved_in	GO:0060068	vagina development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19785 ensembl:ENSMUSP00000101215	P		Seeded From UniProt	complete
involved_in	GO:0060065	uterus development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19785 ensembl:ENSMUSP00000101215	P		Seeded From UniProt	complete
involved_in	GO:0050727	regulation of inflammatory response	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19785 ensembl:ENSMUSP00000101215	P		Seeded From UniProt	complete
involved_in	GO:0048863	stem cell differentiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19785 ensembl:ENSMUSP00000101215	P		Seeded From UniProt	complete
involved_in	GO:0048146	positive regulation of fibroblast proliferation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19785 ensembl:ENSMUSP00000101215	P		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19785 ensembl:ENSMUSP00000101215	P		Seeded From UniProt	complete
enables	GO:0043565	sequence-specific DNA binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19785 ensembl:ENSMUSP00000101215	F		Seeded From UniProt	complete
involved_in	GO:0042981	regulation of apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19785 ensembl:ENSMUSP00000101215	P		Seeded From UniProt	complete
involved_in	GO:0034121	regulation of toll-like receptor signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19785 ensembl:ENSMUSP00000101215	P		Seeded From UniProt	complete
involved_in	GO:0008584	male gonad development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19785 ensembl:ENSMUSP00000101215	P		Seeded From UniProt	complete
involved_in	GO:0008209	androgen metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19785 ensembl:ENSMUSP00000101215	P		Seeded From UniProt	complete
enables	GO:0008134	transcription factor binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19785 ensembl:ENSMUSP00000101215	F		Seeded From UniProt	complete
involved_in	GO:0006355	regulation of transcription, DNA-templated	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19785 ensembl:ENSMUSP00000101215	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19785 ensembl:ENSMUSP00000101215	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19785 ensembl:ENSMUSP00000101215	C		Seeded From UniProt	complete
enables	GO:0004879	nuclear receptor activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19785 ensembl:ENSMUSP00000101215	F		Seeded From UniProt	complete
enables	GO:0003682	chromatin binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19785 ensembl:ENSMUSP00000101215	F		Seeded From UniProt	complete
involved_in	GO:0002064	epithelial cell development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19785 ensembl:ENSMUSP00000101215	P		Seeded From UniProt	complete
involved_in	GO:0001547	antral ovarian follicle growth	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19785 ensembl:ENSMUSP00000101215	P		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001292 InterPro:IPR001723 InterPro:IPR024178	F		Seeded From UniProt	complete
enables	GO:0003700	DNA-binding transcription factor activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001628	F		Seeded From UniProt	complete
enables	GO:0003707	steroid hormone receptor activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001723 InterPro:IPR024178	F		Seeded From UniProt	complete
enables	GO:0005496	steroid binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001292 InterPro:IPR024178	F		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001292 InterPro:IPR001628 InterPro:IPR001723 InterPro:IPR024178	C		Seeded From UniProt	complete
involved_in	GO:0006355	regulation of transcription, DNA-templated	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001292 InterPro:IPR001628 InterPro:IPR001723 InterPro:IPR013088 InterPro:IPR024178	P		Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001628 InterPro:IPR013088 InterPro:IPR024178	F		Seeded From UniProt	complete
enables	GO:0030284	estrogen receptor activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001292	F		Seeded From UniProt	complete
involved_in	GO:0043401	steroid hormone mediated signaling pathway	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001292	P		Seeded From UniProt	complete
enables	GO:0043565	sequence-specific DNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001628	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:19022902^[38]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P03372-1	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:18474858^[39]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P03372-1	F		Seeded From UniProt	complete
involved_in	GO:0051000	positive regulation of nitric-oxide synthase activity	PMID:21937726^[40]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045429	positive regulation of nitric oxide biosynthetic process	PMID:21937726^[40]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007165	signal transduction	PMID:10749889^[41] PMID:10970861^[42]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006351	transcription, DNA-templated	PMID:2040605^[43]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0030284	estrogen receptor activity	PMID:11004670^[44]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0051897	positive regulation of protein kinase B signaling	Reactome:R-HSA-2316434	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0033146	regulation of intracellular estrogen receptor signaling pathway	Reactome:R-HSA-8931987	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030111	regulation of Wnt signaling pathway	Reactome:R-HSA-8939256	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0016579	protein deubiquitination	Reactome:R-HSA-5688426	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006367	transcription initiation from RNA polymerase II promoter	Reactome:R-HSA-383280	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006357	regulation of transcription by RNA polymerase II	Reactome:R-HSA-8866910	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-2400009 Reactome:R-HSA-2316434	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	Reactome:R-HSA-9038163 Reactome:R-HSA-9038161 Reactome:R-HSA-9038052 Reactome:R-HSA-9038029 Reactome:R-HSA-9032751 Reactome:R-HSA-9023884 Reactome:R-HSA-9023861 Reactome:R-HSA-9023860 Reactome:R-HSA-9023845 Reactome:R-HSA-9023840 Reactome:R-HSA-9018503 Reactome:R-HSA-9018499 Reactome:R-HSA-9018325 Reactome:R-HSA-9012319 Reactome:R-HSA-9012315 Reactome:R-HSA-9012000 Reactome:R-HSA-9011997 Reactome:R-HSA-9011985 Reactome:R-HSA-9011984 Reactome:R-HSA-9011983 Reactome:R-HSA-9011981 Reactome:R-HSA-9011952 Reactome:R-HSA-9011949 Reactome:R-HSA-9009541 Reactome:R-HSA-9009536 Reactome:R-HSA-9009533 Reactome:R-HSA-9009526 Reactome:R-HSA-9009371 Reactome:R-HSA-9008285 Reactome:R-HSA-9008271 Reactome:R-HSA-9008270 Reactome:R-HSA-9008267 Reactome:R-HSA-9008258 Reactome:R-HSA-8954208 Reactome:R-HSA-8954207 Reactome:R-HSA-8939904 Reactome:R-HSA-8939204 Reactome:R-HSA-8939203 Reactome:R-HSA-8939201 Reactome:R-HSA-8937369 Reactome:R-HSA-8932084 Reactome:R-HSA-8932070 Reactome:R-HSA-8932037 Reactome:R-HSA-8932021 Reactome:R-HSA-8931981 Reactome:R-HSA-8864395 Reactome:R-HSA-6783238 Reactome:R-HSA-4090408 Reactome:R-HSA-376419 Reactome:R-HSA-1254386	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		Seeded From UniProt	complete
part_of	GO:0005794	Golgi apparatus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0333 UniProtKB-SubCell:SL-0132	C		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0238	F		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
part_of	GO:0016021	integral component of membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0812	C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1003 UniProtKB-SubCell:SL-0039	C		Seeded From UniProt	complete
enables	GO:0005496	steroid binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0754	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
enables	GO:0008289	lipid binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0446	F		Seeded From UniProt	complete
	GO:0071391	cellular response to estrogen stimulus	PMID:8402691^[45]	ECO:0000314			P		Table 3 and Table 2 show the effect of estrogen on estrogen receptors and the cell cycle of cells given estrogen. Figure 4 shows the colony growth of the cells in relation to the concentration of estrogen.	complete CACAO 3328
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 ^1.6 Laganière, J et al. (2005) Functional genomics identifies a mechanism for estrogen activation of the retinoic acid receptor alpha1 gene in breast cancer cells. Mol. Endocrinol. 19 1584-92 PubMed GONUTS page
↑ ^2.0 ^2.1 Vaquerizas, JM et al. (2009) A census of human transcription factors: function, expression and evolution. Nat. Rev. Genet. 10 252-63 PubMed GONUTS page
↑ Lim, SK et al. (2011) Tyrosine phosphorylation of transcriptional coactivator WW-domain binding protein 2 regulates estrogen receptor α function in breast cancer via the Wnt pathway. FASEB J. 25 3004-18 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 ^4.6 ^4.7 ^4.8 Sabbah, M et al. (1998) Oestrogen receptor facilitates the formation of preinitiation complex assembly: involvement of the general transcription factor TFIIB. Biochem. J. 336 ( Pt 3) 639-46 PubMed GONUTS page
↑ Britschgi, A et al. (2017) The Hippo kinases LATS1 and 2 control human breast cell fate via crosstalk with ERα. Nature 541 541-545 PubMed GONUTS page
↑ ^6.0 ^6.1 Wärnmark, A et al. (2001) The N-terminal regions of estrogen receptor alpha and beta are unstructured in vitro and show different TBP binding properties. J. Biol. Chem. 276 45939-44 PubMed GONUTS page
↑ Chen, M et al. (2008) ERAP75 functions as a coactivator to enhance estrogen receptor alpha transactivation in prostate stromal cells. Prostate 68 1273-82 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 ^8.3 Di Leva, G et al. (2010) MicroRNA cluster 221-222 and estrogen receptor alpha interactions in breast cancer. J. Natl. Cancer Inst. 102 706-21 PubMed GONUTS page
↑ ^9.0 ^9.1 Koyama, S et al. (2010) Repression of estrogen receptor beta function by putative tumor suppressor DBC1. Biochem. Biophys. Res. Commun. 392 357-62 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 ^10.3 ^10.4 Gururaj, AE et al. (2007) Estrogen induces expression of BCAS3, a novel estrogen receptor-alpha coactivator, through proline-, glutamic acid-, and leucine-rich protein-1 (PELP1). Mol. Endocrinol. 21 1847-60 PubMed GONUTS page
↑ Zhang, X et al. (2012) Peptidylarginine deiminase 2-catalyzed histone H3 arginine 26 citrullination facilitates estrogen receptor α target gene activation. Proc. Natl. Acad. Sci. U.S.A. 109 13331-6 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 Stedronsky, K et al. (2002) The affinity and activity of the multiple hormone response element in the proximal promoter of the human oxytocin gene. J. Neuroendocrinol. 14 472-85 PubMed GONUTS page
↑ ^13.0 ^13.1 Kouzmenko, AP et al. (2004) Wnt/beta-catenin and estrogen signaling converge in vivo. J. Biol. Chem. 279 40255-8 PubMed GONUTS page
↑ Leung, KC et al. (2003) Estrogen inhibits GH signaling by suppressing GH-induced JAK2 phosphorylation, an effect mediated by SOCS-2. Proc. Natl. Acad. Sci. U.S.A. 100 1016-21 PubMed GONUTS page
↑ Saville, B et al. (2000) Ligand-, cell-, and estrogen receptor subtype (alpha/beta)-dependent activation at GC-rich (Sp1) promoter elements. J. Biol. Chem. 275 5379-87 PubMed GONUTS page
↑ Porter, W et al. (1997) Functional synergy between the transcription factor Sp1 and the estrogen receptor. Mol. Endocrinol. 11 1569-80 PubMed GONUTS page
↑ ^17.0 ^17.1 ^17.2 van de Stolpe, A et al. (2004) Estrogen receptor (ER)-mediated transcriptional regulation of the human corticotropin-releasing hormone-binding protein promoter: differential effects of ERalpha and ERbeta. Mol. Endocrinol. 18 2908-23 PubMed GONUTS page
↑ Yahata, T et al. (2001) Selective coactivation of estrogen-dependent transcription by CITED1 CBP/p300-binding protein. Genes Dev. 15 2598-612 PubMed GONUTS page
↑ Stoner, M et al. (2000) Inhibition of vascular endothelial growth factor expression in HEC1A endometrial cancer cells through interactions of estrogen receptor alpha and Sp3 proteins. J. Biol. Chem. 275 22769-79 PubMed GONUTS page
↑ Liu, H et al. (2005) Estrogen receptor inhibits interleukin-6 gene expression by disruption of nuclear factor kappaB transactivation. Cytokine 31 251-7 PubMed GONUTS page
↑ Stein, B & Yang, MX (1995) Repression of the interleukin-6 promoter by estrogen receptor is mediated by NF-kappa B and C/EBP beta. Mol. Cell. Biol. 15 4971-9 PubMed GONUTS page
↑ Curtis, CD et al. (2007) Interaction of the tumor metastasis suppressor nonmetastatic protein 23 homologue H1 and estrogen receptor alpha alters estrogen-responsive gene expression. Cancer Res. 67 10600-7 PubMed GONUTS page
↑ ^23.0 ^23.1 ^23.2 Greene, GL et al. (1986) Sequence and expression of human estrogen receptor complementary DNA. Science 231 1150-4 PubMed GONUTS page
↑ Scordalakes, EM et al. (2002) Roles of estrogen receptor alpha and androgen receptor in the regulation of neuronal nitric oxide synthase. J. Comp. Neurol. 453 336-44 PubMed GONUTS page
↑ Qi, C et al. (2002) Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha. J. Biol. Chem. 277 28624-30 PubMed GONUTS page
↑ Watson, CS et al. (2002) The dynamic and elusive membrane estrogen receptor-alpha. Steroids 67 429-37 PubMed GONUTS page
↑ Yoffou, PH et al. (2011) Subtype specific elevated expression of hyaluronidase-1 (HYAL-1) in epithelial ovarian cancer. PLoS ONE 6 e20705 PubMed GONUTS page
↑ Matsuda, K et al. (2002) Colocalization and ligand-dependent discrete distribution of the estrogen receptor (ER)alpha and ERbeta. Mol. Endocrinol. 16 2215-30 PubMed GONUTS page
↑ ^29.0 ^29.1 Lu, Q et al. (2004) Striatin assembles a membrane signaling complex necessary for rapid, nongenomic activation of endothelial NO synthase by estrogen receptor alpha. Proc. Natl. Acad. Sci. U.S.A. 101 17126-31 PubMed GONUTS page
↑ Ross-Innes, CS et al. (2010) Cooperative interaction between retinoic acid receptor-alpha and estrogen receptor in breast cancer. Genes Dev. 24 171-82 PubMed GONUTS page
↑ Rouleau, N et al. (2002) Novel ATPase of SNF2-like protein family interacts with androgen receptor and modulates androgen-dependent transcription. Mol. Biol. Cell 13 2106-19 PubMed GONUTS page
↑ Steele-Perkins, G et al. (2001) Tumor formation and inactivation of RIZ1, an Rb-binding member of a nuclear protein-methyltransferase superfamily. Genes Dev. 15 2250-62 PubMed GONUTS page
↑ Kim, JH et al. (2008) CCAR1, a key regulator of mediator complex recruitment to nuclear receptor transcription complexes. Mol. Cell 31 510-9 PubMed GONUTS page
↑ Poulard, C et al. (2012) Activation of rapid oestrogen signalling in aggressive human breast cancers. EMBO Mol Med 4 1200-13 PubMed GONUTS page
↑ Tarallo, R et al. (2011) Identification of proteins associated with ligand-activated estrogen receptor α in human breast cancer cell nuclei by tandem affinity purification and nano LC-MS/MS. Proteomics 11 172-9 PubMed GONUTS page
↑ Métivier, R et al. (2001) Synergism between ERalpha transactivation function 1 (AF-1) and AF-2 mediated by steroid receptor coactivator protein-1: requirement for the AF-1 alpha-helical core and for a direct interaction between the N- and C-terminal domains. Mol. Endocrinol. 15 1953-70 PubMed GONUTS page
↑ Benecke, A et al. (2000) Synergy between estrogen receptor alpha activation functions AF1 and AF2 mediated by transcription intermediary factor TIF2. EMBO Rep. 1 151-7 PubMed GONUTS page
↑ Powell, E & Xu, W (2008) Intermolecular interactions identify ligand-selective activity of estrogen receptor alpha/beta dimers. Proc. Natl. Acad. Sci. U.S.A. 105 19012-7 PubMed GONUTS page
↑ Dai, SY et al. (2008) Prediction of the tissue-specificity of selective estrogen receptor modulators by using a single biochemical method. Proc. Natl. Acad. Sci. U.S.A. 105 7171-6 PubMed GONUTS page
↑ ^40.0 ^40.1 Kim, KH et al. (2011) Splice isoform estrogen receptors as integral transmembrane proteins. Mol. Biol. Cell 22 4415-23 PubMed GONUTS page
↑ Kahlert, S et al. (2000) Estrogen receptor alpha rapidly activates the IGF-1 receptor pathway. J. Biol. Chem. 275 18447-53 PubMed GONUTS page
↑ Flouriot, G et al. (2000) Identification of a new isoform of the human estrogen receptor-alpha (hER-alpha) that is encoded by distinct transcripts and that is able to repress hER-alpha activation function 1. EMBO J. 19 4688-700 PubMed GONUTS page
↑ Reese, JC & Katzenellenbogen, BS (1991) Mutagenesis of cysteines in the hormone binding domain of the human estrogen receptor. Alterations in binding and transcriptional activation by covalently and reversibly attaching ligands. J. Biol. Chem. 266 10880-7 PubMed GONUTS page
↑ Anandappa, SY et al. (2000) Variant estrogen receptor alpha mRNAs in human breast cancer specimens. Int. J. Cancer 88 209-16 PubMed GONUTS page
↑ Zajchowski, DA et al. (1993) Estrogen inhibits the growth of estrogen receptor-negative, but not estrogen receptor-positive, human mammary epithelial cells expressing a recombinant estrogen receptor. Cancer Res. 53 5004-11 PubMed GONUTS page

[PMID:15831516-1] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 ^1.6 Laganière, J et al. (2005) Functional genomics identifies a mechanism for estrogen activation of the retinoic acid receptor alpha1 gene in breast cancer cells. Mol. Endocrinol. 19 1584-92 PubMed GONUTS page

[PMID:19274049-2] 2.0 ^2.1 Vaquerizas, JM et al. (2009) A census of human transcription factors: function, expression and evolution. Nat. Rev. Genet. 10 252-63 PubMed GONUTS page

[PMID:21642474-3] Lim, SK et al. (2011) Tyrosine phosphorylation of transcriptional coactivator WW-domain binding protein 2 regulates estrogen receptor α function in breast cancer via the Wnt pathway. FASEB J. 25 3004-18 PubMed GONUTS page

[PMID:9841876-4] 4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 ^4.6 ^4.7 ^4.8 Sabbah, M et al. (1998) Oestrogen receptor facilitates the formation of preinitiation complex assembly: involvement of the general transcription factor TFIIB. Biochem. J. 336 ( Pt 3) 639-46 PubMed GONUTS page

[PMID:28068668-5] Britschgi, A et al. (2017) The Hippo kinases LATS1 and 2 control human breast cell fate via crosstalk with ERα. Nature 541 541-545 PubMed GONUTS page

[PMID:11595744-6] 6.0 ^6.1 Wärnmark, A et al. (2001) The N-terminal regions of estrogen receptor alpha and beta are unstructured in vitro and show different TBP binding properties. J. Biol. Chem. 276 45939-44 PubMed GONUTS page

[PMID:18563714-7] Chen, M et al. (2008) ERAP75 functions as a coactivator to enhance estrogen receptor alpha transactivation in prostate stromal cells. Prostate 68 1273-82 PubMed GONUTS page

[PMID:20388878-8] 8.0 ^8.1 ^8.2 ^8.3 Di Leva, G et al. (2010) MicroRNA cluster 221-222 and estrogen receptor alpha interactions in breast cancer. J. Natl. Cancer Inst. 102 706-21 PubMed GONUTS page

[PMID:20074560-9] 9.0 ^9.1 Koyama, S et al. (2010) Repression of estrogen receptor beta function by putative tumor suppressor DBC1. Biochem. Biophys. Res. Commun. 392 357-62 PubMed GONUTS page

[PMID:17505058-10] 10.0 ^10.1 ^10.2 ^10.3 ^10.4 Gururaj, AE et al. (2007) Estrogen induces expression of BCAS3, a novel estrogen receptor-alpha coactivator, through proline-, glutamic acid-, and leucine-rich protein-1 (PELP1). Mol. Endocrinol. 21 1847-60 PubMed GONUTS page

[PMID:22853951-11] Zhang, X et al. (2012) Peptidylarginine deiminase 2-catalyzed histone H3 arginine 26 citrullination facilitates estrogen receptor α target gene activation. Proc. Natl. Acad. Sci. U.S.A. 109 13331-6 PubMed GONUTS page

[PMID:12047722-12] 12.0 ^12.1 ^12.2 Stedronsky, K et al. (2002) The affinity and activity of the multiple hormone response element in the proximal promoter of the human oxytocin gene. J. Neuroendocrinol. 14 472-85 PubMed GONUTS page

[PMID:15304487-13] 13.0 ^13.1 Kouzmenko, AP et al. (2004) Wnt/beta-catenin and estrogen signaling converge in vivo. J. Biol. Chem. 279 40255-8 PubMed GONUTS page

[PMID:12552091-14] Leung, KC et al. (2003) Estrogen inhibits GH signaling by suppressing GH-induced JAK2 phosphorylation, an effect mediated by SOCS-2. Proc. Natl. Acad. Sci. U.S.A. 100 1016-21 PubMed GONUTS page

[PMID:10681512-15] Saville, B et al. (2000) Ligand-, cell-, and estrogen receptor subtype (alpha/beta)-dependent activation at GC-rich (Sp1) promoter elements. J. Biol. Chem. 275 5379-87 PubMed GONUTS page

[PMID:9328340-16] Porter, W et al. (1997) Functional synergy between the transcription factor Sp1 and the estrogen receptor. Mol. Endocrinol. 11 1569-80 PubMed GONUTS page

[PMID:15345745-17] 17.0 ^17.1 ^17.2 van de Stolpe, A et al. (2004) Estrogen receptor (ER)-mediated transcriptional regulation of the human corticotropin-releasing hormone-binding protein promoter: differential effects of ERalpha and ERbeta. Mol. Endocrinol. 18 2908-23 PubMed GONUTS page

[PMID:11581164-18] Yahata, T et al. (2001) Selective coactivation of estrogen-dependent transcription by CITED1 CBP/p300-binding protein. Genes Dev. 15 2598-612 PubMed GONUTS page

[PMID:10816575-19] Stoner, M et al. (2000) Inhibition of vascular endothelial growth factor expression in HEC1A endometrial cancer cells through interactions of estrogen receptor alpha and Sp3 proteins. J. Biol. Chem. 275 22769-79 PubMed GONUTS page

[PMID:16043358-20] Liu, H et al. (2005) Estrogen receptor inhibits interleukin-6 gene expression by disruption of nuclear factor kappaB transactivation. Cytokine 31 251-7 PubMed GONUTS page

[PMID:7651415-21] Stein, B & Yang, MX (1995) Repression of the interleukin-6 promoter by estrogen receptor is mediated by NF-kappa B and C/EBP beta. Mol. Cell. Biol. 15 4971-9 PubMed GONUTS page

[PMID:17975005-22] Curtis, CD et al. (2007) Interaction of the tumor metastasis suppressor nonmetastatic protein 23 homologue H1 and estrogen receptor alpha alters estrogen-responsive gene expression. Cancer Res. 67 10600-7 PubMed GONUTS page

[PMID:3753802-23] 23.0 ^23.1 ^23.2 Greene, GL et al. (1986) Sequence and expression of human estrogen receptor complementary DNA. Science 231 1150-4 PubMed GONUTS page

[PMID:12389206-24] Scordalakes, EM et al. (2002) Roles of estrogen receptor alpha and androgen receptor in the regulation of neuronal nitric oxide synthase. J. Comp. Neurol. 453 336-44 PubMed GONUTS page

[PMID:12039952-25] Qi, C et al. (2002) Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha. J. Biol. Chem. 277 28624-30 PubMed GONUTS page

[PMID:11960618-26] Watson, CS et al. (2002) The dynamic and elusive membrane estrogen receptor-alpha. Steroids 67 429-37 PubMed GONUTS page

[PMID:21695196-27] Yoffou, PH et al. (2011) Subtype specific elevated expression of hyaluronidase-1 (HYAL-1) in epithelial ovarian cancer. PLoS ONE 6 e20705 PubMed GONUTS page

[PMID:12351687-28] Matsuda, K et al. (2002) Colocalization and ligand-dependent discrete distribution of the estrogen receptor (ER)alpha and ERbeta. Mol. Endocrinol. 16 2215-30 PubMed GONUTS page

[PMID:15569929-29] 29.0 ^29.1 Lu, Q et al. (2004) Striatin assembles a membrane signaling complex necessary for rapid, nongenomic activation of endothelial NO synthase by estrogen receptor alpha. Proc. Natl. Acad. Sci. U.S.A. 101 17126-31 PubMed GONUTS page

[PMID:20080953-30] Ross-Innes, CS et al. (2010) Cooperative interaction between retinoic acid receptor-alpha and estrogen receptor in breast cancer. Genes Dev. 24 171-82 PubMed GONUTS page

[PMID:12058073-31] Rouleau, N et al. (2002) Novel ATPase of SNF2-like protein family interacts with androgen receptor and modulates androgen-dependent transcription. Mol. Biol. Cell 13 2106-19 PubMed GONUTS page

[PMID:11544182-32] Steele-Perkins, G et al. (2001) Tumor formation and inactivation of RIZ1, an Rb-binding member of a nuclear protein-methyltransferase superfamily. Genes Dev. 15 2250-62 PubMed GONUTS page

[PMID:18722177-33] Kim, JH et al. (2008) CCAR1, a key regulator of mediator complex recruitment to nuclear receptor transcription complexes. Mol. Cell 31 510-9 PubMed GONUTS page

[PMID:23065768-34] Poulard, C et al. (2012) Activation of rapid oestrogen signalling in aggressive human breast cancers. EMBO Mol Med 4 1200-13 PubMed GONUTS page

[PMID:21182205-35] Tarallo, R et al. (2011) Identification of proteins associated with ligand-activated estrogen receptor α in human breast cancer cell nuclei by tandem affinity purification and nano LC-MS/MS. Proteomics 11 172-9 PubMed GONUTS page

[PMID:11682626-36] Métivier, R et al. (2001) Synergism between ERalpha transactivation function 1 (AF-1) and AF-2 mediated by steroid receptor coactivator protein-1: requirement for the AF-1 alpha-helical core and for a direct interaction between the N- and C-terminal domains. Mol. Endocrinol. 15 1953-70 PubMed GONUTS page

[PMID:11265755-37] Benecke, A et al. (2000) Synergy between estrogen receptor alpha activation functions AF1 and AF2 mediated by transcription intermediary factor TIF2. EMBO Rep. 1 151-7 PubMed GONUTS page

[PMID:19022902-38] Powell, E & Xu, W (2008) Intermolecular interactions identify ligand-selective activity of estrogen receptor alpha/beta dimers. Proc. Natl. Acad. Sci. U.S.A. 105 19012-7 PubMed GONUTS page

[PMID:18474858-39] Dai, SY et al. (2008) Prediction of the tissue-specificity of selective estrogen receptor modulators by using a single biochemical method. Proc. Natl. Acad. Sci. U.S.A. 105 7171-6 PubMed GONUTS page

[PMID:21937726-40] 40.0 ^40.1 Kim, KH et al. (2011) Splice isoform estrogen receptors as integral transmembrane proteins. Mol. Biol. Cell 22 4415-23 PubMed GONUTS page

[PMID:10749889-41] Kahlert, S et al. (2000) Estrogen receptor alpha rapidly activates the IGF-1 receptor pathway. J. Biol. Chem. 275 18447-53 PubMed GONUTS page

[PMID:10970861-42] Flouriot, G et al. (2000) Identification of a new isoform of the human estrogen receptor-alpha (hER-alpha) that is encoded by distinct transcripts and that is able to repress hER-alpha activation function 1. EMBO J. 19 4688-700 PubMed GONUTS page

[PMID:2040605-43] Reese, JC & Katzenellenbogen, BS (1991) Mutagenesis of cysteines in the hormone binding domain of the human estrogen receptor. Alterations in binding and transcriptional activation by covalently and reversibly attaching ligands. J. Biol. Chem. 266 10880-7 PubMed GONUTS page

[PMID:11004670-44] Anandappa, SY et al. (2000) Variant estrogen receptor alpha mRNAs in human breast cancer specimens. Int. J. Cancer 88 209-16 PubMed GONUTS page

[PMID:8402691-45] Zajchowski, DA et al. (1993) Estrogen inhibits the growth of estrogen receptor-negative, but not estrogen receptor-positive, human mammary epithelial cells expressing a recombinant estrogen receptor. Cancer Res. 53 5004-11 PubMed GONUTS page

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

[9]

[10]

[11]

[12]

[13]

[14]

[15]

[16]

[17]

[18]

[19]

[20]

[21]

[22]

[23]

[24]

[25]

[26]

[27]

[28]

[29]

[30]

[31]

[32]

[33]

[34]

[35]

[36]

[37]

[38]

[39]

[40]

[41]

[42]

[43]

[44]

[45]

HUMAN:ESR1

Contents

Annotations

Notes

References

a

b

c

d

e

g

h

i

l

m

n

o

p

r

s

t

u

v

z

Navigation menu

Personal tools

Namespaces

Variants

Views

More

Search

Navigation

Cacao

Links

Tools