Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Estrogen receptor  

UniProtKB / Swiss-Prot ID :  ESR1_HUMAN

Gene Name (Synonyms) : 
ESR1, ESR, NR3A1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Isoform 1: Nucleus. Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note=A minor fraction is associated with the inner membrane. Isoform 3: Nucleus. Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell me 

Protein 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. Isoform 3 is involved in activation of NOS3 and endothelial nitric oxide production. Isoforms lacking one or several functional domains are thought to modulate transcriptional activty by competitive ligand or DNA binding and/or heterodimerization with the full length receptor. Isoform 3 can bind to ERE and inhibit isoform 1. 

Protein Sequence MTMTLHTKASGMALLHQIQGNELEPLNRPQLKIPLERPLGEVYLDSSKPAVYNYPEGAAYEFNAAAAANA...
Predicted Secondary Structure CCCCCCCCHHHHHHHHHHCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCC...
Protein Variant
LocationDescription
6H -> Y (in a breast cancer sample;somatic mutation).
77G -> S (in dbSNP:rs9340773). VAR_018905
160G -> C. VAR_004671
264M -> I (in a breast cancer sample;somatic mutation).
364V -> E (in estrogen resistance; dominant-negative inhibitor of the wild-type ESR).
400G -> V (destabilizes the receptor anddecreases its affinity for estradiol at
411D -> RNQGKCVEGMVEIFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGVYTFLSSTLKSLEEKDHIHRVLDKITDTLIH
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2Phosphothreonine---MTMTLH
---CCCCCC
20.90Phosphositeplus
Link-
4Phosphothreonine-MTMTLHTK
-CCCCCCCC
13.25Phosphositeplus
Link-
7PhosphothreonineMTLHTKASG
CCCCCCHHH
31.27Phosphositeplus
Link-
7Phosphothreonine.MTLHTKASG
CCCCCCHHH
31.27UniProtKB
Link-
10O-linked (GalNAc...)HTKASGMAL
CCCHHHHHH
30.56HPRD
Link-
10PhosphoserineHTKASGMAL
CCCHHHHHH
30.56Phosphositeplus
Link-
10Phosphoserine.HTKASGMAL
CCCHHHHHH
30.56UniProtKB
Link-
46PhosphoserineVYLDSSKPA
CCCCCCCCC
37.35PhosphoELM
Link-
46PhosphoserineVYLDSSKPA
CCCCCCCCC
37.35Phosphositeplus
Link-
47PhosphoserineYLDSSKPAV
CCCCCCCCC
42.18PhosphoELM
Link-
47PhosphoserineYLDSSKPAV
CCCCCCCCC
42.18Phosphositeplus
Link-
52PhosphotyrosineKPAVYNYPE
CCCCCCCCC
15.87PhosphoELM
Link-
52PhosphotyrosineKPAVYNYPE
CCCCCCCCC
15.87Phosphositeplus
Link-
102PhosphoserinePPLNSVSPS
CCCCCCCCC
31.49Phosphositeplus
Link-
102Phosphoserine (GSK-3_beta)PPLNSVSPS
CCCCCCCCC
31.49PhosphoELM
Link-
102Phosphoserine (MNAT1)PPLNSVSPS
CCCCCCCCC
31.49HPRD
Link-
104PhosphoserineLNSVSPSPL
CCCCCCCCC
21.34Phosphositeplus
Link-
104Phosphoserine (CDK_group;CDK_group;GSK-3_beta;GSK-3_beta)LNSVSPSPL
CCCCCCCCC
21.34PhosphoELM
Link-
104Phosphoserine (MNAT1)LNSVSPSPL
CCCCCCCCC
21.34HPRD
Link-
104Phosphoserine; by CDK2.LNSVSPSPL
CCCCCCCCC
21.34UniProtKB
Link-
106PhosphoserineSVSPSPLML
CCCCCCCCC
24.14Phosphositeplus
Link-
106Phosphoserine (CDK_group;GSK-3_beta)SVSPSPLML
CCCCCCCCC
24.14PhosphoELM
Link-
106Phosphoserine (MNAT1)SVSPSPLML
CCCCCCCCC
24.14HPRD
Link-
106Phosphoserine; by CDK2.SVSPSPLML
CCCCCCCCC
24.14UniProtKB
Link-
118PhosphoserinePPQLSPFLQ
CCCCCCCCC
14.36Phosphositeplus
Link-
118Phosphoserine (CDK7)PPQLSPFLQ
CCCCCCCCC
14.36HPRD
Link-
118Phosphoserine (MAPK1)PPQLSPFLQ
CCCCCCCCC
14.36HPRD
Link-
118Phosphoserine (MAPK_group;MAPK_group;RSK_group;MAPK3;MAPK1;GSK-3_)PPQLSPFLQ
CCCCCCCCC
14.36PhosphoELM
Link-
118Phosphoserine (RPS6KA1)PPQLSPFLQ
CCCCCCCCC
14.36HPRD
Link-
118Phosphoserine.PPQLSPFLQ
CCCCCCCCC
14.36UniProtKB
Link-
154PhosphoserineYRPNSDNRR
CCCCCCCCC
38.66PhosphoELM
Link-
154PhosphoserineYRPNSDNRR
CCCCCCCCC
38.66Phosphositeplus
Link-
167PhosphoserineERLASTNDK
CCCCCCCCC
32.13Phosphositeplus
Link-
167Phosphoserine (AKT1)ERLASTNDK
CCCCCCCCC
32.13HPRD
Link-
167Phosphoserine (AKT2)ERLASTNDK
CCCCCCCCC
32.13HPRD
Link-
167Phosphoserine (RPS6KA1)ERLASTNDK
CCCCCCCCC
32.13HPRD
Link-
167Phosphoserine (RPS6KA3)ERLASTNDK
CCCCCCCCC
32.13HPRD
Link-
167Phosphoserine (RSK_group;RSK_group;PKB_beta)ERLASTNDK
CCCCCCCCC
32.13PhosphoELM
Link-
167Phosphoserine; by CK2.ERLASTNDK
CCCCCCCCC
32.13UniProtKB
Link-
212PhosphoserineFFKRSIQGH
HHHHHHHCC
21.61PhosphoELM
Link-
212PhosphoserineFFKRSIQGH
HHHHHHHCC
21.61Phosphositeplus
Link-
219PhosphotyrosineGHNDYMCPA
CCCCCCCCC
13.11PhosphoELM
Link-
219PhosphotyrosineGHNDYMCPA
CCCCCCCCC
13.11Phosphositeplus
Link-
236PhosphoserineNRRKSCQAC
HHCCCCHHH
15.06Phosphositeplus
Link-
236Phosphoserine (PKA_group)NRRKSCQAC
HHCCCCHHH
15.06PhosphoELM
Link-
244N6-acetyllysineCRLRKCYEV
HHHHHHHHH
45.84Phosphositeplus
Link-
252N6-acetyllysineVGMMKGGIR
HCCCHHHHH
45.13Phosphositeplus
Link-
260Asymmetric dimethylarginine; by PRMT1.RKDRRGGRM
HHHHHHHHH
63.15UniProtKB
Link-
266Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)GRMLKHKRQ
HHHHHHHHH
37.42Phosphositeplus
Link-
266N6-acetyllysineGRMLKHKRQ
HHHHHHHHH
37.42Phosphositeplus
Link-
268Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)MLKHKRQRD
HHHHHHHHH
48.95Phosphositeplus
Link-
268N6-acetyllysineMLKHKRQRD
HHHHHHHHH
48.95Phosphositeplus
Link-
282PhosphoserineGEVGSAGDM
CCCCCCCCC
33.96PhosphoELM
Link-
282PhosphoserineGEVGSAGDM
CCCCCCCCC
33.96Phosphositeplus
Link-
294PhosphoserineNLWPSPLMI
HCCCCCCCH
21.05PhosphoELM
Link-
294PhosphoserineNLWPSPLMI
HCCCCCCCH
21.05Phosphositeplus
Link-
299N6-acetyllysinePLMIKRSKK
CCCHHHCCC
36.33Phosphositeplus
Link-
302Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IKRSKKNSL
HHHCCCCCC
61.07Phosphositeplus
Link-
302N6-acetyllysineIKRSKKNSL
HHHCCCCCC
61.07Phosphositeplus
Link-
302N6-methyllysineIKRSKKNSL
HHHCCCCCC
61.07Phosphositeplus
Link-
303N6-acetyllysineKRSKKNSLA
HHCCCCCCC
53.68Phosphositeplus
Link-
305PhosphoserineSKKNSLALS
CCCCCCCCC
24.73Phosphositeplus
Link
305Phosphoserine (PAK1)SKKNSLALS
CCCCCCCCC
24.73HPRD
Link
305Phosphoserine (PAK1)SKKNSLALS
CCCCCCCCC
24.73PhosphoELM
Link
311PhosphothreonineALSLTADQM
CCCCCHHHH
25.47Phosphositeplus
Link
311Phosphothreonine (MAPK14)ALSLTADQM
CCCCCHHHH
25.47HPRD
Link
311Phosphothreonine (MAPK_group;MAPK14)ALSLTADQM
CCCCCHHHH
25.47PhosphoELM
Link
472N6-acetyllysineSLEEKDHIH
CCCCHHHHH
45.27Phosphositeplus
Link
537DePhosphotyrosineVVPLYDLLL
CCCCCHHHH
9.85HPRD
Link
537DePhosphotyrosineVVPLYDLLL
CCCCCHHHH
9.85HPRD
Link
537PhosphotyrosineVVPLYDLLL
CCCCCHHHH
9.85Phosphositeplus
Link
537Phosphotyrosine (LCK)VVPLYDLLL
CCCCCHHHH
9.85HPRD
Link
537Phosphotyrosine (Lck;SRC)VVPLYDLLL
CCCCCHHHH
9.85PhosphoELM
Link
537Phosphotyrosine (SRC)VVPLYDLLL
CCCCCHHHH
9.85HPRD
Link
537Phosphotyrosine; by Tyr-kinases.VVPLYDLLL
CCCCCHHHH
9.85UniProtKB
Link
554PhosphoserineHAPTSRGGA
CCCCCCCCC
28.06PhosphoELM
Link-
554PhosphoserineHAPTSRGGA
CCCCCCCCC
28.06Phosphositeplus
Link-
559PhosphoserineRGGASVEET
CCCCCCCCC
33.08PhosphoELM
Link-
559PhosphoserineRGGASVEET
CCCCCCCCC
33.08Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
JUN_HUMANphysical interactionMINT-18664MINT11477071
JUN_HUMANphysical interactionMINT-18663MINT11477071
JUN_HUMANphysical interactionMINT-18885MINT11477071
HS90B_HUMANphysical interactionMINT-17321MINT11795466
JUNB_HUMANphysical interactionMINT-19190MINT11477071
BRCA1_HUMANphysical interactionMINT-13785MINT1244506
BRCA1_HUMANphysical interactionMINT-13786MINT1244506
MDM2_HUMANphysical interactionMINT-16348MINT11178989
CUED2_HUMANphysical interactionMINT-4788057MINT17347654
GRIP1_HUMANdirect interactionMINT-4791385MINT17545997
L3R2A_HUMANphysical interactionMINT-50573MINT15474036
L3R2A_HUMANphysical interactionMINT-50571MINT15474036
L3R2A_HUMANphysical interactionMINT-50906MINT15474036
UBE3A_HUMANphysical interactionDIP:10895EDIP9891052
ZBT17_HUMANphysical interactionDIP:10805EDIP11117529
ANM2_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
physical interaction
EBI-78498
EBI-78641
EBI-78636
intact12039952
12039952
12039952
12039952
12039952
SMRD1_HUMANphysical interactionEBI-1383336
intact12917342
NCOA3_HUMANphysical interactionEBI-1108892
intact11353774
MLL2_HUMANdirect interaction
physical interaction
physical interaction
EBI-996263
EBI-996195
EBI-996
intact16603732
16603732
16603732
RBBP5_HUMANphysical interaction
physical interaction
EBI-996195
EBI-996116
intact16603732
16603732
ASH2L_HUMANphysical interaction
physical interaction
EBI-996195
EBI-996116
intact16603732
16603732
WDR5B_HUMANphysical interaction
physical interaction
EBI-996195
EBI-996116
intact16603732
16603732
NCOA6_HUMANphysical interaction
physical interaction
EBI-286402
EBI-286348
intact10866662
10866662
BDNF_HUMANin vitroHPRD:00589HPRD11923430
1433F_HUMANin vitroHPRD:00589HPRD11266503
BRCA1_HUMANin vivoHPRD:00589HPRD10334989
PO4F2_HUMANin vitro
yeast 2-hybrid
HPRD:00589HPRD9448000
CALM_HUMANin vivoHPRD:00589HPRD11981030
MPIP2_HUMANin vitro
in vivo
HPRD:00589HPRD11689696
EGFR_HUMANin vitroHPRD:00589HPRD11887937
NR2F6_HUMANin vitroHPRD:00589HPRD10713182
COT1_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:00589HPRD12093745
ESR1_HUMANin vitroHPRD:00589HPRD10567404
11953755
FHL2_HUMANyeast 2-hybridHPRD:00589HPRD15666801
PHB2_HUMANin vitroHPRD:00589HPRD10938099
TIF1B_HUMANin vitroHPRD:00589HPRD9774463
JUNB_HUMANin vitroHPRD:00589HPRD11477071
3MG_HUMANin vitro
in vivo
HPRD:00589HPRD14761960
RBM23_HUMANin vitroHPRD:00589HPRD15694343
PIAS3_HUMANin vitro
in vivo
HPRD:00589HPRD11117529
ZBT17_HUMANin vitroHPRD:00589HPRD11117529
GNAI1_HUMANin vitro
in vivo
HPRD:00589HPRD11369763
IGF1R_HUMANin vivoHPRD:00589HPRD10749889
NFKB1_HUMANin vitroHPRD:00589HPRD7651415
TF65_HUMANin vitroHPRD:00589HPRD7651415
ERBB2_HUMANin vitro
in vivo
HPRD:00589HPRD15173068
JUND_HUMANin vitroHPRD:00589HPRD11477071
RXRA_HUMANin vitroHPRD:00589HPRD9717844
SOS1_HUMANin vitroHPRD:00589HPRD15173068
SRBP1_HUMANin vitro
in vivo
HPRD:00589HPRD12021179
SP1_HUMANin vitro
in vivo
HPRD:00589HPRD15637147
10446910
TSC2_HUMANin vitro
in vivo
HPRD:00589HPRD15851513
USF1_HUMANin vitroHPRD:00589HPRD15111769
CITE1_HUMANin vitro
in vivo
HPRD:00589HPRD11581164
HNF4A_HUMANin vitro
yeast 2-hybrid
HPRD:00589HPRD9717844
SMAD4_HUMANin vivo
yeast 2-hybrid
HPRD:00589HPRD11555647
12576474
PO4F1_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:00589HPRD9448000
KAPCA_HUMANin vitroHPRD:00589HPRD9891036
PRS8_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:00589HPRD8598193
14702340
MK03_HUMANin vitro
in vivo
HPRD:00589HPRD12118371
SP3_HUMANin vitro
in vivo
HPRD:00589HPRD10816575
FOXO3_HUMANin vitro
yeast 2-hybrid
HPRD:00589HPRD11435445
RNF4_HUMANin vitro
in vivo
HPRD:00589HPRD11696545
BCAR1_HUMANin vivoHPRD:00589HPRD15020686
ANM1_HUMANin vitroHPRD:00589HPRD11050077
SMAD3_HUMANin vitro
in vivo
HPRD:00589HPRD11555647
P55G_HUMANin vivoHPRD:00589HPRD15001646
STUB1_HUMANin vivoHPRD:00589HPRD16037132
RARA_HUMANin vitroHPRD:00589HPRD9717844
CSN5_HUMANin vivoHPRD:00589HPRD15899841
ERR1_HUMANin vitroHPRD:00589HPRD9058380
THA_HUMANin vitro
yeast 2-hybrid
HPRD:00589HPRD9717844
THB_HUMANin vitroHPRD:00589HPRD9717844
NR0B1_HUMANin vitroHPRD:00589HPRD11053406
TF2B_HUMANin vitroHPRD:00589HPRD7641693
9841876
UBC9_HUMANyeast 2-hybridHPRD:00589HPRD15666801
CCNH_HUMANin vivoHPRD:00589HPRD12527756
TRI59_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:00589HPRD15941852
CCNT1_HUMANin vitro
in vivo
HPRD:00589HPRD15940264
TIP60_HUMANin vitro
in vivo
HPRD:00589HPRD16260778
TBB5_HUMANin vivoHPRD:00589HPRD15556606
TBA1B_HUMANin vivoHPRD:00589HPRD15556606
HSP74_HUMANin vivoHPRD:00589HPRD15556606
WISP2_HUMANENSP00000206249STRING
MK01_HUMANENSP00000206249STRING
NEU1_HUMANENSP00000206249STRING
TSC2_HUMANENSP00000206249STRING
STUB1_HUMANENSP00000206249STRING
CCND1_HUMANENSP00000206249STRING
AHR_HUMANENSP00000206249STRING
CITE1_HUMANENSP00000206249STRING
PIAS1_HUMANENSP00000206249STRING
NR0B2_HUMANENSP00000206249STRING
MDM2_HUMANENSP00000206249STRING
CP19A_HUMANENSP00000206249STRING
CP1B1_HUMANENSP00000206249STRING
CCNT1_HUMANENSP00000206249STRING
CBP_HUMANENSP00000206249STRING
MK03_HUMANENSP00000206249STRING
EP300_HUMANENSP00000206249STRING
PRGC1_HUMANENSP00000206249STRING
TDG_HUMANENSP00000206249STRING
FGF7_HUMANENSP00000206249STRING
NCOA2_HUMANENSP00000206249STRING
IGF1R_HUMANENSP00000206249STRING
NCOR1_HUMANENSP00000206249STRING
P53_HUMANENSP00000206249STRING
ERBB2_HUMANENSP00000206249STRING
PSN2_HUMANENSP00000206249STRING
CALM_HUMANENSP00000206249STRING
P85A_HUMANENSP00000206249STRING
EGFR_HUMANENSP00000206249STRING
BARX2_HUMANENSP00000206249STRING
TFF1_HUMANENSP00000206249STRING
STA5B_HUMANENSP00000206249STRING
MED1_HUMANENSP00000206249STRING
MED1_HUMANENSP00000206249STRING
MED1_HUMANENSP00000206249STRING
MMP26_HUMANENSP00000206249STRING
IGF1B_HUMANENSP00000206249STRING
JUNB_HUMANENSP00000206249STRING
IRS1_HUMANENSP00000206249STRING
ETV5_HUMANENSP00000206249STRING
TAD3L_HUMANENSP00000206249STRING
CP7B1_HUMANENSP00000206249STRING
VEGFA_HUMANENSP00000206249STRING
NCOA1_HUMANENSP00000206249STRING
NCOA1_HUMANENSP00000206249STRING
COT1_HUMANENSP00000206249STRING
SP1_HUMANENSP00000206249STRING
MTA1_HUMANENSP00000206249STRING
ZN398_HUMANENSP00000206249STRING
CAV1_HUMANENSP00000206249STRING
FOXO3_HUMANENSP00000206249STRING
TIF1A_HUMANENSP00000206249STRING
STA5A_HUMANENSP00000206249STRING
SMAD4_HUMANENSP00000206249STRING
FHL2_HUMANENSP00000206249STRING
NCOR2_HUMANENSP00000206249STRING
RFX4_HUMANENSP00000206249STRING
RFX4_HUMANENSP00000206249STRING
RFX4_HUMANENSP00000206249STRING
RFX4_HUMANENSP00000206249STRING
RFX4_HUMANENSP00000206249STRING
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Disease Reference
Kegg disease
H00026 Endometrial Cancer
OMIM disease
615363Estrogen resistance (ESTRR)
Drug Reference
Kegg drug
D00067 Estrone (JAN/USP/INN); Estrone (TN)
D00105 Estradiol (JAN/USP/INN); Climara (TN); Divigel (TN); Estrace (TN); Estraderm (TN); Estrasorb (TN); E
D00185 Estriol (JP16/USP); Estriel (TN)
D00312 Estrone sodium sulfate; Sodium estrone sulfate
D00554 Ethinylestradiol (JP16/INN); Ethinyl estradiol (USP); Estinyl (TN)
D00575 Mestranol (JP16/USP/INN)
D00577 Diethylstilbestrol (USP/INN); Stilbestrol (TN)
D00898 Dienestrol (USP/INN); DV (TN)
D00946 Fosfestrol (JAN/INN); Diethylstilbestrol diphosphate (USP); Stilphostrol (TN)
D00948 Estropipate (USP); Piperazine estrone sulfate; Ogen (TN)
D00962 Clomifene citrate (JP16); Clomiphene citrate (USP); Clomid (TN); Serophene (TN)
D00963 Exemestane (JAN/USP/INN); Aromasin (TN)
D00964 Letrozole (JAN/USP/INN); Femara (TN)
D00966 Tamoxifen citrate (JP16/USP); Nolvadex (TN)
D00967 Toremifene citrate (JAN/USAN); Fareston (TN)
D01161 Fulvestrant (JAN/USAN/INN); Faslodex (TN)
D01265 Epitiostanol (JAN/INN)
D01413 Estradiol valerate (JAN/USP/INN); Deladumone (TN)
D01602 Mepitiostane (JP16/INN); Thioderon (TN)
D01617 Estradiol dipropionate (JAN); Ovahormon (TN)
D01639 Tibolone (JAN/USAN/INN)
D01953 Estradiol benzoate (JP16); Ovahormon (TN)
D01986 Estriol tripropionate (JAN); Estriol (TN)
D01989 Estriol diacetate benzoate (JAN); Estriol benzoate diacetate; Holin (TN)
D02217 Raloxifene hydrochloride (JAN/USP); LY 156758; Evista (TN)
D02758 Acolbifene hydrochloride (USAN)
D02993 Arzoxifene hydrochloride (USAN)
D03062 Bazedoxifene acetate (JAN/USAN); Viviant (TN)
D03911 Droloxifene (USAN/INN)
D03912 Droloxifene citrate (USAN)
D04041 Equilin (USP)
D04061 Estradiol acetate (USAN); Femring (TN)
D04063 Estradiol cypionate (USP); Depo-estradiol (TN)
D04064 Estradiol enanthate (USAN)
D04065 Estradiol undecylate (USAN/INN); Delestrec (TN)
D04070 Conjugated estrogens (JAN); Estrogens, conjugated (USP); Premarin (TN)
D04071 Estrogens, esterified (USP); Amnestrogen (TN)
D04496 Idoxifene (USAN/INN)
D04672 Lasofoxifene tartrate (JAN/USAN)
D05106 Nafoxidine hydrochloride (USAN)
D05192 Nitromifene citrate (USAN)
D05987 Synthetic conjugated estrogens, B (USAN); Enjuvia (TN)
D06245 Trioxifene mesylate (USAN)
D06551 Afimoxifene (USAN/INN); Tamogel (TN)
D07221 Promestriene (INN); Colpotrophine (TN)
D07434 Polyestradiol phosphate (INN); Estradurin (TN)
D07726 Clomifene (INN); Clomiphene; Clomifene (TN)
D07826 Hexestrol diphosphate sodium; Diethylstilbestrol diphosphate tetrasodium salt; Stilphostrol (TN)
D07918 Estradiol hemihydrate; Estrasorb (TN); Vagifem (TN)
D07919 Estradiol 17 beta-hemisuccinate; 17beta-Estradiol hemisuccinate; Eutocol (TN)
D07920 Estriol succinate; Estriol 16alfa, 17beta-di (hydrogen succinate); Sinapause (TN)
D07921 Estriol sodium succinate (BAN); Estriol 16alpha, 17beta-di (sodium succinate); Styptanon (TN)
D07928 Ethinylestradiol propanesulfonate; Turisteron (TN)
D08301 Ormeloxifene (INN); Centron (TN)
D08465 Raloxifene (INN); Eviden (TN); Raxeto (TN)
D08559 Tamoxifen (INN); Tamoxifen (TN); Tamoplex (TN)
D08620 Toremifene (INN); Fareston (TN)
D08910 Enclomiphene (USAN)
D08958 Ospemifene (INN/USAN/BAN); Osphena (TN)
D09834 Levormeloxifene fumarate (JAN)
D10008 Fispemifene (USAN/INN)
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Methylation
ReferencePubMed
"Regulation of estrogen rapid signaling through arginine methylationby PRMT1.";
Le Romancer M., Treilleux I., Leconte N., Robin-Lespinasse Y.,Sentis S., Bouchekioua-Bouzaghou K., Goddard S., Gobert-Gosse S.,Corbo L.;
Mol. Cell 31:212-221(2008).
Cited for: METHYLATION AT ARG-260 BY PRMT1, MUTAGENESIS OF ARG-260, SUBCELLULARLOCATION, AND INTERACTION WITH PI3KR1/2; SRC AND PTK2/FAK1.
Phosphorylation
ReferencePubMed
"Potentiation of human estrogen receptor alpha transcriptionalactivation through phosphorylation of serines 104 and 106 by thecyclin A-CDK2 complex.";
Rogatsky I., Trowbridge J.M., Garabedian M.J.;
J. Biol. Chem. 274:22296-22302(1999).
Cited for: PHOSPHORYLATION AT SER-104 AND SER-106, AND MUTAGENESIS.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-7 AND SER-10, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures