ESR2_HUMAN - dbPTM
ESR2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ESR2_HUMAN
UniProt AC Q92731
Protein Name Estrogen receptor beta
Gene Name ESR2
Organism Homo sapiens (Human).
Sequence Length 530
Subcellular Localization Nucleus .
Protein Description Nuclear hormone receptor. Binds estrogens with an affinity similar to that of ESR1, and activates expression of reporter genes containing estrogen response elements (ERE) in an estrogen-dependent manner. [PubMed: 20074560 Isoform beta-cx lacks ligand binding ability and has no or only very low ere binding activity resulting in the loss of ligand-dependent transactivation ability. DNA-binding by ESR1 and ESR2 is rapidly lost at 37 degrees Celsius in the absence of ligand while in the presence of 17 beta-estradiol and 4-hydroxy-tamoxifen loss in DNA-binding at elevated temperature is more gradual.]
Protein Sequence MDIKNSPSSLNSPSSYNCSQSILPLEHGSIYIPSSYVDSHHEYPAMTFYSPAVMNYSIPSNVTNLEGGPGRQTTSPNVLWPTPGHLSPLVVHRQLSHLYAEPQKSPWCEARSLEHTLPVNRETLKRKVSGNRCASPVTGPGSKRDAHFCAVCSDYASGYHYGVWSCEGCKAFFKRSIQGHNDYICPATNQCTIDKNRRKSCQACRLRKCYEVGMVKCGSRRERCGYRLVRRQRSADEQLHCAGKAKRSGGHAPRVRELLLDALSPEQLVLTLLEAEPPHVLISRPSAPFTEASMMMSLTKLADKELVHMISWAKKIPGFVELSLFDQVRLLESCWMEVLMMGLMWRSIDHPGKLIFAPDLVLDRDEGKCVEGILEIFDMLLATTSRFRELKLQHKEYLCVKAMILLNSSMYPLVTATQDADSSRKLAHLLNAVTDALVWVIAKSGISSQQQSMRLANLLMLLSHVRHASNKGMEHLLNMKCKNVVPVYDLLLEMLNAHVLRGCKSSITGSECSPAEDSKSKEGSQNPQSQ
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
4Sumoylation----MDIKNSPSSLN
----CCCCCCHHHCC
47.29-
36PhosphorylationSIYIPSSYVDSHHEY
CEECCHHHCCCCCCC
16.77-
56PhosphorylationYSPAVMNYSIPSNVT
ECCCCCCCCCCCCCC
7.0022817900
87PhosphorylationWPTPGHLSPLVVHRQ
CCCCCCCCHHHHHHH
15.5422817900
105PhosphorylationLYAEPQKSPWCEARS
HHCCCCCCCCHHHCC
20.569636657
135PhosphorylationVSGNRCASPVTGPGS
HCCCCCCCCCCCCCC
24.43-
165PhosphorylationGYHYGVWSCEGCKAF
CCCCEEEECCHHHHH
10.419528769
176PhosphorylationCKAFFKRSIQGHNDY
HHHHHHHHHCCCCCC
21.6122266331
200PhosphorylationIDKNRRKSCQACRLR
ECCCHHHCCHHHCCC
15.0622266331
210PhosphorylationACRLRKCYEVGMVKC
HHCCCCCEEECCEEC
19.3824719451
320 (in isoform 7)Phosphorylation-10.0426503514
323PhosphorylationIPGFVELSLFDQVRL
CCCEEEECHHHHHHH
17.3123403867
324 (in isoform 7)Phosphorylation-9.5426503514
331 (in isoform 7)Phosphorylation-2.9726503514
415PhosphorylationSSMYPLVTATQDADS
CCCCCCHHCCCCCCH
31.5030206219
417PhosphorylationMYPLVTATQDADSSR
CCCCHHCCCCCCHHH
20.0230206219
422PhosphorylationTATQDADSSRKLAHL
HCCCCCCHHHHHHHH
33.4924719451
423PhosphorylationATQDADSSRKLAHLL
CCCCCCHHHHHHHHH
33.7030206219
463PhosphorylationANLLMLLSHVRHASN
HHHHHHHHHHHHHHH
18.90-
469PhosphorylationLSHVRHASNKGMEHL
HHHHHHHHHHHHHHH
32.71-
484 (in isoform 4)Phosphorylation-2.9222210691
488PhosphorylationCKNVVPVYDLLLEML
CCCCCCHHHHHHHHH
8.53-
491 (in isoform 4)Phosphorylation-3.3022210691
492 (in isoform 2)Phosphorylation-4.7722210691

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
36YPhosphorylationKinaseABL1P00519
GPS
165SPhosphorylationKinaseRPS6KA1Q15418
GPS
-KUbiquitinationE3 ubiquitin ligaseSTUB1Q9UNE7
PMID:16940184
-KUbiquitinationE3 ubiquitin ligaseMDM2Q00987
PMID:22349818

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
87SPhosphorylation

15862947
105SPhosphorylation

15862947

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of ESR2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ESR1_HUMANESR1physical
9473491
NCOA6_HUMANNCOA6physical
11773444
MED12_HUMANMED12physical
11867769
MED1_HUMANMED1physical
11867769
MED14_HUMANMED14physical
11867769
MED23_HUMANMED23physical
11867769
MED24_HUMANMED24physical
11867769
MED16_HUMANMED16physical
11867769
MED17_HUMANMED17physical
11867769
MED7_HUMANMED7physical
11867769
MED6_HUMANMED6physical
11867769
MED20_HUMANMED20physical
11867769
MED21_HUMANMED21physical
11867769
MED10_HUMANMED10physical
11867769
CCNC_HUMANCCNCphysical
11867769
CDK8_HUMANCDK8physical
11867769
MKNK2_HUMANMKNK2physical
11013076
SRC_HUMANSRCphysical
11013076
UBE3A_HUMANUBE3Aphysical
17962381
SP1_HUMANSP1physical
18765668
CBP_HUMANCREBBPphysical
18765668
EP300_HUMANEP300physical
18765668
MSH2_HUMANMSH2physical
15886699
NCOA1_HUMANNCOA1physical
11500849
NCOA2_HUMANNCOA2physical
11500849
MED1_HUMANMED1physical
11500849
ZNHI3_HUMANZNHIT3physical
11500849
TRIP4_HUMANTRIP4physical
11500849
JHD2C_HUMANJMJD1Cphysical
11500849
IKBB_HUMANNFKBIBphysical
11500849
NRIP1_HUMANNRIP1physical
11500849
SERPH_HUMANSERPINH1physical
11500849
TIF1A_HUMANTRIM24physical
11500849
NCOA3_HUMANNCOA3physical
11500849
EP300_HUMANEP300physical
11500849
MED1_HUMANMED1physical
10770935
ESR2_HUMANESR2physical
20353944
HS90A_HUMANHSP90AA1physical
20353944
KLF5_HUMANKLF5physical
21487105
WWP1_HUMANWWP1physical
21487105
NRIP1_HUMANNRIP1physical
15604093
PNRC1_HUMANPNRC1physical
15604093
PRGC1_HUMANPPARGC1Aphysical
15604093
PNRC2_HUMANPNRC2physical
15604093
NCOA6_HUMANNCOA6physical
15604093
SRC_HUMANSRCphysical
12630920
NCOA2_HUMANNCOA2physical
12630920
NCOA1_HUMANNCOA1physical
12554772
NCOA2_HUMANNCOA2physical
12554772
NCOA3_HUMANNCOA3physical
12554772
NCOA1_HUMANNCOA1physical
11376110
NCOA2_HUMANNCOA2physical
11376110
NCOA3_HUMANNCOA3physical
11376110
NCOA1_HUMANNCOA1physical
11014206
NCOA2_HUMANNCOA2physical
11014206
TRAM1_HUMANTRAM1physical
11014206
NCOA3_HUMANNCOA3physical
9765300
MDM2_HUMANMDM2physical
22349818
ARI5A_HUMANARID5Aphysical
15941852
SRA1_HUMANSRA1physical
20398657
PPP5_HUMANPPP5Cphysical
14764652
ESR1_HUMANESR1physical
21182203
ESR2_HUMANESR2physical
21182203
ACTB_HUMANACTBphysical
21182203
STAU1_HUMANSTAU1physical
21182203
EXOS4_HUMANEXOSC4physical
21182203
HSP7C_HUMANHSPA8physical
21182203
MED17_HUMANMED17physical
21182203
MED4_HUMANMED4physical
21182203
MYLK2_HUMANMYLK2physical
21182203
NCOA3_HUMANNCOA3physical
21182203
NRIP1_HUMANNRIP1physical
21182203
PTCD3_HUMANPTCD3physical
21182203
PABP5_HUMANPABPC5physical
21182203
TIF1A_HUMANTRIM24physical
21182203
ZCCHV_HUMANZC3HAV1physical
21182203
RT15_HUMANMRPS15physical
21182203
RT22_HUMANMRPS22physical
21182203
RT02_HUMANMRPS2physical
21182203
RT27_HUMANMRPS27physical
21182203
RT31_HUMANMRPS31physical
21182203
RS4X_HUMANRPS4Xphysical
21182203
RS11_HUMANRPS11physical
21182203
RS18_HUMANRPS18physical
21182203
RLA0_HUMANRPLP0physical
21182203
RL36L_HUMANRPL36ALphysical
21182203
MEOX2_HUMANMEOX2physical
24722188
NT2NL_HUMANNOTCH2NLphysical
24722188
RFX6_HUMANRFX6physical
24722188
PLS1_HUMANPLSCR1physical
24722188
PLS1_HUMANPLSCR1physical
25416956
UBE3A_HUMANUBE3Aphysical
25408199
PRS8_HUMANPSMC5physical
15604093
NCOA1_HUMANNCOA1physical
15604093
AGR3_HUMANAGR3physical
25640309
CASC3_HUMANCASC3physical
25640309
CASZ1_HUMANCASZ1physical
25640309
DKK3_HUMANDKK3physical
25640309
FA84B_HUMANFAM84Bphysical
25640309
I13R2_HUMANIL13RA2physical
25640309
IL24_HUMANIL24physical
25640309
ITIH5_HUMANITIH5physical
25640309
KLK9_HUMANKLK9physical
25640309
MRC2_HUMANMRC2physical
25640309
TFF1_HUMANTFF1physical
25640309
TSP50_HUMANPRSS50physical
25640309

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00255Diethylstilbestrol
DB00783Estradiol
DB01196Estramustine
DB04573Estriol
DB04574Estropipate
DB00481Raloxifene
DB00675Tamoxifen
DB01108Trilostane
Regulatory Network of ESR2_HUMAN

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Related Literatures of Post-Translational Modification

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