dbPTM

ESR1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ESR1_MOUSE
UniProt AC	P19785
Protein Name	Estrogen receptor
Gene Name	Esr1
Organism	Mus musculus (Mouse).
Sequence Length	599
Subcellular Localization	Nucleus . Cytoplasm. Golgi apparatus. Cell membrane. Colocalizes with ZDHHC7 and ZDHHC21 in the Golgi apparatus where most probably palmitoylation occurs. Associated with the plasma membrane when palmitoylated..
Protein Description	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..
Protein Sequence	MTMTLHTKASGMALLHQIQGNELEPLNRPQLKMPMERALGEVYVDNSKPTVFNYPEGAAYEFNAAAAAAAAASAPVYGQSGIAYGPGSEAAAFSANSLGAFPQLNSVSPSPLMLLHPPPQLSPFLHPHGQQVPYYLENEPSAYAVRDTGPPAFYRSNSDNRRQNGRERLSSSNEKGNMIMESAKETRYCAVCNDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQACRLRKCYEVGMMKGGIRKDRRGGRMLKHKRQRDDLEGRNEMGASGDMRAANLWPSPLVIKHTKKNSPALSLTADQMVSALLDAEPPMIYSEYDPSRPFSEASMMGLLTNLADRELVHMINWAKRVPGFGDLNLHDQVHLLECAWLEILMIGLVWRSMEHPGKLLFAPNLLLDRNQGKCVEGMVEIFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGVYTFLSSTLKSLEEKDHIHRVLDKITDTLIHLMAKAGLTLQQQHRRLAQLLLILSHIRHMSNKGMEHLYNMKCKNVVPLYDLLLEMLDAHRLHAPASRMGVPPEEPSQTQLATTSSTSAHSLQTYYIPPEAEGFPNTI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	O-linked_Glycosylation	MTLHTKASGMALLHQ CEEECHHHHHHHHHH	30.56	8999954
50	O-linked_Glycosylation	YVDNSKPTVFNYPEG EECCCCCCEECCCCC	41.27	8999954
108	Phosphorylation	FPQLNSVSPSPLMLL CCCCCCCCCCCEEEC	21.34	-
110	Phosphorylation	QLNSVSPSPLMLLHP CCCCCCCCCEEECCC	24.14	-
122	Phosphorylation	LHPPPQLSPFLHPHG CCCCCCCCCCCCCCC	14.36	14647453
156	Phosphorylation	GPPAFYRSNSDNRRQ CCCCCCCCCCCCCCC	29.34	8541227
158	Phosphorylation	PAFYRSNSDNRRQNG CCCCCCCCCCCCCCH	37.19	8541227
171	Phosphorylation	NGRERLSSSNEKGNM CHHHHHCCCCHHCCC	41.60	14647453
216	Phosphorylation	CKAFFKRSIQGHNDY HHHHHHHHHCCCCCC	21.61	-
264	Asymmetric dimethylarginine	GGIRKDRRGGRMLKH CCCCCCCCCCCCCCC	63.15	-
264	Methylation	GGIRKDRRGGRMLKH CCCCCCCCCCCCCCC	63.15	-
287	Phosphorylation	GRNEMGASGDMRAAN CCCCCCCCCCCCHHH	29.60	-
298	Phosphorylation	RAANLWPSPLVIKHT CHHHCCCCCEEEEEC	21.20	8541227
451	S-palmitoylation	LQGEEFVCLKSIILL CCCCCEEEEEEEHHH	4.87	22031296
464	Phosphorylation	LLNSGVYTFLSSTLK HHCCCHHHHHHHHHH	18.72	-
468	Phosphorylation	GVYTFLSSTLKSLEE CHHHHHHHHHHHHHH	39.65	-
541	Phosphorylation	CKNVVPLYDLLLEML CCCCCHHHHHHHHHH	9.85	-
575	O-linked_Glycosylation	SQTQLATTSSTSAHS CCCCEECCCCCCCCE	18.31	8999954

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
108	S	Phosphorylation	Kinase	CDK2	P97377	Uniprot
110	S	Phosphorylation	Kinase	CDK2	P97377	Uniprot
171	S	Phosphorylation	Kinase	RPS6KB1	Q8BSK8	GPS
171	S	Phosphorylation	Kinase	CK2	-	Uniprot
216	S	Phosphorylation	Kinase	PRKCA	P20444	GPS
309	S	Phosphorylation	Kinase	PAK1	O88643	GPS
541	Y	Phosphorylation	Kinase	TYR-KINASES	-	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	Stub1	Q9WUD1	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
122	S	Phosphorylation	-
Dephosphorylation at Ser-122 by PPP5C inhibits its transactivation activity (By similarity).
264	R	Methylation	-
Demethylated by JMJD6 at Arg-264.
264	R	Methylation	-
Dimethylated by PRMT1 at Arg-264.
451	C	Palmitoylation	22031296
Palmitoylated at Cys-451 by ZDHHC7 and ZDHHC21.

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 ESR1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SMCE1_HUMAN	SMARCE1	physical	12145209
JUN_MOUSE	Jun	physical	19605792
NCOA2_MOUSE	Ncoa2	physical	20211142
PO4F1_MOUSE	Pou4f1	physical	20211142
PO4F2_MOUSE	Pou4f2	physical	20211142
SMCE1_HUMAN	SMARCE1	physical	16769725
KDM4B_MOUSE	Kdm4b	physical	21445275
LEF1_MOUSE	Lef1	physical	18202148
TF7L1_MOUSE	Tcf7l1	physical	18202148
CTNB1_MOUSE	Ctnnb1	physical	18202148
STA5A_MOUSE	Stat5a	physical	15304355
SRC_MOUSE	Src	physical	17921256
NOS3_MOUSE	Nos3	physical	17921256

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ESR1_MOUSE

Related Literatures of Post-Translational Modification

O-linked Glycosylation
Reference	PubMed
"Glycosylation of the murine estrogen receptor-alpha."; Cheng X., Hart G.W.; J. Steroid Biochem. Mol. Biol. 75:147-158(2000). Cited for: GLYCOSYLATION AT SER-10; THR-50 AND THR-575.	11226831 [Abstract]
"A subpopulation of estrogen receptors are modified by O-linked N-acetylglucosamine."; Jiang M.S., Hart G.W.; J. Biol. Chem. 272:2421-2428(1997). Cited for: GLYCOSYLATION AT THR-575.	8999954 [Abstract]
Palmitoylation
Reference	PubMed
"DHHC-7 and -21 are palmitoylacyltransferases for sex steroidreceptors."; Pedram A., Razandi M., Deschenes R.J., Levin E.R.; Mol. Biol. Cell 23:188-199(2012). Cited for: PALMITOYLATION AT CYS-451, AND MUTAGENESIS OF CYS-451.	22031296 [Abstract]

show

show

show

show