ESR1_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ESR1_RAT
• UniProt AC: P06211
• Protein Name: Estrogen receptor
• Gene Name: Esr1
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 600
• 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 (By similarity)..
• Protein Sequence: MTMTLHTKASGMALLHQIQGNELEPLNRPQLKMPMERALGEVYVDNSKPAVFNYPEGAAYEFNAAAAAAAAGASAPVYGQSSITYGPGSEAAAFGANSLGAFPQLNSVSPSPLMLLHPPPHVSPFLHPHGHQVPYYLENEPSAYAVRDTGPPAFYRSNSDNRRQNGRERLSSSSEKGNMIMESAKETRYCAVCNDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQACRLRKCYEVGMMKGGIRKDRRGGRMLKHKRQRDDLEGRNEMGTSGDMRAANLWPSPLVIKHTKKNSPALSLTADQMVSALLDAEPPLIYSEYDPSRPFSEASMMGLLTNLADRELVHMINWAKRVPGFGDLNLHDQVHLLECAWLEILMIGLVWRSMEHPGKLLFAPNLLLDRNQGKCVEGMVEIFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGVYTFLSSTLKSLEEKDHIHRVLDKINDTLIHLMAKAGLTLQQQHRRLAQLLLILSHIRHMSNKGMEHLYNMKCKNVVPLYDLLLEMLDAHRLHAPASRMGVPPEEPSQSQLTTTSSTSAHSLQTYYIPPEAEGFPNTI

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
10	O-linked_Glycosylation	MTLHTKASGMALLHQ CEEECHHHHHHHHHH	30.56	-
109	Phosphorylation	FPQLNSVSPSPLMLL CCCCCCCCCCCEEEC	21.34	-
111	Phosphorylation	QLNSVSPSPLMLLHP CCCCCCCCCEEECCC	24.14	-
123	Phosphorylation	LHPPPHVSPFLHPHG CCCCCCCCCCCCCCC	13.60	12388160
172	Phosphorylation	NGRERLSSSSEKGNM CHHHHCCCCCHHCCC	42.34	-
251	Phosphorylation	ACRLRKCYEVGMMKG HHHHHHHHHHHCCCC	19.38	-
265	Asymmetric dimethylarginine	GGIRKDRRGGRMLKH CCCCCCCCCCCCCCC	63.15	-
265	Methylation	GGIRKDRRGGRMLKH CCCCCCCCCCCCCCC	63.15	-
452	S-palmitoylation	LQGEEFVCLKSIILL CCCCCEEEEEEEHHH	4.87	-
455	Phosphorylation	EEFVCLKSIILLNSG CCEEEEEEEHHHCCC	11.25	16641100
469	Phosphorylation	GVYTFLSSTLKSLEE CHHHHHHHHHHHHHH	39.65	16641100
542	Phosphorylation	CKNVVPLYDLLLEML CCCCCHHHHHHHHHH	9.85	-
576	O-linked_Glycosylation	SQSQLTTTSSTSAHS CCCCCCCCCCCCCCE	18.55	-

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
109	S	Phosphorylation	Kinase	CDK2	Q63699	Uniprot
111	S	Phosphorylation	Kinase	CDK2	Q63699	Uniprot
172	S	Phosphorylation	Kinase	CK2	-	Uniprot
542	Y	Phosphorylation	Kinase	TYR-KINASES	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
123	S	Phosphorylation	Dephosphorylation at Ser-123 by PPP5C inhibits its transactivation activity (By similarity).	-
265	R	Methylation	Demethylated by JMJD6 at Arg-265.	-
265	R	Methylation	Dimethylated by PRMT1 at Arg-265.	-
452	C	Palmitoylation	Palmitoylated at Cys-452 by ZDHHC7 and ZDHHC21.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of ESR1_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UBC_RAT	Ubc	physical	21808025
BAG1_RAT	Bag1	physical	21808025
NEDD8_RAT	Nedd8	physical	21808025
PRS8_RAT	Psmc5	physical	11818503
UBA3_RAT	Uba3	physical	11818503
TSC1_RAT	Tsc1	physical	15851513
DAAF4_RAT	Dyx1c1	physical	19423554

Drug and Disease Associations

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