PREY

ESR1

ER, ESR, ESRA, ESTRR, Era, NR3A1, RP1-130E4.1
estrogen receptor 1
GO Process (22)
GO Function (16)
GO Component (6)
Homo sapiens

Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Publication

The N-terminal regions of estrogen receptor alpha and beta are unstructured in vitro and show different TBP binding properties.

Waernmark A, Wikstroem A, Wright AP, Gustafsson JA, Haerd T

The N-terminal regions of the estrogen receptor alpha (ER alpha-N) and beta (ER beta-N) were expressed and purified to homogeneity. Using NMR and circular dichroism spectroscopy, we conclude that both ER alpha-N and ER beta-N are unstructured in solution. The TATA box-binding protein (TBP) has been shown previously to interact with ER alpha-N in vitro and to potentiate ER-activated transcription. ... [more]

J. Biol. Chem. Dec. 07, 2001; 276(49);45939-44 [Pubmed: 11595744]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
ESR1 TBP
Affinity Capture-MS
Affinity Capture-MS

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.

High-BioGRID
2804694
ESR1 TBP
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
-

Curated By

  • BioGRID