Title : Molecular cloning and characterization of PELP1, a novel human coregulator of estrogen receptor alpha.

Pub. Date : 2001 Oct 12

PMID : 11481323






4 Functional Relationships(s)
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1 We report the characterization of a new NR coregulator: proline-, glutamic acid-, leucine-rich protein 1 (PELP1), a novel human protein that comprises 1,282 amino acids and is localized on chromosome 17. Proline proline, glutamate and leucine rich protein 1 Homo sapiens
2 The primary structure of PELP1 consists of several motifs present in most transcriptional regulators including nine NR-interacting boxes (LXXLL motifs), a zinc finger, and glutamic acid- and proline-rich regions. Glutamic Acid proline, glutamate and leucine rich protein 1 Homo sapiens
3 The primary structure of PELP1 consists of several motifs present in most transcriptional regulators including nine NR-interacting boxes (LXXLL motifs), a zinc finger, and glutamic acid- and proline-rich regions. Proline proline, glutamate and leucine rich protein 1 Homo sapiens
4 PELP1 interacts with ERalpha and also with general transcriptional coactivators p300 and cAMP response element-binding protein-binding protein. Cyclic AMP proline, glutamate and leucine rich protein 1 Homo sapiens