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transducin-like enhancer protein 1; E(Sp1) homolog; enhancer of split groucho-like protein 1; ESG1 (TLE1)

Function: - transcriptional corepressor that binds to a number of transcription factors - inhibits NF-kappa-B-regulated gene expression - inhibits the transcriptional activation mediated by FOXA2, & by CTNNB1 & TCF family members in Wnt signaling - the effects of full-length TLE family members may be modulated by association with dominant-negative AES - unusual function as coactivator for ESRRG - phosphorylated, probably by CDK1 - degree of phosphorylation varies throughout the cell cycle, - highest at the G2/M transition - hyperphosphorylated in response to cell differentiation & interaction with HES1 or RUNX1 - homooligomer & heterooligomer with other family members - binds LEF1, RUNX1, RUNX3, FOXA2, KDM6A, UTY, histone H3, HESX1, ESRRG & the NF-kappa-B subunit RELA - interacts with HES1 (via WRPW motif) Structure: - belongs to the WD repeat groucho/TLE family - contains 6 WD repeats Compartment: - nucleus - nuclear & chromatin-associated, depending on isoforms & phosphorylation status - hyperphosphorylation decreases the affinity for nuclear components Expression: - in all tissues examined, mostly in brain, liver & muscle

General

transducin-like enhancer protein (ESG)

Properties

SIZE: entity length = 770 aa MW = 83 kD COMPARTMENT: cell nucleus MOTIF: glutamine-rich region {1-131} MOTIF: glutamine residue (SEVERAL) proline-rich region SITE: 132-199 MOTIF: proline residue (SEVERAL) CCN {200-268} MOTIF: nuclear translocation signal {225-228} Ser phosphorylation site {S239} Ser phosphorylation site {S259} Ser phosphorylation site {S263} Ser phosphorylation site {S267} serine-rich region {269-449} MOTIF: serine residue (SEVERAL) Ser phosphorylation site {S284} Ser phosphorylation site {S286} WD repeat {470-501} WD repeat {528-558} WD repeat {572-602} WD repeat {614-644} WD repeat {696-726} WD repeat {737-767}

Database Correlations

OMIM 600189 UniProt Q04724 PFAM correlations Entrez Gene 7088 Kegg hsa:7088

References

UniProt :accession Q04724