Search
activating transcription factor 7-interacting protein 1 (ATFa-associated modulator, hAM, ATF-IP, ATF-interacting protein, MBD1-containing chromatin-associated factor 1, P621, ATF7IP, MCAF, MCAF1)
Function:
- recruiter that couples transcriptional factors to general transcription apparatus & thereby modulates transcription regulation & chromatin formation
- can both act as an activator or a repressor depending on the context
- mediates MBD1-dependent transcriptional repression, probably by recruiting complexes containing SETDB1
- required to stimulate histone methyltransferase activity of SETDB1 & facilitate the conversion of dimethylated to trimethylated H3 Lys-9
- complex formed with MBD1 & SETDB1 represses transcription & couples DNA methylation & histone Lys-9 trimethylation interacts with MBD1; the interaction is enhanced when MBD1 is sumoylated
- probably forms a complex with SETDB1 & MBD1
- interacts with SUMO ubiquitin-like proteins (SUMO1, SUNO2 & SUMO3), with a preference for SUMO2 & SUMO3
- interacts with SP1, ATF7 & ZHX1
Structure: belongs to the MCAF family contains 1 fibronectin F3 module
Compartment: nucleus
Alternative splicing: named isoforms=3
Pathology:
- interacts with Epstein-Barr virus BRLF1/Rta protein, leading to promote & regulate host genes in Epstein- Barr virus- infected cells
Related
activating transcription factor 7-interacting protein 2 (MBD1-containing chromatin-associated factor 2, ATF7IP2, MCAF2)
General
phosphoprotein
transcription factor (TF)
Properties
SIZE: MW = 136 kD
entity length = 1270 aa
COMPARTMENT: cell nucleus
MOTIF: Ser phosphorylation site {S113}
glutamate-rich region {349-580}
MOTIF: glutamate residue (SEVERAL)
Ser phosphorylation site {S477}
Ser phosphorylation site {S496}
nuclear translocation signal {553-571}
SETDB1 interaction {562-817}
MOTIF: coiled coil {617-665}
Ser phosphorylation site {S673}
SUMO interaction {965-975}
MBD1 interaction {1154-1270}
MOTIF: fibronectin type III domain or F3 module {1157-1261}
Database Correlations
UniProt Q6VMQ6
References
UniProt :accession Q6VMQ6