p400 Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. May be required for transcriptional activation of E2F1 and MYC target genes during cellular proliferation. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. May regulate ZNF42 transcription activity. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome. Belongs to the SNF2/RAD54 helicase family. SWR1 subfamily. Ubiquitously expressed. 5 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: Apoptosis; EC 3.6.1.-; EC 3.6.4.-; Helicase
Chromosomal Location of mouse Ortholog: 5|5 F
Cellular Component:  NuA4 histone acetyltransferase complex; nuclear speck; nucleus; Swr1 complex
Molecular Function:  ATP binding; chromatin binding; DNA binding; helicase activity; hydrolase activity; nucleotide binding; protein antigen binding; protein binding
Biological Process:  chromatin organization; histone H2A acetylation; histone H4 acetylation
Reference #:  Q8CHI8 (UniProtKB)
Alt. Names/Synonyms: 1700020J09Rik; AU023439; Domino homolog; E1A binding protein p400; E1A-binding protein p400; Ep400; Kiaa1498; mDo; mDomino; mKIAA1498; OTTMUSP00000018627; p40; p400; p400 kDa SWI2/SNF2-related protein
Gene Symbols: Ep400
Molecular weight: 337,180 Da
Basal Isoelectric point: 9.23  Predict pI for various phosphorylation states
Select Structure to View Below

p400

Protein Structure Not Found.

Cross-references to other databases:  AlphaFold  |  STRING  |  BioGPS  |  Pfam  |  ENZYME  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene