P300

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E1A binding protein p300
P300

PDB ID : 2K8F
PDB2K8F 1L3E 3BIY 1P4Q 3I3J 3IO2
HGNC(alias)EP300 (p300,KAT3B)
Gene CardEP300
Entrez2033
RefSeqNM_001429
UniProtQ09472
UCSCBrowser view
WikipediaEP300
Protein FamilyTAZ domain
Typehistone acetylation complexes
Ensembl Exp.Human

Function

p300 is the adenovirus E1A-associated cellular transcriptional co-activator protein. It is a histone acetyltransferase that regulates transcription via chromatin remodeling and plays an important role in the processes of cell proliferation and differentiation. p300 mediates cAMP-gene regulation by binding specifically to phosphorylated CREB protein. It is a co-activator of HIF1A (hypoxia-inducible factor 1 alpha), and plays a role in the stimulation of hypoxia-induced genes such as VEGF. p300 defects are a cause of Rubinstein-Taybi syndrome and may also play a role in epithelial cancer.

ENCODE ChIP-seq Datasets

Indicated in the matrix are the numbers of datasets specified by lab and cell line; when the number is greater than 1, multiple ChIP-seq experiments have been performed, some upon treatments. Click the numbers to download the data files on ChIP-seq peaks, alignments, etc.

+/-
HudsonAlpha
Stanford
GM12878 1
H1-hESC 1
HeLa-S3 1
HepG2 1 1
K562 1
SK-N-SH_RA 1
T-47D 1


Average Profiles of Modified Histones around the Summit of ChIP-seq Peaks

Average histone modification profiles are shown for the [-2 kb, +2 kb] window around the summits of TF ChIP-seq peaks, separately for peaks that are proximal ([-1kb, +1kb]) to an annotated transcript (dashed lines) start sites and for peaks that are distal (more than 1kb) to all annotated transcripts (solid lines) start sites. Proximal profiles are arranged such that the transcriptional direction of the nearest transcript is toward the right. Histone modification data were generated by the Broad team, using antibodies to pull down modified histones followed by deep sequencing of the genomic DNA associated with the modified histones. Only histone modification data from the same cell line as the TF ChIP-seq data are shown.

Mouse over a curve to reveal its identity. Mouse over a histone modification in the legend to show its curves and gray out other histone modifications in the figures. Click a histone modification in the legend to toggle on/off its curve in all figures. Click the “Proximal” or “Distal” button in the legend to show only the average histone modification profiles anchored around ChIP-seq peaks that are proximal or distal to annotated transcripts.

Average Profiles of Nucleosomes around the Summit of ChIP-seq Peaks

Average nucleosome occupancy profiles are shown for the [-2 kb, +2 kb] window around the summits of TF ChIP-seq peaks, separately for peaks that are proximal to an annotated transcript (red lines) and for peaks that are distal to all annotated transcripts (blue lines), as defined in the previous section. Nucleosome positioning data in GM12878 and K562 were generated by the Stanford team, with micrococcal nuclease digestion of chromatin followed by deep sequencing of mononucleosomal DNA.

Motifs Enriched in the Top 500 ChIP-seq Peaks

The sequences of the top 500 TF ChIP-seq peaks were used to identify enriched motifs de novo, using the MEME-ChIP suite of tools. Five motifs are reported (M1 to M5), with motif name, sequence logo, and number of peaks out of the top 500 peaks that contain a site for the motif. The motifs are then used to scan the entire set of ChIP-seq peaks and the two flanking (control) regions using the FIMO tool, and two quantities are reported for bins of peaks sorted by their ChIP-seq q-values: percentage of the peaks that contain a site for the motif, and the distribution of the distances of the motif site to the summit of the peak.

Select MotifCell Line:   Lab:   Protocol:   Treatment:   Antibody:  

Cell Line:GM12878   Lab:HudsonAlpha   Protocol:PCR1x   Treatment:None   Antibody:p300   

Binding of Other Transcription Factors or Histone Marks at the P300 Peaks

Select HeatmapLab:   Cellline:  

  • Comparison with the P300 peaks in A549 cells generated by HAIB