id: Pfam:PF06001
pfam_id: PF06001
name: CREB-binding protein/p300, atypical RING domain
short_name: RING_CBP-p300
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF06001
counters:
  proteins: 4477
  matches: 4480
  proteomes: 1232
  taxa: 4016
  structures: 36
  alphafold_models: 170
  domain_architectures: 120
provenance:
  snapshot_id: interpro-pfam-duf-2026-10-10
  path: data/worklists/interpro-pfam-duf-2026-10-10.json
  sha256: 17fb625876c9326ed284263a47bcd84e0d7844a31c040dc06cd2260c36f1c383
  generated_at: '2026-10-10T07:44:21.614711Z'
  source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/
interpro_id: InterPro:IPR010303
description: CBP (CREB-binding protein) and p300 (also known as CREBBP or KAT3A and EP300 or KAT3B, respectively)
  are two histone acetyltransferases (HATs) that associate with and acetylate transcriptional regulators
  and chromatin. The catalytic core of animal CBP-p300 contains a bromodomain, a CH2 region containing
  a discontinuous PHD domain interrupted by this RING domain, and a HAT domain. Bromodomain-RING-PHD forms
  a compact module in which the RING domain is juxtaposed with the HAT substrate-binding site. This RING
  domain contains only a single zinc ion-binding cluster instead of two; instead of a second zinc atom,
  a network of hydrophobic interactions stabilizes the domain. The RING domain has an inhibitory role.
  Disease mutations that disrupt RING attachment lead to upregulation of HAT activity. HAT regulation
  may require repositioning of the RING domain to facilitate access to an otherwise partially occluded
  HAT active site. Plant CBP-p300 type HATs lack a bromodomain whose role in the animal animal CBP-p300's
  is to bind acetylated histones; it has been suggested that these plant proteins may utilise a different
  domain or another bromodomain protein to perform this function [[cite:PUB00074827]]. This RING domain
  has also been referred to as DUF902.