id: Pfam:PF12014
pfam_id: PF12014
name: Cyclin D1 binding domain
short_name: Cyclin_D1_bind
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF12014
counters:
  proteins: 4404
  matches: 4415
  proteomes: 2264
  taxa: 6018
  structures: 2
  alphafold_models: 3724
  domain_architectures: 75
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/
description: Ubiquitin-dependent proteolysis of cyclin D1 is associated with normal and tumour cell proliferation
  and survival. The best characterised member of this family is the SCF FBXO31 (Skp1-Cul1-Rbx1-FBXO31)
  ubiquitin ligase complex mediates genotoxic stress-induced cyclin D1 degradation [[cite:PUB00098610]].
  FBXO31 possesses a unique substrate-binding beta barrel domain, whereas cyclin D1 binds to FBXO31 by
  tucking its free C-terminal carboxylate tail into an open cavity of the C-terminal FBXO31 beta-barrel.
  Biophysical and functional studies demonstrated that SCFFBXO31 is capable of recruiting and ubiquitinating
  cyclin D1 in a phosphorylation-independent manner.