Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The HCF repeat is an unusual proteolytic cleavage signal.

Genes & development - 15 Oct 1995

Wilson A C, Peterson M G, Herr W

Abstract excerpt

The herpes simplex virus VP16-associated protein HCF is a nuclear host-cell factor that exists as a family of polypeptides encoded by a single gene. The mature HCF polypeptides are amino- and carboxy-terminal fragments of a large approximately 300-kD precursor protein that arise through cleavage at one or more centrally located sites. The sites of cleavage are the HCF repeats, highly conserved 26-amino-acid...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Base Sequence
Share to Cell Line

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Molecular Sequence Data

Share to Mutation

Share to Recombinant Proteins

Share to RNA, Messenger

Share to Transcription Factors

Source

Identifiers

PMID: 7590226
DOI: 10.1101/gad.9.20.2445

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The HCF repeat is an unusual proteolytic cleavage signal.PMID 7590226Read ↗

Protein interactions in the herpes simplex virus type 1 VP16-induced complex: VP16 peptide inhibition and mutational analysis of host cell factor requirements.Semantic proximity Read ↗

Proteolytic processing is necessary to separate and ensure proper cell growth and cytokinesis functions of HCF-1.Semantic proximity Read ↗

Proteolysis of HCF-1 by Ser/Thr glycosylation-incompetent O-GlcNAc transferase:UDP-GlcNAc complexes.Semantic proximity Read ↗

O-GlcNAc transferase catalyzes site-specific proteolysis of HCF-1.Semantic proximity Read ↗

Conserved residues in the HIV-1 Nef hydrophobic pocket are essential for recruitment and activation of the Hck tyrosine kinase.Semantic proximity Read ↗

The conserved threonine-rich region of the HCF-1PRO repeat activates promiscuous OGT:UDP-GlcNAc glycosylation and proteolysis activities.Semantic proximity Read ↗

Zhangfei: a second cellular protein interacts with herpes simplex virus accessory factor HCF in a manner similar to Luman and VP16Semantic proximity Read ↗

Dispersed and conserved hydrophobic residues of HIV-1 Vif are essential for CBFβ recruitment and A3G suppression.Semantic proximity Read ↗

The Herpesvirus Transactivator VP16 Mimics a Human Basic Domain Leucine Zipper Protein, Luman, in Its Interaction with HCFSemantic proximity Read ↗

Primary structure and compartmentalization of Drosophila melanogaster host cell factor.Semantic proximity Read ↗

The Neuronal Host Cell Factor-Binding Protein Zhangfei Inhibits Herpes Simplex Virus ReplicationSemantic proximity Read ↗

How kelch domain-containing protein 3 distinguishes between the C-end degron of herpesviral protein UL49.5 and its mutants - Insights from molecular dynamics.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.