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

A protein conjugation system in yeast with homology to biosynthetic enzyme reaction of prokaryotes.

The Journal of biological chemistry - 17 Mar 2000

Furukawa K, Mizushima N, Noda T, Ohsumi Y

Abstract excerpt

Protein conjugation, such as ubiquitination, is the process by which the C-terminal glycine of a small modifier protein is covalently attached to target protein(s) through sequential reactions with an activating enzyme and conjugating enzymes. Here we report on a novel protein conjugation system in yeast. A newly identified ubiquitin related modifier, Urm1 is a 99-amino acid protein terminated with...

Read the complete abstract on PubMed

Topics

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

Share to Fungal Proteins
Share to Prokaryotic Cells
Share to Protein Processing, Post-Translational

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

Share to Saccharomyces cerevisiae

Share to Saccharomyces cerevisiae Proteins

Share to Sequence Homology, Amino Acid

Share to Temperature

Share to Two-Hybrid System Techniques

Source

Identifiers

PMID: 10713047
DOI: 10.1074/jbc.275.11.7462

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

A protein conjugation system in yeast with homology to biosynthetic enzyme reaction of prokaryotes.PMID 10713047Read ↗

Urm1: A Non-Canonical UBL.Semantic proximity Read ↗

Urm1 at the crossroad of modifications. 'Protein Modifications: Beyond the Usual Suspects' Review Series.Semantic proximity Read ↗

Evolutionary diversification of the autophagy-related ubiquitin-like conjugation systemsSemantic proximity Read ↗

The Uba4 domain interplay is mediated via a thioester that is critical for tRNA thiolation through Urm1 thiocarboxylation.Semantic proximity Read ↗

The prokaryotic antecedents of the ubiquitin-signaling system and the early evolution of ubiquitin-like β-grasp domainsSemantic proximity Read ↗

The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer.Semantic proximity Read ↗

Contrasting duplication patterns reflect functional diversities of ubiquitin and ubiquitin‐like protein modifiers in plantsSemantic proximity Read ↗

What Was the Set of Ubiquitin and Ubiquitin-Like Conjugating Enzymes in the Eukaryote Common Ancestor?Semantic proximity Read ↗

Overexpression of UBA5 in Cells Mimics the Phenotype of Cells Lacking UBA5.Semantic proximity Read ↗

New insights into the role of the small ubiquitin-like modifier (SUMO) in plants.Semantic proximity Read ↗

SUMO conjugation and deconjugation.Semantic proximity Read ↗

Hub1 is an essential ubiquitin-like protein without functioning as a typical modifier in fission yeast.Semantic proximity Read ↗

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