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

Urm1: A Non-Canonical UBL.

Biomolecules - 22 Jan 2021

Termathe Martin, Leidel Sebastian A

Abstract excerpt

Urm1 (ubiquitin related modifier 1) is a molecular fossil in the class of ubiquitin-like proteins (UBLs). It encompasses characteristics of classical UBLs, such as ubiquitin or SUMO (small ubiquitin-related modifier), but also of bacterial sulfur-carrier proteins (SCP). Since its main function is to modify tRNA, Urm1 acts in a non-canonical manner. Uba4, the activating enzyme of Urm1, contains two domains: a...

Read the complete abstract on PubMed

Topics

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

Share to Gene Expression Regulation, Fungal
Share to Homeostasis
Share to RNA, Transfer

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Small Ubiquitin-Related Modifier Proteins

Share to Stress, Physiological

Share to Sulfurtransferases

Share to Ubiquitin

Share to Ubiquitins

Source

Open in PubMed Open full text

Identifiers

PMID: 33499055
DOI: 10.3390/biom11020139
PMCID: PMC7911844

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Urm1: A Non-Canonical UBL.PMID 33499055Read ↗

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

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

Molecular basis for thiocarboxylation and release of Urm1 by its E1-activating enzyme Uba4.Semantic proximity Read ↗

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

A guide to UFMylation, an emerging posttranslational modificationSemantic proximity Read ↗

The Post-Translational Role of UFMylation in Physiology and DiseaseSemantic proximity Read ↗

A Concerted Action of UBA5 C-Terminal Unstructured Regions Is Important for Transfer of Activated UFM1 to UFC1.Semantic proximity Read ↗

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

Ubiquitin-Like Modifiers: Emerging Regulators of Protozoan ParasitesSemantic proximity Read ↗

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

TusA Is a Versatile Protein That Links Translation Efficiency to Cell Division in Escherichia coli.Semantic proximity Read ↗

tRNA 2’-O-methylation modulates small RNA silencing and life span in <i>Drosophila</i>Semantic proximity Read ↗

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