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

Differential ubiquitin binding by the acidic loops of Ube2g1 and Ube2r1 enzymes distinguishes their Lys-48-ubiquitylation activities.

The Journal of biological chemistry - 23 Jan 2015

Choi Yun-Seok, Lee Yun-Ju, Lee Seo-Yeon, Shi Lei, Ha Jung-Hye, Cheong Hae-Kap, Cheong Chaejoon, Cohen Robert E, Ryu Kyoung-Seok

Abstract excerpt

The ubiquitin E2 enzymes, Ube2g1 and Ube2r1, are able to synthesize Lys-48-linked polyubiquitins without an E3 ligase but how that is accomplished has been unclear. Although both E2s contain essential acidic loops, only Ube2r1 requires an additional C-terminal extension (184-196) for efficient Lys-48-ubiquitylation activity. The presence of Tyr-102 and Tyr-104 in the Ube2g1 acidic loop enhanced both ubiquitin...

Read the complete abstract on PubMed

Topics

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

Share to Disulfides
Share to Esters

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

Share to Lysine

Share to Magnetic Resonance Spectroscopy

Share to Polyubiquitin

Share to Ubiquitin

Share to Ubiquitin-Conjugating Enzymes

Share to Ubiquitination

Source

Open in PubMed Open full text

Identifiers

PMID: 25471371
DOI: 10.1074/jbc.M114.624809
PMCID: PMC4303676

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

Differential ubiquitin binding by the acidic loops of Ube2g1 and Ube2r1 enzymes distinguishes their Lys-48-ubiquitylation activities.PMID 25471371Read ↗

Dimeric Ube2g2 simultaneously engages donor and acceptor ubiquitins to form Lys48‐linked ubiquitin chainsSemantic proximity Read ↗

Pivotal role for the ubiquitin Y59-E51 loop in lysine 48 polyubiquitination.Semantic proximity Read ↗

Determinants of chemoselectivity in ubiquitination by the J2 family of ubiquitin-conjugating enzymesSemantic proximity Read ↗

Shared and distinct mechanisms of UBA1 inactivation across different diseasesSemantic proximity Read ↗

The molecular basis of lysine 48 ubiquitin chain synthesis by Ube2K.Semantic proximity Read ↗

Engineering the orthogonal ubiquitin E1-E2 pairs for identification of K27 chain linkage substrates.Semantic proximity Read ↗

Domain alternation and active site remodeling are conserved structural features of ubiquitin E1.Semantic proximity Read ↗

RING E3-Catalyzed E2 Self-Ubiquitination Attenuates the Activity of Ube2E Ubiquitin-Conjugating Enzymes.Semantic proximity Read ↗

The unifying catalytic mechanism of the RING-between-RING E3 ubiquitin ligase familySemantic proximity Read ↗

Dissecting the Specificity of Adenosyl Sulfamate Inhibitors Targeting the Ubiquitin-Activating Enzyme.Semantic proximity Read ↗

Mutations in the hydrophobic core of ubiquitin differentially affect its recognition by receptor proteins.Semantic proximity Read ↗

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

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