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 ubiquitin-associated domain of cellular inhibitor of apoptosis proteins facilitates ubiquitylation.

The Journal of biological chemistry - 12 Sept 2014

Budhidarmo Rhesa, Day Catherine L

Abstract excerpt

The cellular inhibitor of apoptosis (cIAP) proteins are essential RING E3 ubiquitin ligases that regulate apoptosis and inflammatory responses. cIAPs contain a ubiquitin-associated (UBA) domain that binds ubiquitin and is implicated in the regulation of cell survival and proteasomal degradation. Here we show that mutation of the MGF and LL motifs in the UBA domain of cIAP1 caused unfolding and increased cIAP1...

Read the complete abstract on PubMed

Topics

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

Share to Apoptosis
Share to Inhibitor of Apoptosis Proteins
Share to Proteasome Endopeptidase Complex

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Interaction Maps

Share to Proteolysis

Share to Ubiquitin

Share to Ubiquitin-Protein Ligases

Share to Ubiquitination

Source

Open in PubMed Open full text

Identifiers

PMID: 25065467
DOI: 10.1074/jbc.M113.545475
PMCID: PMC4162175

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

The ubiquitin-associated domain of cellular inhibitor of apoptosis proteins facilitates ubiquitylation.PMID 25065467Read ↗

The RING domain of cIAP1 mediates the degradation of RING-bearing inhibitor of apoptosis proteins by distinct pathways.Semantic proximity Read ↗

Recent advances in understanding inhibitor of apoptosis proteinsSemantic proximity Read ↗

Distinct BIR domains of cIAP1 mediate binding to and ubiquitination of tumor necrosis factor receptor-associated factor 2 and second mitochondrial activator of caspases.Semantic proximity Read ↗

Mcl-1 Ubiquitination: Unique Regulation of an Essential Survival ProteinSemantic proximity Read ↗

CUL4A ubiquitin ligase: a promising drug target for cancer and other human diseasesSemantic proximity Read ↗

Hid, Rpr and Grim negatively regulate DIAP1 levels through distinct mechanisms.Semantic proximity Read ↗

cIAP2 represses IKKα/β-mediated activation of MDM2 to prevent p53 degradation.Semantic proximity Read ↗

A family of unconventional deubiquitinases with modular chain specificity determinantsSemantic proximity Read ↗

DCAF1 (VprBP): emerging physiological roles for a unique dual-service E3 ubiquitin ligase substrate receptorSemantic proximity Read ↗

X-linked inhibitor of apoptosis protein (XIAP) regulation of cyclin D1 protein expression and cancer cell anchorage-independent growth via its E3 ligase-mediated protein phosphatase 2A/c-Jun axis.Semantic proximity Read ↗

A novel function of cIAP1 as a mediator of CHIP-driven eIF4E regulation.Semantic proximity Read ↗

Ubiquitination of the transcription factor c-MAF is mediated by multiple lysine residues.Semantic proximity Read ↗

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