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

Features of the parkin/ariadne-like ubiquitin ligase, HHARI, that regulate its interaction with the ubiquitin-conjugating enzyme, Ubch7.

The Journal of biological chemistry - 1 Jun 2001

Ardley H C, Tan N G, Rose S A, Markham A F, Robinson P A

Abstract excerpt

We recently reported the identification of a RING finger-containing protein, HHARI (human homologue of Drosophila ariadne), which binds to the human ubiquitin-conjugating enzyme UbcH7 in vitro. We now demonstrate that HHARI interacts and co-localizes with UbcH7 in mammalian cells, particularly in the perinuclear region. We have further defined a minimal interaction region of HHARI comprising residues 186-254,...

Read the complete abstract on PubMed

Topics

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

Share to COS Cells
Share to Insect Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ligases

Share to Microscopy, Confocal

Share to Precipitin Tests

Share to Proto-Oncogene Proteins c-myc

Share to Ubiquitin-Conjugating Enzymes

Share to Zinc Fingers

Source

Identifiers

PMID: 11278816
DOI: 10.1074/jbc.M011028200

Genes

RING1
CBL

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Features of the parkin/ariadne-like ubiquitin ligase, HHARI, that regulate its interaction with the ubiquitin-conjugating enzyme, Ubch7.PMID 11278816Read ↗

Structure of the C-terminal RING finger from a RING-IBR-RING/TRIAD motif reveals a novel zinc-binding domain distinct from a RING.Semantic proximity Read ↗

The acidic N-terminus of HHARI and neddylation are essential for the activation and maintenance of RIG-I-mediated type I interferon responseSemantic proximity Read ↗

Structure and function of Parkin E3 ubiquitin ligase reveals aspects of RING and HECT ligases.Semantic proximity Read ↗

Parkin–phosphoubiquitin complex reveals cryptic ubiquitin-binding site required for RBR ligase activitySemantic proximity Read ↗

SH3 Domains from a Subset of BAR Proteins Define a Ubl-Binding Domain and Implicate Parkin in Synaptic UbiquitinationSemantic proximity Read ↗

Structure of the human Parkin ligase domain in an autoinhibited state.Semantic proximity Read ↗

The ring between ring fingers (RBR) protein familySemantic proximity Read ↗

TRIAD1 and HHARI bind to and are activated by distinct neddylated Cullin‐RING ligase complexesSemantic proximity Read ↗

Ariadne-1: a vital Drosophila gene is required in development and defines a new conserved family of ring-finger proteins.Semantic proximity Read ↗

Structure of the Parkin in-between-ring domain provides insights for E3-ligase dysfunction in autosomal recessive Parkinson's disease.Semantic proximity Read ↗

Comparative Genomics of the RBR Family, Including the Parkinson's Disease–Related Gene Parkin and the Genes of the Ariadne SubfamilySemantic proximity Read ↗

Parkin and relatives: the RBR family of ubiquitin ligasesSemantic proximity Read ↗

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