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

Identification of a nuclear export signal and protein interaction domains in deformed epidermal autoregulatory factor-1 (DEAF-1).

The Journal of biological chemistry - 30 Jul 2004

Jensik Philip J, Huggenvik Jodi I, Collard Michael W

Abstract excerpt

Deformed epidermal autoregulatory factor-1 (DEAF-1) is a DNA-binding protein required for embryonic development and linked to clinical depression and suicidal behavior in humans. Although primarily nuclear, cytoplasmic localization of DEAF-1 has been observed, and this suggests the presence of a nuclear export signal (NES). Using a series of fluorescent fusion proteins, an NES with a novel spacing of leucines...

Read the complete abstract on PubMed

Topics

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

Share to Active Transport, Cell Nucleus
Share to Cysteine

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

Share to Fatty Acids, Unsaturated

Share to Histidine

Share to Leucine

Share to Nuclear Localization Signals

Share to Precipitin Tests

Source

Identifiers

PMID: 15161925
DOI: 10.1074/jbc.M400946200

Genes

NES

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

Identification of a nuclear export signal and protein interaction domains in deformed epidermal autoregulatory factor-1 (DEAF-1).PMID 15161925Read ↗

Functional analysis of novel DEAF1 variants identified through clinical exome sequencing expands DEAF1-associated neurodevelopmental disorder (DAND) phenotype.Semantic proximity Read ↗

Structural and functional analysis of the DEAF-1 and BS69 MYND domains.Semantic proximity Read ↗

Structure and functional analysis of the MYND domain.Semantic proximity Read ↗

Mutations affecting the SAND domain of DEAF1 cause intellectual disability with severe speech impairment and behavioral problems.Semantic proximity Read ↗

An evolutionarily conserved fission yeast protein, Ned1, implicated in normal nuclear morphology and chromosome stability, interacts with Dis3, Pim1/RCC1 and an essential nucleoporin.Semantic proximity Read ↗

Multiple and surprising new functions for emerin, a nuclear membrane protein.Semantic proximity Read ↗

Deformed epidermal autoregulatory factor-1 (DEAF1) interacts with the Ku70 subunit of the DNA-dependent protein kinase complex.Semantic proximity Read ↗

Insights Into SND1 Oncogene Promoter RegulationSemantic proximity Read ↗

Novel nesprin-1 mutations associated with dilated cardiomyopathy cause nuclear envelope disruption and defects in myogenesis.Semantic proximity Read ↗

Identification of CASZ1 NES reveals potential mechanisms for loss of CASZ1 tumor suppressor activity in neuroblastoma.Semantic proximity Read ↗

Using a simple cellular assay to map NES motifs in cancer-related proteins, gain insight into CRM1-mediated NES export, and search for NES-harbouring micropeptidesSemantic proximity Read ↗

Sem1 is a functional component of the nuclear pore complex-associated messenger RNA export machinery.Semantic proximity Read ↗

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