Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
Combined Automated Annotation using Multiple IEA Methods
Arginine and glutamate-rich 1 (ARGLU1) interacts with mediator subunit 1 (MED1) and is required for estrogen receptor-mediated gene transcription and breast cancer cell growth.
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ARGLU1 binds directly to a far C-terminal region of MED1 and colocalizes with MED1 in the nucleus.
"We found that ARGLU1 (arginine and glutamate rich 1) not only colocalizes with MED1 in the nucleus, but also directly interacts with a far C-terminal region of MED1."
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ARGLU1 is recruited to endogenous estrogen receptor target gene promoters in a ligand-dependent manner and is required for their expression.
"Importantly, ARGLU1 is recruited, in a ligand-dependent manner, to endogenous estrogen receptor target gene promoters and is required for their expression."
Dynamic protein-protein interaction wiring of the human spliceosome.
The three clades of the telomere-associated TLO gene family of Candida albicans have different splicing, localization, and expression features.
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Mitochondrial localisation is restricted to the gamma clade of the TLO family; the alpha and beta clades are nuclear.
"clade α and clade β have no introns and encode proteins that localize primarily to the nucleus; clade γ sometimes undergoes splicing, and the gene products localize within the mitochondria as well as the nuclei."
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TLO proteins carry a conserved Med2 domain, i.e. they are Mediator tail subunit paralogs, and the family is a Candida albicans-specific expansion.
"The 14 expressed TLO gene family members have a conserved Med2 domain at the N terminus, suggesting a role in general transcription."
The protein interaction landscape of the human CMGC kinase group.
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The study identified candidate substrates for CMGC kinases in addition to binding partners.
"Furthermore, the analysis revealed a kinase-kinase subnetwork and candidate substrates for CMGC kinases."
E-cadherin interactome complexity and robustness resolved by quantitative proteomics.
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The study used proximity biotinylation to identify 561 proteins near the E-cadherin cytoplasmic tail, i.e. neighbourhood rather than binding.
"We used proximity biotinylation and quantitative proteomics to identify 561 proteins in the vicinity of the cytoplasmic tail of E-cadherin."
An Ultraconserved Element (UCE) controls homeostatic splicing of ARGLU1 mRNA.
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Raising ARGLU1 protein shifts its own transcript towards intron retention and NMD and away from the productive isoform; loss of protein shifts it the other way.
"Further, overexpression of the ARGLU1 protein shifted the splicing of endogenous ARGLU1 mRNA, resulting in an increase in the retained intron isoform and nonsense mediated decay susceptible isoform and a decrease in the fully spliced isoform."
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The isoform structure was confirmed in three human cell lines.
"This was confirmed in HeLa, HEK293 Flp-In TRex and MCF7 cells by RT-PCR and Northern blot (Figure 2A and B, Supplementary Figure S1B)."
ARGLU1 is a transcriptional coactivator and splicing regulator important for stress hormone signaling and development.
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The C-terminal region alone coactivates GR as well as the full-length protein; the N-terminal region alone does not.
"These studies revealed that the construct containing only the C-terminus (ARGLU1C-term) retained the ability to coactivate GR, comparable to that of the full-length protein; whereas, the construct containing only the N-terminus (ARGLU1N-term) did not (Figure 2B)."
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The degenerate LXXLL motifs do not account for coactivation.
"These data suggest that while the C-terminal domain is important for activation, these motifs alone cannot account for the ARGLU1 mediated transactivation of GR, thus, other non-canonical interactions are likely involved."
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Purified ARGLU1 binds G-rich CGG(A/G)GG RNA elements in vitro.
"Computational analysis of the microarray data found full length ARGLU1 preferentially bound to CGG(A/G)GG type k-mers (Figure 3C, Supplementary Figure S9)."
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ARGLU1 and its N-terminal region, but not its C-terminal region, enrich specific endogenous pre-mRNAs in cells.
"Our results showed that full-length ARGLU1 and ARGLU1N-term (but not ARGLU1C-term) pulldowns enrich Lpin1 and Bin1 pre-mRNA"
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A splicing target lacking G-rich sequence near its splice sites is not bound, so some ARGLU1-dependent splicing changes are indirect.
"In contrast, Brwd3 pre-mRNA (undergoes ARGLU1-dependent AS but does not contain G-rich sequences near splice sites) is not enriched (Supplementary Figure S9E)."
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ARGLU1 interacts reciprocally with PUF60, U2AF2 and JMJD6.
"The MS results were confirmed with co-IP western blotting experiments in which ARGLU1 was found to interact with PUF60, U2AF2 and JMJD6 (Figure 3B)."
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ARGLU1 colocalizes strongly with the nuclear speckle marker SRSF2.
"Studies performed with GFP-tagged nuclear speckle marker SRSF2 demonstrated very high co-localization with ARGLU1 with a Pearson correlation coefficient (PCC) of 0.83"
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Glucocorticoid-induced alternative splicing changes are largely lost without ARGLU1.
"Treatment with dexamethasone, a GR activator, also induces changes in the pattern of alternatively spliced genes, many of which were lost when ARGLU1 was absent."
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Distinct biogenesis pathways may have led to functional divergence of the human and Drosophila Arglu1 sisRNA.
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The ARGLU1-derived sisRNA binds ARGLU1 protein and relocates it to nuclear speckles, relieving its splicing-inhibitory activity on the host gene.
"Mechanistically, Arglu1 sisRNA represses the splicing-inhibitory activity of ARGLU1 protein by binding to ARGLU1 protein and promoting its localization to nuclear speckles, away from the Arglu1 gene locus."
Deletion of ARGLU1 causes global defects in alternative splicing in vivo and mouse cortical malformations primarily via apoptosis.
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Arglu1 ablation in mouse embryonic cortex causes widespread alternative splicing changes enriched for neuronal genes.
"RNA seq analysis reveals widespread changes in alternative splicing in the mutant mouse embryonic cortex, preferentially affecting genes involved in neuronal functions."
ARGLU1 enhances promoter-proximal pausing of RNA polymerase II and stimulates DNA damage repair.
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ARGLU1 has no known structural or functional domains and is predicted intrinsically disordered.
"Computational prediction suggests that ARGLU1 contains intrinsically disordered regions and lacks any known structural or functional domains."
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ARGLU1 enhances promoter-proximal RNA polymerase II pausing, proposed to act by inhibiting the JMJD6-BRD4 interaction.
"Transcriptional effects induced by ARGLU1 occur via enhancement of promoter-proximal RNA polymerase II pausing, likely by inhibiting the interaction between JMJD6 and BRD4."
Systematic identification of post-transcriptional regulatory modules.
PAK1 mediated phosphorylation of ARGLU1 promotes tumorigenic potential of Breast cancer.
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PAK1 phosphorylates ARGLU1 at Ser-77, the same residue reported by five independent phosphoproteomic studies in UniProt.
"we identified and confirmed that PAK1 phosphorylated ARGLU1 at Ser 77"
miR-335-5p Inhibits Progression of Uterine Leiomyoma by Targeting ARGLU1
ARGLU1 bioinformatics results
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The PANTHER mitochondrion donor is a fungal Med2-family TLO paralog that also matches the ARGLU1 family signature, not a Swiss-Prot ARGLU1 ortholog.
"a **fungal Med2-family protein that also matches the ARGLU1 family signature**"
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The cadherin-binding annotation comes from a proximity assay, not a direct binding assay.
"the assay measures proximity, not binding"
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GO:1990935 splicing factor binding exists and is the informative replacement term for ARGLU1 interactions with U2AF2 and PUF60.
"`GO:1990935 splicing factor binding` is active, is a molecular function"
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ARGLU1's experimentally delimited N-terminal RNA-binding region has a serine-arginine repeat composition that makes the SRPK2 interaction structurally coherent.
"The N-terminal RNA-binding region is not merely "arginine-rich": it is a genuine **RS-repeat (SR-protein-like) region**"