Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping
Gene Ontology annotation based on curation of immunofluorescence data
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Expression of functional interleukin-15 receptor and autocrine production of interleukin-15 as mechanisms of tumor propagation in multiple myeloma.
Altered natural killer cell differentiation in CD34+ progenitors from chronic myeloid leukemia patients.
IL-21 up-regulates the expression of genes associated with innate immunity and Th1 response.
The human plasma proteome: a nonredundant list developed by combination of four separate sources.
Interleukin-15 enhances human neutrophil phagocytosis by a Syk-dependent mechanism: importance of the IL-15Ralpha chain.
Soluble interleukin-15 receptor alpha (IL-15R alpha)-sushi as a selective and potent agonist of IL-15 action through IL-15R beta/gamma. Hyperagonist IL-15 x IL-15R alpha fusion proteins.
Divergent effects of IL-12 and IL-23 on the production of IL-17 by human T cells.
Mechanistic and structural insight into the functional dichotomy between IL-2 and IL-15.
CD4 ligation on human blood monocytes triggers macrophage differentiation and enhances HIV infection.
A proteome-scale map of the human interactome network.
Deficiency of Interleukin-15 Confers Resistance to Obesity by Diminishing Inflammation and Enhancing the Thermogenic Function of Adipose Tissues.
Chromosomal assignment and genomic structure of Il15.
Cloning of a T cell growth factor that interacts with the beta chain of the interleukin-2 receptor.
Role of IL-15 in HIV-1-associated hypergammaglobulinaemia.
IL15:IL15RA binds IL2RB:JAK1 and IL2RG:JAK3
IL15 binds IL2RB:JAK1 and IL2RG:JAK3
IL15RA:IL15:IL2RB:JAK1:IL2RG:JAK3 phosphorylates JAK3 and JAK1
IL15:IL15RA:IL2RB:JAK1:IL2RG:JAK3 translocates from the plasma membrane to the endosome
IL15:IL15RA:p-Y-IL2RB:p-Y-JAK1:p-Y-IL2RG:p-Y-JAK3 phosphorylates STAT3 and STAT5
p-Y-STAT3 and p-STAT5 dissociates from IL15:IL15RA:IL2RB:p-JAK1:IL2RG:p-JAK3:p-Y-STAT3:p-STAT5
IL15:IL15RA:p-Y-IL2RB:p-Y-JAK1:p-Y-IL2RG:p-Y-JAK3 binds STAT3 and STAT5
IL15:IL15RA:p-Y-IL2RB:p-Y-JAK1:p-Y-IL2RG:p-Y-JAK3:p-Y-SHC1:GRB2 binds SOS1,SOS2
Falcon deep research on IL15 GO-relevant functions
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IL15 functions primarily as an IL15RA-bound cytokine delivered by trans-presentation or as soluble IL15/IL15RA heterodimer, rather than only as free soluble cytokine.
"A central concept for GO curation is that IL-15 is not best modeled as a freely diffusing cytokine under physiologic conditions. Instead, IL-15 is commonly delivered by **trans-presentation**: an “IL-15-presenting” cell displays a **membrane IL-15/IL-15Rα complex** that stimulates neighboring lymphocytes through **IL2RB/IL2RG**."
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Specific receptor-binding terms and cell-type-specific immune process terms are preferable to generic protein binding or broad proliferation annotations.
"Prefer specific terms supported by direct assays (cytokine activity, IL15RA binding, trans-presentation, NK/CD8/B/neutrophil processes, JAK/STAT signaling, isoform-localization) and avoid generic “protein binding,” broad “cell population proliferation,” or over-broad immune/developmental annotations unless directly tested in the relevant lineage/context."
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IL15 receptor signaling activates JAK1/JAK3 and STAT3/STAT5 downstream of IL2RB/IL2RG.
"IL-15 receptor signaling activates JAK1/JAK3 and predominantly STAT5, with STAT3 also activated in some T-cell/IEL contexts downstream of IL2RB/IL2RG."
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IL15 isoforms support both secretory/extracellular localization and intracellular cytoplasm/nucleus localization depending on the signal peptide.
"The 21-aa short signal peptide isoform is largely nonsecreted and localizes to cytoplasmic and nuclear compartments, supporting isoform-specific intracellular annotations."