Gene Ontology annotation through association of InterPro records with GO terms
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
A-kinase-interacting protein localizes protein kinase A in the nucleus.
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AKIP1 binds the N-terminal A helix of the PKA catalytic subunit.
"we identified a PKA-interacting protein (AKIP1) that binds to the amino terminus (residues 1-39) of the C subunit of PKA."
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The contact is the catalytic subunit A helix and the AKIP1 C-terminus.
"The interaction was localized to the A helix (residues 14-39) of the C subunit and to the carboxyl terminus of AKIP1."
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AKIP1 is nuclear, in speckles.
"In normal breast (Hs 578 Bst) and HeLa cells, AKIP1 is present in the nucleus as speckles."
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AKIP1 raises nuclear PKA catalytic subunit on cAMP stimulation.
"Upon stimulation with forskolin, HeLa cells expressing AKIP1 accumulated higher levels of the endogenous C subunit in the nucleus."
Quantitative fragmentomics allow affinity mapping of interactomes.
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A systematic PDZ-PBM affinity screen, the source of 18 PDZ-partner rows.
"Here, we measure the affinities of 65,000 interactions involving PDZ domains and their target PDZ-binding motifs (PBM)"
A reference map of the human binary protein interactome.
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
A-kinase-interacting protein 1 (AKIP1) acts as a molecular determinant of PKA in NF-kappaB signaling.
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PKA phosphorylation of p65 on Ser-276 is the mechanism.
"attenuated PKA-dependent phosphorylation of p65 on Ser-276"
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AKIP1 reverses PKA's inhibitory effect on NF-kappaB.
"This inhibitory function of PKAc in NF-kappaB signaling was reversed by overexpression of AKIP1 in 293 cells."
AKIP1 enhances NF-kappaB-dependent gene expression by promoting the nuclear retention and phosphorylation of p65.
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AKIP1 binds p65 directly, by two-hybrid, pull-down and co-immunoprecipitation.
"The interaction between AKIP1 and p65 was confirmed by glutathione S-transferase pull-down assay in vitro and immunoprecipitation-Western blotting assay in vivo."
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The PKA catalytic subunit is in the AKIP1-p65 complex and phosphorylates p65.
"We found that the PKAc was present in the AKIP1.p65 complex and enhanced the transcriptional activity of NF-kappaB by phosphorylating p65."
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Knocking down AKIP1 abolishes PMA-induced NF-kappaB gene expression.
"When AKIP1 was knocked down by RNA interference, the PMA-mediated NF-kappaB-dependent gene expression was abolished, indicating a physiological role of AKIP1."
A kinase interacting protein (AKIP1) is a key regulator of cardiac stress.
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AKIP1 localizes to interfibrillary mitochondria in cardiac myocytes.
"AKIP1 is preferentially localized to interfibrillary mitochondria and up-regulated in this cardiac mitochondrial subpopulation on ischemic injury."
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Mouse and human AKIP1a are only about 70% identical.
"Because there is only 70% homology between the mouse and human AKIP1a"
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The NF-kappaB effect depends on splice variant: AKIP1b represses via SIRT1.
"AKIP1b was shown to recruit the histone deacetylase silent mating type information regulation 2 homolog (SIRT1) in a NEDDylation (NEDD8, neural precursor cell expressed, developmentally down-regulated 8-mediated)-dependent manner and repress transcription"
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AKIP1a, the canonical isoform, enhances.
"In contrast, AKIP1a was shown to recruit NF-κB in a PKA-dependent manner and enhance transcription"
Breast cancer-associated gene 3 (BCA3) is a novel Rac1-interacting protein.
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AKIP1 (BCA3) binds GTP-bound Rac1 directly.
"BCA3 binds directly to Rac and, in vivo, binds GTP-Rac but not GDP-Rac."
AKIP1 promotes early recurrence of hepatocellular carcinoma through activating the Wnt/β-catenin/CBP signaling pathway.
Affinage mechanistic annotation for AKIP1 (human)
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Affinage summarises the NF-kappaB mechanism as p65 Ser-276 phosphorylation - the canonical pathway.
"in cells with high AKIP1, PKA-activating agents enhance p65–PKAc interaction, p65 Ser-276 phosphorylation, and NF-κB-dependent transcription"