Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Mutations in a new photoreceptor-pineal gene on 17p cause Leber congenital amaurosis.
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AIPL1 is a photoreceptor/pineal gene with TPR motifs and LCA-associated mutations.
"We describe here a new photoreceptor/pineal-expressed gene, AIPL1 (encoding aryl-hydrocarbon interacting protein-like 1), that maps within the LCA4 candidate region and whose protein contains three tetratricopeptide (TPR) motifs"
The inherited blindness associated protein AIPL1 interacts with the cell cycle regulator protein NUB1.
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AIPL1 interacts with NUB1 and is present in human photoreceptors.
"The AIPL1-NUB1 interaction was verified by co-immunoprecipitation studies in Y79 retinoblastoma cells"
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AIPL1 is expressed in developing and adult photoreceptors.
"AIPL1 is present in the developing photoreceptor layer of the human retina and within the photoreceptors of the adult retina"
AIPL1, a protein implicated in Leber's congenital amaurosis, interacts with and aids in processing of farnesylated proteins.
Genome-wide YFP fluorescence complementation screen identifies new regulators for telomere signaling in human cells.
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The study is a large-scale telomere-interactome screen, not AIPL1-focused mechanistic work.
"we identified over 300 proteins that associated with the six core telomeric proteins"
Interaction of aryl hydrocarbon receptor-interacting protein-like 1 with the farnesyl moiety.
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AIPL1 binds farnesylated-Cys through its FKBP-like domain.
"farnesylated-Cys binds exclusively to the FKBP domain of AIPL1"
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The Discussion reports lack of canonical PPIase activity for the AIPL1 FKBP-like domain, citing earlier biochemical work.
"the FKBP domain of AIPL1 does not bind FK506 or exhibit peptidylprolylisomerase activity"
The integrity and organization of the human AIPL1 functional domains is critical for its role as a HSP90-dependent co-chaperone for rod PDE6.
The Leber Congenital Amaurosis-Linked Protein AIPL1 and Its Critical Role in Photoreceptors.
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Review summarizing AIPL1 as an HSP90/HSP70 co-chaperone for PDE6.
"AIPL1 functions as a photoreceptor-specific molecular co-chaperone that interacts specifically with the molecular chaperones HSP90 and HSP70"
A reference map of the human binary protein interactome.
Molecular insights into the maturation of phosphodiesterase 6 by the specialized chaperone complex of HSP90 with AIPL1.
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Mouse AIPL1 binds human HSP90 in the biochemical assays and supports maturation of human PDE6C in the heterologous expression system.
"AIPL1 preferentially binds to HSP90 in the closed state with a stoichiometry of 1:2"
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Disrupting the tested mouse AIPL1–HSP90 interface impairs maturation of heterologously expressed PDE6C.
"Disruption of the AIPL1 interaction with HSP90 impedes maturation of PDE6"
The ubiquitin-like modifier FAT10 inhibits retinal PDE6 activity and mediates its proteasomal degradation.
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The study reports that AIPL1 stabilizes the FAT10 monomer and PDE6–FAT10 conjugate; FAT10 conjugation targets PDE6 for degradation and noncovalent FAT10 association inhibits PDE6 activity.
"We found that AIPL1 stabilizes the FAT10 monomer and the PDE6-FAT10 conjugate."
Effective AAV-mediated gene replacement therapy in retinal organoids modeling AIPL1-associated LCA4.
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AIPL1 replacement in human retinal organoids restores PDE6 abundance and lowers elevated cGMP, with no notable PDE6 transcript change, supporting post-transcriptional rescue in models without overt photoreceptor degeneration.
"Our data suggest that this is a post-transcriptional phenomenon, since no notable changes in PDE6 transcripts or the transcriptome in general were detected either by qPCR or RNA-seq after AAV7m8.hRKp.AIPL1 treatment."
Restoring Sight: The Journey of AIPL1 from Discovery to Therapy.
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Review summarizing AIPL1 as a retina-specific, structurally distinct FKBP-family member essential for PDE6 biogenesis, with FKBP-like, TPR, and primate-specific proline-rich domains, and as the target of LCA4 gene-replacement therapy.
UniProtKB record for human AIPL1 (Q9NZN9)
Proteostasis PN projected annotations report