Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
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
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
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Ca2+-calmodulin inhibits Ca2+ release mediated by type-1, -2 and -3 inositol trisphosphate receptors.
Distinct localization and function of (1,4,5)IP(3) receptor subtypes and the (1,3,4,5)IP(4) receptor GAP1(IP4BP) in highly purified human platelet membranes.
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In human platelets, type I IP3R is in intracellular membranes whereas type III IP3R is the plasma-membrane, surface-labelled subtype.
"The PM fractions were found to contain the type III (1,4,5)IP(3)R and GAP1(IP4BP) in contrast to IM, which contained type I (1,4,5)IP(3)R"
Ca2+ entry through plasma membrane IP3 receptors.
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About two functional IP3R channels per cell sit in the B-cell plasma membrane with an externally accessible pore region, carrying a substantial part of BCR-evoked Ca2+ entry.
"IP(3)Rs are unusual among endoplasmic reticulum proteins in being also functionally expressed at the PM"
IRBIT suppresses IP3 receptor activity by competing with IP3 for the common binding site on the IP3 receptor.
Hypoxia differently modulates gene expression of inositol 1,4,5-trisphosphate receptors in mouse kidney and HEK 293 cell line.
An IRBIT homologue lacks binding activity to inositol 1,4,5-trisphosphate receptor due to the unique N-terminal appendage.
Defining the membrane proteome of NK cells.
Antagonism of Beclin 1-dependent autophagy by BCL-2 at the endoplasmic reticulum requires NAF-1.
The homocysteine-inducible endoplasmic reticulum (ER) stress protein Herp counteracts mutant α-synuclein-induced ER stress via the homeostatic regulation of ER-resident calcium release channel proteins.
Role of the inositol 1,4,5-trisphosphate receptor/Ca2+-release channel in autophagy.
The Bcl-2 protein family member Bok binds to the coupling domain of inositol 1,4,5-trisphosphate receptors and protects them from proteolytic cleavage.
Recessive and Dominant De Novo ITPR1 Mutations Cause Gillespie Syndrome.
A Restricted Repertoire of De Novo Mutations in ITPR1 Cause Gillespie Syndrome with Evidence for Dominant-Negative Effect.
IRBIT controls apoptosis by interacting with the Bcl-2 homolog, Bcl2l10, and by promoting ER-mitochondria contact.
Tespa1 regulates T cell receptor-induced calcium signals by recruiting inositol 1,4,5-trisphosphate receptors.
Conformational motions and ligand-binding underlying gating and regulation in IP(3)R channel.
Molecular cloning of a cDNA for the human inositol 1,4,5-trisphosphate receptor type 1, and the identification of a third alternatively spliced variant.
The human type 1 inositol 1,4,5-trisphosphate receptor from T lymphocytes. Structure, localization, and tyrosine phosphorylation.
Induction of inositol 1,4,5 trisphosphate receptor genes by ionizing radiation.
IP3R tetramer:I(1,4,5)P3:4xCa2+ transports Ca2+ from platelet dense tubular system to cytosol
Binding of IP3 to IP3 receptor
ER calcium channels open in response to activated PKA
PKG1 phosphorylates IRAG:IP3R1 inhibiting IP3-stimulated Ca2+ release
AHCYL1:NAD+ binds ITPR1:I(1,3,5)P3 tetramer, inhibiting it
UniProtKB record for human ITPR1