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
A human protein-protein interaction network: a resource for annotating the proteome.
The structure of the mammalian signal recognition particle (SRP) receptor as prototype for the interaction of small GTPases with Longin domains.
Subcellular localization of APMCF1 and its biological significance of expression pattern in normal and malignant human tissues.
Different effects of Sec61α, Sec62 and Sec63 depletion on transport of polypeptides into the endoplasmic reticulum of mammalian cells.
MTR120/KIAA1383, a novel microtubule-associated protein, promotes microtubule stability and ensures cytokinesis.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Multimodal cell maps as a foundation for structural and functional genomics.
Expression of SRPRB (SRP Receptor subunit beta)
Structure of a prehandover mammalian ribosomal SRP·SRP receptor targeting complex.
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Cryo-EM structure of the mammalian translating ribosome with SRP and SRP receptor in a prehandover conformation; GTP-bound SRbeta and eukaryote-specific SRP/SR proteins form a large assembly at the distal SRP RNA site, and SRP/SR GTP hydrolysis is delayed at this stage to allow signal-sequence handover.
Receptor compaction and GTPase rearrangement drive SRP-mediated cotranslational protein translocation into the ER.
Examining SRP pathway function in mRNA localization to the endoplasmic reticulum.
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CRISPR/Cas9 knockout of SRPRB (SRbeta) in mammalian cells profoundly destabilizes SRalpha (proteasome-sensitive) and redistributes residual SRalpha to the cytosol, yet steady-state ER mRNA localization is largely unaltered, uncoupling ER mRNA localization from SRP receptor expression.
Signal recognition particle receptor-β (SR-β) coordinates cotranslational N-glycosylation.
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SRbeta (SRPRB) is required for assembly of an N-glycosylation-competent translocon; perturbing the SRbeta GTP-binding site (mutation or guanine-analog probes) causes hypoglycosylation and reduces SRbeta association with the oligosaccharyltransferase (OST) complex without disrupting SRalpha-SRbeta association, revealing a function coordinating ER translation with N-glycosylation.