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
Electronic Gene Ontology annotations created by ARBA machine learning models
Signal recognition particle components in the nucleolus.
Protein SRP68 of human signal recognition particle: identification of the RNA and SRP72 binding domains.
Protein-induced conformational changes of RNA during the assembly of human signal recognition particle.
A new mechanism of 6-((2-(dimethylamino)ethyl)amino)-3-hydroxy-7H-indeno(2,1-c)quinolin-7-one dihydrochloride (TAS-103) action discovered by target screening with drug-immobilized affinity beads.
Insights into RNA biology from an atlas of mammalian mRNA-binding proteins.
SRP RNA remodeling by SRP68 explains its role in protein translocation.
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Crystal structures of SRP68-RBD alone and with SRP RNA and SRP19; SRP68-RBD is a TPR-like module that binds the RNA three-way junction, bends the RNA, and opens the conserved 5f loop required for translocation.
Host factors that interact with the pestivirus N-terminal protease, Npro, are components of the ribonucleoprotein complex.
Structures of human SRP72 complexes provide insights into SRP RNA remodeling and ribosome interaction.
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Crystal structures of SRP68-PBD/SRP72-PBD and SRP72-RBD bound to the SRP S domain (SRP RNA, SRP19, SRP68); SRP72-RBD remodels the 5f loop involved in ribosome binding and SRP68/72 make multiple ribosome contacts.
Human apo-SRP72 and SRP68/72 complex structures reveal the molecular basis of protein translocation.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
SRPassing Co-translational Targeting: The Role of the Signal Recognition Particle in Protein Targeting and mRNA Protection.
CFTR interactome mapping using the mammalian membrane two-hybrid high-throughput screening system.
OpenCell: Endogenous tagging for the cartography of human cellular organization.
Differential CFTR-Interactome Proximity Labeling Procedures Identify Enrichment in Multiple SLC Transporters.
Nascent polypeptide:mRNA:ribosome complex binds signal recognition particle (SRP)
UniProt entry Q9UHB9 (SRP68_HUMAN), Signal recognition particle subunit SRP68
Reconstitution of the human SRP system and quantitative and systematic analysis of its ribosome interactions.
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Reconstitution of recombinant human SRP shows the SRP68/72 heterodimer binds the 80S ribosome with ultrasensitive (avidity-driven, multi-site) nanomolar affinity dominated by the SRP72 C-terminus, quantifying the SRP68/72 contribution to SRP-ribosome engagement.
The nucleolar phase of signal recognition particle assembly.
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Quantitative proteomics shows SRP proteins (including SRP68) associate with scores of nucleolar/ribosome-biogenesis factors; an intact nucleolus is required for proper SRP protein localization, and some SRP proteins are detected in Cajal bodies, defining a nucleolar phase of SRP assembly.
Identification of biallelic germline variants of SRP68 in a sporadic case with severe congenital neutropenia.
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Biallelic germline SRP68 loss-of-function variants cause severe congenital neutropenia; patient granulocytic cells show reduced SRP68 protein, impaired granulopoiesis, ER-stress (spliced XBP1) and p53-pathway activation.