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

GO_REF:0000117

Electronic Gene Ontology annotations created by ARBA machine learning models

PMID:16672232

Protein SRP68 of human signal recognition particle: identification of the RNA and SRP72 binding domains.

SRP68 and SRP72 form a heterodimer; ~150 N-terminal residues of SRP72, within a predicted tandem array of four TPR-like motifs, mediate binding to SRP68.

PMID:17254600

Protein-induced conformational changes of RNA during the assembly of human signal recognition particle.

SRP68/72, together with SRP19, rearranges the 7SL RNA into an SRP54-binding-competent state, demonstrating SRP72's role in SRP assembly.

PMID:18089836

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.

Identifies the signal recognition particle (SRP) as the cellular target of TAS-103; primarily characterizes SRP54 but assays the intact SRP complex.

PMID:22541560

Exome sequencing identifies autosomal-dominant SRP72 mutations associated with familial aplasia and myelodysplasia.

Heterozygous SRP72 mutations cause autosomal-dominant aplastic anemia/myelodysplasia (BMFS1); variants mislocalize the protein and the R207H variant affects ER localization.

PMID:22658674

Insights into RNA biology from an atlas of mammalian mRNA-binding proteins.

Interactome-capture identifies SRP72 among HeLa mRNA-binding proteins, supporting general RNA-binding activity.

PMID:22681889

The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts.

Genome-wide mRNA-interactome study identifying SRP72 as an RNA-binding protein.

PMID:24965446

Host factors that interact with the pestivirus N-terminal protease, Npro, are components of the ribonucleoprotein complex.

SRP72 co-purifies with the pestivirus Npro protease among ribosomal/ribonucleoprotein components.

PMID:27899666

Structures of human SRP72 complexes provide insights into SRP RNA remodeling and ribosome interaction.

The SRP72-PBD is a TPR that binds an extended linear SRP68 motif with high affinity; the SRP72-RBD is a flexible peptide crawling along the 5e/5f loops of SRP RNA, forming an RNA kink-turn and remodeling the ribosome-binding 5f-loop.
Docking into cryo-EM density reveals multiple contact sites between SRP68/72 and the ribosome, explaining SRP72's role in the SRP pathway.

PMID:28369529

Human apo-SRP72 and SRP68/72 complex structures reveal the molecular basis of protein translocation.

Crystal structures of human apo-SRP72 and the SRP68/72 complex; the SRP68-binding domain of SRP72 contains four atypical TPRs and a flexible C-terminal cap, and cancer-associated mutations disrupt the SRP68-SRP72 interaction and ER co-localization.

PMID:32296183

A reference map of the human binary protein interactome.

PMID:33961781

Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.

PMID:34208095

SRPassing Co-translational Targeting: The Role of the Signal Recognition Particle in Protein Targeting and mRNA Protection.

Review of SRP function in co-translational protein targeting and signal-sequence recognition; basis for the ComplexPortal NAS annotations.

PMID:35271311

OpenCell: Endogenous tagging for the cartography of human cellular organization.

Reactome:R-HSA-1799332

Nascent polypeptide:mRNA:ribosome complex binds signal recognition particle (SRP)

file:human/SRP72/SRP72-uniprot.txt

UniProt entry O76094 (SRP72_HUMAN), Signal recognition particle subunit SRP72

SRP72 is the largest subunit of the SRP (7SL RNA + SRP9/14/19/54/68/72); forms a heterodimer with SRP68; binds 7SL RNA in presence of SRP68; cytoplasmic and ER-localized; heterozygous mutations cause BMFS1.

PMID:38858088

The nucleolar phase of signal recognition particle assembly.

GFP-SRP72 co-immunoprecipitates other SRP subunits (RNase-sensitive S-domain/Alu-domain contacts) and localizes to the nucleolus (periphery of the dense fibrillar component) and to Cajal bodies; five SRP proteins including SRP72 assemble with 7SL RNA in the nucleolus before SRP54 joins in the cytoplasm.

PMID:30670445

Genetic predisposition to MDS: clinical features and clonal evolution.

Review summarizing germline predisposition syndromes to MDS/bone marrow failure, including heterozygous SRP72 mutations described in two autosomal-dominant families with aplastic anemia/myelodysplasia.

PMID:39621795

Flaviviruses induce ER-specific remodelling of protein synthesis.

Zika virus bypasses the SRP receptor via interactions between viral non-structural proteins and the host translational machinery, with NS3 engaging SRP54 and the translocon; SRP72 is implicated in the SRP machinery engaged during ER-translation remodeling.

PMID:39952919

7SL RNA and signal recognition particle orchestrate a global cellular response to acute thermal stress.

Under acute heat shock, 7SL RNA and SRP (independent of signal peptides) selectively arrest transcription and translation; SRP binds ribosomes and inhibits new protein synthesis, revealing an SRP function in the acute thermal-stress response beyond protein secretion.