Annotation inferences using phylogenetic trees
Gene Ontology annotation based on curation of immunofluorescence data
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Combined Automated Annotation using Multiple IEA Methods
The N-terminal region of the alpha-subunit of the TRAP complex has a conserved cluster of negative charges.
-
TRAP-alpha is a single-spanning ER membrane protein found in proximity to nascent polypeptides during translocation
-
Conservation across eukaryotes (human, fish, plants) with preserved charge distribution and glycosylation sites
Translocon-associated protein alpha transcripts are induced by granulocyte-macrophage colony-stimulating factor and exhibit complex alternative polyadenylation.
-
TRAP-alpha mRNA is upregulated by GM-CSF
-
Higher expression in proliferating vs quiescent cells
-
Gene located on chromosome 6
Simultaneous induction of the four subunits of the TRAP complex by ER stress accelerates ER degradation.
-
All four TRAP subunits induced by ER stress via XBP1/IRE1alpha pathway
-
TRAP complex associates with ERAD substrates at late stage
-
Preferential binding to misfolded proteins over correctly folded substrates
-
TRAP involved in ERAD pathway, not just nascent polypeptide biosynthesis
Palmitoylated calnexin is a key component of the ribosome-translocon complex.
An AP-MS- and BioID-compatible MAC-tag enables comprehensive mapping of protein interactions and subcellular localizations.
OpenCell: Endogenous tagging for the cartography of human cellular organization.
Visualization of translation and protein biogenesis at the ER membrane.
-
Near-atomic resolution cryo-ET structure of SEC61-TRAP-OSTA translocon complex
-
TRAP present in both signal peptide and multipass translocon variants
-
AlphaFold model of TRAP fits structural density
-
TRAP makes specific interactions with SEC61 and OSTA within the translocon
Expression of SSR1 (Trap alpha)
Deep research review of SSR1
-
TRAP-alpha is the alpha subunit of the ER-resident TRAP complex that stably associates with the Sec61 protein-conducting channel and the ribosome
-
TRAP assists co-translational translocation of secretory and membrane proteins, especially those with weak or atypical signal peptides
-
Cryo-EM structures show TRAP-alpha contains a prominent luminal domain positioned directly beneath the Sec61alpha channel exit and a long, diagonal transmembrane helix