a chaperone protein that promotes the dimerization of transcription factors containing basic leucine zipper (bZIP) domains thus promoting transcriptional activation. Plays a role in mRNA processing and export. May function as scaffold that mediates interactions between proteins and/or RNA. Integral part of the THO/TREX complex that is recruited to transcribed genes and travels with the RNA polymerase during elongation. Is part of the exon junction complex that remains associated with spliced mRNA and plays an important role in mRNA export and nonsense-mediated RNA decay. Nuclear localization, translocates to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Two differentially spliced isoforms have been described. Note: This description may include information from UniProtKB.
Protein type: Transcription, coactivator/corepressor; RNA-binding; Spliceosome; Chaperone
Molecular Function: nucleotide binding; protein binding
Biological Process: intronless viral mRNA export from host nucleus; mRNA 3'-end processing; mRNA export from nucleus; nuclear mRNA splicing, via spliceosome; osteoblast differentiation; positive regulation of RNA elongation; regulation of DNA recombination; replication fork processing; RNA export from nucleus; termination of RNA polymerase II transcription
LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.