Rabbit Anti-ALYREF Recombinant Antibody (CBYJT-1031) (CBMAB-T0035-YJ)

Aly/REF Export Factor

ALYREF is a heat stable, nuclear protein and plays a role as a molecular chaperone. ALYREF is thought to regulate dimerization, DNA binding, and transcriptional activity of basic region-leucine zipper (bZIP) proteins.

Aly/REF Export Factor; Transcriptional Coactivator Aly/REF; BZIP-Enhancing Factor BEF; Ally Of AML-1 And LEF-1; THO Complex 4; THOC4; Tho4

Export adapter involved in nuclear export of spliced and unspliced mRNA. Binds mRNA which is thought to be transferred to the NXF1-NXT1 heterodimer for export (TAP/NFX1 pathway) (PubMed:15833825, PubMed:15998806, PubMed:17190602, PubMed:11707413, PubMed:11675789, PubMed:11979277, PubMed:18364396, PubMed:22144908, PubMed:22893130, PubMed:23222130, PubMed:25662211). Component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA (PubMed:15833825, PubMed:15998806, PubMed:17190602). TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm (PubMed:15833825, PubMed:15998806, PubMed:17190602). TREX recruitment occurs via an interaction between ALYREF/THOC4 and the cap-binding protein NCBP1 (PubMed:15833825, PubMed:15998806, PubMed:17190602). The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production; ALYREF/THOC4 mediates the recruitment of the TREX complex to the intronless viral mRNA (PubMed:18974867). Required for TREX complex assembly and for linking DDX39B to the cap-binding complex (CBC) (PubMed:15998806, PubMed:17984224). In conjunction with THOC5 functions in NXF1-NXT1 mediated nuclear export of HSP70 mRNA; both proteins enhance the RNA binding activity of NXF1 and are required for NXF1 localization to the nuclear rim (PubMed:19165146). Involved in the nuclear export of intronless mRNA; proposed to be recruited to intronless mRNA by ATP-bound DDX39B. Involved in transcription elongation and genome stability (PubMed:12438613, PubMed:17984224). Involved in mRNA export of C5-methylcytosine (m5C)-containing mRNAs: specifically recognizes and binds m5C mRNAs and mediates their nucleo-cytoplasmic shuttling (PubMed:28418038).
Acts as chaperone and promotes the dimerization of transcription factors containing basic leucine zipper (bZIP) domains and thereby promotes transcriptional activation.

mRNA 3'-end processing Source: Reactome
mRNA export from nucleus Source: UniProtKB
mRNA splicing, via spliceosome Source: Reactome
Osteoblast differentiation Source: UniProtKB
Positive regulation of DNA-templated transcription, elongation Source: UniProtKB
Regulation of DNA recombination Source: UniProtKB
Replication fork processing Source: UniProtKB
RNA export from nucleus Source: UniProtKB
Viral mRNA export from host cell nucleus Source: UniProtKB
Viral process Source: UniProtKB-KW

Nucleus; Nucleus speckle; Cytoplasm. Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and DDX39B in the nucleus and nuclear speckles. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA (PubMed:19324961). Localizes to regions surrounding nuclear speckles known as perispeckles in which TREX complex assembly seems to occur (PubMed:23826332).

Arg-204 is dimethylated, probably to asymmetric dimethylarginine. Arginine methylation reduces RNA binding.2 Publications
Citrullinated by PADI4.