Alyref
entrez
21681
canonical
uniprot
O08583
canonical
ensembl
ENSMUSG00000025134
resolver
ensp
ENSMUSP00000026125
resolver
genesymbol
Alyref
resolver
genesymbol_syn
Aly
resolver
genesymbol_syn
Ref1
resolver
genesymbol_syn
Refbp1
resolver
genesymbol_syn
THOC4
resolver
uniprot
Q0VBL5
resolver
uniprot
Q8CBM4
resolver
uniprot
Q9JJW7
resolver
uniprot_entry
THOC4_MOUSE
resolver
uniprot_sec
Q0VBL5
resolver
uniprot_sec
Q8CBM4
resolver
uniprot_sec
Q9JJW7
resolver
amino_acid_sequence
MADKMDMSLDDIIKLNRSQRGGRGGGRGRGRAGSQGGRGGAVQAAARVNRGGGPMRNRPAIARGAAGGGRNRPAPYSRPKQLPDKWQHDLFDSGFGGGAGVETGGKLLVSNLDFGVSDADIQELFAEFGTLKKAAVHYDRSGRSLGTADVHFERKADALKAMKQYNGVPLDGRPMNIQLVTSQIDTQRRPAQSINRGGMTRNRGSGGFGGGGTRRGTRGGSRGRGRGTGRNSKQQLSAEELDAQLDAYNARMDTS
uniprot
proteins
function
FUNCTION: 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:10786854, PubMed:11158589, PubMed:9119228). Functions as an mRNA export adapter; component of the transcription/export (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. 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 via the TAP/NXF1 pathway. Involved in the nuclear export of intronless mRNA; proposed to be recruited to intronless mRNA by ATP-bound DDX39B. Plays a key role in mRNP recognition and mRNA packaging by bridging the mRNP-bound EJC and the TREX core complex. TREX recruitment occurs via an interaction between ALYREF/THOC4 and the cap-binding protein NCBP1. Required for TREX complex assembly and for linking DDX39B to the cap-binding complex (CBC). Binds mRNA which is thought to be transferred to the NXF1-NXT1 heterodimer for export (TAP/NXF1 pathway). 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. Involved in mRNA export of C5-methylcytosine (m5C)-containing mRNAs: specifically recognizes and binds m5C mRNAs and mediates their nucleo-cytoplasmic shuttling. Acts as a chaperone and promotes the dimerization of transcription factors containing basic leucine zipper (bZIP) domains and thereby promotes transcriptional activation. Involved in transcription elongation and genome stability (By similarity). {ECO:0000250|UniProtKB:Q86V81, ECO:0000269|PubMed:10786854, ECO:0000269|PubMed:11158589, ECO:0000269|PubMed:9119228}.
uniprot
proteins
mass_dalton
26940
uniprot
proteins
post_translational_modification
PTM: Arg-50 and Arg-203 are dimethylated, probably to asymmetric dimethylarginine. Arginine methylation reduces RNA binding (By similarity). {ECO:0000250}.; PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}.
uniprot
proteins
protein_family
THOC4 family
uniprot
proteins
pubmed
10786854
uniprot
proteins
pubmed
11158589
uniprot
proteins
pubmed
12809490
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24463520
uniprot
proteins
pubmed
9119228
uniprot
proteins
sequence_length
255
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9119228}. Nucleus speckle {ECO:0000250|UniProtKB:Q86V81}. Cytoplasm {ECO:0000269|PubMed:9119228}. Note=Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and DDX39B in the nucleus and nuclear speckles. Localizes to regions surrounding nuclear speckles known as perispeckles in which TREX complex assembly seems to occur. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. {ECO:0000250|UniProtKB:Q86V81}.
uniprot
proteins