ALYREF
entrez
10189
canonical
uniprot
Q86V81
canonical
ensembl
ENSG00000183684
resolver
ensp
ENSP00000421592
resolver
enst
ENST00000505490
resolver
genesymbol
ALYREF
resolver
genesymbol_syn
ALY
resolver
genesymbol_syn
BEF
resolver
genesymbol_syn
THOC4
resolver
hgnc
HGNC:19071
resolver
uniprot
E9PB61
resolver
uniprot
O43672
resolver
uniprot_entry
E9PB61_HUMAN
resolver
uniprot_entry
THOC4_HUMAN
resolver
uniprot_sec
O43672
resolver
amino_acid_sequence
MADKMDMSLDDIIKLNRSQRGGRGGGRGRGRAGSQGGRGGGAQAAARVNRGGGPIRNRPAIARGAAGGGGRNRPAPYSRPKQLPDKWQHDLFDSGFGGGAGVETGGKLLVSNLDFGVSDADIQELFAEFGTLKKAAVHYDRSGRSLGTADVHFERKADALKAMKQYNGVPLDGRPMNIQLVTSQIDAQRRPAQSVNRGGMTRNRGAGGFGGGGGTRRGTRGGARGRGRGAGRNSKQQLSAEELDAQLDAYNARMDTS
uniprot
proteins
function
FUNCTION: 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 (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 via the TAP/NXF1 pathway (PubMed:15833825, PubMed:15998806, PubMed:17190602). Involved in the nuclear export of intronless mRNA; proposed to be recruited to intronless mRNA by ATP-bound DDX39B (PubMed:17984224). Plays a key role in mRNP recognition and mRNA packaging by bridging the mRNP-bound EJC and the TREX core complex (PubMed:37020021). TREX recruitment occurs via an interaction between ALYREF/THOC4 and the cap-binding protein NCBP1 (PubMed:15833825, PubMed:15998806, PubMed:17190602, PubMed:37020021). Required for TREX complex assembly and for linking DDX39B to the cap-binding complex (CBC) (PubMed:15998806, PubMed:17984224, PubMed:37020021). Binds mRNA which is thought to be transferred to the NXF1-NXT1 heterodimer for export (TAP/NXF1 pathway) (PubMed:11675789, PubMed:11707413, PubMed:11979277, PubMed:15833825, PubMed:15998806, PubMed:17190602, PubMed:18364396, PubMed:22144908, PubMed:22893130, PubMed:23222130, PubMed:25662211). 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 mRNA export of C5-methylcytosine (m5C)-containing mRNAs: specifically recognizes and binds m5C mRNAs and mediates their nucleo-cytoplasmic shuttling (PubMed:28418038). Acts as a chaperone and promotes the dimerization of transcription factors containing basic leucine zipper (bZIP) domains and thereby promotes transcriptional activation (PubMed:10488337). Involved in transcription elongation and genome stability (PubMed:12438613). {ECO:0000269|PubMed:10488337, ECO:0000269|PubMed:11675789, ECO:0000269|PubMed:11707413, ECO:0000269|PubMed:11979277, ECO:0000269|PubMed:12438613, ECO:0000269|PubMed:15833825, ECO:0000269|PubMed:15998806, ECO:0000269|PubMed:17190602, ECO:0000269|PubMed:17984224, ECO:0000269|PubMed:18364396, ECO:0000269|PubMed:19165146, ECO:0000269|PubMed:22144908, ECO:0000269|PubMed:22893130, ECO:0000269|PubMed:23222130, ECO:0000269|PubMed:25662211, ECO:0000269|PubMed:28418038, ECO:0000269|PubMed:37020021}.; FUNCTION: (Microbial infection) 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. {ECO:0000269|PubMed:12438613, ECO:0000269|PubMed:18974867}.
uniprot
proteins
mass_dalton
26888
uniprot
proteins
mutagenesis
MUTAGEN 87; /note="W->S: Disrupts interaction with the EJC-RNA complex and abolishes multimerization; when associated with S-92."; /evidence="ECO:0000269|PubMed:37020021"; MUTAGEN 92; /note="F->S: Disrupts interaction with the EJC-RNA complex and abolishes multimerization; when associated with S-87."; /evidence="ECO:0000269|PubMed:37020021"; MUTAGEN 115; /note="F->S: Disrupts interaction with the EJC-RNA complex and abolishes multimerization; when associated with 139-Y--R-144 del and 165-E--A-170."; /evidence="ECO:0000269|PubMed:37020021"; MUTAGEN 139..144; /note="YDRSGR->SGG: Disrupts interaction with the EJC-RNA complex and abolishes multimerization; when associated with S-115 and 165-E--A-170."; /evidence="ECO:0000269|PubMed:37020021"; MUTAGEN 165..170; /note="QYNGVP->EYNGAA: Disrupts interaction with the EJC-RNA complex and abolishes multimerization; when associated with S-115 and 139-Y--R-144 del."; /evidence="ECO:0000269|PubMed:37020021
uniprot
proteins
post_translational_modification
PTM: Arg-204 is dimethylated, probably to asymmetric dimethylarginine. Arginine methylation reduces RNA binding. {ECO:0000269|PubMed:20129943, ECO:0000269|Ref.4}.; PTM: Citrullinated by PADI4. {ECO:0000250}.
uniprot
proteins
protein_family
ALYREF family
uniprot
proteins
pubmed
10488337
uniprot
proteins
pubmed
11118221
uniprot
proteins
pubmed
11546873
uniprot
proteins
pubmed
11675789
uniprot
proteins
pubmed
11707413
uniprot
proteins
pubmed
11979277
uniprot
proteins
pubmed
11991638
uniprot
proteins
pubmed
12176931
uniprot
proteins
pubmed
12438613
uniprot
proteins
pubmed
12944400
uniprot
proteins
pubmed
14730019
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15782174
uniprot
proteins
pubmed
15833825
uniprot
proteins
pubmed
15998806
uniprot
proteins
pubmed
16314458
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
17190602
uniprot
proteins
pubmed
17234882
uniprot
proteins
pubmed
17984224
uniprot
proteins
pubmed
18364396
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18974867
uniprot
proteins
pubmed
19165146
uniprot
proteins
pubmed
19324961
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19586903
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20129943
uniprot
proteins
pubmed
21253573
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22144908
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
22893130
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23222130
uniprot
proteins
pubmed
23826332
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25662211
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
28418038
uniprot
proteins
pubmed
30538201
uniprot
proteins
pubmed
37020021
uniprot
proteins
pubmed
9731529
uniprot
proteins
pubmed
9952027
uniprot
proteins
sequence_length
257
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10488337, ECO:0000269|PubMed:19324961, ECO:0000269|PubMed:23826332, ECO:0000269|PubMed:28418038, ECO:0000305|PubMed:18974867}. Nucleus speckle {ECO:0000269|PubMed:19324961, ECO:0000269|PubMed:23826332}. Cytoplasm {ECO:0000269|PubMed:19324961, ECO:0000269|PubMed:28418038}. Note=Colocalizes with the core EJC, 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). {ECO:0000269|PubMed:19324961, ECO:0000269|PubMed:23826332}.
uniprot
proteins