MAGOH
entrez
4116
canonical
uniprot
P61326
canonical
ensembl
ENSG00000162385
resolver
ensp
ENSP00000360525
resolver
genesymbol
MAGOH
resolver
genesymbol_syn
MAGOHA
resolver
hgnc
HGNC:6815
resolver
uniprot
B1ARP8
resolver
uniprot
B2R5A2
resolver
uniprot
O35169
resolver
uniprot
P50606
resolver
uniprot
Q5SW69
resolver
uniprot_entry
MGN_HUMAN
resolver
uniprot_sec
B1ARP8
resolver
uniprot_sec
B2R5A2
resolver
uniprot_sec
O35169
resolver
uniprot_sec
P50606
resolver
uniprot_sec
Q5SW69
resolver
amino_acid_sequence
MESDFYLRYYVGHKGKFGHEFLEFEFRPDGKLRYANNSNYKNDVMIRKEAYVHKSVMEELKRIIDDSEITKEDDALWPPPDRVGRQELEIVIGDEHISFTTSKIGSLIDVNQSKDPEGLRVFYYLVQDLKCLVFSLIGLHFKIKPI
uniprot
proteins
function
FUNCTION: Required for pre-mRNA splicing as component of the spliceosome (PubMed:11991638). Plays a redundant role with MAGOHB as core component of the exon junction complex (EJC) and in the nonsense-mediated decay (NMD) pathway (PubMed:23917022). The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). The MAGOH-RBM8A heterodimer inhibits the ATPase activity of EIF4A3, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The MAGOH-RBM8A heterodimer interacts with the EJC key regulator PYM1 leading to EJC disassembly in the cytoplasm and translation enhancement of EJC-bearing spliced mRNAs by recruiting them to the ribosomal 48S pre-initiation complex. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the function is different from the established EJC assembly. {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:12730685, ECO:0000269|PubMed:16209946, ECO:0000269|PubMed:22203037, ECO:0000269|PubMed:23917022}.
uniprot
proteins
mass_dalton
17164
uniprot
proteins
mutagenesis
MUTAGEN 16..17; /note="KF->EA: Impaired nonsense-mediated decay activity."; /evidence="ECO:0000269|PubMed:16209946"; MUTAGEN 41..42; /note="KN->DA: Complete loss of nonsense-mediated decay activity."; /evidence="ECO:0000269|PubMed:16209946"; MUTAGEN 66..68; /note="DSE->RSR: Slightly reduced nonsense-mediated decay activity."; /evidence="ECO:0000269|PubMed:16209946"; MUTAGEN 68; /note="E->R: Abolishes interaction with PYM1 leading to increase EJC association with spliced mRNAs; when associated with R-72; K-73 and R-117."; /evidence="ECO:0000269|PubMed:19410547"; MUTAGEN 72..73; /note="ED->RK: Fully active."; /evidence="ECO:0000269|PubMed:16209946"; MUTAGEN 72; /note="E->R: Abolishes interaction with PYM1 leading to increase EJC association with spliced mRNAs; when associated with R-68; K-73 and R-117."; /evidence="ECO:0000269|PubMed:19410547"; MUTAGEN 73; /note="D->K: Abolishes interaction with PYM1 leading to increase EJC association with spliced mRNAs; when associated with R-68; R-72 and R-117."; /evidence="ECO:0000269|PubMed:19410547"; MUTAGEN 85..87; /note="RQE->EQR: Fully active."; /evidence="ECO:0000269|PubMed:16209946"; MUTAGEN 117; /note="E->R: Abolishes interaction with PYM1 leading to increase EJC association with spliced mRNAs; when associated with R-68; R-72 and K-73."; /evidence="ECO:0000269|PubMed:19410547"; MUTAGEN 130..134; /note="KCLVF->ECLVA: Complete loss of nonsense-mediated decay activity."; /evidence="ECO:0000269|PubMed:16209946"; MUTAGEN 136; /note="L->R: Complete loss of nonsense-mediated decay activity."; /evidence="ECO:0000269|PubMed:16209946
uniprot
proteins
protein_family
Mago nashi family
uniprot
proteins
pubmed
10662555
uniprot
proteins
pubmed
11042152
uniprot
proteins
pubmed
11991638
uniprot
proteins
pubmed
12730685
uniprot
proteins
pubmed
12781131
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14968132
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16170325
uniprot
proteins
pubmed
16209946
uniprot
proteins
pubmed
16314458
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
16923391
uniprot
proteins
pubmed
16931718
uniprot
proteins
pubmed
18026120
uniprot
proteins
pubmed
19033377
uniprot
proteins
pubmed
19324961
uniprot
proteins
pubmed
19410547
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
20479275
uniprot
proteins
pubmed
22203037
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23917022
uniprot
proteins
pubmed
37020021
uniprot
proteins
pubmed
9479507
uniprot
proteins
sequence_length
146
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19324961}. Nucleus speckle {ECO:0000269|PubMed:19324961}. Cytoplasm {ECO:0000269|PubMed:19324961}. Note=Detected in granule-like structures in the dendroplasm (By similarity). Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and UAP56 in the nucleus and nuclear speckles (PubMed:19324961). {ECO:0000250, ECO:0000250|UniProtKB:Q27W02, ECO:0000269|PubMed:19324961}.
uniprot
proteins