EIF4A3
entrez
9775
canonical
uniprot
P38919
canonical
ensembl
ENSG00000141543
resolver
ensembl
ENSG00000291508
resolver
ensp
ENSP00000460439
resolver
ensp
ENSP00000497641
resolver
ensp
ENSP00000497661
resolver
ensp
ENSP00000516984
resolver
ensp
ENSP00000516985
resolver
ensp
ENSP00000516986
resolver
enst
ENST00000576547
resolver
enst
ENST00000647795
resolver
enst
ENST00000649764
resolver
enst
ENST00000707787
resolver
enst
ENST00000707791
resolver
enst
ENST00000707792
resolver
genesymbol
EIF4A3
resolver
genesymbol_syn
DDX48
resolver
genesymbol_syn
KIAA0111
resolver
hgnc
HGNC:18683
resolver
uniprot
I3L3H2
resolver
uniprot
Q15033
resolver
uniprot
Q6IBQ2
resolver
uniprot
Q96A18
resolver
uniprot_entry
I3L3H2_HUMAN
resolver
uniprot_entry
IF4A3_HUMAN
resolver
uniprot_sec
Q15033
resolver
uniprot_sec
Q6IBQ2
resolver
uniprot_sec
Q96A18
resolver
activity_regulation
ACTIVITY REGULATION: The ATPase activity is increased some 4-fold in the presence of RNA. {ECO:0000269|PubMed:22961380}.
uniprot
proteins
amino_acid_sequence
MATTATMATSGSARKRLLKEEDMTKVEFETSEEVDVTPTFDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILAPTRELAVQIQKGLLALGDYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFKEQIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRILVKRDELTLEGIKQFFVAVEREEWKFDTLCDLYDTLTITQAVIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLIINYDLPNNRELYIHRIGRSGRYGRKGVAINFVKNDDIRILRDIEQYYSTQIDEMPMNVADLI
uniprot
proteins
disease_involvement
DISEASE: Richieri-Costa-Pereira syndrome (RCPS) [MIM:268305]: A syndrome characterized by a unique pattern of anomalies consisting of microstomia, micrognathia, abnormal fusion of mandible, cleft palate/Robin sequence, absence of central lower incisors, minor ears anomalies, hypoplastic first ray, abnormal tibiae, hypoplastic halluces, and clubfeet. Learning disability is also a common finding. {ECO:0000269|PubMed:24360810}. Note=The disease is caused by variants affecting the gene represented in this entry. EIF4A3 mutations resulting in Richieri-Costa-Pereira syndrome include a repeat expansion of 18 or 20 nucleotides in the 5' untranslated region. Affected individuals have 14 to 16 repeats, while healthy individuals have 3 to 12 repeats (PubMed:24360810). {ECO:0000269|PubMed:24360810}.
uniprot
proteins
ec_number
3.6.4.13
uniprot
proteins
function
FUNCTION: ATP-dependent RNA helicase (PubMed:16170325). Involved in pre-mRNA splicing as component of the spliceosome (PubMed:11991638, PubMed:22961380, PubMed:28076346, PubMed:28502770, PubMed:29301961). Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs (PubMed:16170325, PubMed:16209946, PubMed:16314458, PubMed:16923391, PubMed:16931718, PubMed:19033377, PubMed:20479275). 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). Its RNA-dependent ATPase and RNA-helicase activities are induced by CASC3, but abolished in presence of the MAGOH-RBM8A heterodimer, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The inhibition of ATPase activity by the MAGOH-RBM8A heterodimer increases the RNA-binding affinity of the EJC. Involved in translational enhancement of spliced mRNAs after formation of the 80S ribosome complex. Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions. Shows higher affinity for single-stranded RNA in an ATP-bound core EJC complex than after the ATP is hydrolyzed. 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 (PubMed:22203037). Involved in craniofacial development (PubMed:24360810). {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:15034551, ECO:0000269|PubMed:16170325, ECO:0000269|PubMed:16209946, ECO:0000269|PubMed:16314458, ECO:0000269|PubMed:16923391, ECO:0000269|PubMed:16931718, ECO:0000269|PubMed:17375189, ECO:0000269|PubMed:19033377, ECO:0000269|PubMed:19409878, ECO:0000269|PubMed:20479275, ECO:0000269|PubMed:22203037, ECO:0000269|PubMed:22961380, ECO:0000269|PubMed:24360810, ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961}.
uniprot
proteins
mass_dalton
46871
uniprot
proteins
mutagenesis
MUTAGEN 88; /note="K->A: ATPase activity is not increased by the presence of CASC3. Does not prevent EJC formation. Prevents the EJC disassembly."; /evidence="ECO:0000269|PubMed:16170325"; MUTAGEN 99; /note="C->Q: No effect on interaction with CWC22."; /evidence="ECO:0000269|PubMed:24218557"; MUTAGEN 270; /note="D->K: Loss of CWC22-binding and loss of incorporation into EJCs; when associated with K-273."; /evidence="ECO:0000269|PubMed:22959432"; MUTAGEN 273; /note="D->K: Loss of CWC22-binding and loss of incorporation into EJCs; when associated with K-270."; /evidence="ECO:0000269|PubMed:22959432"; MUTAGEN 276..277; /note="TI->GD: Loss of CWC22-binding and loss of incorporation into EJCs."; /evidence="ECO:0000269|PubMed:22959432"; MUTAGEN 300..301; /note="AN->RD: Decreased interaction with CWC22."; /evidence="ECO:0000269|PubMed:24218557"; MUTAGEN 301..303; /note="NFT->LAG: Loss of CWC22-binding and loss of incorporation into EJCs."; /evidence="ECO:0000269|PubMed:22959432"; MUTAGEN 334; /note="T->V: Reduced incorporation into EJCs."; /evidence="ECO:0000269|PubMed:23236153"; MUTAGEN 401; /note="D->K: Loss of incorporation into EJCs; when associated with R-402."; /evidence="ECO:0000269|PubMed:22961380"; MUTAGEN 402; /note="E->R: Loss of incorporation into EJCs; when associated with K-401."; /evidence="ECO:0000269|PubMed:22961380
uniprot
proteins
protein_family
DEAD box helicase family
uniprot
proteins
protein_family
eIF4A subfamily
uniprot
proteins
pubmed
10623621
uniprot
proteins
pubmed
11991638
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14730019
uniprot
proteins
pubmed
15034551
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15715967
uniprot
proteins
pubmed
16170325
uniprot
proteins
pubmed
16209946
uniprot
proteins
pubmed
16314458
uniprot
proteins
pubmed
16495234
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
16923391
uniprot
proteins
pubmed
16931718
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17375189
uniprot
proteins
pubmed
18423201
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19033377
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19409878
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20479275
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22203037
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
22959432
uniprot
proteins
pubmed
22961380
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23236153
uniprot
proteins
pubmed
23917022
uniprot
proteins
pubmed
24218557
uniprot
proteins
pubmed
24360810
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25220460
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
25772364
uniprot
proteins
pubmed
26382858
uniprot
proteins
pubmed
28076346
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28502770
uniprot
proteins
pubmed
29301961
uniprot
proteins
pubmed
30538148
uniprot
proteins
pubmed
37020021
uniprot
proteins
pubmed
7788527
uniprot
proteins
sequence_length
411
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10623621, ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:22961380, ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961}. Nucleus speckle {ECO:0000269|PubMed:10623621}. Cytoplasm {ECO:0000250|UniProtKB:Q3B8Q2}. Note=Nucleocytoplasmic shuttling protein. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Detected in dendritic layer as well as the nuclear and cytoplasmic (somatic) compartments of neurons. Colocalizes with STAU1 and FMR1 in dendrites (By similarity). {ECO:0000250|UniProtKB:Q3B8Q2}.
uniprot
proteins