EIF4G1
entrez
1981
canonical
uniprot
Q04637
canonical
ensembl
ENSG00000114867
resolver
ensp
ENSP00000316879
resolver
ensp
ENSP00000317600
resolver
ensp
ENSP00000338020
resolver
ensp
ENSP00000343450
resolver
ensp
ENSP00000371767
resolver
ensp
ENSP00000376320
resolver
ensp
ENSP00000391935
resolver
ensp
ENSP00000411826
resolver
genesymbol
EIF4G1
resolver
genesymbol_syn
EIF4F
resolver
genesymbol_syn
EIF4G
resolver
genesymbol_syn
EIF4GI
resolver
hgnc
HGNC:3296
resolver
uniprot
B2RU06
resolver
uniprot
B2RU10
resolver
uniprot
B4DSI9
resolver
uniprot
D3DNT2
resolver
uniprot
D3DNT4
resolver
uniprot
D3DNT5
resolver
uniprot
E9PFM1
resolver
uniprot
G5E9S1
resolver
uniprot
O43177
resolver
uniprot
O95065
resolver
uniprot
O95066
resolver
uniprot
Q5HYG0
resolver
uniprot
Q6ZN21
resolver
uniprot
Q8N102
resolver
uniprot
Q96I65
resolver
uniprot_entry
B2RU06_HUMAN
resolver
uniprot_entry
B2RU10_HUMAN
resolver
uniprot_entry
B4DSI9_HUMAN
resolver
uniprot_entry
IF4G1_HUMAN
resolver
uniprot_entry
O95065_HUMAN
resolver
uniprot_entry
Q96I65_HUMAN
resolver
uniprot_sec
D3DNT2
resolver
uniprot_sec
D3DNT4
resolver
uniprot_sec
D3DNT5
resolver
uniprot_sec
E9PFM1
resolver
uniprot_sec
G5E9S1
resolver
uniprot_sec
O43177
resolver
uniprot_sec
O95066
resolver
uniprot_sec
Q5HYG0
resolver
uniprot_sec
Q6ZN21
resolver
uniprot_sec
Q8N102
resolver
amino_acid_sequence
MNKAPQSTGPPPAPSPGLPQPAFPPGQTAPVVFSTPQATQMNTPSQPRQHFYPSRAQPPSSAASRVQSAAPARPGPAAHVYPAGSQVMMIPSQISYPASQGAYYIPGQGRSTYVVPTQQYPVQPGAPGFYPGASPTEFGTYAGAYYPAQGVQQFPTGVAPTPVLMNQPPQIAPKRERKTIRIRDPNQGGKDITEEIMSGARTASTPTPPQTGGGLEPQANGETPQVAVIVRPDDRSQGAIIADRPGLPGPEHSPSESQPSSPSPTPSPSPVLEPGSEPNLAVLSIPGDTMTTIQMSVEESTPISRETGEPYRLSPEPTPLAEPILEVEVTLSKPVPESEFSSSPLQAPTPLASHTVEIHEPNGMVPSEDLEPEVESSPELAPPPACPSESPVPIAPTAQPEELLNGAPSPPAVDLSPVSEPEEQAKEVTASMAPPTIPSATPATAPSATSPAQEEEMEEEEEEEEGEAGEAGEAESEKGGEELLPPESTPIPANLSQNLEAAAATQVAVSVPKRRRKIKELNKKEAVGDLLDAFKEANPAVPEVENQPPAGSNPGPESEGSGVPPRPEEADETWDSKEDKIHNAENIQPGEQKYEYKSDQWKPLNLEEKKRYDREFLLGFQFIFASMQKPEGLPHISDVVLDKANKTPLRPLDPTRLQGINCGPDFTPSFANLGRTTLSTRGPPRGGPGGELPRGPAGLGPRRSQQGPRKEPRKIIATVLMTEDIKLNKAEKAWKPSSKRTAADKDRGEEDADGSKTQDLFRRVRSILNKLTPQMFQQLMKQVTQLAIDTEERLKGVIDLIFEKAISEPNFSVAYANMCRCLMALKVPTTEKPTVTVNFRKLLLNRCQKEFEKDKDDDEVFEKKQKEMDEAATAEERGRLKEELEEARDIARRRSLGNIKFIGELFKLKMLTEAIMHDCVVKLLKNHDEESLECLCRLLTTIGKDLDFEKAKPRMDQYFNQMEKIIKEKKTSSRIRFMLQDVLDLRGSNWVPRRGDQGPKTIDQIHKEAEMEEHREHIKVQQLMAKGSDKRRGGPPGPPISRGLPLVDDGGWNTVPISKGSRPIDTSRLTKITKPGSIDSNNQLFAPGGRLSWGKGSSGGSGAKPSDAASEAARPATSTLNRFSALQQAVPTESTDNRRVVQRSSLSRERGEKAGDRGDRLERSERGGDRGDRLDRARTPATKRSFSKEVEERSRERPSQPEGLRKAASLTEDRDRGRDAVKREAALPPVSPLKAALSEEELEKKSKAIIEEYLHLNDMKEAVQCVQELASPSLLFIFVRHGVESTLERSAIAREHMGQLLHQLLCAGHLSTAQYYQGLYEILELAEDMEIDIPHVWLYLAELVTPILQEGGVPMGELFREITKPLRPLGKAASLLLEILGLLCKSMGPKKVGTLWREAGLSWKEFLPEGQDIGAFVAEQKVEYTLGEESEAPGQRALPSEELNRQLEKLLKEGSSNQRVFDWIEANLSEQQIVSNTLVRALMTAVCYSAIIFETPLRVDVAVLKARAKLLQKYLCDEQKELQALYALQALVVTLEQPPNLLRMFFDALYDEDVVKEDAFYSWESSKDPAEQQGKGVALKSVTAFFKWLREAEEESDHN
uniprot
proteins
disease_involvement
DISEASE: Parkinson disease 18 (PARK18) [MIM:614251]: An autosomal dominant, late-onset form of Parkinson disease. Parkinson disease is a complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability, as well as by a clinically significant response to treatment with levodopa. The pathology involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. {ECO:0000269|PubMed:21907011}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (PubMed:29987188). Exists in two complexes, either with EIF1 or with EIF4E (mutually exclusive) (PubMed:29987188). Together with EIF1, is required for leaky scanning, in particular for avoiding cap-proximal start codon (PubMed:29987188). Together with EIF4E, antagonizes the scanning promoted by EIF1-EIF4G1 and locates the start codon (through a TISU element) without scanning (PubMed:29987188). As a member of the eIF4F complex, required for endoplasmic reticulum stress-induced ATF4 mRNA translation (PubMed:29062139). {ECO:0000269|PubMed:29062139, ECO:0000269|PubMed:29987188}.
uniprot
proteins
mass_dalton
175491
uniprot
proteins
mutagenesis
MUTAGEN 174..178; /note="KRERK->AAAAA: Loss of PABPC1 binding; when associated with 184-AAAA-187."; /evidence="ECO:0000269|PubMed:10996799"; MUTAGEN 180; /note="I->A: Loss of PABPC1 binding."; /evidence="ECO:0000269|PubMed:12086624"; MUTAGEN 182; /note="I->A: Loss of PABPC1 binding."; /evidence="ECO:0000269|PubMed:12086624"; MUTAGEN 184..187; /note="DPNQ->AAAA: Loss of PABPC1 binding; when associated with 174-AAAAA-178."; MUTAGEN 192; /note="I->A: Loss of PABPC1 binding."; /evidence="ECO:0000269|PubMed:12086624"; MUTAGEN 196; /note="I->A: Loss of PABPC1 binding."; /evidence="ECO:0000269|PubMed:12086624"; MUTAGEN 612; /note="Y->A,F: Abolishes binding to EIF4E."; /evidence="ECO:0000269|PubMed:7651417"; MUTAGEN 617..618; /note="LL->AA: Abolishes binding to EIF4E."; /evidence="ECO:0000269|PubMed:7651417"; MUTAGEN 682; /note="G->A,V,W,R,E: Reduced cleavage by protease 2A from human rhinovirus 2."; /evidence="ECO:0000269|PubMed:8961935"; MUTAGEN 768; /note="L->A: Abolishes binding to EIF4A; when associated with A-770 and A-775."; /evidence="ECO:0000269|PubMed:9372926"; MUTAGEN 771; /note="L->A: Abolishes binding to EIF4A; when associated with A-767 and A-775."; /evidence="ECO:0000269|PubMed:9372926"; MUTAGEN 776; /note="F->A: Abolishes binding to EIF4A; when associated with A-767 and A-770."; /evidence="ECO:0000269|PubMed:9372926"; MUTAGEN 842..843; /note="LL->AA: Abolishes binding to EIF4A; when associated with A-850 and K-851."; /evidence="ECO:0000269|PubMed:9372926"; MUTAGEN 851..852; /note="FE->AK: Abolishes binding to EIF4A; when associated with A-841 and A-842."; /evidence="ECO:0000269|PubMed:9372926"; MUTAGEN 896; /note="L->A: Abolishes binding to EIF4A; when associated with A-92 and A-95."; /evidence="ECO:0000269|PubMed:9372926"; MUTAGEN 902; /note="I->A: Abolishes binding to EIF4A; when associated with A-895 and A-95."; /evidence="ECO:0000269|PubMed:9372926"; MUTAGEN 905; /note="L->A: Abolishes binding to EIF4A; when associated with A-895 and A-92."; /evidence="ECO:0000269|PubMed:9372926"; MUTAGEN 974; /note="R->A: Abolishes binding to EIF4A; when associated with A-976."; /evidence="ECO:0000269|PubMed:9372926"; MUTAGEN 977; /note="F->A: Abolishes binding to EIF4A; when associated with A-973."; /evidence="ECO:0000269|PubMed:9372926"; MUTAGEN 985; /note="L->A: Slightly reduced binding to EIF4A; when associated with A-989."; /evidence="ECO:0000269|PubMed:9372926"; MUTAGEN 990; /note="W->A: Slightly reduced binding to EIF4A; when associated with A-984."; /evidence="ECO:0000269|PubMed:9372926
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at multiple sites in vivo. Phosphorylation at Ser-1185 by PRKCA induces binding to MKNK1. {ECO:0000269|PubMed:21576361}.; PTM: Following infection by certain enteroviruses, rhinoviruses and aphthoviruses, EIF4G1 is cleaved by the viral protease 2A, or the leader protease in the case of aphthoviruses. This shuts down the capped cellular mRNA transcription. {ECO:0000269|PubMed:11034318, ECO:0000269|PubMed:8396129, ECO:0000269|PubMed:9755863}.
uniprot
proteins
protein_family
Eukaryotic initiation factor 4G family
uniprot
proteins
pubmed
10872469
uniprot
proteins
pubmed
10970864
uniprot
proteins
pubmed
10996799
uniprot
proteins
pubmed
11034318
uniprot
proteins
pubmed
11154262
uniprot
proteins
pubmed
12052860
uniprot
proteins
pubmed
12086624
uniprot
proteins
pubmed
1429670
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15314025
uniprot
proteins
pubmed
16513844
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
16698552
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17284590
uniprot
proteins
pubmed
17924679
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
17984221
uniprot
proteins
pubmed
18025107
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18799579
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21576361
uniprot
proteins
pubmed
21907011
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
22872150
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24423872
uniprot
proteins
pubmed
26740508
uniprot
proteins
pubmed
29062139
uniprot
proteins
pubmed
29987188
uniprot
proteins
pubmed
31403400
uniprot
proteins
pubmed
7651417
uniprot
proteins
pubmed
7935836
uniprot
proteins
pubmed
8396129
uniprot
proteins
pubmed
8521827
uniprot
proteins
pubmed
8961935
uniprot
proteins
pubmed
9372926
uniprot
proteins
pubmed
9418880
uniprot
proteins
pubmed
9755181
uniprot
proteins
pubmed
9755863
uniprot
proteins
pubmed
9857202
uniprot
proteins
pubmed
9878069
uniprot
proteins
sequence_length
1599
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17984221}. Nucleus {ECO:0000269|PubMed:17984221}. Cytoplasm, Stress granule {ECO:0000269|PubMed:22872150}.
uniprot
proteins