EIF4ENIF1
entrez
56478
canonical
uniprot
Q9NRA8
canonical
ensembl
ENSG00000184708
resolver
ensp
ENSP00000328103
resolver
ensp
ENSP00000342927
resolver
ensp
ENSP00000380659
resolver
ensp
ENSP00000562351
resolver
ensp
ENSP00000597408
resolver
genesymbol
EIF4ENIF1
resolver
hgnc
HGNC:16687
resolver
uniprot
B1AKL2
resolver
uniprot
B1AKL3
resolver
uniprot
B2RBF1
resolver
uniprot
Q8NCF2
resolver
uniprot
Q9H708
resolver
uniprot_entry
4ET_HUMAN
resolver
uniprot_sec
B1AKL2
resolver
uniprot_sec
B1AKL3
resolver
uniprot_sec
B2RBF1
resolver
uniprot_sec
Q8NCF2
resolver
uniprot_sec
Q9H708
resolver
amino_acid_sequence
MDRRSMGETESGDAFLDLKKPPASKCPHRYTKEELLDIKELPHSKQRPSCLSEKYDSDGVWDPEKWHASLYPASGRSSPVESLKKELDTDRPSLVRRIVDPRERVKEDDLDVVLSPQRRSFGGGCHVTAAVSSRRSGSPLEKDSDGLRLLGGRRIGSGRIISARTFEKDHRLSDKDLRDLRDRDRERDFKDKRFRREFGDSKRVFGERRRNDSYTEEEPEWFSAGPTSQSETIELTGFDDKILEEDHKGRKRTRRRTASVKEGIVECNGGVAEEDEVEVILAQEPAADQEVPRDAVLPEQSPGDFDFNEFFNLDKVPCLASMIEDVLGEGSVSASRFSRWFSNPSRSGSRSSSLGSTPHEELERLAGLEQAILSPGQNSGNYFAPIPLEDHAENKVDILEMLQKAKVDLKPLLSSLSANKEKLKESSHSGVVLSVEEVEAGLKGLKVDQQVKNSTPFMAEHLEETLSAVTNNRQLKKDGDMTAFNKLVSTMKASGTLPSQPKVSRNLESHLMSPAEIPGQPVPKNILQELLGQPVQRPASSNLLSGLMGSLEPTTSLLGQRAPSPPLSQVFQTRAASADYLRPRIPSPIGFTPGPQQLLGDPFQGMRKPMSPITAQMSQLELQQAALEGLALPHDLAVQAANFYQPGFGKPQVDRTRDGFRNRQQRVTKSPAPVHRGNSSSPAPAASITSMLSPSFTPTSVIRKMYESKEKSKEEPASGKAALGDSKEDTQKASEENLLSSSSVPSADRDSSPTTNSKLSALQRSSCSTPLSQANRYTKEQDYRPKATGRKTPTLASPVPTTPFLRPVHQVPLVPHVPMVRPAHQLHPGLVQRMLAQGVHPQHLPSLLQTGVLPPGMDLSHLQGISGPILGQPFYPLPAASHPLLNPRPGTPLHLAMVQQQLQRSVLHPPGSGSHAAAVSVQTTPQNVPSRSGLPHMHSQLEHRPSQRSSSPVGLAKWFGSDVLQQPLPSMPAKVISVDELEYRQ
uniprot
proteins
function
FUNCTION: EIF4E-binding protein that regulates translation and stability of mRNAs in processing bodies (P-bodies) (PubMed:16157702, PubMed:24335285, PubMed:27342281, PubMed:32354837). Plays a key role in P-bodies to coordinate the storage of translationally inactive mRNAs in the cytoplasm and prevent their degradation (PubMed:24335285, PubMed:32354837). Acts as a binding platform for multiple RNA-binding proteins: promotes deadenylation of mRNAs via its interaction with the CCR4-NOT complex, and blocks decapping via interaction with eIF4E (EIF4E and EIF4E2), thereby protecting deadenylated and repressed mRNAs from degradation (PubMed:27342281, PubMed:32354837). Component of a multiprotein complex that sequesters and represses translation of proneurogenic factors during neurogenesis (By similarity). Promotes miRNA-mediated translational repression (PubMed:24335285, PubMed:27342281, PubMed:28487484). Required for the formation of P-bodies (PubMed:16157702, PubMed:22966201, PubMed:27342281, PubMed:32354837). Involved in mRNA translational repression mediated by the miRNA effector TNRC6B by protecting TNRC6B-targeted mRNAs from decapping and subsequent decay (PubMed:32354837). Also acts as a nucleoplasmic shuttling protein, which mediates the nuclear import of EIF4E and DDX6 by a piggy-back mechanism (PubMed:10856257, PubMed:28216671). {ECO:0000250|UniProtKB:Q9EST3, ECO:0000269|PubMed:10856257, ECO:0000269|PubMed:16157702, ECO:0000269|PubMed:22966201, ECO:0000269|PubMed:24335285, ECO:0000269|PubMed:27342281, ECO:0000269|PubMed:28216671, ECO:0000269|PubMed:28487484, ECO:0000269|PubMed:32354837}.
uniprot
proteins
mass_dalton
108201
uniprot
proteins
mutagenesis
MUTAGEN 30..36; /note="YTKEELL->ATKEEAA: Abolished interaction with EIF4E2."; /evidence="ECO:0000269|PubMed:23991149, ECO:0000269|PubMed:28487484"; MUTAGEN 30; /note="Y->A: Abolishes interaction with EIF4E and EIF4E2. Impaired ability to repress mRNA translation."; /evidence="ECO:0000269|PubMed:10856257, ECO:0000269|PubMed:16157702, ECO:0000269|PubMed:24335285, ECO:0000269|PubMed:28487484"; MUTAGEN 35..36; /note="LL->AA: Abolished interaction with EIF4E2."; /evidence="ECO:0000269|PubMed:23991149"; MUTAGEN 54..61; /note="KYDSDGVW->ADSDAA: Strongly reduced interaction with EIF4E and EIF4E2."; /evidence="ECO:0000269|PubMed:23991149"; MUTAGEN 195..196; /note="RR->NS: Abolishes the nuclear localization."; /evidence="ECO:0000269|PubMed:10856257"; MUTAGEN 301; /note="S->A: In S6A mutant; abolished phosphorylation by MAPK8/JNK1; impaired P-body assembly in response to oxidative stress when associated with A-374, A-513, A-587, A-693 and A-752."; /evidence="ECO:0000269|PubMed:22966201"; MUTAGEN 374; /note="S->A: In S6A mutant; abolished phosphorylation by MAPK8/JNK1; impaired P-body assembly in response to oxidative stress when associated with A-301, A-513, A-587, A-693 and A-752."; /evidence="ECO:0000269|PubMed:22966201"; MUTAGEN 513; /note="S->A: In S6A mutant; abolished phosphorylation by MAPK8/JNK1; impaired P-body assembly in response to oxidative stress when associated with A-301, A-374, A-587, A-693 and A-752."; /evidence="ECO:0000269|PubMed:22966201"; MUTAGEN 587; /note="S->A: In S6A mutant; abolished phosphorylation by MAPK8/JNK1; impaired P-body assembly in response to oxidative stress when associated with A-301, A-374, A-513, A-693 and A-752."; /evidence="ECO:0000269|PubMed:22966201"; MUTAGEN 693; /note="S->A: In S6A mutant; abolished phosphorylation by MAPK8/JNK1; impaired P-body assembly in response to oxidative stress when associated with A-301, A-374, A-513, A-587 and A-752."; /evidence="ECO:0000269|PubMed:22966201"; MUTAGEN 752; /note="S->A: In S6A mutant; abolished phosphorylation by MAPK8/JNK1; impaired P-body assembly in response to oxidative stress when associated with A-301, A-374, A-513, A-587 and A-693."; /evidence="ECO:0000269|PubMed:22966201"; MUTAGEN 955..958; /note="LAKW->AAKA: Abolished interaction with LSM14A."; /evidence="ECO:0000269|PubMed:29510985"; MUTAGEN 958; /note="W->A: Abolished interaction with LSM14A."; /evidence="ECO:0000269|PubMed:29510985"; MUTAGEN 959; /note="F->A: Abolished interaction with LSM14A."; /evidence="ECO:0000269|PubMed:29510985"; MUTAGEN 961; /note="S->A: Does not affect interaction with LSM14A."; /evidence="ECO:0000269|PubMed:29510985"; MUTAGEN 970; /note="S->A: Does not affect interaction with LSM14A."; /evidence="ECO:0000269|PubMed:29510985"; MUTAGEN 978..981; /note="VDEL->ADEA: Abolished interaction with LSM14A."; /evidence="ECO:0000269|PubMed:29510985"; MUTAGEN 978; /note="V->A: Abolished interaction with LSM14A."; /evidence="ECO:0000269|PubMed:29510985"; MUTAGEN 982; /note="E->K: Abolished interaction with LSM14A."; /evidence="ECO:0000269|PubMed:29510985
uniprot
proteins
post_translational_modification
PTM: Phosphorylation by MAPK8/JNK1 and or MAPK9/JNK2 in response to oxidative stress promotes P-body assembly (PubMed:22966201). Phosphorylated during meiotic maturation (By similarity). {ECO:0000250|UniProtKB:Q9EST3, ECO:0000269|PubMed:22966201}.
uniprot
proteins
protein_family
4E-T/EIF4E-T family
uniprot
proteins
pubmed
10591208
uniprot
proteins
pubmed
10856257
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15461802
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16157702
uniprot
proteins
pubmed
16699599
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18669648
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
22090346
uniprot
proteins
pubmed
22966201
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23991149
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24335285
uniprot
proteins
pubmed
25923732
uniprot
proteins
pubmed
26027925
uniprot
proteins
pubmed
26489469
uniprot
proteins
pubmed
27342281
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28216671
uniprot
proteins
pubmed
28487484
uniprot
proteins
pubmed
29510985
uniprot
proteins
pubmed
31422817
uniprot
proteins
pubmed
31439631
uniprot
proteins
pubmed
32354837
uniprot
proteins
sequence_length
985
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:16157702, ECO:0000269|PubMed:22966201, ECO:0000269|PubMed:23991149, ECO:0000269|PubMed:24335285, ECO:0000269|PubMed:32354837}. Cytoplasm {ECO:0000269|PubMed:10856257, ECO:0000269|PubMed:22090346, ECO:0000269|PubMed:28216671}. Nucleus {ECO:0000269|PubMed:10856257, ECO:0000269|PubMed:22090346, ECO:0000269|PubMed:28216671}. Nucleus, PML body {ECO:0000269|PubMed:22090346}. Nucleus speckle {ECO:0000269|PubMed:22090346}. Note=Predominantly cytoplasmic (PubMed:10856257). Mainly localizes to processing bodies (P-bodies) (PubMed:16157702). Shuttles between the nucleus and the cytoplasm in a CRM1-dependent manner (PubMed:10856257). Localization to nuclear foci and speckles requires active transcription (PubMed:22090346). {ECO:0000269|PubMed:10856257, ECO:0000269|PubMed:16157702, ECO:0000269|PubMed:22090346}.
uniprot
proteins