I4E1B_HUMAN
ID I4E1B_HUMAN Reviewed; 242 AA.
AC A6NMX2;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 3.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Eukaryotic translation initiation factor 4E type 1B;
GN Name=EIF4E1B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [2]
RP GENE FAMILY.
RX PubMed=16191198; DOI=10.1186/1471-2148-5-48;
RA Joshi B., Lee K., Maeder D.L., Jagus R.;
RT "Phylogenetic analysis of eIF4E-family members.";
RL BMC Evol. Biol. 5:48-48(2005).
CC -!- FUNCTION: Recognizes and binds the 7-methylguanosine-containing mRNA
CC cap during an early step in the initiation of protein synthesis and
CC facilitates ribosome binding by inducing the unwinding of the mRNAs
CC secondary structure. {ECO:0000250}.
CC -!- SUBUNIT: eIF4F is a multi-subunit complex, the composition of which
CC varies with external and internal environmental conditions. It is
CC composed of at least EIF4A, EIF4E AND EIF4G (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC A6NMX2; Q13541: EIF4EBP1; NbExp=3; IntAct=EBI-18394358, EBI-74090;
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC091934; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS47345.1; -.
DR RefSeq; NP_001092878.1; NM_001099408.1.
DR RefSeq; XP_011532801.1; XM_011534499.2.
DR AlphaFoldDB; A6NMX2; -.
DR SMR; A6NMX2; -.
DR BioGRID; 128966; 3.
DR IntAct; A6NMX2; 1.
DR STRING; 9606.ENSP00000323714; -.
DR GlyGen; A6NMX2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; A6NMX2; -.
DR PhosphoSitePlus; A6NMX2; -.
DR BioMuta; EIF4E1B; -.
DR MassIVE; A6NMX2; -.
DR MaxQB; A6NMX2; -.
DR PaxDb; A6NMX2; -.
DR PeptideAtlas; A6NMX2; -.
DR PRIDE; A6NMX2; -.
DR ProteomicsDB; 1567; -.
DR Antibodypedia; 63751; 30 antibodies from 10 providers.
DR DNASU; 253314; -.
DR Ensembl; ENST00000318682.11; ENSP00000323714.6; ENSG00000175766.13.
DR Ensembl; ENST00000504597.5; ENSP00000427633.1; ENSG00000175766.13.
DR Ensembl; ENST00000647833.1; ENSP00000497422.1; ENSG00000175766.13.
DR GeneID; 253314; -.
DR KEGG; hsa:253314; -.
DR MANE-Select; ENST00000318682.11; ENSP00000323714.6; NM_001099408.2; NP_001092878.1.
DR UCSC; uc010jkf.1; human.
DR CTD; 253314; -.
DR DisGeNET; 253314; -.
DR GeneCards; EIF4E1B; -.
DR HGNC; HGNC:33179; EIF4E1B.
DR HPA; ENSG00000175766; Group enriched (brain, epididymis, retina).
DR neXtProt; NX_A6NMX2; -.
DR OpenTargets; ENSG00000175766; -.
DR PharmGKB; PA162384974; -.
DR VEuPathDB; HostDB:ENSG00000175766; -.
DR eggNOG; KOG1670; Eukaryota.
DR GeneTree; ENSGT00940000160838; -.
DR HOGENOM; CLU_043552_1_1_1; -.
DR InParanoid; A6NMX2; -.
DR OMA; NKFGGRW; -.
DR OrthoDB; 1394271at2759; -.
DR PhylomeDB; A6NMX2; -.
DR TreeFam; TF101526; -.
DR PathwayCommons; A6NMX2; -.
DR SignaLink; A6NMX2; -.
DR BioGRID-ORCS; 253314; 15 hits in 1069 CRISPR screens.
DR GenomeRNAi; 253314; -.
DR Pharos; A6NMX2; Tdark.
DR PRO; PR:A6NMX2; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; A6NMX2; protein.
DR Bgee; ENSG00000175766; Expressed in primary visual cortex and 48 other tissues.
DR ExpressionAtlas; A6NMX2; baseline and differential.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IBA:GO_Central.
DR GO; GO:0005845; C:mRNA cap binding complex; ISS:UniProtKB.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR Gene3D; 3.30.760.10; -; 1.
DR InterPro; IPR023398; TIF_eIF4e-like.
DR InterPro; IPR001040; TIF_eIF_4E.
DR InterPro; IPR019770; TIF_eIF_4E_CS.
DR PANTHER; PTHR11960; PTHR11960; 1.
DR Pfam; PF01652; IF4E; 1.
DR SUPFAM; SSF55418; SSF55418; 1.
DR PROSITE; PS00813; IF4E; 1.
PE 1: Evidence at protein level;
KW Initiation factor; Protein biosynthesis; Reference proteome; RNA-binding;
KW Translation regulation.
FT CHAIN 1..242
FT /note="Eukaryotic translation initiation factor 4E type 1B"
FT /id="PRO_0000342513"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..65
FT /note="EIF4EBP1/2/3 binding"
FT /evidence="ECO:0000250"
FT REGION 98..102
FT /note="EIF4EBP1/2/3 binding"
FT /evidence="ECO:0000250"
FT REGION 157..164
FT /note="EIF4EBP1/2/3 binding"
FT /evidence="ECO:0000250"
FT BINDING 81..82
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT /ligand_part_id="ChEBI:CHEBI:74429"
FT /ligand_part_note="m7GTP residue in mRNA cap"
FT /evidence="ECO:0000250"
FT BINDING 127..128
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT /ligand_part_id="ChEBI:CHEBI:74429"
FT /ligand_part_note="m7GTP residue in mRNA cap"
FT /evidence="ECO:0000250"
FT BINDING 182..187
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT /ligand_part_id="ChEBI:CHEBI:74429"
FT /ligand_part_note="m7GTP residue in mRNA cap"
FT /evidence="ECO:0000250"
FT BINDING 230..232
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT /ligand_part_id="ChEBI:CHEBI:74429"
FT /ligand_part_note="m7GTP residue in mRNA cap"
FT /evidence="ECO:0000250"
FT VARIANT 227
FT /note="D -> Y (in dbSNP:rs13163938)"
FT /id="VAR_044209"
SQ SEQUENCE 242 AA; 27596 MW; C441D5F0A082339D CRC64;
MLAVEVSEAE GGIREWEEEE KEEEAAERTP TGEKSPNSPR TLLSLRGKAR TGGPMEVKLE
LHPLQNRWAL WFFKNDRSRA WQDNLHLVTK VDTVEDFWAL YSHIQLASKL SSGCDYALFK
DGIQPMWEDS RNKRGGRWLV SLAKQQRHIE LDRLWLETLL CLIGESFEEH SREVCGAVVN
IRTKGDKIAV WTREAENQAG VLHVGRVYKE RLGLSPKTII GYQAHADTAT KSNSLAKNKF
VV
