4EBP1_BOVIN
ID 4EBP1_BOVIN Reviewed; 118 AA.
AC Q0P5A7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Eukaryotic translation initiation factor 4E-binding protein 1;
DE Short=4E-BP1;
DE Short=eIF4E-binding protein 1;
GN Name=EIF4EBP1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal spinal cord;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Repressor of translation initiation that regulates EIF4E
CC activity by preventing its assembly into the eIF4F complex:
CC hypophosphorylated form competes with EIF4G1/EIF4G3 and strongly binds
CC to EIF4E, leading to repress translation. In contrast,
CC hyperphosphorylated form dissociates from EIF4E, allowing interaction
CC between EIF4G1/EIF4G3 and EIF4E, leading to initiation of translation.
CC Mediates the regulation of protein translation by hormones, growth
CC factors and other stimuli that signal through the MAP kinase and mTORC1
CC pathways. {ECO:0000250|UniProtKB:Q13541}.
CC -!- SUBUNIT: Hypophosphorylated EIF4EBP1 competes with EIF4G1/EIF4G3 to
CC interact with EIF4E; insulin stimulated MAP-kinase (MAPK1 and MAPK3) or
CC mTORC1 phosphorylation of EIF4EBP1 causes dissociation of the complex
CC allowing EIF4G1/EIF4G3 to bind and consequent initiation of
CC translation. Interacts (via TOS motif) with RPTOR; promoting
CC phosphorylation by mTORC1. {ECO:0000250|UniProtKB:Q13541}.
CC -!- DOMAIN: The TOS motif mediates interaction with RPTOR, leading to
CC promote phosphorylation by mTORC1 complex.
CC {ECO:0000250|UniProtKB:Q13541}.
CC -!- PTM: Phosphorylated on serine and threonine residues in response to
CC insulin, EGF and PDGF. Phosphorylation at Thr-37, Thr-46, Ser-65 and
CC Thr-70, corresponding to the hyperphosphorylated form, is regulated by
CC mTORC1 and abolishes binding to EIF4E. {ECO:0000250|UniProtKB:Q13541}.
CC -!- PTM: Ubiquitinated: when eIF4E levels are low, hypophosphorylated form
CC is ubiquitinated by the BCR(KLHL25) complex, leading to its degradation
CC and serving as a homeostatic mechanism to maintain translation and
CC prevent eIF4E inhibition when eIF4E levels are low. Not ubiquitinated
CC when hyperphosphorylated (at Thr-37, Thr-46, Ser-65 and Thr-70) or
CC associated with eIF4E. {ECO:0000250|UniProtKB:Q13541}.
CC -!- SIMILARITY: Belongs to the eIF4E-binding protein family. {ECO:0000305}.
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DR EMBL; BC120290; AAI20291.1; -; mRNA.
DR RefSeq; NP_001071361.1; NM_001077893.2.
DR AlphaFoldDB; Q0P5A7; -.
DR SMR; Q0P5A7; -.
DR STRING; 9913.ENSBTAP00000039615; -.
DR PaxDb; Q0P5A7; -.
DR PeptideAtlas; Q0P5A7; -.
DR PRIDE; Q0P5A7; -.
DR Ensembl; ENSBTAT00000039828; ENSBTAP00000039615; ENSBTAG00000027654.
DR GeneID; 509613; -.
DR KEGG; bta:509613; -.
DR CTD; 1978; -.
DR VEuPathDB; HostDB:ENSBTAG00000027654; -.
DR VGNC; VGNC:28412; EIF4EBP1.
DR eggNOG; ENOG502S4SY; Eukaryota.
DR GeneTree; ENSGT00940000159932; -.
DR HOGENOM; CLU_111706_0_0_1; -.
DR InParanoid; Q0P5A7; -.
DR OMA; HSVHAES; -.
DR OrthoDB; 1597535at2759; -.
DR TreeFam; TF101530; -.
DR Reactome; R-BTA-166208; mTORC1-mediated signalling.
DR Reactome; R-BTA-72662; Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
DR Proteomes; UP000009136; Chromosome 27.
DR Bgee; ENSBTAG00000027654; Expressed in granulosa cell and 106 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:AgBase.
DR GO; GO:0008190; F:eukaryotic initiation factor 4E binding; ISS:AgBase.
DR GO; GO:0030371; F:translation repressor activity; ISS:UniProtKB.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0045947; P:negative regulation of translational initiation; ISS:UniProtKB.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0031929; P:TOR signaling; ISS:UniProtKB.
DR InterPro; IPR008606; EIF4EBP.
DR InterPro; IPR037582; EIF4EBP1.
DR PANTHER; PTHR12669:SF14; PTHR12669:SF14; 1.
DR Pfam; PF05456; eIF_4EBP; 1.
PE 3: Inferred from homology;
KW Acetylation; Isopeptide bond; Phosphoprotein; Protein synthesis inhibitor;
KW Reference proteome; Translation regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q13541"
FT CHAIN 2..118
FT /note="Eukaryotic translation initiation factor 4E-binding
FT protein 1"
FT /id="PRO_0000315284"
FT REGION 27..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 54..60
FT /note="YXXXXLphi motif"
FT /evidence="ECO:0000250|UniProtKB:P70445"
FT MOTIF 114..118
FT /note="TOS motif"
FT /evidence="ECO:0000250|UniProtKB:Q13541"
FT COMPBIAS 34..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q13541"
FT MOD_RES 37
FT /note="Phosphothreonine; by MTOR"
FT /evidence="ECO:0000250|UniProtKB:Q13541"
FT MOD_RES 41
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13541"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60876"
FT MOD_RES 46
FT /note="Phosphothreonine; by MTOR"
FT /evidence="ECO:0000250|UniProtKB:Q13541"
FT MOD_RES 50
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13541"
FT MOD_RES 54
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q13541"
FT MOD_RES 65
FT /note="Phosphoserine; by DYRK2, MAPK1, MAPK3 and MTOR"
FT /evidence="ECO:0000250|UniProtKB:Q13541"
FT MOD_RES 70
FT /note="Phosphothreonine; by MTOR"
FT /evidence="ECO:0000250|UniProtKB:Q13541"
FT MOD_RES 77
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13541"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13541"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60876"
FT MOD_RES 101
FT /note="Phosphoserine; by DYRK2"
FT /evidence="ECO:0000250|UniProtKB:Q13541"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13541"
FT CROSSLNK 57
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q13541"
SQ SEQUENCE 118 AA; 12588 MW; D3716D4929AD91B7 CRC64;
MSGGSSCSQT PSRAIPTTRR VVLADGVQLP PGDYSTTPGG TLFSTTPGGT RIIYDRKFLM
ECRNSPVTKT PPRDLPTIPG VTSPTGDEPP TEARQNHLRS SPEDKPAGGE ESQFEMDI
