AC MF_03001; DC Protein; auto TR HAMAP; MF_03001; -; 1; level=0 XX Names: eIF3b XX ID EIF3B case DE RecName: Full=Eukaryotic translation initiation factor 3 subunit B; DE Short=eIF3b; DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 9; DE AltName: Full=eIF-3-eta; else case DE RecName: Full=Eukaryotic translation initiation factor 3 subunit B; DE Short=eIF3b; DE AltName: Full=Eukaryotic translation initiation factor 3 90 kDa subunit homolog; DE Short=eIF3 p90; DE AltName: Full=Translation initiation factor eIF3, p90 subunit homolog; else case DE RecName: Full=Eukaryotic translation initiation factor 3 subunit B; DE Short=eIF3b; DE AltName: Full=eIF-3-eta; DE AltName: Full=eIF3 p110; else DE RecName: Full=Eukaryotic translation initiation factor 3 subunit B; DE Short=eIF3b; DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 9; end case case GN Name=EIF3B; Synonyms=EIF3S9; else case GN Name=eif-3.B; else case GN Name=eIF3b; Synonyms=eIF3-S9; else case GN Name=PRT1; end case XX case CC -!- FUNCTION: RNA-binding component of the eukaryotic translation CC initiation factor 3 (eIF-3) complex, which is required for several CC steps in the initiation of protein synthesis. The eIF-3 complex CC associates with the 40S ribosome and facilitates the recruitment of CC eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre- CC initiation complex (43S PIC). The eIF-3 complex stimulates mRNA CC recruitment to the 43S PIC and scanning of the mRNA for AUG CC recognition. The eIF-3 complex is also required for disassembly and CC recycling of post-termination ribosomal complexes and subsequently CC prevents premature joining of the 40S and 60S ribosomal subunits prior CC to initiation. The eIF-3 complex specifically targets and initiates CC translation of a subset of mRNAs involved in cell proliferation, CC including cell cycling, differentiation and apoptosis, and uses CC different modes of RNA stem-loop binding to exert either translational CC activation or repression. else CC -!- FUNCTION: RNA-binding component of the eukaryotic translation CC initiation factor 3 (eIF-3) complex, which is involved in protein CC synthesis of a specialized repertoire of mRNAs and, together with other CC initiation factors, stimulates binding of mRNA and methionyl-tRNAi to CC the 40S ribosome. The eIF-3 complex specifically targets and initiates CC translation of a subset of mRNAs involved in cell proliferation. end case case CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3 CC (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C, CC EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and CC EIF3M. The eIF-3 complex appears to include 3 stable modules: module A CC is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of CC EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D, CC EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and CC EIF3H of module B, thereby linking the three modules. EIF3J is a labile CC subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex CC interacts with RPS6KB1 under conditions of nutrient depletion. CC Mitogenic stimulation leads to binding and activation of a complex CC composed of MTOR and RPTOR, leading to phosphorylation and release of CC RPS6KB1 and binding of EIF4B to eIF-3. Also interacts with UPF2. CC Interacts with METTL3. else case and not CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3 CC (eIF-3) complex, which is composed of 13 subunits: @gn(EIF3A), CC @gn(EIF3B), @gn(EIF3C), @gn(EIF3D), @gn(EIF3E), @gn(EIF3F), @gn(EIF3G), CC @gn(EIF3H), @gn(EIF3I), @gn(EIF3J), @gn(EIF3K), @gn(EIF3L) and CC @gn(EIF3M). else case CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3 CC (eIF-3) complex. The eIF-3 complex interacts with pix. else CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3 CC (eIF-3) complex. end case CC -!- SUBCELLULAR LOCATION: Cytoplasm. case CC -!- DOMAIN: The RRM domain mediates interaction with EIF3J. CC -!- PTM: Phosphorylated. Phosphorylation is enhanced upon serum CC stimulation. end case CC -!- SIMILARITY: Belongs to the eIF-3 subunit B family. XX DR PROSITE; PS50102; RRM; 1; trigger=yes DR PROSITE; PS00678; WD_REPEATS_1; 1; trigger=no DR PROSITE; PS50082; WD_REPEATS_2; 1; trigger=no DR PROSITE; PS50294; WD_REPEATS_REGION; 1; trigger=no DR Pfam; PF08662; eIF2A; 1; trigger=no DR Pfam; PF00076; RRM_1; 1; trigger=no DR REP; Repeat_WD40; WD40; 5-7; trigger=strict XX case KW Acetylation end case KW Cytoplasm KW Initiation factor case KW Phosphoprotein end case KW Protein biosynthesis KW RNA-binding XX GO GO:0003723; F:RNA binding GO GO:0003743; F:translation initiation factor activity GO GO:0001732; P:formation of cytoplasmic translation initiation complex GO GO:0002183; P:cytoplasmic translational initiation GO GO:0005737; C:cytoplasm GO GO:0005852; C:eukaryotic translation initiation factor 3 complex GO GO:0016282; C:eukaryotic 43S preinitiation complex GO GO:0033290; C:eukaryotic 48S preinitiation complex XX FT From: EIF3B_HUMAN (P55884) case FT REGION 124..413 FT /note="Sufficient for interaction with EIF3E" FT REGION 170..274 FT /note="Sufficient for interaction with EIF3J" FT MOD_RES 1 FT /note="N-acetylmethionine" FT Tag: acetyl; Condition: M FT MOD_RES 83 FT /note="Phosphoserine" FT Condition: S FT MOD_RES 85 FT /note="Phosphoserine" FT Condition: S FT MOD_RES 119 FT /note="Phosphoserine" FT Condition: S FT MOD_RES 125 FT /note="Phosphoserine" FT Condition: S FT MOD_RES 152 FT /note="Phosphoserine" FT Condition: S FT MOD_RES 154 FT /note="Phosphoserine" FT Condition: S FT MOD_RES 164 FT /note="Phosphoserine" FT Condition: S end case FT From: EIF3B_YEAST (P06103) case FT REGION 1..136 FT /note="Sufficient for interaction with HCR1 and TIF32" FT REGION 28..261 FT /note="Sufficient for interaction with PIC8" end case XX Size: 621-814; Related: None; Template: P55884; Q8JZQ9; Q4G061; Q9XWI6; Q0E940; Q10425; P06103; Scope: Eukaryota Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.17 2021/03/19 //