Q8JZQ9

FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of posttermination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. SUBUNIT: Interacts with UPF2 (By similarity). Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and EIF3H of module B, thereby linking the three modules. EIF3J is a labile subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex may also interact with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation may lead to binding and activation of a complex composed of MTOR and RPTOR, leading to phosphorylation and release of RPS6KB1 and binding of EIF4B to eIF-3. SUBCELLULAR LOCATION: Cytoplasm (Probable). TISSUE SPECIFICITY: Ubiquitously expressed. DOMAIN: The RRM domain mediates interaction with EIF3J (By similarity). PTM: Phosphorylated. Phosphorylation is enhanced upon serum stimulation (By similarity). DISRUPTION PHENOTYPE: Embryonic death. SIMILARITY: Belongs to the eIF-3 subunit B family. SIMILARITY: Contains 1 RRM (RNA recognition motif) domain. SIMILARITY: Contains 5 WD repeats. GENE SYNONYMS:Eif3b Eif3s9. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License., SEQUENCE 803 AA; 91370 MW; D770AC70BFE9832F CRC64;

EIF3B_MOUSE

urn:biopax:ModificationFeature:EIF3B_MOUSE_1, urn:biopax:ModificationFeature:EIF3B_MOUSE_10, urn:biopax:ModificationFeature:EIF3B_MOUSE_11, urn:biopax:ModificationFeature:EIF3B_MOUSE_12, urn:biopax:ModificationFeature:EIF3B_MOUSE_13, urn:biopax:ModificationFeature:EIF3B_MOUSE_14, urn:biopax:ModificationFeature:EIF3B_MOUSE_15, urn:biopax:ModificationFeature:EIF3B_MOUSE_16, urn:biopax:ModificationFeature:EIF3B_MOUSE_17, urn:biopax:ModificationFeature:EIF3B_MOUSE_18, urn:biopax:ModificationFeature:EIF3B_MOUSE_19, urn:biopax:ModificationFeature:EIF3B_MOUSE_2, urn:biopax:ModificationFeature:EIF3B_MOUSE_3, urn:biopax:ModificationFeature:EIF3B_MOUSE_4, urn:biopax:ModificationFeature:EIF3B_MOUSE_5, urn:biopax:ModificationFeature:EIF3B_MOUSE_6, urn:biopax:ModificationFeature:EIF3B_MOUSE_7, urn:biopax:ModificationFeature:EIF3B_MOUSE_8, urn:biopax:ModificationFeature:EIF3B_MOUSE_9

MQDAENVAVPEAAEERAEPARQQPASESPPTDEAAGSGGSEVGQTEDAEEDAEAGPEPEVRAKPAAQSEEETATSPAASPTPQSAERSPSQEPSAPGKAEAVGEQARGHPSAGAEEEGGSDGSAAEAEPRALENGEADEPSFSDPEDFVDDVSEEELLGDVLKDRPQEADGIDSVIVVDNVPQVGPDRLEKLKNVIHKIFSKFGKIINDYYPEEDGKTKGYIFLEYASPAHAVDAVKNADGYKLDKQHTFRVNLFTDFDKYMTISDEWDIPEKQPFKDLGNLRYWLEEAECRDQYSVIFESGDRTSIFWNDVKDPVSIEERARWTETYVRWSPKGTYLATFHQRGIALWGGDKFKQIQRFSHQGVQLIDFSPCERYLVTFSPLMDTQDDPQAIIIWDILTGHKKRGFHCESSAHWPIFKWSHDGKFFARMTLDTLSIYETPSMGLLDKKSLKISGIKDFSWSPGGNIIAFWVPEDKDIPARVTLMQLPTRQEIRVRNLFNVVDCKLHWQKNGDYLCVKVDRTPKGTQGVVTNFEIFRMREKQVPVDVVEMKETIIAFAWEPNGSKFAVLHGEAPRISVSFYHVKSNGKIELIKMFDKQQANTIFWSPQGQFVVLAGLRSMNGALAFVDTSDCTVMNIAEHYMASDVEWDPTGRYVVTSVSWWSHKVDNAYWLWTFQGRLLQKNNKDRFCQLLWRPRPPTLLSQDQIKQIKKDLKKYSKIFEQKDRLSQSKASKELVERRRTMMEDFRQYRKMAQELYMKQKNERLELRGGVDTDELDSNVDDWEEETIEFFVTEEVIPLGSQE