Search by BoMiProt ID - Bomi5617


Primary Information

BoMiProt ID Bomi5617
Protein Name Eukaryotic translation initiation factor 3 subunit B
Organism Bos taurus
Uniprot IdA7MB16
Milk FractionExosomes
Ref Sequence Id NP_001095826.1
Aminoacid Length 786
Molecular Weight 88919
Fasta Sequence https://www.uniprot.org/uniprot/A7MB16.fasta
Gene Name EIF3B
Gene Id 789999
Protein Existence Status reviewed

Secondary Information

Protein Function RNA-binding 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 specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression.
Biochemical Properties The eIF3b protein in mammals contains two domains. The N-terminal domain (NTD) consists of a structurally uncanonical RNA recognition motif (RRM) and the WD40β domain.The sheet area of eIF3b-RRM in humans (residues 185-268), is mostly negatively charged.The typical RRM, a common structural motif, contains conserved ribonucleoprotein1 (RNP1) and ribonucleoprotein2 (RNP2) sequences, which include conserved aromatic residues necessary for interaction with RNA. The RNP2 of eIF3b has a shortage of aromatic residues.The WD40β domain of eIF3b (residues 306 -705), a nine-bladed β-propeller fold, is highly conserved from yeast to humans.
PTMs Acetylation, Phosphorylation
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|A7MB16|EIF3B_BOVIN Eukaryotic translation initiation factor 3 subunit B OS=Bos taurus OX=9913 GN=EIF3B PE=2 SV=1 MQDAENVAAPEAAEQRAEPGPEQAAAEPSPGAEVARPGVQEAAGGEDAEAGPGPEGPAEP AADGEGKADATPGATPPPPEESSAQLAGEAPAEQAQDAAAEAGS*104EGAGGDPDGAAEDGGA DEPS*124FS*126DPEDFVDDVS*136EEELLADVLKDRPQEADGIDSVIVVDNVPQVGPDRLEKLKNVIH KIFSKFGKITNDFYPEEDGRTKGYIFLEYAS*211PAHALDAVKNADGYKLDKQHTFRVNLFTD FDKYMTISDEWDIPEKQPFKDLGNLRYWLEEAECRDQYSVIFESGDRTSIFWNDVKDPVS IEERARWTETYVRWSPKGTYLATFHQRGIALWGGEKFKQIQRFSHQGVQLIDFSPCERYL VTFSPLMDTQDDPQAIIIWDILTGQKKRGFHCESSAHWPIFKWSHDGKFFARMTLDTLSI YETPSMGLLDKKSLKISGIKDFSWSPGGNIIAFWVPEDKDIPARVTLMQLPTRQEIRVRN LFNVVDCKLHWQKNGDYLCVKVDRTPKGTQGVVTNFEIFRMREKQVPVDVVEMKETIIAF AWEPNGSKFAVLHGEAPRISVSFYHVKNNGKIELIKMFDKQQANTIFWSPQGQFVVLAGL RSMNGALAFVDTSDCTVMNIAEHYMASDVEWDPTGRYVVTSVSWWSHKVDNAYWLWTFQG RLLQKNSKDRFCQLLWRPRPPTLLSQDQIKQIKKDLKKYSKIFEQKDRLSQSKASKELVE RRRTMMEDFRKYRKMAQELYMEQKNARLELRGGVDTDELDSNVDDWEEETIEFFVTEEII PLGNQE
Predicted Disorder Regions 1-130
DisProt Annotation
TM Helix Prediction No TM helices
Significance of PTMs seven phosphorylation sites (Ser-83, Ser-85, Ser-119, Ser-125, Ser-152, Ser-154, and Ser-164) and one acetylation site (Met-1) which are related to the activity and function of eif3b
Bibliography 1.Feng, X., Li, J., & Liu, P. (2018). The Biological Roles of Translation Initiation Factor 3b. International journal of biological sciences, 14(12), 1630–1635. https://doi.org/10.7150/ijbs.26932