EIF3E_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EIF3E_RAT
• UniProt AC: Q641X8
• Protein Name: Eukaryotic translation initiation factor 3 subunit E {ECO:0000255|HAMAP-Rule:MF_03004}
• Gene Name: Eif3e
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 445
• Subcellular Localization: Cytoplasm . Nucleus, PML body .
• Protein Description: 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 pre-initiation 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 post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. 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. Required for nonsense-mediated mRNA decay (NMD); may act in conjunction with UPF2 to divert mRNAs from translation to the NMD pathway. May interact with MCM7 and EPAS1 and regulate the proteasome-mediated degradation of these proteins..
• Protein Sequence: MAEYDLTTRIAHFLDRHLVFPLLEFLSVKEIYNEKELLQGKLDLLSDTNMVDFAMDVYKNLYSDDIPHALREKRTTVVAQLKQLQAETEPIVKMFEDPETTRQMQSTRDGRMLFDYLADKHGFRQEYLDTLYRYAKFQYECGNYSGAAEYLYFFRVLVPATDRNALSSLWGKLASEILMQNWDAAMEDLTRLKETIDNNSVSSPLQSLQQRTWLIHWSLFVFFNHPKGRDNIIDLFLYQPQYLNAIQTMCPHILRYLTTAVITNKDVRKRRQVLKDLVKVIQQESYTYKDPITEFVECLYVNFDFDGAQKKLRECESVLVNDFFLVACLEDFIENARLFIFETFCRIHQCISINMLADKLNMTPEEAERWIVNLIRNARLDAKIDSKLGHVVMGNNAVSPYQQVIEKTKSLSFRSQMLAMNIEKKLNQNSRSEAPNWATQDSGFY

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAEYDLTTR ------CCCCCCHHH	24.85	-
202	Phosphorylation	TIDNNSVSSPLQSLQ HHCCCCCCCHHHHHH	26.51	27097102
203	Phosphorylation	IDNNSVSSPLQSLQQ HCCCCCCCHHHHHHH	27.72	27097102
275	Acetylation	RKRRQVLKDLVKVIQ HHHHHHHHHHHHHHH	50.59	22902405
399	Phosphorylation	VMGNNAVSPYQQVIE EECCCCCCHHHHHHH	18.58	27097102
401	Phosphorylation	GNNAVSPYQQVIEKT CCCCCCHHHHHHHHH	12.22	23984901
439	Phosphorylation	SEAPNWATQDSGFY- CCCCCCCCCCCCCC-	25.23	23984901
442	Phosphorylation	PNWATQDSGFY---- CCCCCCCCCCC----	22.45	16641100
445	Phosphorylation	ATQDSGFY------- CCCCCCCC-------	22.59	23984901

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of EIF3E_RAT !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EIF3E_RAT !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of EIF3E_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of EIF3E_RAT !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.