EIF3F_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EIF3F_MOUSE
• UniProt AC: Q9DCH4
• Protein Name: Eukaryotic translation initiation factor 3 subunit F {ECO:0000255|HAMAP-Rule:MF_03005}
• Gene Name: Eif3f
• Organism: Mus musculus (Mouse).
• Sequence Length: 361
• Subcellular Localization: Cytoplasm .
• 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.; Deubiquitinates activated NOTCH1, promoting its nuclear import, thereby acting as a positive regulator of Notch signaling..
• Protein Sequence: MASPAVPANVPPATAAAAPAPVVTAAPASAPTPSTPAPTPAATPAASPAPVSSDPAVAAPAAPGQTPASAPAPAQTPAPSQPGPALPGPFPGGRVVRLHPVILASIVDSYERRNEGAARVIGTLLGTVDKHSVEVTNCFSVPHNESEDEVAVDMEFAKNMYELHKKVSPNELILGWYATGHDITEHSVLIHEYYSREAPNPIHLTVDTGLQHGRMSIKAYVSTLMGVPGRTMGVMFTPLTVKYAYYDTERIGVDLIMKTCFSPNRVIGLSSDLQQVGGASARIQDALSTVLQYAEDVLSGKVSADNTVGRFLMSLVNQVPKIVPDDFETMLNSNINDLLMVTYLANLTQSQIALNEKLVNL

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	------MASPAVPAN ------CCCCCCCCC	24.99	-
52	Phosphorylation	AASPAPVSSDPAVAA CCCCCCCCCCCCCCC	28.15	-
218	Ubiquitination	QHGRMSIKAYVSTLM CCCCHHHHHHHHHHH	26.76	-
242	Acetylation	MFTPLTVKYAYYDTE EEEEEEEEEEEECCH	20.94	23236377
242	Ubiquitination	MFTPLTVKYAYYDTE EEEEEEEEEEEECCH	20.94	-
245	Phosphorylation	PLTVKYAYYDTERIG EEEEEEEEECCHHHC	9.97	-
258	Ubiquitination	IGVDLIMKTCFSPNR HCCEEEHHHCCCCCC	34.84	-
259	Phosphorylation	GVDLIMKTCFSPNRV CCEEEHHHCCCCCCE	11.03	27087446
262	Phosphorylation	LIMKTCFSPNRVIGL EEHHHCCCCCCEEEE	24.34	27087446
270	Phosphorylation	PNRVIGLSSDLQQVG CCCEEEECCCHHHHC	19.32	26745281
271	Phosphorylation	NRVIGLSSDLQQVGG CCEEEECCCHHHHCC	47.59	25777480
301	Ubiquitination	AEDVLSGKVSADNTV HHHHHCCCCCCCCHH	29.64	-
321	Ubiquitination	SLVNQVPKIVPDDFE HHHHCCCCCCCCCHH	58.44	-
357	Ubiquitination	SQIALNEKLVNL--- HHHHHHHHHHCC---	57.57	-

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
52	S	Phosphorylation	Kinase	CDK11	P24788	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	Fbxo32	Q9CPU7	PMID:22199232

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EIF3F_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of EIF3F_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference

Drug and Disease Associations

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