EIF3H_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EIF3H_MOUSE
• UniProt AC: Q91WK2
• Protein Name: Eukaryotic translation initiation factor 3 subunit H {ECO:0000255|HAMAP-Rule:MF_03007}
• Gene Name: Eif3h
• Organism: Mus musculus (Mouse).
• Sequence Length: 352
• 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..
• Protein Sequence: MASRKEGTGSTATSSGSAGGAVGKGKGKGGSGDSAVKQVQIDGLVVLKIIKHYQEEGQGTEVVQGVLLGLVVEDRLEITNCFPFPQHTEDDADFDEVQYQMEMMRSLRHVNIDHLHVGWYQSTYYGSFVTRALLDSQFSYQHAIEESVVLIYDPIKTAQGSLSLKAYRLTPKLMEVCKEKDFSPEALKKASITFEHMFEEVPIVIKNSHLINVLMWELEKKSAVADKHELLSLASSNHLGKSLQLLMDRVDEMSQDIIKYNTYMRNTSKQQQQKHQYQQRRQQENMQRQSRGEPPLPEEDLSKLFKPHQAPARMDSLLIAGQINTYCQNIKEFTAQNLGKLFMAQALQEYNN

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
3	Phosphorylation	-----MASRKEGTGS -----CCCCCCCCCC	42.46	29514104
8	Phosphorylation	MASRKEGTGSTATSS CCCCCCCCCCCCCCC	29.11	29472430
10	Phosphorylation	SRKEGTGSTATSSGS CCCCCCCCCCCCCCC	18.08	29472430
11	Phosphorylation	RKEGTGSTATSSGSA CCCCCCCCCCCCCCC	34.99	28066266
13	Phosphorylation	EGTGSTATSSGSAGG CCCCCCCCCCCCCCC	24.42	28066266
14	Phosphorylation	GTGSTATSSGSAGGA CCCCCCCCCCCCCCC	30.18	29472430
15	Phosphorylation	TGSTATSSGSAGGAV CCCCCCCCCCCCCCC	32.20	22668510
17	Phosphorylation	STATSSGSAGGAVGK CCCCCCCCCCCCCCC	26.20	25521595
24	Acetylation	SAGGAVGKGKGKGGS CCCCCCCCCCCCCCC	51.34	22733758
26	Acetylation	GGAVGKGKGKGGSGD CCCCCCCCCCCCCCC	62.02	22733758
172	Malonylation	KAYRLTPKLMEVCKE HHEECCHHHHHHHHH	56.05	26320211
177	Glutathionylation	TPKLMEVCKEKDFSP CHHHHHHHHHCCCCH	2.76	24333276
180	Acetylation	LMEVCKEKDFSPEAL HHHHHHHCCCCHHHH	49.95	22826441
183	Phosphorylation	VCKEKDFSPEALKKA HHHHCCCCHHHHHHC	31.78	25521595
188	Ubiquitination	DFSPEALKKASITFE CCCHHHHHHCCEEHH	54.03	-
191	Phosphorylation	PEALKKASITFEHMF HHHHHHCCEEHHHHH	30.92	26824392
193	Phosphorylation	ALKKASITFEHMFEE HHHHCCEEHHHHHHC	22.07	26239621
227	Acetylation	KKSAVADKHELLSLA HCCCCCCHHHHHHHH	29.28	23806337
227	Ubiquitination	KKSAVADKHELLSLA HCCCCCCHHHHHHHH	29.28	-
254	Phosphorylation	MDRVDEMSQDIIKYN HHHHHHHHHHHHHHH	23.74	28066266
259	Ubiquitination	EMSQDIIKYNTYMRN HHHHHHHHHHHHHCC	32.55	-
274	Acetylation	TSKQQQQKHQYQQRR CCHHHHHHHHHHHHH	28.47	23806337
290	Phosphorylation	QENMQRQSRGEPPLP HHHHHHHHCCCCCCC	44.43	27149854
303	Ubiquitination	LPEEDLSKLFKPHQA CCHHHHHHHCCCCCC	66.30	-
306	Malonylation	EDLSKLFKPHQAPAR HHHHHHCCCCCCCCC	52.61	26320211
306	Ubiquitination	EDLSKLFKPHQAPAR HHHHHHCCCCCCCCC	52.61	-

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

Oops, there are no upstream regulatory protein records of EIF3H_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EIF3H_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 EIF3H_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of EIF3H_MOUSE !!

Drug and Disease Associations

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