EIF3M_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EIF3M_MOUSE
• UniProt AC: Q99JX4
• Protein Name: Eukaryotic translation initiation factor 3 subunit M {ECO:0000255|HAMAP-Rule:MF_03012}
• Gene Name: Eif3m
• Organism: Mus musculus (Mouse).
• Sequence Length: 374
• 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: MSVPAFIDISEEDQAAELRAYLKSKGAELSEENSEGGLHVDLAQIIEACDVCLKEDDKDVESVMNSVVSLLLILEPDKQEALIESLCEKLVKFREGERPSLRLQLLSNLFHGMDKNTPVRYTVYCSLIKVAASCGAIQYIPTELDQVRKWISDWKLTTEKKHTLLRLLYEALVDCKKSDAASKVMVELLGSYTEDNASQARVDAHRCIVRALKDPNAFLFDHLLTLKPVKFLEGELIHDLLTIFVSAKLASYVKFYQNNKDFIDSLGLLHEQNMAKMRLLTFMGMAVENKEISFDTMQQELQIGADDVEAFVIDAVRTKMVYCKIDQTQRKVVVSHSTHRTFGKQQWQQLYDTLNAWKQNLNKVKNSLLSLSDT

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	------MSVPAFIDI ------CCCCCEEEC	36.49	-
2	Phosphorylation	------MSVPAFIDI ------CCCCCEEEC	36.49	26824392
10	Phosphorylation	VPAFIDISEEDQAAE CCCEEECCHHHHHHH	31.05	25293948
100	Phosphorylation	FREGERPSLRLQLLS HCCCCCCHHHHHHHH	32.13	26060331
125	S-nitrosylation	PVRYTVYCSLIKVAA CCCHHHHHHHHHHHH	2.01	20925432
125	S-nitrosocysteine	PVRYTVYCSLIKVAA CCCHHHHHHHHHHHH	2.01	-
152	Phosphorylation	DQVRKWISDWKLTTE HHHHHHHHCCCCCHH	35.98	-
176	Malonylation	YEALVDCKKSDAASK HHHHHHCCCCCHHHH	51.34	26320211
227	Ubiquitination	FDHLLTLKPVKFLEG HHCCCCCCCHHHHCC	42.39	22790023
227	Acetylation	FDHLLTLKPVKFLEG HHCCCCCCCHHHHCC	42.39	23954790
230	Ubiquitination	LLTLKPVKFLEGELI CCCCCCHHHHCCCHH	53.40	-
254	Acetylation	AKLASYVKFYQNNKD HHHHHHHHHHHCCHH	30.07	-
254	Ubiquitination	AKLASYVKFYQNNKD HHHHHHHHHHHCCHH	30.07	22790023
260	Ubiquitination	VKFYQNNKDFIDSLG HHHHHCCHHHHHHHH	62.66	22790023
319	Malonylation	VIDAVRTKMVYCKID HHHHHHCCEEEEECC	18.79	26320211
324	Ubiquitination	RTKMVYCKIDQTQRK HCCEEEEECCCCCCE	31.46	-
335	Phosphorylation	TQRKVVVSHSTHRTF CCCEEEEECCHHHCC	10.50	29514104
337	Phosphorylation	RKVVVSHSTHRTFGK CEEEEECCHHHCCCH	20.57	26824392
338	Phosphorylation	KVVVSHSTHRTFGKQ EEEEECCHHHCCCHH	15.23	25266776
344	Ubiquitination	STHRTFGKQQWQQLY CHHHCCCHHHHHHHH	34.82	22790023
351	Phosphorylation	KQQWQQLYDTLNAWK HHHHHHHHHHHHHHH	11.53	25367039
353	Phosphorylation	QWQQLYDTLNAWKQN HHHHHHHHHHHHHHH	14.35	25367039
365	Ubiquitination	KQNLNKVKNSLLSLS HHHHHHHHHHHHHCC	42.29	-
367	Phosphorylation	NLNKVKNSLLSLSDT HHHHHHHHHHHCCCC	25.60	24899341
372	Phosphorylation	KNSLLSLSDT----- HHHHHHCCCC-----	35.51	26370283

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

Oops, there are no upstream regulatory protein records of EIF3M_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EIF3M_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 EIF3M_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of EIF3M_MOUSE !!

Drug and Disease Associations

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