EI3JA_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EI3JA_MOUSE
• UniProt AC: Q3UGC7
• Protein Name: Eukaryotic translation initiation factor 3 subunit J-A {ECO:0000255|HAMAP-Rule:MF_03009}
• Gene Name: Eif3j1
• Organism: Mus musculus (Mouse).
• Sequence Length: 261
• 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. This subunit binds directly within the mRNA entry channel of the 40S ribosome to the aminoacyl (A) site. It may regulate the interaction between the 43S PIC and mRNA..
• Protein Sequence: MAAAAAAAAAAGDSDSWDADTFSMEDPVRKVAGGGTAGGDRWEGEDEDEDVKDNWDDDDDENKEEAEVKPEVKISEKKKIAEKIKEKERQQKKRQEEIKKRLEEPEESKVLTPEEQLADKLRLKKLQEESDLELAKETFGVNNTVYGIDAMNPSSRDDFTEFGKLLKDKITQYEKSLYYASFLEALVRDVCISLEIDDLKKITNSLTVLCSEKQKQEKQSKAKKKKKGVVPGGGLKATMKDDLADYGGYEGGYVQDYEDFM

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
14	Phosphorylation	AAAAAGDSDSWDADT HHHHHCCCCCCCCCC		26824392
16	Phosphorylation	AAAGDSDSWDADTFS HHHCCCCCCCCCCCC		26824392
21	Phosphorylation	SDSWDADTFSMEDPV CCCCCCCCCCCCCCC		23684622
23	Phosphorylation	SWDADTFSMEDPVRK CCCCCCCCCCCCCHH		23684622
108	Phosphorylation	RLEEPEESKVLTPEE HHCCHHHHCCCCHHH		29514104
112	Phosphorylation	PEESKVLTPEEQLAD HHHHCCCCHHHHHHH		25521595
120	Ubiquitination	PEEQLADKLRLKKLQ HHHHHHHHHHHHHHH		-
120	Malonylation	PEEQLADKLRLKKLQ HHHHHHHHHHHHHHH		26320211
120	Acetylation	PEEQLADKLRLKKLQ HHHHHHHHHHHHHHH		23806337
130	Phosphorylation	LKKLQEESDLELAKE HHHHHHHHCHHHHHH		25521595
164	Ubiquitination	DDFTEFGKLLKDKIT CCHHHHHHHHHHHHH		-
169	Ubiquitination	FGKLLKDKITQYEKS HHHHHHHHHHHHHHH		27667366
201	Acetylation	LEIDDLKKITNSLTV CCHHHHHHHHHHHHH		22826441
211	Phosphorylation	NSLTVLCSEKQKQEK HHHHHHCCHHHHHHH		-
227	Malonylation	SKAKKKKKGVVPGGG HHHHHHCCCCCCCCC		26320211
238	Phosphorylation	PGGGLKATMKDDLAD CCCCHHHHHCCHHHH		20531401
246	Phosphorylation	MKDDLADYGGYEGGY HCCHHHHCCCCCCCC		22817900
257	Phosphorylation	EGGYVQDYEDFM--- CCCCCCCHHHHC---		-

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

Oops, there are no upstream regulatory protein records of EI3JA_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EI3JA_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 EI3JA_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of EI3JA_MOUSE !!

Drug and Disease Associations

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