EIF3L_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EIF3L_MOUSE
• UniProt AC: Q8QZY1
• Protein Name: Eukaryotic translation initiation factor 3 subunit L {ECO:0000255|HAMAP-Rule:MF_03011}
• Gene Name: Eif3l
• Organism: Mus musculus (Mouse).
• Sequence Length: 564
• 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: MSYPADDYESEAAYDPYAYPGDYDMHTGDPKQDLAYERQYEQQTYQVIPEVIKNFIQYFHKTVSDLIDQKVYELQASRVSSDVIDQKVYEIQDIYENSWTKLTERFFKNTPWPEAEAIAPQVGNDAVFLILYKELYYRHIYAKVSGGPSLEQRFESYYNYCNLFNYILNADGPAPLELPNQWLWDIIDEFIYQFQSFSQYRCKTAKKSEGEMDFLRSNPKVWNVHSVLNVLHSLVDKSNINRQLEVYTSGGDPESVAGEYGRHSLYKMLGYFSLVGLLRLHSLLGDYYQAIKVLENIELNKKSMYSRVPECQVTTYYYVGFAYLMMRRYQDAIRVFANILLYIQRTKSMFQRTTYKYEMINKQNEQMHALLAIALTMYPMRIDESIHLQLREKYGDKMLRMQKGDPQVYEELFSYACPKFLSPVVPNYDNVHPNYHKEPFLQQLKVFSDEVQQQAQLSTIRSFLKLYTTMPVAKLAGFLDLTEQEFRIQLLVFKHKMKNLVWTSGISALDGEFQSASEVDFYIDKDMIHIADTKVARRYGDFFIRQIHKFEELNRTLKKMGQRP

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	------MSYPADDYE ------CCCCCCCCC	39.56	-
2	Phosphorylation	------MSYPADDYE ------CCCCCCCCC	39.56	23737553
3	Phosphorylation	-----MSYPADDYES -----CCCCCCCCCC	10.92	23737553
8	Phosphorylation	MSYPADDYESEAAYD CCCCCCCCCCCCCCC	23.15	23737553
10	Phosphorylation	YPADDYESEAAYDPY CCCCCCCCCCCCCCC	26.72	23737553
14	Phosphorylation	DYESEAAYDPYAYPG CCCCCCCCCCCCCCC	25.21	23737553
17	Phosphorylation	SEAAYDPYAYPGDYD CCCCCCCCCCCCCCC	18.83	23737553
19	Phosphorylation	AAYDPYAYPGDYDMH CCCCCCCCCCCCCCC	11.25	23737553
23	Phosphorylation	PYAYPGDYDMHTGDP CCCCCCCCCCCCCCC	22.53	23737553
27	Phosphorylation	PGDYDMHTGDPKQDL CCCCCCCCCCCHHHH	36.32	23737553
36	Phosphorylation	DPKQDLAYERQYEQQ CCHHHHHHHHHHHHH	20.95	25367039
40	Phosphorylation	DLAYERQYEQQTYQV HHHHHHHHHHHHHHH	23.17	25367039
44	Phosphorylation	ERQYEQQTYQVIPEV HHHHHHHHHHHHHHH	18.67	25159016
45	Phosphorylation	RQYEQQTYQVIPEVI HHHHHHHHHHHHHHH	9.10	26370283
58	Phosphorylation	VIKNFIQYFHKTVSD HHHHHHHHHHHHHHH	11.66	20139300
64	Phosphorylation	QYFHKTVSDLIDQKV HHHHHHHHHHHHHHH	31.75	27742792
72	Phosphorylation	DLIDQKVYELQASRV HHHHHHHHHHHHHCC	20.25	22817900
77	Phosphorylation	KVYELQASRVSSDVI HHHHHHHHCCCCHHH	21.91	25367039
80	Phosphorylation	ELQASRVSSDVIDQK HHHHHCCCCHHHCCH	21.51	25338131
89	Phosphorylation	DVIDQKVYEIQDIYE HHHCCHHEEHHHHHH	17.85	22817900
101	Ubiquitination	IYENSWTKLTERFFK HHHCCHHHHHHHHHH	47.34	22790023
101	Acetylation	IYENSWTKLTERFFK HHHCCHHHHHHHHHH	47.34	23954790
207	Ubiquitination	YRCKTAKKSEGEMDF CCCCCCCCCCCCCHH	51.80	22790023
247	Phosphorylation	INRQLEVYTSGGDPE CCCEEEEEECCCCHH	5.94	22817900
301	Acetylation	LENIELNKKSMYSRV HHHCCCCCCCHHHCC	59.87	23236377
318	Phosphorylation	CQVTTYYYVGFAYLM CEEEEEHHHHHHHHH	5.45	-
323	Phosphorylation	YYYVGFAYLMMRRYQ EHHHHHHHHHHHHHH	7.89	-
329	Phosphorylation	AYLMMRRYQDAIRVF HHHHHHHHHHHHHHH	10.61	-
403	Ubiquitination	DKMLRMQKGDPQVYE HHHHHHCCCCHHHHH	56.81	22790023
414	Phosphorylation	QVYEELFSYACPKFL HHHHHHHHHHCHHHH	25.17	25367039
415	Phosphorylation	VYEELFSYACPKFLS HHHHHHHHHCHHHHC	12.61	22817900
417	Glutathionylation	EELFSYACPKFLSPV HHHHHHHCHHHHCCC	2.60	24333276
437	Ubiquitination	NVHPNYHKEPFLQQL CCCCCCCCCHHHHHH	57.64	22790023
437	Acetylation	NVHPNYHKEPFLQQL CCCCCCCCCHHHHHH	57.64	23236377
445	Ubiquitination	EPFLQQLKVFSDEVQ CHHHHHHHHCCHHHH	36.57	-
465	Ubiquitination	STIRSFLKLYTTMPV HHHHHHHHHHHHHCH	37.12	-
465	Acetylation	STIRSFLKLYTTMPV HHHHHHHHHHHHHCH	37.12	23806337
465	Malonylation	STIRSFLKLYTTMPV HHHHHHHHHHHHHCH	37.12	26320211
474	Ubiquitination	YTTMPVAKLAGFLDL HHHHCHHHHHCCCCC	38.82	-
534	Ubiquitination	MIHIADTKVARRYGD HEEECCHHHHHHHHH	34.15	27667366
549	Malonylation	FFIRQIHKFEELNRT HHHHHHHHHHHHHHH	56.98	26320211
549	Acetylation	FFIRQIHKFEELNRT HHHHHHHHHHHHHHH	56.98	23954790
549	Ubiquitination	FFIRQIHKFEELNRT HHHHHHHHHHHHHHH	56.98	-

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

Oops, there are no upstream regulatory protein records of EIF3L_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EIF3L_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 EIF3L_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of EIF3L_MOUSE !!

Drug and Disease Associations

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