dbPTM

EIF3D_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EIF3D_MOUSE
UniProt AC	O70194
Protein Name	Eukaryotic translation initiation factor 3 subunit D {ECO:0000255\|HAMAP-Rule:MF_03003}
Gene Name	Eif3d
Organism	Mus musculus (Mouse).
Sequence Length	548
Subcellular Localization	Cytoplasm .
Protein Description	mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, a complex required for several steps in the initiation of protein synthesis of a specialized repertoire of mRNAs. 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. In the eIF-3 complex, EIF3D specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs..
Protein Sequence	MAKFMTPVIQDNPSGWGPCAVPEQFRDMPYQPFSKGDRLGKVADWTGATYQDKRYTNKYSSQFGGGSQYAYFHEEDETSFQLVDTARTQKTAYQRNRMRFAQRNLRRDKDRRNMVQFNLQTLPKSAKQKERERIRLQKKFQKQFGVRQKWDQKSQKPRDSSVEVRSDWEVKEEMDFPQLMKMRYLEVSEPQDIECCGALEYYDKAFDRITTRSEKPLRSIKRIFHTVTTTDDPVIRKLAKTQGNVFATDAILATLMSCTRSVYSWDIVVQRVGSKLFFDKRDNSDFDLLTVSETANEPPQDEGNSFNSPRNLAMEATYINHNFSQQCLRMGRERYNFPNPNPFVEDDMDKNEIASVAYRYRRWKLGDDIDLIVRCEHDGVMTGANGEVSFINIKTLNEWDSRHCNGVDWRQKLDSQRGAVIATELKNNSYKLARWTCCALLAGSEYLKLGYVSRYHVKDSSRHVILGTQQFKPNEFASQINLSVENAWGILRCVIDICMKLEEGKYLILKDPNKQVIRVYSLPDGTFSSEEDEEDEEEEEEEEEEEET

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
19	S-palmitoylation	NPSGWGPCAVPEQFR CCCCCCCCCCCHHHC	5.41	28526873
19	Glutathionylation	NPSGWGPCAVPEQFR CCCCCCCCCCCHHHC	5.41	24333276
30	Phosphorylation	EQFRDMPYQPFSKGD HHHCCCCCCCCCCCC	23.37	29514104
35	Ubiquitination	MPYQPFSKGDRLGKV CCCCCCCCCCCCCCC	66.27	22790023
41	Acetylation	SKGDRLGKVADWTGA CCCCCCCCCCCCCCC	38.55	23806337
46	Phosphorylation	LGKVADWTGATYQDK CCCCCCCCCCCCCCH	19.93	28725479
49	Phosphorylation	VADWTGATYQDKRYT CCCCCCCCCCCHHCC	24.06	25367039
50	Phosphorylation	ADWTGATYQDKRYTN CCCCCCCCCCHHCCC	17.74	28725479
53	Acetylation	TGATYQDKRYTNKYS CCCCCCCHHCCCCCC	31.60	23806337
53	Ubiquitination	TGATYQDKRYTNKYS CCCCCCCHHCCCCCC	31.60	27667366
53	Malonylation	TGATYQDKRYTNKYS CCCCCCCHHCCCCCC	31.60	26320211
90	Ubiquitination	VDTARTQKTAYQRNR ECCHHHHHHHHHHHH	34.21	-
95	Dimethylation	TQKTAYQRNRMRFAQ HHHHHHHHHHHHHHH	21.75	-
97	Dimethylation	KTAYQRNRMRFAQRN HHHHHHHHHHHHHHH	21.60	-
99	Dimethylation	AYQRNRMRFAQRNLR HHHHHHHHHHHHHHH	22.10	-
103	Dimethylation	NRMRFAQRNLRRDKD HHHHHHHHHHHCCHH	40.49	-
106	Dimethylation	RFAQRNLRRDKDRRN HHHHHHHHCCHHHHH	48.58	-
121	Phosphorylation	MVQFNLQTLPKSAKQ HHHHHHHHCCCCHHH	48.47	26824392
124	Acetylation	FNLQTLPKSAKQKER HHHHHCCCCHHHHHH	67.18	23806337
142	Malonylation	RLQKKFQKQFGVRQK HHHHHHHHHHCCCCC	51.21	26320211
154	Phosphorylation	RQKWDQKSQKPRDSS CCCCCCCCCCCCCCC	37.49	29176673
160	Phosphorylation	KSQKPRDSSVEVRSD CCCCCCCCCCCCCCC	37.25	25521595
161	Phosphorylation	SQKPRDSSVEVRSDW CCCCCCCCCCCCCCC	26.96	25521595
171	Acetylation	VRSDWEVKEEMDFPQ CCCCCHHCCCCCHHH	36.12	23806337
258	Glutathionylation	ILATLMSCTRSVYSW HHHHHHHCCCCCCCH	1.98	24333276
275	Ubiquitination	VVQRVGSKLFFDKRD HEEEECCCCEEECCC	43.30	22790023
290	Phosphorylation	NSDFDLLTVSETANE CCCCEEEEEEECCCC	29.32	23649490
292	Phosphorylation	DFDLLTVSETANEPP CCEEEEEEECCCCCC	24.80	23649490
294	Phosphorylation	DLLTVSETANEPPQD EEEEEEECCCCCCCC	27.55	23649490
308	Phosphorylation	DEGNSFNSPRNLAME CCCCCCCCHHHHHHH	24.19	-
317	Phosphorylation	RNLAMEATYINHNFS HHHHHHHHCCCCCHH	16.19	25367039
318	Phosphorylation	NLAMEATYINHNFSQ HHHHHHHCCCCCHHH	13.53	18563927
327	Glutathionylation	NHNFSQQCLRMGRER CCCHHHHHHHCCHHH	1.70	24333276
404	Glutathionylation	NEWDSRHCNGVDWRQ CCCCCCCCCCCCHHH	4.63	24333276
514	Malonylation	LILKDPNKQVIRVYS EEEECCCCCEEEEEE	51.86	26320211
520	Phosphorylation	NKQVIRVYSLPDGTF CCCEEEEEECCCCCC	8.47	23984901
521	Phosphorylation	KQVIRVYSLPDGTFS CCEEEEEECCCCCCC	30.48	25159016
526	Phosphorylation	VYSLPDGTFSSEEDE EEECCCCCCCCCCCC	27.94	23984901
527	Phosphorylation	YSLPDGTFSSEEDEE EECCCCCCCCCCCCC	10.40	17242355
528	Phosphorylation	SLPDGTFSSEEDEED ECCCCCCCCCCCCCC	36.36	23984901
529	Phosphorylation	LPDGTFSSEEDEEDE CCCCCCCCCCCCCCH	40.59	27087446
548	Phosphorylation	EEEEEEET------- HHHHHHCC-------	47.38	22324799

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
Oops, there are no upstream regulatory protein records of EIF3D_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of EIF3D_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of EIF3D_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of EIF3D_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of EIF3D_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528 AND SER-529, ANDMASS SPECTROMETRY.	17242355 [Abstract]
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells."; Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.; J. Proteome Res. 6:3174-3186(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529 AND THR-548, ANDMASS SPECTROMETRY.	17622165 [Abstract]