EIF3A_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EIF3A_DROME
• UniProt AC: Q9VN25
• Protein Name: Eukaryotic translation initiation factor 3 subunit A {ECO:0000255|HAMAP-Rule:MF_03000}
• Gene Name: eIF3a {ECO:0000255|HAMAP-Rule:MF_03000}
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 1140
• Subcellular Localization: Cytoplasm .
• Protein Description: RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation..
• Protein Sequence: MARYTQRPENALKRANEFIEVGKPLRALDTLQEVFRNKRWNYAYSETVIEPLMFKYLYLCVELKKSHIAKEGLFQYRNMFQLVNVNSLENVIRGYLKMAEEHTEAAQAQSSAAVAVLELDDLDNIATPESILMSAVCGEDAQDRSDRTILLPWVKFLWESYCQCLELLRVNTHCEALYHDIARMAFQFCLKYNRKSEFRRLCDKLRKHLEDICKSSNQTTGVSINKVETQQLCLDTRLYLLDSAIQMELWQEAYKAIEDIHGLMALSKKTPVPKTMANYYQKLAMVFSKAGNQLFHAAALLKLFQLTRELKKNLTKDDLQRMAAHVLLATLSIPLPSAHPEFDRFIEADKSPLEKAQKLAVLLGLPQPPTRVSLIREVVRLNVPQLVSEDFRNLYNWLEVDFNPLNLCKRIQSIVDFIENGPENALLTPYIQSLKDVTIMRLIRQISQVYESIKFQRLLQLASFCNIFELEKLLVESVRHNDMQIRIDHQKNSIYFGTDLTESQREYRPDGPALQSMPSEQIRSQLVNMSTVLTRAVSIVYPNRERDQRAKLRNQMVNHYHEIKDREHQRILQRQKIIEDRKEYIEKQNNAREEEEARRQEEESRKAKLAEQKRLEQEQEERERKRHQNEIQAIREKSLKEKVQQISQTAHGKKMLSKLDEEGIKKLDAEQIAKRESEELQREAKELQSKLKSQEKKIDYFERAKRLEEIPLFEKYLAEKQVKDKEFWEATEKTRIENAIAERKDAVAQQERLKRMYPDRDEFLEALKKERASLYVEKLKKFEAALEAERKKRLADRIIRRREERRQAFLREKEEERLRKEEEIRLAQAAEERAAAEARRLEREAEDEKRRAQYEKQRAKEEEAERKIKEDRDRLSRELASERERTEKDRDTWRPRGGDRPSASNGGSSEWRRAAPAASERNDRGGERIERGGERIERGGERLERGGERIERGGDRDRKDNEGADSSWRVRREPDSQRAAAPKDSGAPQSRDDKWRRGGERDRDFRIDGARRDRDDGPRRDRDDGPRRDRDDERGGFRRADGARRTDEPQRETGGNWRDAPRHADRETRRPAERRDRDVRETRGDQRGSAPKEAASGGVGGNWRTAPATREEKPAAKRDQAQEKENKAGDDGEWTSVKRR

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
70	Acetylation	LKKSHIAKEGLFQYR HHHHHHCCCCHHHHC	52.27	21791702
538	Phosphorylation	TVLTRAVSIVYPNRE HHHHHHHHHHCCCCH	12.83	21082442
677	Phosphorylation	EQIAKRESEELQREA HHHHHHHHHHHHHHH	40.16	19429919
693	Phosphorylation	ELQSKLKSQEKKIDY HHHHHHHHHHHHHHH	54.75	25749252
892	Phosphorylation	RTEKDRDTWRPRGGD HHHHHHCCCCCCCCC	25.03	21082442
902	Phosphorylation	PRGGDRPSASNGGSS CCCCCCCCCCCCCCH	45.27	22817900
904	Phosphorylation	GGDRPSASNGGSSEW CCCCCCCCCCCCHHH	40.10	22817900
908	Phosphorylation	PSASNGGSSEWRRAA CCCCCCCCHHHHHHC	26.87	18327897
919	Phosphorylation	RRAAPAASERNDRGG HHHCCCHHHCCCCCC	38.91	21082442
967	Phosphorylation	DNEGADSSWRVRREP CCCCCCCCCCCCCCC	21.32	19429919
985	Phosphorylation	RAAAPKDSGAPQSRD CCCCCCCCCCCCCCC	42.87	21082442
1046	Phosphorylation	RADGARRTDEPQRET CCCCCCCCCCCCHHC	38.88	21082442
1053	Phosphorylation	TDEPQRETGGNWRDA CCCCCHHCCCCCCCC	53.21	22817900
1082	Phosphorylation	RDRDVRETRGDQRGS HCHHHHHHHCCCCCC	29.41	21082442
1089	Phosphorylation	TRGDQRGSAPKEAAS HHCCCCCCCCHHHHC	43.52	27626673

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

Oops, there are no upstream regulatory protein records of EIF3A_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EIF3A_DROME !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of EIF3A_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EI3F1_DROME	CG9769	physical	22036573

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-908, AND MASSSPECTROMETRY.
PubMed: 18327897