dbPTM

EIF3C_DROME - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EIF3C_DROME
UniProt AC	A1ZAX1
Protein Name	Eukaryotic translation initiation factor 3 subunit C {ECO:0000255\|HAMAP-Rule:MF_03002}
Gene Name	eIF3c {ECO:0000255\|HAMAP-Rule:MF_03002}
Organism	Drosophila melanogaster (Fruit fly).
Sequence Length	910
Subcellular Localization	Cytoplasm .
Protein Description	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	MSRFFANGSESESESSEEEIQATNFNKASAFQFSDDEEEVKRVVRSTKEKRYENLTSIIKTIRNHKKIKDIPNTLSSFEDLTRAYQKALPVISKEENGITPRFYIRCLAELEDFINEVWEDREGRKNLSKNNSKSLGTLRQKVRKYIKDFEDDLSRFREAPDQESEAEDEVVALESDGGDAGDDSDAGVKPTEAVPKAVKSAPAKAAPADDDDSDDSIDWDSDSESETESSDDENQYQNMRERFLKRTTEKEEKDDDKRKDKRKEQKTKIRKRAEDDEDGEWETVVKGHVVEKPKMFEKDAEIDVPLVLAKLLEIMSARGKKRTDRRLQIDLLFELRDISDQHNLGTAVSVKIHFNIISAIYDYNQKISEPMKLEHWALLLEVMQSMMKLLLANADIIMSESVAEEHEEYATSPFYVRGCPLAAVERLDDEFVKLLKECDPHSNDYVSRLKDEVNVVKTIELVLQYFERSGTNNERCRIYLRKIEHLYYKFDPEVLKKKRGELPATTSTSVDVMDKLCKFIYAKDDTDRIRTRAILAHIYHHAMHDNWFQARDLVLMSHLQDNIDAADPATRILYNRMMANLGLCAFRQGNVKDAHHCLVDLMVTGKPKELLAQGLLPQRQHERSAEQEKIEKQRQMPFHMHINLELLECVYLVSAMLLEIPYIAAHEFDARRRMISKTFYQQLRSSERQSLVGPPESMREHVVAAAKAMRCGNWQACANFIVNKKMNTKVWDLFYESDRVREMLTKFIKEESLRTYLFTYSNVYTSISIPSLAQMYELPVPKVHSIISKMIINEELMASLDDPSETVGMHRSEPSRLQALAMQFVDKVTNLVDVNEKVFDMKQGNFFQRGNMGNRGDRGYNRNQNNQGGNWLGQRRDRNNRNRNQRGHHKNNQDRQQQQQQQVQTIDEE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Phosphorylation	SRFFANGSESESESS CCCCCCCCCCCCCCC	37.44	19429919
11	Phosphorylation	FFANGSESESESSEE CCCCCCCCCCCCCHH	48.39	19429919
13	Phosphorylation	ANGSESESESSEEEI CCCCCCCCCCCHHHH	52.65	19429919
15	Phosphorylation	GSESESESSEEEIQA CCCCCCCCCHHHHHH	52.94	19429919
16	Phosphorylation	SESESESSEEEIQAT CCCCCCCCHHHHHHC	45.00	19429919
29	Phosphorylation	ATNFNKASAFQFSDD HCCCCCCCCCCCCCC	31.09	29892262
34	Phosphorylation	KASAFQFSDDEEEVK CCCCCCCCCCHHHHH	33.11	21082442
135	Phosphorylation	LSKNNSKSLGTLRQK CCCCCCCCHHHHHHH	31.67	27626673
165	Phosphorylation	REAPDQESEAEDEVV HHCCCCCCCCCCCEE	36.15	21082442
176	Phosphorylation	DEVVALESDGGDAGD CCEEEEECCCCCCCC	42.26	21082442
185	Phosphorylation	GGDAGDDSDAGVKPT CCCCCCCCCCCCCCC	33.81	21082442
192	Phosphorylation	SDAGVKPTEAVPKAV CCCCCCCCCCCCHHH	30.75	22668510
490	Acetylation	KIEHLYYKFDPEVLK EHHHHHHHCCHHHHH	29.72	19608861
630	Acetylation	ERSAEQEKIEKQRQM HHHHHHHHHHHHHCC	56.72	19608861
678	Acetylation	ARRRMISKTFYQQLR HHHHHHHHHHHHHHH	31.56	19608861
838	Acetylation	NLVDVNEKVFDMKQG HCCCCCHHHHCCCCC	42.89	19608861

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 EIF3C_DROME !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of EIF3C_DROME !!

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 EIF3C_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EIF3L_DROME	CG5642	physical	22036573
EIF3K_DROME	CG10306	physical	22036573
EI3F1_DROME	CG9769	physical	22036573
EIF3A_DROME	eIF3-S10	physical	22036573
EI3D1_DROME	eIF-3p66	physical	22036573

Drug and Disease Associations

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

Regulatory Network of EIF3C_DROME

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-165; SER-176 ANDSER-185, AND MASS SPECTROMETRY.	18327897 [Abstract]
"An integrated chemical, mass spectrometric and computational strategyfor (quantitative) phosphoproteomics: application to Drosophilamelanogaster Kc167 cells."; Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,Juenger M.A., Eng J.K., Aebersold R., Tao W.A.; Mol. Biosyst. 3:275-286(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, AND MASSSPECTROMETRY.	17372656 [Abstract]