EIF3C_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EIF3C_ARATH
• UniProt AC: O49160
• Protein Name: Eukaryotic translation initiation factor 3 subunit C {ECO:0000255|HAMAP-Rule:MF_03002}
• Gene Name: TIF3C1
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 900
• 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: MTSRFFTQVGSESEDESDYEVEVNEVQNDDVNNRYLQSGSEDDDDTDTKRVVKPAKDKRFEEMTYTVDQMKNAMKINDWVSLQENFDKVNKQLEKVMRITEAVKPPTLYIKTLVMLEDFLNEALANKEAKKKMSTSNSKALNSMKQKLKKNNKLYEDDINKYREAPEVEEEKQPEDDDDDDDDDDEVEDDDDSSIDGPTVDPGSDVDEPTDNLTWEKMLSKKDKLLEKLMNKDPKEITWDWVNKKFKEIVAARGKKGTARFELVDQLTHLTKIAKTPAQKLEILFSVISAQFDVNPGLSGHMPINVWKKCVLNMLTILDILVKYSNIVVDDTVEPDENETSKPTDYDGKIRVWGNLVAFLERVDTEFFKSLQCIDPHTREYVERLRDEPMFLALAQNIQDYFERMGDFKAAAKVALRRVEAIYYKPQEVYDAMRKLAELVEEEEETEEAKEESGPPTSFIVVPEVVPRKPTFPESSRAMMDILVSLIYRNGDERTKARAMLCDINHHALMDNFVTARDLLLMSHLQDNIQHMDISTQILFNRTMAQLGLCAFRAGMITESHSCLSELYSGQRVRELLAQGVSQSRYHEKTPEQERMERRRQMPYHMHLNLELLEAVHLICAMLLEVPNMAANSHDAKRRVISKNFRRLLEISERQAFTAPPENVRDHVMAATRALTKGDFQKAFEVLNSLEVWRLLKNRDSILDMVKDRIKEEALRTYLFTYSSSYESLSLDQLAKMFDVSEPQVHSIVSKMMINEELHASWDQPTRCIVFHEVQHSRLQSLAFQLTEKLSILAESNERAMESRTGGGGLDLSSRRRDNNQDYAGAASGGGGYWQDKANYGQGRQGNRSGYGGGRSSGQNGQWSGQNRGGGYAGRVGSGNRGMQMDGSSRMVSLNRGVRT

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
7	Phosphorylation	-MTSRFFTQVGSESE -CCCCCCCCCCCCCC	21.45	23776212
11	Phosphorylation	RFFTQVGSESEDESD CCCCCCCCCCCCCCC	38.81	23776212
13	Phosphorylation	FTQVGSESEDESDYE CCCCCCCCCCCCCCE	52.63	23776212
17	Phosphorylation	GSESEDESDYEVEVN CCCCCCCCCCEEEEE	58.79	23776212
19	Phosphorylation	ESEDESDYEVEVNEV CCCCCCCCEEEEEEC	31.02	23776212
35	Phosphorylation	NDDVNNRYLQSGSED CCCCCCCCCCCCCCC	15.94	19880383
38	Phosphorylation	VNNRYLQSGSEDDDD CCCCCCCCCCCCCCC	41.51	30291188
40	Phosphorylation	NRYLQSGSEDDDDTD CCCCCCCCCCCCCCC	43.00	30291188
46	Phosphorylation	GSEDDDDTDTKRVVK CCCCCCCCCCCCCCC	53.19	23776212
48	Phosphorylation	EDDDDTDTKRVVKPA CCCCCCCCCCCCCCC	23.89	23776212
193	Phosphorylation	EVEDDDDSSIDGPTV CCCCCCCCCCCCCCC	35.87	27531888
194	Phosphorylation	VEDDDDSSIDGPTVD CCCCCCCCCCCCCCC	31.52	27531888
204	Phosphorylation	GPTVDPGSDVDEPTD CCCCCCCCCCCCCCC	39.59	19376835
701	Phosphorylation	RLLKNRDSILDMVKD HHHCCCHHHHHHHHH	23.09	19880383
805	Phosphorylation	ERAMESRTGGGGLDL HHHHHHCCCCCCCCC	49.83	19880383
813	Phosphorylation	GGGGLDLSSRRRDNN CCCCCCCHHCCCCCC	22.82	19880383
814	Phosphorylation	GGGLDLSSRRRDNNQ CCCCCCHHCCCCCCC	36.78	19880383
893	Phosphorylation	DGSSRMVSLNRGVRT CCCCCCEECCCCCCC	15.58	19376835

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
-	K	Ubiquitination	E3 ubiquitin ligase	TaMAB2	-	PMID:31824527

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EIF3C_ARATH !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of EIF3C_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EIF3H_ARATH	TIF3H1	physical	15548739
CSN8_ARATH	COP9	physical	9849901
CSN1_ARATH	FUS6	physical	9849901
EIF3B_ARATH	TIF3B1	physical	11029466

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks.";
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.;
Plant Physiol. 150:889-903(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38; SER-40; SER-204 ANDSER-893, AND MASS SPECTROMETRY.
PubMed: 19376835

"Site-specific phosphorylation profiling of Arabidopsis proteins bymass spectrometry and peptide chip analysis.";
de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C.,Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,Hirt H.;
J. Proteome Res. 7:2458-2470(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38 AND SER-40, AND MASSSPECTROMETRY.
PubMed: 18433157