EIF3C_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EIF3C_SCHPO
• UniProt AC: O14164
• Protein Name: Eukaryotic translation initiation factor 3 subunit C {ECO:0000255|HAMAP-Rule:MF_03002}
• Gene Name: nip1
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 918
• 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: MSRFFKGGSSDSDAESVDSSEENRLTSSRLKKQDDSSSEEESSEEESASSSESESSEEESESEESEVEVPKKKAVAASEDSESDSESSEEEEETESEEDSEVSDESESESESESESEEESESEEESDESERSGPSSFLKKPEKEEAKPAGLKFLRGESSEESSDEEEGRRVVKSAKDKRYEEFISCMETIKNAMSSNNWIVVSNEFDHLNKVSQKCKEAGRNPPPYIEFLSALDQKLESADKAFIKSLDAANGRAFNALKQRVRKNNRQFQSDIDRYRKDPEGFMKPAELNEIPKPAGKAGQDEVIVDGVATRGIVAPTEGLGKPEEITPADIFKYLRAIFEARGKKSTDRSEQIRLLEKLSTIAVTDYQRLRVKVALLAVRFDINTGSGQYMPIDQWNAALTELHSILDIFDANPKIVIVEQVEDENEEEEEAIAAAENNNGVIQVQGSVVSFLERLDDEFTRSLQMIDPHTPEYIDRLKDETSLYTLLVRSQGYLERIGVVENTARLIMRRLDRVYYKPEQVIRANEEVAWRSFPPTFDLTITPRATTTTPDILIHSLCVYLYNNGVSLLRTRAMLCHIYHEALQNRFYKARDMLLMSHLQDSVHAADIATQILHNRTMVQIGLCAFRNGMVQETQYALQDISTTGRVKELLGQGIQAPKFGQFTPDQDRLDKQLVLPFHMHINLELLECVYLTCSMLMEIPAMAAASSTASDSRKRVISRPFRRMLEYIDRQLFVGPPENTREYIMQASKALADGEWRRCEEFIHAIKIWSLMPDADKIKQMLSEKIREEGLRTYLLAYAAFYDSVSLEFLATTFDLPVQRVTVIVSRLLSKREIHAALDQVHGAIIFERVEINKLESLTVSLSEKTAQLNEANEKLYEQKTQHTNPQENRRRDKGGSVKRRNERTENRNRSDMN

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
9	Phosphorylation	SRFFKGGSSDSDAES CCCCCCCCCCCCCCC	39.37	29996109
10	Phosphorylation	RFFKGGSSDSDAESV CCCCCCCCCCCCCCC	44.39	28889911
12	Phosphorylation	FKGGSSDSDAESVDS CCCCCCCCCCCCCCC	40.44	28889911
16	Phosphorylation	SSDSDAESVDSSEEN CCCCCCCCCCCHHHH	32.70	28889911
19	Phosphorylation	SDAESVDSSEENRLT CCCCCCCCHHHHHHH	37.18	28889911
20	Phosphorylation	DAESVDSSEENRLTS CCCCCCCHHHHHHHH	44.45	28889911
26	Phosphorylation	SSEENRLTSSRLKKQ CHHHHHHHHHHHHCC	22.78	25720772
132	Phosphorylation	ESDESERSGPSSFLK CCCHHHHCCCHHHCC	51.51	28889911
158	Phosphorylation	LKFLRGESSEESSDE CHHHCCCCCCCCCCH	45.96	24763107
159	Phosphorylation	KFLRGESSEESSDEE HHHCCCCCCCCCCHH	40.87	24763107
162	Phosphorylation	RGESSEESSDEEEGR CCCCCCCCCCHHHHH	38.75	24763107
163	Phosphorylation	GESSEESSDEEEGRR CCCCCCCCCHHHHHH	52.93	24763107
667	Phosphorylation	APKFGQFTPDQDRLD CCCCCCCCCCHHHCC	20.33	28889911

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

Oops, there are no upstream regulatory protein records of EIF3C_SCHPO !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EIF3C_SCHPO !!

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_SCHPO !!

Protein-Protein Interaction

Oops, there are no PPI records of EIF3C_SCHPO !!

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 fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-12; SER-16;SER-19; SER-20 AND THR-667, AND MASS SPECTROMETRY.
PubMed: 18257517