EIF3A_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EIF3A_SCHPO
• UniProt AC: O74760
• Protein Name: Eukaryotic translation initiation factor 3 subunit A {ECO:0000255|HAMAP-Rule:MF_03000}
• Gene Name: tif32
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 932
• 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: MAPPQGKPENVLRLADELIALDQHSSALQSLHETIVLKRSRNAQGFSLEPIMMRFIELCVHLRKGKIAKEGLYTYKNAVQNTSVTAIENVVKHFIELANKRVQEAQEKADKISVEYVDDLEATETPESIMMSLVSGDLSKSRTDRALVTPWLKFLWDAYRTVLDILRNNARLEVMYQLIANSAFQFCLKYQRKTEFRRLCELLRSHLGNASKFSNAPHSINLNDAETMQRHLDMRFSQLNVAVELELWQEAFRSIEDIHSLLTFSKRAPAAVMLGNYYRKLIKIFLVCDNYLLHAAAWNRYFTFTNVQKPATANFVILSALSIPIIDANKLSGPSIEAEDAKSKNARLALLLNLSKTPTRETLIKDAISRGVLSFCDQAIRDLYQILEVEFHPLSICKKLQPIIKRLAESNDTAQYIRPLQQVILTRLFQQLSQVYDSISLKYVMDLATFEEPYDFNPGQIEKFIMNGNKKGAFSIRLNHIENSISFSSDLFSNPIKSSDSVSLQSTPSELITSQLTRIAKSLSSVLMRFDTDFCLLRKQQAEAAYERAQAGVEQERKAVIAQRSLLELRRGQADTLATQREAELAAQRALKQKQESEAESLRVQEEINKRNAERIRREKEAIRINEAKKLAEELKAKGGLEVNAEDLEHLDADKLRAMQIEQVEKQNKSMNERLRVIGKRIDHLERAYRREAIPLWEEDAKQQAEHDREIFYEREKQRKEVQERKHEQAIKDKKAFAQFASYIHAYKQNIDDERDKAYQEAYAKAKNVIDAERERQRKEIFEQKLAEAIREAEEEAARAAEEEANRELHEQEEAQKRAIEERTRAAREAKEREQREMAEKLERQRRIQQERDEEISRKLAEKAAARRANIGASSPSPGAWRRGGASAGGVSRDSPRYSRGGYSRGSVPPRETLAPSKGAYVPPSRRNQQQQ

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
40	Phosphorylation	ETIVLKRSRNAQGFS HHHHHHCCCCCCCCC	28.44	25720772
374	Phosphorylation	AISRGVLSFCDQAIR HHHHHHHHHHHHHHH	22.79	28889911
498	Phosphorylation	LFSNPIKSSDSVSLQ CCCCCCCCCCCCCCC	39.85	25720772
499	Phosphorylation	FSNPIKSSDSVSLQS CCCCCCCCCCCCCCC	28.98	25720772
501	Phosphorylation	NPIKSSDSVSLQSTP CCCCCCCCCCCCCCH	18.63	28889911
503	Phosphorylation	IKSSDSVSLQSTPSE CCCCCCCCCCCCHHH	25.33	28889911
874	Phosphorylation	RRANIGASSPSPGAW HHCCCCCCCCCCCCC	37.25	28889911
875	Phosphorylation	RANIGASSPSPGAWR HCCCCCCCCCCCCCC	28.94	28889911
877	Phosphorylation	NIGASSPSPGAWRRG CCCCCCCCCCCCCCC	37.60	28889911
887	Phosphorylation	AWRRGGASAGGVSRD CCCCCCCCCCCCCCC	30.62	25720772
899	Phosphorylation	SRDSPRYSRGGYSRG CCCCCCCCCCCCCCC	26.23	29996109
904	Phosphorylation	RYSRGGYSRGSVPPR CCCCCCCCCCCCCCC	33.18	29996109
907	Phosphorylation	RGGYSRGSVPPRETL CCCCCCCCCCCCCCC	30.27	29996109

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

Oops, there are no upstream regulatory protein records of EIF3A_SCHPO !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EIF3A_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 EIF3A_SCHPO !!

Protein-Protein Interaction

Oops, there are no PPI records of EIF3A_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-374; SER-501; SER-874;SER-875 AND SER-877, AND MASS SPECTROMETRY.
PubMed: 18257517