EIF3B_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EIF3B_SCHPO
• UniProt AC: Q10425
• Protein Name: Eukaryotic translation initiation factor 3 subunit B {ECO:0000255|HAMAP-Rule:MF_03001}
• Gene Name: SPAC25G10.08
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 725
• 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: MSEILIEEIKDQIVVKDEEIDVSELEVKLNVTKPVGYDTVVVIEGAPVVEEAKQQDFFRFLSSKVLAKIGKVKENGFYMPFEEKNGKKMSLGLVFADFENVDGADLCVQELDGKQILKNHTFVVRKLNQLEKAFSTPDEFSFEEREFKEREHLRSWLTDYYGRDQFISYYGNRVSVNWNRKSDVPEQIVDRENWTETYVQWSPMGTYLVSLHLRGIQLWGGESWGMCARFLHPYVKFVDFSPNEKYLVSWSYEPVRLPPIGHPARETMPFTDDDEGKHCFVWDIASGRILRSFKIPPQPEGSKDGKKVIWPIFKWSADDKYLARVTVGQSISVYETPSLALVDKKTIKIDGVQNFEWCPVSDALGRDSKEQLLAYWTPEITNQPARVALISIPSKSTIRTKNLFNVSDCKLYWQSNGDYLCVKVDRHTKTKKSTFSNLEIFRIREKNIPVEVVDLKDVVLNFAWEPKSDRFAIISANDQVLNSTNVKTNLSFYGFEQKKNTPSTFRHIITFDKKTCNSLFMAPKGRFMVAATLGSSTQYDLEFYDLDFDTEKKEPDALANVQQIGSAEHFGMTELEWDPSGRYVTTSSTIWRHKLENGYRLCDFRGTLLREEMIGEFKQFIWRPRPPSPLTKEDMKKIRKKLKDYNRLFDEEDIAEQSSANRELAARRRQLISEWQKYRDEVIARVAEERAITGQPAITVPAEEEEIIQETVEEVISEEIEPVED

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
23	Phosphorylation	KDEEIDVSELEVKLN CCCEECHHEEEEEEE	32.49	28889911
135	Phosphorylation	NQLEKAFSTPDEFSF HHHHHHHCCCCCCCC	43.84	28889911
136	Phosphorylation	QLEKAFSTPDEFSFE HHHHHHCCCCCCCCH	28.45	28889911
141	Phosphorylation	FSTPDEFSFEEREFK HCCCCCCCCHHHHHH	29.69	28889911
433	Phosphorylation	RHTKTKKSTFSNLEI CCCCCCCCCCCCEEE	35.92	25720772
434	Phosphorylation	HTKTKKSTFSNLEIF CCCCCCCCCCCEEEE	39.71	25720772
488	Phosphorylation	LNSTNVKTNLSFYGF CCCCCCCCCEEEEEC	36.79	25720772
628	Phosphorylation	IWRPRPPSPLTKEDM HCCCCCCCCCCHHHH	34.91	29996109

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

Oops, there are no upstream regulatory protein records of EIF3B_SCHPO !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EIF3B_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 EIF3B_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
YE38_SCHPO	pdc1	genetic	22681890
BDC1_SCHPO	bdc1	genetic	22681890
PROB_SCHPO	SPAC17H9.13c	genetic	22681890
AATC_SCHPO	SPAC10F6.13c	genetic	22681890
CLR2_SCHPO	clr2	genetic	22681890
SWD1_SCHPO	swd1	genetic	22681890
SGF73_SCHPO	sgf73	genetic	22681890
CYB51_SCHPO	SPBC29A10.16c	genetic	22681890
SGF29_SCHPO	sgf29	genetic	22681890
MDV1_SCHPO	caf4	physical	23695164
MDV1_SCHPO	caf4	physical	26771498
GLRX4_SCHPO	grx4	physical	26771498
TAS3_SCHPO	tas3	physical	26771498

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-23; SER-135 AND THR-136,AND MASS SPECTROMETRY.
PubMed: 18257517