EI2BB_SCHPO - dbPTM
EI2BB_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EI2BB_SCHPO
UniProt AC Q9UT76
Protein Name Probable translation initiation factor eIF-2B subunit beta
Gene Name tif222
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 393
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP..
Protein Sequence MSTINVEHTYPAVSSLIADLKSRKVQGPFAVAVETALVMRQVISQTRWSTVDQLIDTVRAVGSTLVKAQPTEFSCGNIIRRILRLIREEYQELLKTADENEKLIVSSSNSSSPSQKRDIPSNEKLVQSHEPVSVQMYSSMLNLLGRPTLESPTHSKTVGDSRVTGGMDMRAVIISGIQDVIDELDKINTDIEVQSMDHLHSNEIILTQGCSKTVEAFLRFAAKKRKFSVIVAEGFPNNQKGSHAMAKRLAQAGIDTTVISDATIFAIMSRVNKVILGTHAILGNGGLVTYSGAQLVAQAARHHATPVVVCSGIYKLSPVYPYDLESIIQLSSPDKIMSFNEGDLISRAEILNPYYDYIPPDLVDLFITNLGGYPPSYLYRIMNDTYDASDTIL
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 Orthologous
Protein Cluster
106PhosphorylationENEKLIVSSSNSSSP
CCCCEEEECCCCCCH
22.5128889911
107PhosphorylationNEKLIVSSSNSSSPS
CCCEEEECCCCCCHH
23.7319547744
108PhosphorylationEKLIVSSSNSSSPSQ
CCEEEECCCCCCHHH
32.9728889911
110PhosphorylationLIVSSSNSSSPSQKR
EEEECCCCCCHHHCC
33.8529996109
111PhosphorylationIVSSSNSSSPSQKRD
EEECCCCCCHHHCCC
50.9819547744
112PhosphorylationVSSSNSSSPSQKRDI
EECCCCCCHHHCCCC
28.5228889911
114PhosphorylationSSNSSSPSQKRDIPS
CCCCCCHHHCCCCCC
50.7325720772
137PhosphorylationEPVSVQMYSSMLNLL
CCCHHHHHHHHHHHH
4.7821712547
148PhosphorylationLNLLGRPTLESPTHS
HHHHCCCCCCCCCCC
41.6229996109
151PhosphorylationLGRPTLESPTHSKTV
HCCCCCCCCCCCCCC
37.9121712547
153PhosphorylationRPTLESPTHSKTVGD
CCCCCCCCCCCCCCC
48.3229996109
155PhosphorylationTLESPTHSKTVGDSR
CCCCCCCCCCCCCCC
32.2829996109
331PhosphorylationLESIIQLSSPDKIMS
HHHHHHCCCCCCCCC
24.3729996109
332PhosphorylationESIIQLSSPDKIMSF
HHHHHCCCCCCCCCC
45.7924763107

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 EI2BB_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EI2BB_SCHPO !!

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 EI2BB_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MOC3_SCHPOmoc3physical
26771498
CBH1_SCHPOcbh1physical
26771498
YH7G_SCHPOSPBC16G5.16physical
26771498
MEU23_SCHPOmeu23physical
26771498

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EI2BB_SCHPO

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-106; SER-108 ANDSER-112, AND MASS SPECTROMETRY.

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