IF2B_SCHPO - dbPTM
IF2B_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IF2B_SCHPO
UniProt AC P56329
Protein Name Probable eukaryotic translation initiation factor 2 subunit beta
Gene Name tif212
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 321
Subcellular Localization
Protein Description eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S preinitiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B (By similarity)..
Protein Sequence MTETEAVVDQIDLNGALPEKKKKPKKSVAFDDEVDAVSKDGPEASSAGATDEDDSERKSSAKDLTTPVTEGEVDELKDMFSSMKKKKKSKKSSASAEEQTEDITTESGELDFSSMKKKKKKKKSADLSAFEKELEASSTGDATSDLSKQTFDSENMGEHAWLKSDRDYYYPELLNRFFTLLRTNNPELAGEKRKYTIVPPSVHREGKKTIFANISDISKRMHRSLDHVIQFLFAELGTSGSVDGSSRLIIKGRFQQKQIENVLRRYIVEYVTCKTCKSPDTILTKENRIFFMTCEACGSVRSVQAIKTGYQAQIGKRKHVS
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
2Phosphorylation------MTETEAVVD
------CCCCHHHHC
52.1729996109
27PhosphorylationKKKKPKKSVAFDDEV
CCCCCCCCCCCCCCC
25.4625720772
38PhosphorylationDDEVDAVSKDGPEAS
CCCCCHHHCCCCCHH
27.1024763107
45PhosphorylationSKDGPEASSAGATDE
HCCCCCHHHCCCCCC
21.0428889911
46PhosphorylationKDGPEASSAGATDED
CCCCCHHHCCCCCCC
37.4628889911
50PhosphorylationEASSAGATDEDDSER
CHHHCCCCCCCCCCC
38.7228889911
55PhosphorylationGATDEDDSERKSSAK
CCCCCCCCCCHHHCC
52.1825720772
60PhosphorylationDDSERKSSAKDLTTP
CCCCCHHHCCCCCCC
42.2325720772
66PhosphorylationSSAKDLTTPVTEGEV
HHCCCCCCCCCCHHH
24.0624763107
124PhosphorylationKKKKKKKSADLSAFE
CCCCCCCCCCHHHHH
35.5828889911
128PhosphorylationKKKSADLSAFEKELE
CCCCCCHHHHHHHHH
31.3128889911
137PhosphorylationFEKELEASSTGDATS
HHHHHHHCCCCCCCC
21.0328889911
138PhosphorylationEKELEASSTGDATSD
HHHHHHCCCCCCCCH
43.3828889911
139PhosphorylationKELEASSTGDATSDL
HHHHHCCCCCCCCHH
36.2628889911
143PhosphorylationASSTGDATSDLSKQT
HCCCCCCCCHHHHHC
27.7527738172
144PhosphorylationSSTGDATSDLSKQTF
CCCCCCCCHHHHHCC
37.9727738172
164PhosphorylationGEHAWLKSDRDYYYP
CCCEEECCCCCCCHH
35.3925720772

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 IF2B_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IF2B_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 IF2B_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of IF2B_SCHPO !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IF2B_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-45; SER-137; SER-138 ANDTHR-139, AND MASS SPECTROMETRY.

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