IF2B_DROME - dbPTM
IF2B_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IF2B_DROME
UniProt AC P41375
Protein Name Eukaryotic translation initiation factor 2 subunit 2
Gene Name eIF2beta {ECO:0000312|FlyBase:FBgn0004926}
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 312
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 preinitiation complex mediates ribosomal recognition of a start codon during the scanning process of the leader region..
Protein Sequence MDAEDGFDPTLLKKKKKKKTTFDLDAALGLEDDTKKEDPQDEASAEGGAAAEEDNLDLESFGKKKKKKKKPFNMDEIEAAIPSFGGDDVAASEEPEEEEINLDMDFSMAKKKKKSKKKELDELFADQADDDKSEDKENDEDNSSTWFGSDRDYTYDELLKRVFEIILDKNPDMAAGRKPKFVMRPPQVLRVGTKKTSFANFMDIAKTLHRLPKHLLDFLLAELGTSGSMDGNQQLIIKGRFQPKQIENVLRRYIKEYVTCHTCRSPETILQKDTRLFFLQCESCGSRCSVASIKSGFQAVTGKRAAIRAKTT
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
44PhosphorylationEDPQDEASAEGGAAA
CCCCHHHHHCCCHHH
25.4619429919
133PhosphorylationDQADDDKSEDKENDE
HHCCCCCCCCCCCCC
59.0121082442
143PhosphorylationKENDEDNSSTWFGSD
CCCCCCCCCCCCCCC
41.2819429919
144PhosphorylationENDEDNSSTWFGSDR
CCCCCCCCCCCCCCC
35.5919429919
145PhosphorylationNDEDNSSTWFGSDRD
CCCCCCCCCCCCCCC
25.3219429919
244AcetylationIKGRFQPKQIENVLR
EEECCCHHHHHHHHH
53.8021791702
265PhosphorylationVTCHTCRSPETILQK
HCCCCCCCHHHHHCC
29.2719429919
268PhosphorylationHTCRSPETILQKDTR
CCCCCHHHHHCCCCE
30.3019429919
286PhosphorylationLQCESCGSRCSVASI
EEECCCCCCEEHHHH
34.1521082442
289PhosphorylationESCGSRCSVASIKSG
CCCCCCEEHHHHHHC
21.4322817900

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_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IF2B_DROME !!

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_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NFS1_DROMECG12264physical
22036573

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IF2B_DROME

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133 AND THR-145, ANDMASS SPECTROMETRY.
"An integrated chemical, mass spectrometric and computational strategyfor (quantitative) phosphoproteomics: application to Drosophilamelanogaster Kc167 cells.";
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
Mol. Biosyst. 3:275-286(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44, AND MASSSPECTROMETRY.

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