EI2BE_RAT - dbPTM
EI2BE_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EI2BE_RAT
UniProt AC Q64350
Protein Name Translation initiation factor eIF-2B subunit epsilon
Gene Name Eif2b5
Organism Rattus norvegicus (Rat).
Sequence Length 716
Subcellular Localization
Protein Description Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP..
Protein Sequence MAATAAVPSAVGGRANKRGGGSGGGGTQGAEEEPPPPLQAVLVADSFDRRFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLQKSKWCHPTSLNVVRIITSDLYRSLGDVLRDVDAKALVRSDFLLIYGDVVSNINISKALEEHRLRRKLEKNVSVMTMVFKESSPSHPTRCHEDNVVLAVDSTTNRILHFQKTQGLRHFSFPLGLFQGSLDGVEIRYDLLDCHISICSPQVAQLFTDNFDYQTRDDFVRGLLVNEEILGNQIHLHVTSREYGARVSNLHMYSAVCADVIRRWVYPLTPEVNFTDSSTQSYTHSRHNIYRGPEVSLGHGSVLEENVLLGAGTVVGSNCSITNSVIGPNCHIGDNVVLDQAYLWQGVRVAAGAQIHQSLLCDRAEVKERVILKPHCVLTSQVVVGPDIILPEGSVISLHPPDAEEDEDDGQFSDDSGADQEKEKVKLKGYNPAEVGPEGQGYLWKAEDVDEKEDEELRQSLWGLMINMEEESETESERSVDPEELDSRAGSPQLDDIRVFQNEVLGTLQRGREENISCDNLVLEINSLKYAYNISLKEVMQVLSHVVLEFPLQQVDGVLDPNRYCALLLPLLKAWSPVFRNYIKRAADHLEALAAIEDFFLEHETLVPSLAKVLMAFYQLEILAEETILSWFSQRDITDKGQQLRKNQQLQRFIQWLREAEEESSDDD
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
18MethylationVGGRANKRGGGSGGG
HCCCCCCCCCCCCCC
49.12-
22PhosphorylationANKRGGGSGGGGTQG
CCCCCCCCCCCCCCC
37.2223707720
27PhosphorylationGGSGGGGTQGAEEEP
CCCCCCCCCCCCCCC
27.4025575281
56UbiquitinationRRFFPISKDQPRVLL
CCCCCCCCCCCCEEH
62.1923707720
98UbiquitinationCWKAAQIKEHLQKSK
HHHHHHHHHHHHHCC
27.3123707720
125PhosphorylationITSDLYRSLGDVLRD
HHHHHHHHHHHHHHH
24.1323707720
136UbiquitinationVLRDVDAKALVRSDF
HHHHCCHHHHHCCCE
37.4823707720
212UbiquitinationNRILHFQKTQGLRHF
CCEEEEECCCCCCCE
41.7023707720
317PhosphorylationRRWVYPLTPEVNFTD
HHHHCCCCCCCCCCC
16.9523707720
445PhosphorylationLPEGSVISLHPPDAE
CCCCCEEEECCCCCC
20.61-
461PhosphorylationDEDDGQFSDDSGADQ
CCCCCCCCCCCCCCH
32.4011500362
464PhosphorylationDGQFSDDSGADQEKE
CCCCCCCCCCCHHHH
40.6511500362
500UbiquitinationKAEDVDEKEDEELRQ
ECCCCCHHHCHHHHH
67.0323707720
527PhosphorylationSETESERSVDPEELD
CCCCCCCCCCHHHHH
27.1622673903
535PhosphorylationVDPEELDSRAGSPQL
CCHHHHHHCCCCCCC
36.3311500362
539PhosphorylationELDSRAGSPQLDDIR
HHHHCCCCCCCCHHH
14.4211311121
712PhosphorylationLREAEEESSDDD---
HHHHHHHCCCCC---
42.2011500362
713PhosphorylationREAEEESSDDD----
HHHHHHCCCCC----
48.6211500362

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
464SPhosphorylationKinaseCSNK1A1P48729
GPS
535SPhosphorylationKinaseGSK3AP18265
PSP
535SPhosphorylationKinaseGSK3BP49841
PSP
535SPhosphorylationKinaseGSK3BP18266
PSP
535SPhosphorylationKinaseGSK-FAMILY-GPS
535SPhosphorylationKinaseGSK-3_GROUP-PhosphoELM
539SPhosphorylationKinaseDYRK1AQ13627
PSP
539SPhosphorylationKinaseDYRK2Q92630
PSP
539SPhosphorylationKinaseMAPK1P28482
GPS
539SPhosphorylationKinaseDYRK2-Uniprot
712SPhosphorylationKinaseCSNK2A1P19139
GPS
712SPhosphorylationKinaseCK2-FAMILY-GPS
712SPhosphorylationKinaseCK2_GROUP-PhosphoELM
713SPhosphorylationKinaseCSNK2A1P19139
GPS
713SPhosphorylationKinaseCK2-FAMILY-GPS
713SPhosphorylationKinaseCK2_GROUP-PhosphoELM

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
539SPhosphorylation

11311121

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 EI2BE_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBC_HUMANUBCphysical
23707720
NEDD4_MOUSENedd4physical
23707720

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EI2BE_RAT

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS.";
Moser K., White F.M.;
J. Proteome Res. 5:98-104(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-539, AND MASSSPECTROMETRY.

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