EI2BA_HUMAN - dbPTM
EI2BA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EI2BA_HUMAN
UniProt AC Q14232
Protein Name Translation initiation factor eIF-2B subunit alpha
Gene Name EIF2B1
Organism Homo sapiens (Human).
Sequence Length 305
Subcellular Localization
Protein Description Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP..
Protein Sequence MDDKELIEYFKSQMKEDPDMASAVAAIRTLLEFLKRDKGETIQGLRANLTSAIETLCGVDSSVAVSSGGELFLRFISLASLEYSDYSKCKKIMIERGELFLRRISLSRNKIADLCHTFIKDGATILTHAYSRVVLRVLEAAVAAKKRFSVYVTESQPDLSGKKMAKALCHLNVPVTVVLDAAVGYIMEKADLVIVGAEGVVENGGIINKIGTNQMAVCAKAQNKPFYVVAESFKFVRLFPLNQQDVPDKFKYKADTLKVAQTGQDLKEEHPWVDYTAPSLITLLFTDLGVLTPSAVSDELIKLYL
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
11UbiquitinationKELIEYFKSQMKEDP
HHHHHHHHHHHCCCC
38.5922817900
15UbiquitinationEYFKSQMKEDPDMAS
HHHHHHHCCCCCHHH
51.8621890473
15AcetylationEYFKSQMKEDPDMAS
HHHHHHHCCCCCHHH
51.8625953088
15UbiquitinationEYFKSQMKEDPDMAS
HHHHHHHCCCCCHHH
51.8621906983
20SulfoxidationQMKEDPDMASAVAAI
HHCCCCCHHHHHHHH
3.7421406390
29PhosphorylationSAVAAIRTLLEFLKR
HHHHHHHHHHHHHHH
29.5821406692
352-HydroxyisobutyrylationRTLLEFLKRDKGETI
HHHHHHHHHCCCCCH
64.96-
35UbiquitinationRTLLEFLKRDKGETI
HHHHHHHHHCCCCCH
64.9622817900
35AcetylationRTLLEFLKRDKGETI
HHHHHHHHHCCCCCH
64.9619608861
35UbiquitinationRTLLEFLKRDKGETI
HHHHHHHHHCCCCCH
64.9621890473
38UbiquitinationLEFLKRDKGETIQGL
HHHHHHCCCCCHHHH
63.7833845483
382-HydroxyisobutyrylationLEFLKRDKGETIQGL
HHHHHHCCCCCHHHH
63.78-
38UbiquitinationLEFLKRDKGETIQGL
HHHHHHCCCCCHHHH
63.78-
50PhosphorylationQGLRANLTSAIETLC
HHHHHHHHHHHHHHH
18.8722210691
51PhosphorylationGLRANLTSAIETLCG
HHHHHHHHHHHHHHC
30.3422210691
77PhosphorylationELFLRFISLASLEYS
HHHHHHHHHHHCCCC
18.3829083192
80PhosphorylationLRFISLASLEYSDYS
HHHHHHHHCCCCCHH
27.3329083192
83PhosphorylationISLASLEYSDYSKCK
HHHHHCCCCCHHHHC
16.4929083192
84PhosphorylationSLASLEYSDYSKCKK
HHHHCCCCCHHHHCE
22.2429083192
86PhosphorylationASLEYSDYSKCKKIM
HHCCCCCHHHHCEEE
12.2321712546
87PhosphorylationSLEYSDYSKCKKIMI
HCCCCCHHHHCEEEE
36.2521712546
105O-linked_GlycosylationELFLRRISLSRNKIA
HHHHHHHHCCCCHHH
20.6230379171
105PhosphorylationELFLRRISLSRNKIA
HHHHHHHHCCCCHHH
20.6220068231
107PhosphorylationFLRRISLSRNKIADL
HHHHHHCCCCHHHHH
27.3224702127
120AcetylationDLCHTFIKDGATILT
HHHHHHHHCCHHHHH
46.0126051181
130PhosphorylationATILTHAYSRVVLRV
HHHHHHHHHHHHHHH
6.8720393185
145AcetylationLEAAVAAKKRFSVYV
HHHHHHHHHCEEEEE
34.4425953088
145UbiquitinationLEAAVAAKKRFSVYV
HHHHHHHHHCEEEEE
34.4433845483
145MethylationLEAAVAAKKRFSVYV
HHHHHHHHHCEEEEE
34.44-
149PhosphorylationVAAKKRFSVYVTESQ
HHHHHCEEEEEECCC
19.3027251275
160PhosphorylationTESQPDLSGKKMAKA
ECCCCCCCCHHHHHH
56.8225332170
162UbiquitinationSQPDLSGKKMAKALC
CCCCCCCHHHHHHHH
35.68-
163AcetylationQPDLSGKKMAKALCH
CCCCCCHHHHHHHHC
47.8424848925
215SulfoxidationNKIGTNQMAVCAKAQ
CEECCCCHHHHHHCC
3.0721406390
253UbiquitinationVPDKFKYKADTLKVA
CCCHHHHHHHHHHCC
40.1429967540
258UbiquitinationKYKADTLKVAQTGQD
HHHHHHHHCCCCCCC
37.3032015554
2582-HydroxyisobutyrylationKYKADTLKVAQTGQD
HHHHHHHHCCCCCCC
37.30-

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 EI2BA_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EI2BA_HUMAN !!

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 EI2BA_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EI2BG_HUMANEIF2B3physical
17353931
PDIA4_HUMANPDIA4physical
17353931
EI2BE_HUMANEIF2B5physical
17353931
DCD_HUMANDCDphysical
17353931
HNRPL_HUMANHNRNPLphysical
17353931
EI2BE_HUMANEIF2B5physical
10858531
EI2BD_YEASTGCD2physical
21795329
EI2BB_HUMANEIF2B2physical
21795329
EI2BE_YEASTGCD6physical
21795329
EI2BA_HUMANEIF2B1physical
25416956
GORS2_HUMANGORASP2physical
25416956
NTAQ1_HUMANWDYHV1physical
25416956
RD3_HUMANRD3physical
25416956
EI2BE_HUMANEIF2B5physical
26344197
THTM_HUMANMPSTphysical
26344197
SPB13_HUMANSERPINB13physical
26344197
EI2BD_HUMANEIF2B4physical
28514442
EI2BG_HUMANEIF2B3physical
28514442
EI2BE_HUMANEIF2B5physical
28514442
BZW2_HUMANBZW2physical
27173435
MCU_HUMANMCUphysical
27173435

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
603896Leukodystrophy with vanishing white matter (VWM)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EI2BA_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-35, AND MASS SPECTROMETRY.

TOP