EI2BD_HUMAN - dbPTM
EI2BD_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EI2BD_HUMAN
UniProt AC Q9UI10
Protein Name Translation initiation factor eIF-2B subunit delta
Gene Name EIF2B4
Organism Homo sapiens (Human).
Sequence Length 523
Subcellular Localization
Protein Description Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP..
Protein Sequence MAAVAVAVREDSGSGMKAELPPGPGAVGREMTKEEKLQLRKEKKQQKKKRKEEKGAEPETGSAVSAAQCQVGPTRELPESGIQLGTPREKVPAGRSKAELRAERRAKQEAERALKQARKGEQGGPPPKASPSTAGETPSGVKRLPEYPQVDDLLLRRLVKKPERQQVPTRKDYGSKVSLFSHLPQYSRQNSLTQFMSIPSSVIHPAMVRLGLQYSQGLVSGSNARCIALLRALQQVIQDYTTPPNEELSRDLVNKLKPYMSFLTQCRPLSASMHNAIKFLNKEITSVGSSKREEEAKSELRAAIDRYVQEKIVLAAQAISRFAYQKISNGDVILVYGCSSLVSRILQEAWTEGRRFRVVVVDSRPWLEGRHTLRSLVHAGVPASYLLIPAASYVLPEVSKVLLGAHALLANGSVMSRVGTAQLALVARAHNVPVLVCCETYKFCERVQTDAFVSNELDDPDDLQCKRGEHVALANWQNHASLRLLNLVYDVTPPELVDLVITELGMIPCSSVPVVLRVKSSDQ
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
2Acetylation------MAAVAVAVR
------CCEEEEEEE		15.6222814378
10 (in isoform 2)Phosphorylation-50.3529116813
11 (in isoform 2)Phosphorylation-47.9729116813
12PhosphorylationAVAVREDSGSGMKAE
EEEEECCCCCCCCCC		30.0625159151
14PhosphorylationAVREDSGSGMKAELP
EEECCCCCCCCCCCC		39.4023186163
19 (in isoform 2)Phosphorylation-57.1822777824
21 (in isoform 2)Phosphorylation-24.2526657352
23 (in isoform 2)Phosphorylation-31.1926434776
36MalonylationREMTKEEKLQLRKEK
CCCCHHHHHHHHHHH		42.5026320211
65 (in isoform 3)Phosphorylation-20.01-
73 (in isoform 3)Phosphorylation-29.44-
74PhosphorylationAQCQVGPTRELPESG
HHCCCCCCCCCCCCC		30.74-
79 (in isoform 3)Phosphorylation-74.38-
80PhosphorylationPTRELPESGIQLGTP
CCCCCCCCCCCCCCC		38.9823927012
85 (in isoform 3)Phosphorylation-19.8025159151
86PhosphorylationESGIQLGTPREKVPA
CCCCCCCCCHHHCCC		27.9723401153
86 (in isoform 2)Phosphorylation-27.97-
94 (in isoform 2)Phosphorylation-28.46-
100 (in isoform 2)Phosphorylation-8.21-
106 (in isoform 2)Phosphorylation-24.8925159151
129 (in isoform 3)Phosphorylation-32.23-
130PhosphorylationGGPPPKASPSTAGET
CCCCCCCCCCCCCCC		26.0529255136
131 (in isoform 3)Phosphorylation-40.33-
132PhosphorylationPPPKASPSTAGETPS
CCCCCCCCCCCCCCC		28.5230266825
133PhosphorylationPPKASPSTAGETPSG
CCCCCCCCCCCCCCC		41.9130266825
136 (in isoform 3)Phosphorylation-55.89-
137PhosphorylationSPSTAGETPSGVKRL
CCCCCCCCCCCCCCC		23.1029255136
139PhosphorylationSTAGETPSGVKRLPE
CCCCCCCCCCCCCCC		64.7329255136
142UbiquitinationGETPSGVKRLPEYPQ
CCCCCCCCCCCCCCC		52.31-
142AcetylationGETPSGVKRLPEYPQ
CCCCCCCCCCCCCCC		52.3125953088
147PhosphorylationGVKRLPEYPQVDDLL
CCCCCCCCCCHHHHH		9.31-
147NitrationGVKRLPEYPQVDDLL
CCCCCCCCCCHHHHH		9.31-
150 (in isoform 2)Phosphorylation-5.5224719451
152 (in isoform 2)Phosphorylation-40.12-
153 (in isoform 2)Phosphorylation-4.1427251275
157 (in isoform 2)Phosphorylation-43.7524719451
169PhosphorylationPERQQVPTRKDYGSK
HHHCCCCCCCCCCCC		52.0430576142
175UbiquitinationPTRKDYGSKVSLFSH
CCCCCCCCCHHHHHC		24.5321890473
176 (in isoform 1)Ubiquitination-31.3221890473
176UbiquitinationTRKDYGSKVSLFSHL
CCCCCCCCHHHHHCC		31.3221890473
178PhosphorylationKDYGSKVSLFSHLPQ
CCCCCCHHHHHCCCC		27.6827080861
181PhosphorylationGSKVSLFSHLPQYSR
CCCHHHHHCCCCCCC		29.4327080861
186PhosphorylationLFSHLPQYSRQNSLT
HHHCCCCCCCCCCCH		12.1320873877
187PhosphorylationFSHLPQYSRQNSLTQ
HHCCCCCCCCCCCHH		23.3420873877
191PhosphorylationPQYSRQNSLTQFMSI
CCCCCCCCCHHHHCC		25.1828355574
193PhosphorylationYSRQNSLTQFMSIPS
CCCCCCCHHHHCCCH		21.4128450419
196 (in isoform 2)Ubiquitination-2.2621890473
197 (in isoform 2)Ubiquitination-32.4121890473
197PhosphorylationNSLTQFMSIPSSVIH
CCCHHHHCCCHHHHC		32.4127251275
206 (in isoform 2)Phosphorylation-8.5727251275
207 (in isoform 2)Phosphorylation-1.8127251275
211 (in isoform 2)Phosphorylation-10.5224719451
213 (in isoform 2)Phosphorylation-33.7527251275
214PhosphorylationMVRLGLQYSQGLVSG
HHHHCCEECCCCCCC		14.17-
215PhosphorylationVRLGLQYSQGLVSGS
HHHCCEECCCCCCCC		12.5728857561
281UbiquitinationHNAIKFLNKEITSVG
HHHHHHHCHHHHCCC		42.9421890473
282 (in isoform 1)Ubiquitination-53.2821890473
282UbiquitinationNAIKFLNKEITSVGS
HHHHHHCHHHHCCCC		53.2821890473
285PhosphorylationKFLNKEITSVGSSKR
HHHCHHHHCCCCCHH		20.6029514088
286PhosphorylationFLNKEITSVGSSKRE
HHCHHHHCCCCCHHH		30.0929514088
289PhosphorylationKEITSVGSSKREEEA
HHHHCCCCCHHHHHH		30.4529514088
290PhosphorylationEITSVGSSKREEEAK
HHHCCCCCHHHHHHH		29.7829514088
2912-HydroxyisobutyrylationITSVGSSKREEEAKS
HHCCCCCHHHHHHHH		66.58-
291UbiquitinationITSVGSSKREEEAKS
HHCCCCCHHHHHHHH		66.58-
297UbiquitinationSKREEEAKSELRAAI
CHHHHHHHHHHHHHH		47.98-
302 (in isoform 2)Ubiquitination-22.7621890473
303 (in isoform 2)Ubiquitination-9.5921890473
328PhosphorylationRFAYQKISNGDVILV
HHHHHHCCCCCEEEE		41.6221712546
339PhosphorylationVILVYGCSSLVSRIL
EEEEECCHHHHHHHH		23.5027251275
340PhosphorylationILVYGCSSLVSRILQ
EEEECCHHHHHHHHH		36.5521712546
360 (in isoform 2)Phosphorylation-3.4727251275
374MethylationLEGRHTLRSLVHAGV
CCCHHHHHHHHHCCC		29.15-
384PhosphorylationVHAGVPASYLLIPAA
HHCCCCHHHHHHCHH		15.3922817900
385PhosphorylationHAGVPASYLLIPAAS
HCCCCHHHHHHCHHH		13.9722817900
399PhosphorylationSYVLPEVSKVLLGAH
HHHCHHHHHHHHHHH		18.5122817900
442UbiquitinationLVCCETYKFCERVQT
EEECCHHHHHHHHCC		51.46-
466 (in isoform 1)Ubiquitination-50.9421890473
466AcetylationDPDDLQCKRGEHVAL
CHHHCCCCCCCCEEE		50.9424846367
466UbiquitinationDPDDLQCKRGEHVAL
CHHHCCCCCCCCEEE		50.942190698
486 (in isoform 2)Ubiquitination-31.86-
487 (in isoform 2)Ubiquitination-3.6821890473
489PhosphorylationLRLLNLVYDVTPPEL
HHHHHHHCCCCCHHH		14.0922210691
492PhosphorylationLNLVYDVTPPELVDL
HHHHCCCCCHHHHHH		30.1722210691
510PhosphorylationELGMIPCSSVPVVLR
CCCCEECCCCCEEEE		29.0822210691
511PhosphorylationLGMIPCSSVPVVLRV
CCCEECCCCCEEEEE		36.8422210691
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 EI2BD_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EI2BD_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 EI2BD_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EI2BE_HUMANEIF2B5physical
10858531
EI2BE_HUMANEIF2B5physical
22939629
EI2BG_HUMANEIF2B3physical
22939629
EI2BB_HUMANEIF2B2physical
25416956
EI2BA_HUMANEIF2B1physical
26344197
IF2A_HUMANEIF2S1physical
26344197
ZN622_HUMANZNF622physical
26344197
EI2BA_HUMANEIF2B1physical
27173435
EI2BB_HUMANEIF2B2physical
27173435
MCU_HUMANMCUphysical
27173435
BZW2_HUMANBZW2physical
27173435
EI2BE_HUMANEIF2B5physical
27173435
GDIR1_HUMANARHGDIAphysical
27173435
EI2BG_HUMANEIF2B3physical
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 EI2BD_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-86 AND SER-399, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130 AND THR-137, ANDMASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-137, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-86, AND MASSSPECTROMETRY.

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