EIF2D_HUMAN - dbPTM
EIF2D_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EIF2D_HUMAN
UniProt AC P41214
Protein Name Eukaryotic translation initiation factor 2D
Gene Name EIF2D
Organism Homo sapiens (Human).
Sequence Length 584
Subcellular Localization Cytoplasm .
Protein Description Translation initiation factor that is able to deliver tRNA to the P-site of the eukaryotic ribosome in a GTP-independent manner. The binding of Met-tRNA(I) occurs after the AUG codon finds its position in the P-site of 40S ribosomes, the situation that takes place during initiation complex formation on some specific RNAs. Its activity in tRNA binding with 40S subunits does not require the presence of the aminoacyl moiety. Possesses the unique ability to deliver non-Met (elongator) tRNAs into the P-site of the 40S subunit. In addition to its role in initiation, can promote release of deacylated tRNA and mRNA from recycled 40S subunits following ABCE1-mediated dissociation of post-termination ribosomal complexes into subunits..
Protein Sequence MFAKAFRVKSNTAIKGSDRRKLRADVTTAFPTLGTDQVSELVPGKEELNIVKLYAHKGDAVTVYVSGGNPILFELEKNLYPTVYTLWSYPDLLPTFTTWPLVLEKLVGGADLMLPGLVMPPAGLPQVQKGDLCAISLVGNRAPVAIGVAAMSTAEMLTSGLKGRGFSVLHTYQDHLWRSGNKSSPPSIAPLALDSADLSEEKGSVQMDSTLQGDMRHMTLEGEEENGEVHQAREDKSLSEAPEDTSTRGLNQDSTDSKTLQEQMDELLQQCFLHALKCRVKKADLPLLTSTFLGSHMFSCCPEGRQLDIKKSSYKKLSKFLQQMQQEQIIQVKELSKGVESIVAVDWKHPRITSFVIPEPSPTSQTIQEGSREQPYHPPDIKPLYCVPASMTLLFQESGHKKGSFLEGSEVRTIVINYAKKNDLVDADNKNLVRLDPILCDCILEKNEQHTVMKLPWDSLLTRCLEKLQPAYQVTLPGQEPIVKKGRICPIDITLAQRASNKKVTVVRNLEAYGLDPYSVAAILQQRCQASTTVNPAPGAKDSLQVQIQGNQVHHLGWLLLEEYQLPRKHIQGLEKALKPGKKK
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
1Acetylation-------MFAKAFRV
-------CCCEEEEE		7.1322814378
4Acetylation----MFAKAFRVKSN
----CCCEEEEECCC		36.4725953088
4Ubiquitination----MFAKAFRVKSN
----CCCEEEEECCC		36.47-
15UbiquitinationVKSNTAIKGSDRRKL
ECCCCCCCCCCCHHC		50.3124816145
17PhosphorylationSNTAIKGSDRRKLRA
CCCCCCCCCCHHCCC		23.9628787133
45UbiquitinationVSELVPGKEELNIVK
HHHCCCCCCCEEEEE		41.7829967540
52UbiquitinationKEELNIVKLYAHKGD
CCCEEEEEEEECCCC		31.8029967540
152PhosphorylationAIGVAAMSTAEMLTS
HHHHHHHHHHHHHHH		21.5328464451
153PhosphorylationIGVAAMSTAEMLTSG
HHHHHHHHHHHHHHC		17.3528464451
158PhosphorylationMSTAEMLTSGLKGRG
HHHHHHHHHCCCCCC		21.3128464451
159PhosphorylationSTAEMLTSGLKGRGF
HHHHHHHHCCCCCCE		37.8628464451
167PhosphorylationGLKGRGFSVLHTYQD
CCCCCCEEEEEEHHH		26.9628857561
179PhosphorylationYQDHLWRSGNKSSPP
HHHHHHHCCCCCCCC		34.8323186163
182UbiquitinationHLWRSGNKSSPPSIA
HHHHCCCCCCCCCCC		56.7029967540
183PhosphorylationLWRSGNKSSPPSIAP
HHHCCCCCCCCCCCC		52.6725159151
184PhosphorylationWRSGNKSSPPSIAPL
HHCCCCCCCCCCCCH		42.3025159151
187PhosphorylationGNKSSPPSIAPLALD
CCCCCCCCCCCHHCC		34.4625159151
195PhosphorylationIAPLALDSADLSEEK
CCCHHCCCCCCCCCC		25.2422817901
199PhosphorylationALDSADLSEEKGSVQ
HCCCCCCCCCCCCCC		44.2325159151
207SulfoxidationEEKGSVQMDSTLQGD
CCCCCCCCCCCCCCC		4.0521406390
209AcetylationKGSVQMDSTLQGDMR
CCCCCCCCCCCCCCC		26.1919608861
209PhosphorylationKGSVQMDSTLQGDMR
CCCCCCCCCCCCCCC		26.1928555341
210PhosphorylationGSVQMDSTLQGDMRH
CCCCCCCCCCCCCCC		20.8828555341
219PhosphorylationQGDMRHMTLEGEEEN
CCCCCCCEEECCHHC		18.6129214152
237PhosphorylationHQAREDKSLSEAPED
EEHHHCCCHHCCCCC		49.8325159151
239PhosphorylationAREDKSLSEAPEDTS
HHHCCCHHCCCCCCC		38.5125159151
245PhosphorylationLSEAPEDTSTRGLNQ
HHCCCCCCCCCCCCC		30.2725627689
246PhosphorylationSEAPEDTSTRGLNQD
HCCCCCCCCCCCCCC		28.5627251275
254PhosphorylationTRGLNQDSTDSKTLQ
CCCCCCCCCCCHHHH		25.09-
278UbiquitinationCFLHALKCRVKKADL
HHHHHHHHCCCCCCC		6.6829967540
302UbiquitinationSHMFSCCPEGRQLDI
CHHHHCCCCCCCCCC		51.9424816145
306UbiquitinationSCCPEGRQLDIKKSS
HCCCCCCCCCCCHHH		55.1129967540
311UbiquitinationGRQLDIKKSSYKKLS
CCCCCCCHHHHHHHH		44.9930230243
328UbiquitinationLQQMQQEQIIQVKEL
HHHHHHHHHHHHHHH		33.4724816145
333AcetylationQEQIIQVKELSKGVE
HHHHHHHHHHHCCCC		36.2423749302
337UbiquitinationIQVKELSKGVESIVA
HHHHHHHCCCCEEEE		78.56-
342UbiquitinationLSKGVESIVAVDWKH
HHCCCCEEEEEECCC		1.1424816145
343UbiquitinationSKGVESIVAVDWKHP
HCCCCEEEEEECCCC		6.2229967540
352UbiquitinationVDWKHPRITSFVIPE
EECCCCCEEEEECCC		4.4524816145
353PhosphorylationDWKHPRITSFVIPEP
ECCCCCEEEEECCCC		19.8629396449
354PhosphorylationWKHPRITSFVIPEPS
CCCCCEEEEECCCCC		18.3629396449
360UbiquitinationTSFVIPEPSPTSQTI
EEEECCCCCCCCCCC		40.0129967540
361PhosphorylationSFVIPEPSPTSQTIQ
EEECCCCCCCCCCCC		38.8725159151
363PhosphorylationVIPEPSPTSQTIQEG
ECCCCCCCCCCCCCC		37.4930108239
364PhosphorylationIPEPSPTSQTIQEGS
CCCCCCCCCCCCCCC		28.8030108239
366PhosphorylationEPSPTSQTIQEGSRE
CCCCCCCCCCCCCCC		25.1330108239
371PhosphorylationSQTIQEGSREQPYHP
CCCCCCCCCCCCCCC		31.7120068231
378UbiquitinationSREQPYHPPDIKPLY
CCCCCCCCCCCCCCE		23.5524816145
402UbiquitinationFQESGHKKGSFLEGS
EECCCCCCCCCCCCC		54.8629967540
402MalonylationFQESGHKKGSFLEGS
EECCCCCCCCCCCCC		54.8626320211
404PhosphorylationESGHKKGSFLEGSEV
CCCCCCCCCCCCCEE		35.2225159151
409PhosphorylationKGSFLEGSEVRTIVI
CCCCCCCCEEEEEEE		24.4423312004
420AcetylationTIVINYAKKNDLVDA
EEEEEECCCCCCCCC		41.5725953088
430UbiquitinationDLVDADNKNLVRLDP
CCCCCCCCCCCCCCH		52.8129967540
445UbiquitinationILCDCILEKNEQHTV
HHHHEEEECCCCCCC		33.6429967540
446UbiquitinationLCDCILEKNEQHTVM
HHHEEEECCCCCCCE		63.44-
452UbiquitinationEKNEQHTVMKLPWDS
ECCCCCCCEECCHHH		2.7424816145
454UbiquitinationNEQHTVMKLPWDSLL
CCCCCCEECCHHHHH		47.24-
459PhosphorylationVMKLPWDSLLTRCLE
CEECCHHHHHHHHHH		22.7821406692
462PhosphorylationLPWDSLLTRCLEKLQ
CCHHHHHHHHHHHHC		25.3221406692
467UbiquitinationLLTRCLEKLQPAYQV
HHHHHHHHHCCEEEE		39.2029967540
484UbiquitinationPGQEPIVKKGRICPI
CCCCCCCCCCCCCCC		50.6729967540
484AcetylationPGQEPIVKKGRICPI
CCCCCCCCCCCCCCC		50.6726051181
485UbiquitinationGQEPIVKKGRICPID
CCCCCCCCCCCCCCC		42.39-
502UbiquitinationLAQRASNKKVTVVRN
ECHHHCCCCEEEEEC		46.2324816145
569UbiquitinationEEYQLPRKHIQGLEK
HHHCCCHHHHHHHHH		43.0229967540
576UbiquitinationKHIQGLEKALKPGKK
HHHHHHHHHHCCCCC		65.1529967540
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 EIF2D_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EIF2D_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 EIF2D_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SYHC_HUMANHARSphysical
22939629
CALU_HUMANCALUphysical
26344197
CKAP5_HUMANCKAP5physical
26344197
EIF1_HUMANEIF1physical
26344197
SYHC_HUMANHARSphysical
26344197
HNRPR_HUMANHNRNPRphysical
26344197
LSMD1_HUMANNAA38physical
26344197
RCC2_HUMANRCC2physical
26344197
WDR5_HUMANWDR5physical
26344197
ZNHI2_HUMANZNHIT2physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EIF2D_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184 AND SER-199, ANDMASS SPECTROMETRY.

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