IF4H_HUMAN - dbPTM
IF4H_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IF4H_HUMAN
UniProt AC Q15056
Protein Name Eukaryotic translation initiation factor 4H
Gene Name EIF4H
Organism Homo sapiens (Human).
Sequence Length 248
Subcellular Localization Cytoplasm, perinuclear region.
Protein Description Stimulates the RNA helicase activity of EIF4A in the translation initiation complex. Binds weakly mRNA..
Protein Sequence MADFDTYDDRAYSSFGGGRGSRGSAGGHGSRSQKELPTEPPYTAYVGNLPFNTVQGDIDAIFKDLSIRSVRLVRDKDTDKFKGFCYVEFDEVDSLKEALTYDGALLGDRSLRVDIAEGRKQDKGGFGFRKGGPDDRGMGSSRESRGGWDSRDDFNSGFRDDFLGGRGGSRPGDRRTGPPMGSRFRDGPPLRGSNMDFREPTEEERAQRPRLQLKPRTVATPLNQVANPNSAIFGGARPREEVVQKEQE
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------MADFDTYDD
------CCCCCCCCC
26.6119413330
6Phosphorylation--MADFDTYDDRAYS
--CCCCCCCCCCHHH
28.9228796482
7Phosphorylation-MADFDTYDDRAYSS
-CCCCCCCCCCHHHC
20.0728796482
10DimethylationDFDTYDDRAYSSFGG
CCCCCCCCHHHCCCC
32.31-
10MethylationDFDTYDDRAYSSFGG
CCCCCCCCHHHCCCC
32.31-
12NitrationDTYDDRAYSSFGGGR
CCCCCCHHHCCCCCC
13.02-
12PhosphorylationDTYDDRAYSSFGGGR
CCCCCCHHHCCCCCC
13.0227273156
12 (in isoform 2)Phosphorylation-13.02-
13 (in isoform 2)Phosphorylation-20.43-
13PhosphorylationTYDDRAYSSFGGGRG
CCCCCHHHCCCCCCC
20.4322167270
14PhosphorylationYDDRAYSSFGGGRGS
CCCCHHHCCCCCCCC
18.4223401153
14 (in isoform 2)Phosphorylation-18.42-
19DimethylationYSSFGGGRGSRGSAG
HHCCCCCCCCCCCCC
43.09-
19MethylationYSSFGGGRGSRGSAG
HHCCCCCCCCCCCCC
43.09-
21PhosphorylationSFGGGRGSRGSAGGH
CCCCCCCCCCCCCCC
31.9122167270
21 (in isoform 2)Phosphorylation-31.9121406692
22MethylationFGGGRGSRGSAGGHG
CCCCCCCCCCCCCCC
46.00-
24PhosphorylationGGRGSRGSAGGHGSR
CCCCCCCCCCCCCCC
23.7225159151
24 (in isoform 2)Phosphorylation-23.72-
30PhosphorylationGSAGGHGSRSQKELP
CCCCCCCCCCCCCCC
24.0830242111
31MethylationSAGGHGSRSQKELPT
CCCCCCCCCCCCCCC
47.93-
32PhosphorylationAGGHGSRSQKELPTE
CCCCCCCCCCCCCCC
47.5028464451
34UbiquitinationGHGSRSQKELPTEPP
CCCCCCCCCCCCCCC
63.5729967540
38PhosphorylationRSQKELPTEPPYTAY
CCCCCCCCCCCCEEE
73.9826434776
42PhosphorylationELPTEPPYTAYVGNL
CCCCCCCCEEEECCC
18.0820090780
43PhosphorylationLPTEPPYTAYVGNLP
CCCCCCCEEEECCCC
19.7919690332
45 (in isoform 2)Phosphorylation-10.90-
45PhosphorylationTEPPYTAYVGNLPFN
CCCCCEEEECCCCCC
10.9020090780
53O-linked_GlycosylationVGNLPFNTVQGDIDA
ECCCCCCCCCCCHHH
18.00OGP
66PhosphorylationDAIFKDLSIRSVRLV
HHHHHCCCCCEEEEE
26.5324719451
68MethylationIFKDLSIRSVRLVRD
HHHCCCCCEEEEEEE
26.23-
69PhosphorylationFKDLSIRSVRLVRDK
HHCCCCCEEEEEEEC
15.2121712546
76UbiquitinationSVRLVRDKDTDKFKG
EEEEEEECCCCCCCC
52.5422817900
78UbiquitinationRLVRDKDTDKFKGFC
EEEEECCCCCCCCEE
46.9922817900
80 (in isoform 1)Ubiquitination-51.5821906983
80AcetylationVRDKDTDKFKGFCYV
EEECCCCCCCCEEEE
51.5823749302
80UbiquitinationVRDKDTDKFKGFCYV
EEECCCCCCCCEEEE
51.5822817900
802-HydroxyisobutyrylationVRDKDTDKFKGFCYV
EEECCCCCCCCEEEE
51.58-
82UbiquitinationDKDTDKFKGFCYVEF
ECCCCCCCCEEEEEE
57.7422817900
84UbiquitinationDTDKFKGFCYVEFDE
CCCCCCCEEEEEECC
2.5422817900
86NitrationDKFKGFCYVEFDEVD
CCCCCEEEEEECCCC
10.76-
86PhosphorylationDKFKGFCYVEFDEVD
CCCCCEEEEEECCCC
10.7628796482
94PhosphorylationVEFDEVDSLKEALTY
EEECCCCHHHHHHCC
46.6627499020
100PhosphorylationDSLKEALTYDGALLG
CHHHHHHCCCCCCCC
26.9821945579
101PhosphorylationSLKEALTYDGALLGD
HHHHHHCCCCCCCCC
17.1521945579
101NitrationSLKEALTYDGALLGD
HHHHHHCCCCCCCCC
17.15-
101 (in isoform 2)Phosphorylation-17.15-
109MethylationDGALLGDRSLRVDIA
CCCCCCCCEEEEEEC
35.47-
110 (in isoform 2)Phosphorylation-25.85-
110PhosphorylationGALLGDRSLRVDIAE
CCCCCCCEEEEEECC
25.8520068231
120UbiquitinationVDIAEGRKQDKGGFG
EEECCCCCCCCCCCC
73.9529967540
123UbiquitinationAEGRKQDKGGFGFRK
CCCCCCCCCCCCCCC
59.4427667366
1232-HydroxyisobutyrylationAEGRKQDKGGFGFRK
CCCCCCCCCCCCCCC
59.44-
123AcetylationAEGRKQDKGGFGFRK
CCCCCCCCCCCCCCC
59.4425953088
123MalonylationAEGRKQDKGGFGFRK
CCCCCCCCCCCCCCC
59.4426320211
125UbiquitinationGRKQDKGGFGFRKGG
CCCCCCCCCCCCCCC
25.8324816145
130MethylationKGGFGFRKGGPDDRG
CCCCCCCCCCCCCCC
66.99-
136 (in isoform 2)Methylation-44.36-
136MethylationRKGGPDDRGMGSSRE
CCCCCCCCCCCCCCC
44.36-
140PhosphorylationPDDRGMGSSRESRGG
CCCCCCCCCCCCCCC
19.8227135362
145MethylationMGSSRESRGGWDSRD
CCCCCCCCCCCCCCC
42.78-
146 (in isoform 2)Ubiquitination-51.3121906983
150PhosphorylationESRGGWDSRDDFNSG
CCCCCCCCCCCCCCC
30.9720873877
166DimethylationRDDFLGGRGGSRPGD
CCCCCCCCCCCCCCC
44.49-
166MethylationRDDFLGGRGGSRPGD
CCCCCCCCCCCCCCC
44.4924129315
170MethylationLGGRGGSRPGDRRTG
CCCCCCCCCCCCCCC
42.36-
173 (in isoform 2)Phosphorylation-39.30-
174MethylationGGSRPGDRRTGPPMG
CCCCCCCCCCCCCCC
43.93-
175MethylationGSRPGDRRTGPPMGS
CCCCCCCCCCCCCCC
49.10-
176PhosphorylationSRPGDRRTGPPMGSR
CCCCCCCCCCCCCCC
55.7423186163
182PhosphorylationRTGPPMGSRFRDGPP
CCCCCCCCCCCCCCC
23.2228857561
183MethylationTGPPMGSRFRDGPPL
CCCCCCCCCCCCCCC
25.53-
185MethylationPPMGSRFRDGPPLRG
CCCCCCCCCCCCCCC
47.03-
191MethylationFRDGPPLRGSNMDFR
CCCCCCCCCCCCCCC
52.87-
193PhosphorylationDGPPLRGSNMDFREP
CCCCCCCCCCCCCCC
23.6523401153
195SulfoxidationPPLRGSNMDFREPTE
CCCCCCCCCCCCCCH
5.7328465586
198MethylationRGSNMDFREPTEEER
CCCCCCCCCCCHHHH
44.73-
201PhosphorylationNMDFREPTEEERAQR
CCCCCCCCHHHHHHC
51.8028857561
214SumoylationQRPRLQLKPRTVATP
HCCCCCCCCCCEECC
21.35-
214AcetylationQRPRLQLKPRTVATP
HCCCCCCCCCCEECC
21.3521339330
214SumoylationQRPRLQLKPRTVATP
HCCCCCCCCCCEECC
21.35-
214UbiquitinationQRPRLQLKPRTVATP
HCCCCCCCCCCEECC
21.35-
217PhosphorylationRLQLKPRTVATPLNQ
CCCCCCCCEECCHHH
24.0322322096
220PhosphorylationLKPRTVATPLNQVAN
CCCCCEECCHHHCCC
24.7922322096
225 (in isoform 2)Acetylation-5.60-
225UbiquitinationVATPLNQVANPNSAI
EECCHHHCCCCCCCC
5.6033845483
225AcetylationVATPLNQVANPNSAI
EECCHHHCCCCCCCC
5.6019608861
227UbiquitinationTPLNQVANPNSAIFG
CCHHHCCCCCCCCCC
37.1124816145
230PhosphorylationNQVANPNSAIFGGAR
HHCCCCCCCCCCCCC
24.8122322096
237MethylationSAIFGGARPREEVVQ
CCCCCCCCCHHHHHH
33.80-
239MethylationIFGGARPREEVVQKE
CCCCCCCHHHHHHHH
47.34-
245 (in isoform 1)Ubiquitination-50.1621906983
245AcetylationPREEVVQKEQE----
CHHHHHHHHCC----
50.1623749302
245UbiquitinationPREEVVQKEQE----
CHHHHHHHHCC----
50.1633845483
247UbiquitinationEEVVQKEQE------
HHHHHHHCC------
69.5924816145

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 IF4H_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IF4H_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 IF4H_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CK068_HUMANC11orf68physical
16189514
TRA2B_HUMANTRA2Bphysical
22939629
ROA0_HUMANHNRNPA0physical
22939629
SRSF3_HUMANSRSF3physical
22939629
RBMS2_HUMANRBMS2physical
22939629
PUF60_HUMANPUF60physical
22939629
RM09_HUMANMRPL9physical
22939629
RM44_HUMANMRPL44physical
22939629
NDRG1_HUMANNDRG1physical
22863883
6PGD_HUMANPGDphysical
22863883
CK068_HUMANC11orf68physical
25416956
LNX1_HUMANLNX1physical
25416956
FA98B_HUMANFAM98Bphysical
26344197
KDM3A_HUMANKDM3Aphysical
26344197
LIX1L_HUMANLIX1Lphysical
26344197
MESD_HUMANMESDC2physical
26344197
RT36_HUMANMRPS36physical
26344197
PA1B2_HUMANPAFAH1B2physical
26344197
RAVR1_HUMANRAVER1physical
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 IF4H_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides.";
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.;
Nat. Biotechnol. 21:566-569(2003).
Cited for: PROTEIN SEQUENCE OF 2-10, AND ACETYLATION AT ALA-2.
"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-245, AND MASS SPECTROMETRY.
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 SER-32, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-45, AND MASSSPECTROMETRY.
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry.";
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.;
Nat. Methods 2:591-598(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-12, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-12; TYR-45 AND TYR-101,AND MASS SPECTROMETRY.

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