Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Eukaryotic translation initiation factor 4H  

UniProtKB / Swiss-Prot ID :  IF4H_HUMAN

Gene Name (Synonyms) : 
EIF4H, KIAA0038, WBSCR1, WSCR1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm, perinuclear region (By similarity). 

Protein Function :  Stimulates the RNA helicase activity of EIF4A in the translation initiation complex. Binds weakly mRNA. 

Protein Sequence MADFDTYDDRAYSSFGGGRGSRGSAGGHGSRSQKELPTEPPYTAYVGNLPFNTVQGDIDAIFKDLSIRSV...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCHHHCCCCCCCCEEEEECCCCCCCHHHHHHHHCCCCEEEE...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MADFDT
---CCCCCC
26.61UniProtKB
Link-
12PhosphotyrosineDDRAYSSFG
CCCCCCCCC
13.02HPRD
Link-
12PhosphotyrosineDDRAYSSFG
CCCCCCCCC
13.02PhosphoELM
Link-
12PhosphotyrosineDDRAYSSFG
CCCCCCCCC
13.02Phosphositeplus
Link-
12PhosphotyrosineDDRAYSSFG
CCCCCCCCC
13.02SysPTM
Link-
12Phosphotyrosine.DDRAYSSFG
CCCCCCCCC
13.02UniProtKB
Link-
13PhosphoserineDRAYSSFGG
CCCCCCCCC
20.43HPRD
Link-
13PhosphoserineDRAYSSFGG
CCCCCCCCC
20.43SysPTM
Link-
14PhosphoserineRAYSSFGGG
CCCCCCCCC
18.42HPRD
Link-
14PhosphoserineRAYSSFGGG
CCCCCCCCC
18.42Phosphositeplus
Link-
14PhosphoserineRAYSSFGGG
CCCCCCCCC
18.42SysPTM
Link-
21PhosphoserineGGRGSRGSA
CCCCCCCCC
31.91HPRD
Link-
21PhosphoserineGGRGSRGSA
CCCCCCCCC
31.91Phosphositeplus
Link-
24PhosphoserineGSRGSAGGH
CCCCCCCCC
23.72HPRD
Link-
24PhosphoserineGSRGSAGGH
CCCCCCCCC
23.72Phosphositeplus
Link-
32PhosphoserineHGSRSQKEL
CCCCHHHCC
47.50Phosphositeplus
Link-
32Phosphoserine.HGSRSQKEL
CCCCHHHCC
47.50UniProtKB
Link-
42PhosphotyrosineTEPPYTAYV
CCCCCEEEE
18.08Phosphositeplus
Link-
45PhosphotyrosinePYTAYVGNL
CCEEEEECC
10.90HPRD
Link-
45PhosphotyrosinePYTAYVGNL
CCEEEEECC
10.90PhosphoELM
Link-
45PhosphotyrosinePYTAYVGNL
CCEEEEECC
10.90Phosphositeplus
Link-
45Phosphotyrosine.PYTAYVGNL
CCEEEEECC
10.90UniProtKB
Link-
80Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KDTDKFKGF
CCCCCCCCE
51.58Phosphositeplus
Link-
86PhosphotyrosineKGFCYVEFD
CCEEEEEEC
10.76Phosphositeplus
Link-
101PhosphotyrosineEALTYDGAL
HHHHHCCEE
17.15HPRD
Link-
101PhosphotyrosineEALTYDGAL
HHHHHCCEE
17.15PhosphoELM
Link-
101PhosphotyrosineEALTYDGAL
HHHHHCCEE
17.15Phosphositeplus
Link-
101Phosphotyrosine.EALTYDGAL
HHHHHCCEE
17.15UniProtKB
Link-
110PhosphoserineLGDRSLRVD
ECCEEEEEE
25.85HPRD
Link-
110PhosphoserineLGDRSLRVD
ECCEEEEEE
25.85Phosphositeplus
Link-
193PhosphoserinePLRGSNMDF
CCCCCCCCC
23.65HPRD
Link-
193PhosphoserinePLRGSNMDF
CCCCCCCCC
23.65PhosphoELM
Link-
193PhosphoserinePLRGSNMDF
CCCCCCCCC
23.65Phosphositeplus
Link-
193Phosphoserine.PLRGSNMDF
CCCCCCCCC
23.65UniProtKB
Link-
217PhosphothreonineLKPRTVATP
CCCCCCCCC
24.03Phosphositeplus
Link-
220PhosphothreonineRTVATPLNQ
CCCCCCCEE
24.79Phosphositeplus
Link-
230PhosphoserineANPNSAIFG
ECCCCCCCC
24.81Phosphositeplus
Link-
245Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EVVQKEQE
HHHHHHCC
50.16Phosphositeplus
Link-
245N6-acetyllysineEVVQKEQE
HHHHHHCC
50.16HPRD
Link-
245N6-acetyllysineEVVQKEQE
HHHHHHCC
50.16Phosphositeplus
Link-
245N6-acetyllysine.EVVQKEQE
HHHHHHCC
50.16UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
CK068_HUMANphysical interactionEBI-756607
intact16189514
CRCM_HUMANphysical interactionEBI-1065071
intact17353931
CK068_HUMANyeast 2-hybridHPRD:11940HPRD16189514
RS20_HUMANENSP00000265753STRING
RS5_HUMANENSP00000265753STRING
RS18_HUMANENSP00000265753STRING
EIF3D_HUMANENSP00000265753STRING
IF5_HUMANENSP00000265753STRING
EIF3E_HUMANENSP00000265753STRING
RS19_HUMANENSP00000265753STRING
RS13_HUMANENSP00000265753STRING
RS12_HUMANENSP00000265753STRING
RS15_HUMANENSP00000265753STRING
RS25_HUMANENSP00000265753STRING
EIF3K_HUMANENSP00000265753STRING
RS4Y1_HUMANENSP00000265753STRING
RS16_HUMANENSP00000265753STRING
IF2G_HUMANENSP00000265753STRING
EIF3G_HUMANENSP00000265753STRING
IF2A_HUMANENSP00000265753STRING
EIF3J_HUMANENSP00000265753STRING
IF4B_HUMANENSP00000265753STRING
RS11_HUMANENSP00000265753STRING
RL13A_HUMANENSP00000265753STRING
RS27A_HUMANENSP00000265753STRING
UBIQ_HUMANENSP00000265753STRING
EIF3H_HUMANENSP00000265753STRING
RS3_HUMANENSP00000265753STRING
UBIM_HUMANENSP00000265753STRING
RS30_HUMANENSP00000265753STRING
IF4E_HUMANENSP00000265753STRING
RS23_HUMANENSP00000265753STRING
RS9_HUMANENSP00000265753STRING
EIF3F_HUMANENSP00000265753STRING
EIF3F_HUMANENSP00000265753STRING
RS14_HUMANENSP00000265753STRING
PABP1_HUMANENSP00000265753STRING
RS15A_HUMANENSP00000265753STRING
IF4G1_HUMANENSP00000265753STRING
IF4A2_HUMANENSP00000265753STRING
EIF3C_HUMANENSP00000265753STRING
RS7_HUMANENSP00000265753STRING
RS2_HUMANENSP00000265753STRING
RS17_HUMANENSP00000265753STRING
RS3A_HUMANENSP00000265753STRING
RSSA_HUMANENSP00000265753STRING
RS26_HUMANENSP00000265753STRING
RS28_HUMANENSP00000265753STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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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.
"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.
"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.
Phosphorylation
ReferencePubMed
"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.
"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.
"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.
"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.
"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.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures