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Protein Page:
eIF4H (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
eIF4H eukaryotic translation initiation factor 4H stimulates protein translation. May stimulate the activities of EIF4A, EIF4B and EIF4F during the steps involving mRNA binding and utilization in the initiation of protein biosynthesis. Binds mRNA. Two alternatively spliced isoforms have been described. The short isoform is the predominant isoform and is expressed alone in liver and skeletal muscle. Both isoforms are expressed in fibroblast, spleen, testis and bone marrow. Levels are high in lung and pancreas and low in heart, frontal cortex and kidney. Note: This description may include information from UniProtKB.
Protein type: Translation initiation; Translation
Chromosomal Location of Human Ortholog: 7q11.23
Cellular Component: membrane; perinuclear region of cytoplasm; eukaryotic translation initiation factor 4F complex; cytosol
Molecular Function: protein binding; RNA binding; translation factor activity, nucleic acid binding; translation initiation factor activity; nucleotide binding
Biological Process: developmental growth; cellular protein metabolic process; translation; viral reproduction; sexual reproduction; translational initiation; gene expression; regulation of translational initiation
Reference #:  Q15056 (UniProtKB)
Alt. Names/Synonyms: eIF-4H; EIF4H; Eukaryotic translation initiation factor 4H; IF4H; KIAA0038; WBSCR1; Williams-Beuren syndrome chromosomal region 1 protein; Williams-Beuren syndrome chromosome region 1; WSCR1
Gene Symbols: EIF4H
Molecular weight: 27,385 Da
Basal Isoelectric point: 6.67  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

eIF4H

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 Y7-p _MADFDTyDDRAyss
0 244 Y12-p DTyDDRAyssFGGGr
0 3 S13-p TyDDRAyssFGGGrG
0 9 S14-p yDDRAyssFGGGrGs
0 26 R19-m1 yssFGGGrGsrGsAG
0 1 R19-m2 yssFGGGrGsrGsAG
0 11 S21-p sFGGGrGsrGsAGGH
0 11 R22-m1 FGGGrGsrGsAGGHG
0 7 S24-p GGrGsrGsAGGHGsr
0 2 S30-p GsAGGHGsrsQKELP
0 1 R31 sAGGHGsRsQKELPT
0 1 R31-m1 sAGGHGsrsQKELPT
0 1 S32-p AGGHGsrsQKELPTE
0 15 Y42-p ELPTEPPytAyVGNL
0 3 T43-p LPTEPPytAyVGNLP
0 55 Y45-p TEPPytAyVGNLPFN
0 1 S69-p FKDLSIRsVRLVRDK
0 2 K80-ub VRDKDTDkFKGFCyV
0 7 Y86-p DkFKGFCyVEFDEVD
0 1 D93 yVEFDEVDSLKEALT
0 11 Y101-p SLKEALTyDGALLGD
0 4 S110-p GALLGDRsLRVDIAE
0 3 K123-ub AEGRKQDkGGFGFRK
0 1 R136 RKGGPDDRGMGSSRE
0 19 R166-m1 RDDFLGGrGGSrPGD
0 1 R166-m2 RDDFLGGrGGSrPGD
0 1 S169 FLGGrGGSrPGDrrT
0 8 R170-m1 LGGrGGSrPGDrrTG
0 1 R174-m1 GGSrPGDrrTGPPMG
0 2 R175-m1 GSrPGDrrTGPPMGs
0 1 S182-p rTGPPMGsRFRDGPP
0 13 R191-m1 FRDGPPLrGsNMDFR
0 3 S193-p DGPPLrGsNMDFREP
0 5 T201-p NMDFREPtEEERAQR
0 1 K214-ac QRPRLQLkPRtVAtP
0 2 T217-p RLQLkPRtVAtPLNQ
0 11 T220-p LkPRtVAtPLNQVAN
0 30 S230-p NQVANPNsAIFGGAR
0 4 K245-ac PREEVVQkEQE____
0 3 K245-ub PREEVVQkEQE____
  mouse

 
Y7 _MADFDTYDDRAySs
Y12-p DTYDDRAySsFGGGr
S13 TYDDRAySsFGGGrG
S14-p YDDRAySsFGGGrGs
R19-m1 ySsFGGGrGsrGSAG
R19 ySsFGGGRGsrGSAG
S21-p sFGGGrGsrGSAGGH
R22-m1 FGGGrGsrGSAGGHG
S24 GGrGsrGSAGGHGSr
S30 GSAGGHGSrSQKELP
R31-m2 SAGGHGSrSQKELPT
R31 SAGGHGSRSQKELPT
S32 AGGHGSrSQKELPTE
Y42-p ELPTEPPyTAyVGNL
T43 LPTEPPyTAyVGNLP
Y45-p TEPPyTAyVGNLPFN
S69 FKDLSIRSVRLVRDK
K80 VRDKDTDKFKGFCYV
Y86 DKFKGFCYVEFDEVd
D93-ca YVEFDEVdSLKEALT
Y101 SLKEALTYDGALLGD
S110 GALLGDRSLRVDIAE
K123-ub AEGRKQDkGGFGFRK
R136-m1 RKGGPDDrGMGGSRE
R166-m1 RDDFLGGrGGsrPGD
R166 RDDFLGGRGGsrPGD
S169-p FLGGrGGsrPGDRrA
R170-m1 LGGrGGsrPGDRrAG
R174 GGsrPGDRrAGPPMG
R175-m1 GsrPGDRrAGPPMGS
S182 rAGPPMGSRFRDGPP
R191-m1 FRDGPPLrGSNMDFR
S193 DGPPLrGSNMDFREP
T201 NMDFREPTEEERAQR
K214 QRPRLQLKPRtVATP
T217-p RLQLKPRtVATPLNQ
T220 LKPRtVATPLNQVAN
S230-p NQVANPNsAIFGGAR
K245 PREEVVQKEQE____
K245-ub PREEVVQkEQE____
  rat

 
Y7 _MADFDTYDDRAYSS
Y12 DTYDDRAYSSFGGGr
S13 TYDDRAYSSFGGGrG
S14 YDDRAYSSFGGGrGs
R19-m1 YSSFGGGrGsRGSAG
R19 YSSFGGGRGsRGSAG
S21-p SFGGGrGsRGSAGGH
R22 FGGGrGsRGSAGGHG
S24 GGrGsRGSAGGHGSR
S30 GSAGGHGSRSQKELP
R31 SAGGHGSRSQKELPT
R31 SAGGHGSRSQKELPT
S32 AGGHGSRSQKELPTE
Y42-p ELPTEPPyTAYVGNL
T43 LPTEPPyTAYVGNLP
Y45 TEPPyTAYVGNLPFN
S69 FKDLSIRSVRLVRDK
K80 VRDKDTDKFKGFCYV
Y86 DKFKGFCYVEFDEVD
D93 YVEFDEVDSLKEALT
Y101 SLKEALTYDGALLGD
S110 GALLGDRSLRVDIAE
K123 AEGRKQDKGGFGFRK
R136 RKGGPDDRGMGGSRE
R166-m1 RDDFLGGrGGSrPGD
R166 RDDFLGGRGGSrPGD
S169 FLGGrGGSrPGDRRA
R170-m1 LGGrGGSrPGDRRAG
R174 GGSrPGDRRAGPPMG
R175 GSrPGDRRAGPPMGS
S182 RAGPPMGSRFRDGPP
R191-m1 FRDGPPLrGSNMDFR
S193 DGPPLrGSNMDFREP
T201 NMDFREPTEEERAQR
K214-ac QRPRLQLkPRTVATP
T217 RLQLkPRTVATPLNQ
T220 LkPRTVATPLNQVAN
S230 NQVANPNSAIFGGAR
K245-ac PREEVVQkEQE____
K245 PREEVVQKEQE____
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