Eukaryotic translation initiation factor 4H

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

Alternative products

Sequence annotation (Features)

Sequences

References

Cross-references

Entry information

Relevant documents

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

Alternative products

Sequence annotation (Features)

Sequences

References

Cross-references

Entry information

Relevant documents

Molecule processing

Regions

Amino acid modifications

Natural variations

With

Entry

#Exp.

IntAct

Notes

Molecule processing

Regions

Amino acid modifications

Natural variations

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Protein names

Recommended name:
    Eukaryotic translation initiation factor 4H
      Short name=eIF-4H
Alternative name(s):
    Williams-Beuren syndrome chromosomal region 1 protein

Gene names

Name:	EIF4H
Synonyms:	KIAA0038, WBSCR1, WSCR1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Sequence length	248 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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Function	Stimulates the RNA helicase activity of EIF4A in the translation initiation complex. Binds weakly mRNA. Ref.9 Ref.10
Subunit structure	Interacts with HHV-1 Vhs. Ref.13
Subcellular location	Cytoplasm › perinuclear region By similarity.
Tissue specificity	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. Ref.1 Ref.2
Involvement in disease	Haploinsufficiency of EIF4H may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in Williams-Beuren syndrome (WBS) [MIM:194050]. WBS is a rare developmental disorder. It is a contiguous gene deletion syndrome involving genes from chromosome band 7q11.23.
Sequence similarities	Contains 1 RRM (RNA recognition motif) domain.

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Keywords
Biological process	Host-virus interaction Protein biosynthesis
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Disease	Williams-Beuren syndrome
Ligand	RNA-binding
Molecular function	Initiation factor
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW regulation of translational initiation Ref.8 Traceable author statement. Source: ProtInc translation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from Experiment. Source: Reactome eukaryotic translation initiation factor 4F complex Ref.8 Traceable author statement. Source: ProtInc perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	RNA binding Ref.1 Traceable author statement. Source: ProtInc nucleotide binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct translation initiation factor activity Ref.8 Traceable author statement. Source: ProtInc
Complete GO annotation...

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With	Entry	#Exp.	IntAct	Notes
EIF4A1	P60842	1	EBI-748492,EBI-73449

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Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Initiator methionine

1

Removed Ref.7

Chain

2 – 248

247

Eukaryotic translation initiation factor 4H

PRO_0000081619

Domain

42 – 118

77

RRM

Region

137 – 157

21

HHV-1 Vhs binding site

Modified residue

2

1

N-acetylalanine Ref.7 Ref.17

Modified residue

12

1

Phosphotyrosine Ref.11 Ref.12

Modified residue

32

1

Phosphoserine Ref.18

Modified residue

45

1

Phosphotyrosine Ref.11 Ref.14

Modified residue

101

1

Phosphotyrosine Ref.11

Modified residue

193

1

Phosphoserine Ref.15

Modified residue

245

1

N6-acetyllysine Ref.19

Alternative sequence

137 – 156

20

Missing in isoform Short.

VSP_005799

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Sequence		Length	Mass (Da)
Isoform Long [UniParc]. Last modified January 23, 2007. Version 5. Checksum: D3098B7270A9CF38 Show »	FASTA	248	27,385
10 20 30 40 50 60 MADFDTYDDR AYSSFGGGRG SRGSAGGHGS RSQKELPTEP PYTAYVGNLP FNTVQGDIDA 70 80 90 100 110 120 IFKDLSIRSV RLVRDKDTDK FKGFCYVEFD EVDSLKEALT YDGALLGDRS LRVDIAEGRK 130 140 150 160 170 180 QDKGGFGFRK GGPDDRGMGS SRESRGGWDS RDDFNSGFRD DFLGGRGGSR PGDRRTGPPM 190 200 210 220 230 240 GSRFRDGPPL RGSNMDFREP TEEERAQRPR LQLKPRTVAT PLNQVANPNS AIFGGARPRE EVVQKEQE « Hide
Isoform Short. Checksum: 3374AF6A7558B9F7 Show »	FASTA	228	25,200
10 20 30 40 50 60 MADFDTYDDR AYSSFGGGRG SRGSAGGHGS RSQKELPTEP PYTAYVGNLP FNTVQGDIDA 70 80 90 100 110 120 IFKDLSIRSV RLVRDKDTDK FKGFCYVEFD EVDSLKEALT YDGALLGDRS LRVDIAEGRK 130 140 150 160 170 180 QDKGGFGFRK GGPDDRGFRD DFLGGRGGSR PGDRRTGPPM GSRFRDGPPL RGSNMDFREP 190 200 210 220 TEEERAQRPR LQLKPRTVAT PLNQVANPNS AIFGGARPRE EVVQKEQE « Hide

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	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of genes from a 500-kb region at 7q11.23 that is commonly deleted in Williams syndrome patients." Osborne L.R., Martindale D.W., Scherer S.W., Shi X.-M., Huizenga J., Heng H.H.Q., Costa T., Pober B., Lew L., Brinkman J., Rommens J., Koop B.F., Tsui L.-C. Genomics 36:328-336(1996) [PubMed: 8812460] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM SHORT), TISSUE SPECIFICITY. Tissue: Fetal brain.
[2]	"Comparative genomic sequence analysis of the Williams syndrome region (LIMK1-RFC2) of human chromosome 7q11.23." Martindale D.W., Wilson M.D., Wang D., Burke R.D., Chen X., Duronio V., Koop B.F. Mamm. Genome 11:890-898(2000) [PubMed: 11003705] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[3]	"Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1." Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., Nagase T., Seki N., Ishikawa K., Tabata S. DNA Res. 1:27-35(1994) [PubMed: 7584026] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT). Tissue: Bone marrow.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT). Tissue: Brain and Muscle.
[7]	"Exploring proteomes and analyzing protein processing by mass spectrometric 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) [PubMed: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-10, ACETYLATION AT ALA-2. Tissue: Platelet.
[8]	"Purification and characterization of a new eukaryotic protein translation factor. Eukaryotic initiation factor 4H." Richter-Cook N.J., Dever T.E., Hensold J.O., Merrick W.C. J. Biol. Chem. 273:7579-7587(1998) [PubMed: 9516461] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION.
[9]	"Further biochemical and kinetic characterization of human eukaryotic initiation factor 4H." Richter N.J., Rogers G.W. Jr., Hensold J.O., Merrick W.C. J. Biol. Chem. 274:35415-35424(1999) [PubMed: 10585411] [Abstract] Cited for: FUNCTION.
[10]	"Modulation of the helicase activity of eIF4A by eIF4B, eIF4H, and eIF4F." Rogers G.W. Jr., Richter N.J., Lima W.F., Merrick W.C. J. Biol. Chem. 276:30914-30922(2001) [PubMed: 11418588] [Abstract] Cited for: FUNCTION.
[11]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." 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) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-12; TYR-45 AND TYR-101, MASS SPECTROMETRY.
[12]	"Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry 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) [PubMed: 16094384] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-12, MASS SPECTROMETRY. Tissue: T-cell.
[13]	"mRNA decay during herpes simplex virus (HSV) infections: protein-protein interactions involving the HSV virion host shutoff protein and translation factors eIF4H and eIF4A." Feng P., Everly D.N. Jr., Read G.S. J. Virol. 79:9651-9664(2005) [PubMed: 16014927] [Abstract] Cited for: INTERACTION WITH HHV-1 VHS.
[14]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases 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. Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-45, MASS SPECTROMETRY.
[15]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation 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) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, MASS SPECTROMETRY.
[16]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[17]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY.
[18]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, MASS SPECTROMETRY. Tissue: T-cell.
[19]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-245, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Sequence databases
EMBL GenBank DDBJ	AF045555 Genomic DNA. Translation: AAF75557.1. AF045555 Genomic DNA. Translation: AAC04859.2. D26068 mRNA. Translation: BAA05063.1. Different initiation. AK290676 mRNA. Translation: BAF83365.1. CH471200 Genomic DNA. Translation: EAW69616.1. BC010021 mRNA. Translation: AAH10021.1. BC021214 mRNA. Translation: AAH21214.1. BC066928 mRNA. Translation: AAH66928.1.
IPI	IPI00014263. IPI00375127.
RefSeq	NP_071496.1. NP_114381.1.
UniGene	Hs.520943
3D structure databases
SMR	Q15056. Positions 27-125, 31-168.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q15056. 6 interactions.
STRING	Q15056.
PTM databases
PhosphoSite	Q15056.
Proteomic databases
PRIDE	Q15056.
Genome annotation databases
Ensembl	ENST00000265753; ENSP00000265753; ENSG00000106682; Homo sapiens. [Genome view]
GeneID	7458.
KEGG	hsa:7458.
NMPDR	fig\|9606.3.peg.28787.
UCSC	uc003uad.1. human. uc003uae.1. human.
Organism-specific databases
CTD	7458.
GeneCards	GC07P073227.
H-InvDB	HIX0006763.
HGNC	HGNC:12741. EIF4H.
MIM	194050. phenotype. 603431. gene.
Orphanet	904. Williams syndrome.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG18259.
HOGENOM	HBG717808.
HOVERGEN	Q15056.
InParanoid	Q15056.
OMA	SSMDFRE.
OrthoDB	EOG9F20NC.
PhylomeDB	Q15056.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins. REACT_1762. 3' -UTR-mediated translational regulation. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	Q15056.
Bgee	Q15056.
CleanEx	HS_EIF4H.
Genevestigator	Q15056.
Family and domain databases
InterPro	IPR012677. a_b_plait_nuc_bd. IPR000504. RRM_RNP1. [Graphical view]
Gene3D	G3DSA:3.30.70.330. a_b_plait_nuc_bd. 1 hit.
Pfam	PF00076. RRM_1. 1 hit. [Graphical view]
SMART	SM00360. RRM. 1 hit. [Graphical view]
PROSITE	PS50102. RRM. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	29206.
SOURCE	Search...

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Entry name

IF4H_HUMAN

Accession

Primary (citable) accession number: Q15056
Secondary accession number(s): A8K3R1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 23, 2007
Last modified:	January 19, 2010
This is version 103 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM

Translation initiation factors

List of translation initiation factor entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Long (identifier: Q15056-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Short (identifier: Q15056-2)

The sequence of this isoform differs from the canonical sequence as follows:
137-156: Missing.