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Q15056 (IF4H_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length248 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.11

Subcellular location

Cytoplasmperinuclear region By similarity.

Tissue specificity

The short isoform isthe predominant isoform andis 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

EIF4H is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region. Haploinsufficiency of EIF4H may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in the disease.

Sequence similarities

Contains 1 RRM (RNA recognition motif) domain.

Sequence caution

The sequence BAA05063.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processHost-virus interaction
Protein biosynthesis
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   DiseaseWilliams-Beuren syndrome
   LigandRNA-binding
   Molecular functionInitiation factor
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular protein metabolic process

Traceable author statement. Source: Reactome

developmental growth

Inferred from electronic annotation. Source: Ensembl

gene expression

Traceable author statement. Source: Reactome

regulation of translational initiation

Traceable author statement Ref.8. Source: ProtInc

sexual reproduction

Inferred from electronic annotation. Source: Ensembl

translation

Traceable author statement. Source: Reactome

translational initiation

Traceable author statement. Source: Reactome

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

eukaryotic translation initiation factor 4F complex

Traceable author statement Ref.8. Source: ProtInc

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRNA binding

Traceable author statement Ref.1. Source: ProtInc

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

translation factor activity, nucleic acid binding

Traceable author statement Ref.8. Source: ProtInc

translation initiation factor activity

Traceable author statement Ref.8. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

EIF4A1P608422EBI-748492,EBI-73449

Alternative products

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 248247Eukaryotic translation initiation factor 4H
PRO_0000081619

Regions

Domain42 – 11877RRM
Region137 – 15721HHV-1 Vhs binding site

Amino acid modifications

Modified residue21N-acetylalanine Ref.7 Ref.13 Ref.18 Ref.19
Modified residue211Phosphoserine Ref.15 Ref.17
Modified residue241Phosphoserine Ref.15 Ref.17
Modified residue321Phosphoserine Ref.14

Natural variations

Alternative sequence137 – 15620Missing in isoform Short.
VSP_005799

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified January 23, 2007. Version 5.
Checksum: D3098B7270A9CF38

FASTA24827,385
        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 [UniParc].

Checksum: 3374AF6A7558B9F7
Show »

FASTA22825,200

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [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. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HHV-1 VHS.
[12]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-24, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-24, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

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.
CH471200 Genomic DNA. Translation: EAW69615.1.
CH471200 Genomic DNA. Translation: EAW69617.1.
CH471200 Genomic DNA. Translation: EAW69618.1.
CH471200 Genomic DNA. Translation: EAW69619.1.
BC010021 mRNA. Translation: AAH10021.1.
BC021214 mRNA. Translation: AAH21214.1.
BC066928 mRNA. Translation: AAH66928.1.
RefSeqNP_071496.1. NM_022170.1.
NP_114381.1. NM_031992.1.
UniGeneHs.520943.

3D structure databases

ProteinModelPortalQ15056.
SMRQ15056. Positions 27-125.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113297. 32 interactions.
IntActQ15056. 8 interactions.
MINTMINT-5002829.
STRING9606.ENSP00000265753.

Chemistry

ChEMBLCHEMBL1293274.

PTM databases

PhosphoSiteQ15056.

Polymorphism databases

DMDM18276665.

Proteomic databases

PaxDbQ15056.
PRIDEQ15056.

Protocols and materials databases

DNASU7458.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265753; ENSP00000265753; ENSG00000106682. [Q15056-1]
ENST00000353999; ENSP00000265754; ENSG00000106682. [Q15056-2]
ENST00000575843; ENSP00000460568; ENSG00000263344. [Q15056-1]
ENST00000575925; ENSP00000458302; ENSG00000263344. [Q15056-2]
GeneID7458.
KEGGhsa:7458.
UCSCuc003uad.1. human. [Q15056-1]
uc003uae.1. human. [Q15056-2]

Organism-specific databases

CTD7458.
GeneCardsGC07P073588.
HGNCHGNC:12741. EIF4H.
HPAHPA030542.
HPA054330.
MIM603431. gene.
neXtProtNX_Q15056.
Orphanet904. Williams syndrome.
PharmGKBPA162384997.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0724.
HOGENOMHOG000013063.
HOVERGENHBG018193.
InParanoidQ15056.
OMAFREPSDE.
OrthoDBEOG70PC0M.
PhylomeDBQ15056.
TreeFamTF313897.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
REACT_1762. 3' -UTR-mediated translational regulation.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ15056.
BgeeQ15056.
CleanExHS_EIF4H.
GenevestigatorQ15056.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 1 hit.
[Graphical view]
PROSITEPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEIF4H. human.
GeneWikiEIF4H.
GenomeRNAi7458.
NextBio29206.
PROQ15056.
SOURCESearch...

Entry information

Entry nameIF4H_HUMAN
AccessionPrimary (citable) accession number: Q15056
Secondary accession number(s): A8K3R1, D3DXF6, D3DXF8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 141 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Translation initiation factors

List of translation initiation factor entries

Human chromosome 7

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