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Q15056

- IF4H_HUMAN

UniProt

Q15056 - IF4H_HUMAN

Protein

Eukaryotic translation initiation factor 4H

Gene

EIF4H

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 5 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Stimulates the RNA helicase activity of EIF4A in the translation initiation complex. Binds weakly mRNA.2 Publications

    GO - Molecular functioni

    1. nucleotide binding Source: InterPro
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. RNA binding Source: ProtInc
    5. translation factor activity, nucleic acid binding Source: ProtInc
    6. translation initiation factor activity Source: ProtInc

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. developmental growth Source: Ensembl
    3. gene expression Source: Reactome
    4. regulation of translational initiation Source: ProtInc
    5. sexual reproduction Source: Ensembl
    6. translation Source: Reactome
    7. translational initiation Source: Reactome
    8. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Initiation factor

    Keywords - Biological processi

    Host-virus interaction, Protein biosynthesis

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_1258. Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
    REACT_1979. Translation initiation complex formation.
    REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
    REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
    REACT_931. Ribosomal scanning and start codon recognition.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Eukaryotic translation initiation factor 4H
    Short name:
    eIF-4H
    Alternative name(s):
    Williams-Beuren syndrome chromosomal region 1 protein
    Gene namesi
    Name:EIF4H
    Synonyms:KIAA0038, WBSCR1, WSCR1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:12741. EIF4H.

    Subcellular locationi

    Cytoplasmperinuclear region By similarity

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. eukaryotic translation initiation factor 4F complex Source: ProtInc
    3. membrane Source: UniProtKB
    4. perinuclear region of cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    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.

    Keywords - Diseasei

    Williams-Beuren syndrome

    Organism-specific databases

    Orphaneti904. Williams syndrome.
    PharmGKBiPA162384997.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 248247Eukaryotic translation initiation factor 4HPRO_0000081619Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine4 Publications
    Modified residuei21 – 211Phosphoserine2 Publications
    Modified residuei24 – 241Phosphoserine2 Publications
    Modified residuei32 – 321Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ15056.
    PaxDbiQ15056.
    PRIDEiQ15056.

    PTM databases

    PhosphoSiteiQ15056.

    Expressioni

    Tissue specificityi

    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.2 Publications

    Gene expression databases

    ArrayExpressiQ15056.
    BgeeiQ15056.
    CleanExiHS_EIF4H.
    GenevestigatoriQ15056.

    Organism-specific databases

    HPAiHPA030542.
    HPA054330.

    Interactioni

    Subunit structurei

    Interacts with HHV-1 Vhs.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EIF4A1P608422EBI-748492,EBI-73449

    Protein-protein interaction databases

    BioGridi113297. 32 interactions.
    IntActiQ15056. 8 interactions.
    MINTiMINT-5002829.
    STRINGi9606.ENSP00000265753.

    Structurei

    3D structure databases

    ProteinModelPortaliQ15056.
    SMRiQ15056. Positions 27-125.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini42 – 11877RRMPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni137 – 15721HHV-1 Vhs binding siteAdd
    BLAST

    Sequence similaritiesi

    Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0724.
    HOGENOMiHOG000013063.
    HOVERGENiHBG018193.
    InParanoidiQ15056.
    OMAiFREPSDE.
    OrthoDBiEOG70PC0M.
    PhylomeDBiQ15056.
    TreeFamiTF313897.

    Family and domain databases

    Gene3Di3.30.70.330. 1 hit.
    InterProiIPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view]
    PfamiPF00076. RRM_1. 1 hit.
    [Graphical view]
    SMARTiSM00360. RRM. 1 hit.
    [Graphical view]
    PROSITEiPS50102. RRM. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: Q15056-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MADFDTYDDR AYSSFGGGRG SRGSAGGHGS RSQKELPTEP PYTAYVGNLP    50
    FNTVQGDIDA IFKDLSIRSV RLVRDKDTDK FKGFCYVEFD EVDSLKEALT 100
    YDGALLGDRS LRVDIAEGRK QDKGGFGFRK GGPDDRGMGS SRESRGGWDS 150
    RDDFNSGFRD DFLGGRGGSR PGDRRTGPPM GSRFRDGPPL RGSNMDFREP 200
    TEEERAQRPR LQLKPRTVAT PLNQVANPNS AIFGGARPRE EVVQKEQE 248
    Length:248
    Mass (Da):27,385
    Last modified:January 23, 2007 - v5
    Checksum:iD3098B7270A9CF38
    GO
    Isoform Short (identifier: Q15056-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:228
    Mass (Da):25,200
    Checksum:i3374AF6A7558B9F7
    GO

    Sequence cautioni

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

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei137 – 15620Missing in isoform Short. 3 PublicationsVSP_005799Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS5564.1. [Q15056-1]
    CCDS5565.1. [Q15056-2]
    RefSeqiNP_071496.1. NM_022170.1. [Q15056-1]
    NP_114381.1. NM_031992.1. [Q15056-2]
    UniGeneiHs.520943.

    Genome annotation databases

    EnsembliENST00000265753; ENSP00000265753; ENSG00000106682. [Q15056-1]
    ENST00000353999; ENSP00000265754; ENSG00000106682. [Q15056-2]
    GeneIDi7458.
    KEGGihsa:7458.
    UCSCiuc003uad.1. human. [Q15056-1]
    uc003uae.1. human. [Q15056-2]

    Polymorphism databases

    DMDMi18276665.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS5564.1. [Q15056-1 ]
    CCDS5565.1. [Q15056-2 ]
    RefSeqi NP_071496.1. NM_022170.1. [Q15056-1 ]
    NP_114381.1. NM_031992.1. [Q15056-2 ]
    UniGenei Hs.520943.

    3D structure databases

    ProteinModelPortali Q15056.
    SMRi Q15056. Positions 27-125.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113297. 32 interactions.
    IntActi Q15056. 8 interactions.
    MINTi MINT-5002829.
    STRINGi 9606.ENSP00000265753.

    Chemistry

    ChEMBLi CHEMBL1293274.

    PTM databases

    PhosphoSitei Q15056.

    Polymorphism databases

    DMDMi 18276665.

    Proteomic databases

    MaxQBi Q15056.
    PaxDbi Q15056.
    PRIDEi Q15056.

    Protocols and materials databases

    DNASUi 7458.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265753 ; ENSP00000265753 ; ENSG00000106682 . [Q15056-1 ]
    ENST00000353999 ; ENSP00000265754 ; ENSG00000106682 . [Q15056-2 ]
    GeneIDi 7458.
    KEGGi hsa:7458.
    UCSCi uc003uad.1. human. [Q15056-1 ]
    uc003uae.1. human. [Q15056-2 ]

    Organism-specific databases

    CTDi 7458.
    GeneCardsi GC07P073588.
    HGNCi HGNC:12741. EIF4H.
    HPAi HPA030542.
    HPA054330.
    MIMi 603431. gene.
    neXtProti NX_Q15056.
    Orphaneti 904. Williams syndrome.
    PharmGKBi PA162384997.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0724.
    HOGENOMi HOG000013063.
    HOVERGENi HBG018193.
    InParanoidi Q15056.
    OMAi FREPSDE.
    OrthoDBi EOG70PC0M.
    PhylomeDBi Q15056.
    TreeFami TF313897.

    Enzyme and pathway databases

    Reactomei REACT_1258. Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
    REACT_1979. Translation initiation complex formation.
    REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
    REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
    REACT_931. Ribosomal scanning and start codon recognition.

    Miscellaneous databases

    ChiTaRSi EIF4H. human.
    GeneWikii EIF4H.
    GenomeRNAii 7458.
    NextBioi 29206.
    PROi Q15056.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15056.
    Bgeei Q15056.
    CleanExi HS_EIF4H.
    Genevestigatori Q15056.

    Family and domain databases

    Gene3Di 3.30.70.330. 1 hit.
    InterProi IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view ]
    Pfami PF00076. RRM_1. 1 hit.
    [Graphical view ]
    SMARTi SM00360. RRM. 1 hit.
    [Graphical view ]
    PROSITEi PS50102. RRM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiIF4H_HUMAN
    AccessioniPrimary (citable) accession number: Q15056
    Secondary accession number(s): A8K3R1, D3DXF6, D3DXF8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 146 of the entry and version 5 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. Translation initiation factors
      List of translation initiation factor entries
    3. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3