IF4H_HUMAN
ID IF4H_HUMAN Reviewed; 248 AA.
AC Q15056; A8K3R1; D3DXF6; D3DXF8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 5.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Eukaryotic translation initiation factor 4H;
DE Short=eIF-4H;
DE AltName: Full=Williams-Beuren syndrome chromosomal region 1 protein;
GN Name=EIF4H; Synonyms=KIAA0038, WBSCR1, WSCR1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM SHORT), TISSUE SPECIFICITY, AND
RP POSSIBLE INVOLVEMENT IN WBS.
RC TISSUE=Fetal brain;
RX PubMed=8812460; DOI=10.1006/geno.1996.0469;
RA Osborne L.R., Martindale D.W., Scherer S.W., Shi X.-M., Huizenga J.,
RA Heng H.H.Q., Costa T., Pober B., Lew L., Brinkman J., Rommens J.,
RA Koop B.F., Tsui L.-C.;
RT "Identification of genes from a 500-kb region at 7q11.23 that is commonly
RT deleted in Williams syndrome patients.";
RL Genomics 36:328-336(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, AND TISSUE
RP SPECIFICITY.
RX PubMed=11003705; DOI=10.1007/s003350010166;
RA Martindale D.W., Wilson M.D., Wang D., Burke R.D., Chen X., Duronio V.,
RA Koop B.F.;
RT "Comparative genomic sequence analysis of the Williams syndrome region
RT (LIMK1-RFC2) of human chromosome 7q11.23.";
RL Mamm. Genome 11:890-898(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
RC TISSUE=Bone marrow;
RX PubMed=7584026; DOI=10.1093/dnares/1.1.27;
RA Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S.,
RA Nagase T., Seki N., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. I. The
RT coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of
RT randomly sampled cDNA clones from human immature myeloid cell line KG-1.";
RL DNA Res. 1:27-35(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
RC TISSUE=Brain, and Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 2-10, AND ACETYLATION AT ALA-2.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
RP PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RX PubMed=9516461; DOI=10.1074/jbc.273.13.7579;
RA Richter-Cook N.J., Dever T.E., Hensold J.O., Merrick W.C.;
RT "Purification and characterization of a new eukaryotic protein translation
RT factor. Eukaryotic initiation factor 4H.";
RL J. Biol. Chem. 273:7579-7587(1998).
RN [9]
RP FUNCTION.
RX PubMed=10585411; DOI=10.1074/jbc.274.50.35415;
RA Richter N.J., Rogers G.W. Jr., Hensold J.O., Merrick W.C.;
RT "Further biochemical and kinetic characterization of human eukaryotic
RT initiation factor 4H.";
RL J. Biol. Chem. 274:35415-35424(1999).
RN [10]
RP FUNCTION.
RX PubMed=11418588; DOI=10.1074/jbc.m100157200;
RA Rogers G.W. Jr., Richter N.J., Lima W.F., Merrick W.C.;
RT "Modulation of the helicase activity of eIF4A by eIF4B, eIF4H, and eIF4F.";
RL J. Biol. Chem. 276:30914-30922(2001).
RN [11]
RP INTERACTION WITH HHV-1 VHS (MICROBIAL INFECTION).
RX PubMed=16014927; DOI=10.1128/jvi.79.15.9651-9664.2005;
RA Feng P., Everly D.N. Jr., Read G.S.;
RT "mRNA decay during herpes simplex virus (HSV) infections: protein-protein
RT interactions involving the HSV virion host shutoff protein and translation
RT factors eIF4H and eIF4A.";
RL J. Virol. 79:9651-9664(2005).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-24, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-24, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-14; SER-21; SER-24
RP AND SER-230, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [22]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-166, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Stimulates the RNA helicase activity of EIF4A in the
CC translation initiation complex. Binds weakly mRNA.
CC {ECO:0000269|PubMed:10585411, ECO:0000269|PubMed:11418588}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HHV-1 Vhs.
CC {ECO:0000269|PubMed:16014927}.
CC -!- INTERACTION:
CC Q15056; Q9H3H3: C11orf68; NbExp=5; IntAct=EBI-748492, EBI-721765;
CC Q15056; P60842: EIF4A1; NbExp=2; IntAct=EBI-748492, EBI-73449;
CC Q15056; Q8TBB1: LNX1; NbExp=4; IntAct=EBI-748492, EBI-739832;
CC Q15056-2; Q9H3H3-3: C11orf68; NbExp=8; IntAct=EBI-12222405, EBI-12002214;
CC Q15056-2; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-12222405, EBI-742054;
CC Q15056-2; Q92796: DLG3; NbExp=3; IntAct=EBI-12222405, EBI-80440;
CC Q15056-2; Q96EF6: FBXO17; NbExp=3; IntAct=EBI-12222405, EBI-2510157;
CC Q15056-2; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-12222405, EBI-79165;
CC Q15056-2; Q9NZD8: SPG21; NbExp=6; IntAct=EBI-12222405, EBI-742688;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=Q15056-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q15056-2; Sequence=VSP_005799;
CC -!- TISSUE SPECIFICITY: The short isoform is the predominant isoform and is
CC expressed alone in liver and skeletal muscle. Both isoforms are
CC expressed in fibroblast, spleen, testis and bone marrow. Levels are
CC high in lung and pancreas and low in heart, frontal cortex and kidney.
CC {ECO:0000269|PubMed:11003705, ECO:0000269|PubMed:8812460}.
CC -!- DISEASE: Note=EIF4H is located in the Williams-Beuren syndrome (WBS)
CC critical region. WBS results from a hemizygous deletion of several
CC genes on chromosome 7q11.23, thought to arise as a consequence of
CC unequal crossing over between highly homologous low-copy repeat
CC sequences flanking the deleted region. Haploinsufficiency of EIF4H may
CC be the cause of certain cardiovascular and musculo-skeletal
CC abnormalities observed in the disease. {ECO:0000269|PubMed:8812460}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA05063.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF045555; AAF75557.1; -; Genomic_DNA.
DR EMBL; AF045555; AAC04859.2; -; Genomic_DNA.
DR EMBL; D26068; BAA05063.1; ALT_INIT; mRNA.
DR EMBL; AK290676; BAF83365.1; -; mRNA.
DR EMBL; CH471200; EAW69616.1; -; Genomic_DNA.
DR EMBL; CH471200; EAW69615.1; -; Genomic_DNA.
DR EMBL; CH471200; EAW69617.1; -; Genomic_DNA.
DR EMBL; CH471200; EAW69618.1; -; Genomic_DNA.
DR EMBL; CH471200; EAW69619.1; -; Genomic_DNA.
DR EMBL; BC010021; AAH10021.1; -; mRNA.
DR EMBL; BC021214; AAH21214.1; -; mRNA.
DR EMBL; BC066928; AAH66928.1; -; mRNA.
DR CCDS; CCDS5564.1; -. [Q15056-1]
DR CCDS; CCDS5565.1; -. [Q15056-2]
DR RefSeq; NP_071496.1; NM_022170.1. [Q15056-1]
DR RefSeq; NP_114381.1; NM_031992.1. [Q15056-2]
DR AlphaFoldDB; Q15056; -.
DR SMR; Q15056; -.
DR BioGRID; 113297; 88.
DR IntAct; Q15056; 26.
DR MINT; Q15056; -.
DR STRING; 9606.ENSP00000265753; -.
DR BindingDB; Q15056; -.
DR ChEMBL; CHEMBL1293274; -.
DR GlyGen; Q15056; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15056; -.
DR MetOSite; Q15056; -.
DR PhosphoSitePlus; Q15056; -.
DR SwissPalm; Q15056; -.
DR BioMuta; EIF4H; -.
DR DMDM; 18276665; -.
DR EPD; Q15056; -.
DR jPOST; Q15056; -.
DR MassIVE; Q15056; -.
DR MaxQB; Q15056; -.
DR PaxDb; Q15056; -.
DR PeptideAtlas; Q15056; -.
DR PRIDE; Q15056; -.
DR ProteomicsDB; 60410; -. [Q15056-1]
DR ProteomicsDB; 60411; -. [Q15056-2]
DR TopDownProteomics; Q15056-1; -. [Q15056-1]
DR TopDownProteomics; Q15056-2; -. [Q15056-2]
DR Antibodypedia; 14587; 219 antibodies from 29 providers.
DR DNASU; 7458; -.
DR Ensembl; ENST00000265753.13; ENSP00000265753.8; ENSG00000106682.16. [Q15056-1]
DR Ensembl; ENST00000353999.6; ENSP00000265754.8; ENSG00000106682.16. [Q15056-2]
DR Ensembl; ENST00000678438.1; ENSP00000504679.1; ENSG00000106682.16. [Q15056-2]
DR GeneID; 7458; -.
DR KEGG; hsa:7458; -.
DR MANE-Select; ENST00000265753.13; ENSP00000265753.8; NM_022170.2; NP_071496.1.
DR UCSC; uc003uad.2; human. [Q15056-1]
DR CTD; 7458; -.
DR DisGeNET; 7458; -.
DR GeneCards; EIF4H; -.
DR HGNC; HGNC:12741; EIF4H.
DR HPA; ENSG00000106682; Low tissue specificity.
DR MIM; 603431; gene.
DR neXtProt; NX_Q15056; -.
DR OpenTargets; ENSG00000106682; -.
DR Orphanet; 904; Williams syndrome.
DR PharmGKB; PA162384997; -.
DR VEuPathDB; HostDB:ENSG00000106682; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000155414; -.
DR HOGENOM; CLU_046195_1_0_1; -.
DR InParanoid; Q15056; -.
DR OMA; EPPYIAY; -.
DR OrthoDB; 1530583at2759; -.
DR PhylomeDB; Q15056; -.
DR TreeFam; TF313897; -.
DR PathwayCommons; Q15056; -.
DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-HSA-72649; Translation initiation complex formation.
DR Reactome; R-HSA-72662; Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
DR Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR SignaLink; Q15056; -.
DR SIGNOR; Q15056; -.
DR BioGRID-ORCS; 7458; 74 hits in 1079 CRISPR screens.
DR ChiTaRS; EIF4H; human.
DR GeneWiki; EIF4H; -.
DR GenomeRNAi; 7458; -.
DR Pharos; Q15056; Tchem.
DR PRO; PR:Q15056; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q15056; protein.
DR Bgee; ENSG00000106682; Expressed in parotid gland and 209 other tissues.
DR Genevisible; Q15056; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0043024; F:ribosomal small subunit binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0033592; F:RNA strand annealing activity; IBA:GO_Central.
DR GO; GO:0034057; F:RNA strand-exchange activity; IBA:GO_Central.
DR GO; GO:0008135; F:translation factor activity, RNA binding; TAS:ProtInc.
DR GO; GO:0003743; F:translation initiation factor activity; TAS:ProtInc.
DR GO; GO:0048589; P:developmental growth; IEA:Ensembl.
DR GO; GO:0097010; P:eukaryotic translation initiation factor 4F complex assembly; IBA:GO_Central.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IBA:GO_Central.
DR GO; GO:0006446; P:regulation of translational initiation; TAS:ProtInc.
DR GO; GO:0019953; P:sexual reproduction; IEA:Ensembl.
DR CDD; cd12401; RRM_eIF4H; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR034229; eIF4H_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Host-virus interaction; Initiation factor; Methylation; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; RNA-binding;
KW Williams-Beuren syndrome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..248
FT /note="Eukaryotic translation initiation factor 4H"
FT /id="PRO_0000081619"
FT DOMAIN 42..118
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..157
FT /note="HHV-1 Vhs binding site"
FT COMPBIAS 121..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 19
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUK2"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 22
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUK2"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 136
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUK2"
FT MOD_RES 166
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 175
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUK2"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 137..156
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:7584026"
FT /id="VSP_005799"
SQ SEQUENCE 248 AA; 27385 MW; D3098B7270A9CF38 CRC64;
MADFDTYDDR AYSSFGGGRG SRGSAGGHGS RSQKELPTEP PYTAYVGNLP FNTVQGDIDA
IFKDLSIRSV RLVRDKDTDK FKGFCYVEFD EVDSLKEALT YDGALLGDRS LRVDIAEGRK
QDKGGFGFRK GGPDDRGMGS SRESRGGWDS RDDFNSGFRD DFLGGRGGSR PGDRRTGPPM
GSRFRDGPPL RGSNMDFREP TEEERAQRPR LQLKPRTVAT PLNQVANPNS AIFGGARPRE
EVVQKEQE
