IF4H_MOUSE
ID IF4H_MOUSE Reviewed; 248 AA.
AC Q9WUK2; Q9WUK3;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Eukaryotic translation initiation factor 4H;
DE Short=eIF-4H;
DE AltName: Full=Williams-Beuren syndrome chromosomal region 1 protein homolog;
GN Name=Eif4h; Synonyms=Wbscr1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, AND TISSUE
RP SPECIFICITY.
RC STRAIN=129/SvJ;
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM LONG).
RC STRAIN=129/Sv;
RA Green E.D.;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [4]
RP PROTEIN SEQUENCE OF 97-109, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-19; ARG-22; ARG-136; ARG-166 AND
RP ARG-175, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
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 [8]
RP STRUCTURE BY NMR OF 32-125.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RNA binding domain in eukaryotic translation
RT initiation factor 4H.";
RL Submitted (OCT-2006) to the PDB data bank.
CC -!- FUNCTION: Stimulates the RNA helicase activity of EIF4A in the
CC translation initiation complex. Binds weakly mRNA (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=Q9WUK2-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q9WUK2-2; Sequence=VSP_005800;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in heart, liver and testis
CC and at lower levels in brain, spleen, lung, skeletal muscle, kidney and
CC embryonic tissues. Both isoforms are expressed at similar levels.
CC {ECO:0000269|PubMed:11003705}.
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DR EMBL; AF139987; AAD34859.1; -; Genomic_DNA.
DR EMBL; AF139987; AAD34860.1; -; Genomic_DNA.
DR EMBL; AF289664; AAF99330.1; -; Genomic_DNA.
DR EMBL; BC014796; AAH14796.1; -; mRNA.
DR CCDS; CCDS19723.1; -. [Q9WUK2-1]
DR CCDS; CCDS84968.1; -. [Q9WUK2-2]
DR RefSeq; NP_001299796.1; NM_001312867.1. [Q9WUK2-2]
DR RefSeq; NP_291039.1; NM_033561.2. [Q9WUK2-1]
DR PDB; 2DNG; NMR; -; A=34-123.
DR PDBsum; 2DNG; -.
DR AlphaFoldDB; Q9WUK2; -.
DR SMR; Q9WUK2; -.
DR BioGRID; 204551; 12.
DR STRING; 10090.ENSMUSP00000048833; -.
DR iPTMnet; Q9WUK2; -.
DR PhosphoSitePlus; Q9WUK2; -.
DR SwissPalm; Q9WUK2; -.
DR EPD; Q9WUK2; -.
DR jPOST; Q9WUK2; -.
DR MaxQB; Q9WUK2; -.
DR PaxDb; Q9WUK2; -.
DR PRIDE; Q9WUK2; -.
DR ProteomicsDB; 267263; -. [Q9WUK2-1]
DR ProteomicsDB; 267264; -. [Q9WUK2-2]
DR Antibodypedia; 14587; 219 antibodies from 29 providers.
DR DNASU; 22384; -.
DR Ensembl; ENSMUST00000036125; ENSMUSP00000048833; ENSMUSG00000040731. [Q9WUK2-2]
DR Ensembl; ENSMUST00000202622; ENSMUSP00000143910; ENSMUSG00000040731. [Q9WUK2-1]
DR GeneID; 22384; -.
DR KEGG; mmu:22384; -.
DR UCSC; uc008zwp.1; mouse. [Q9WUK2-1]
DR CTD; 7458; -.
DR MGI; MGI:1341822; Eif4h.
DR VEuPathDB; HostDB:ENSMUSG00000040731; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000155414; -.
DR HOGENOM; CLU_046195_1_0_1; -.
DR InParanoid; Q9WUK2; -.
DR OMA; EPPYIAY; -.
DR PhylomeDB; Q9WUK2; -.
DR TreeFam; TF313897; -.
DR Reactome; R-MMU-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-MMU-72649; Translation initiation complex formation.
DR Reactome; R-MMU-72662; Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
DR Reactome; R-MMU-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-MMU-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR BioGRID-ORCS; 22384; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Eif4h; mouse.
DR EvolutionaryTrace; Q9WUK2; -.
DR PRO; PR:Q9WUK2; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9WUK2; protein.
DR Bgee; ENSMUSG00000040731; Expressed in metanephric loop of Henle and 249 other tissues.
DR ExpressionAtlas; Q9WUK2; baseline and differential.
DR Genevisible; Q9WUK2; MM.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043024; F:ribosomal small subunit binding; IBA:GO_Central.
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:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0048589; P:developmental growth; IMP:MGI.
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:0019953; P:sexual reproduction; IMP:MGI.
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 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Initiation factor; Methylation; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q15056"
FT CHAIN 2..248
FT /note="Eukaryotic translation initiation factor 4H"
FT /id="PRO_0000081620"
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 122..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..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:0000250|UniProtKB:Q15056"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15056"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15056"
FT MOD_RES 19
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15056"
FT MOD_RES 22
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15056"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15056"
FT MOD_RES 136
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
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:0007744|PubMed:24129315"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15056"
FT VAR_SEQ 137..156
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_005800"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:2DNG"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:2DNG"
FT HELIX 55..61
FT /evidence="ECO:0007829|PDB:2DNG"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:2DNG"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:2DNG"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:2DNG"
FT STRAND 80..91
FT /evidence="ECO:0007829|PDB:2DNG"
FT HELIX 92..98
FT /evidence="ECO:0007829|PDB:2DNG"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:2DNG"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:2DNG"
SQ SEQUENCE 248 AA; 27341 MW; 23E5393BAF183477 CRC64;
MADFDTYDDR AYSSFGGGRG SRGSAGGHGS RSQKELPTEP PYTAYVGNLP FNTVQGDIDA
IFKDLSIRSV RLVRDKDTDK FKGFCYVEFD EVDSLKEALT YDGALLGDRS LRVDIAEGRK
QDKGGFGFRK GGPDDRGMGG SRESRGGWDS RDDFNSGYRD DFLGGRGGSR PGDRRAGPPM
GSRFRDGPPL RGSNMDFREP TEEERAQRPR LQLKPRTVAT PLNQVANPNS AIFGGARPRE
EVVQKEQE
