ID   EIF3H_HUMAN             Reviewed;         352 AA.
AC   O15372;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   02-MAR-2010, entry version 91.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit H;
DE            Short=eIF3h;
DE   AltName: Full=Eukaryotic translation initiation factor 3 subunit 3;
DE   AltName: Full=eIF-3-gamma;
DE   AltName: Full=eIF3 p40 subunit;
GN   Name=EIF3H; Synonyms=EIF3S3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   MEDLINE=98001678; PubMed=9341143; DOI=10.1074/jbc.272.43.27042;
RA   Asano K., Vornlocher H.-P., Richter-Cook N.J., Merrick W.C.,
RA   Hinnebusch A.G., Hershey J.W.B.;
RT   "Structure of cDNAs encoding human eukaryotic initiation factor 3
RT   subunits. Possible roles in RNA binding and macromolecular assembly.";
RL   J. Biol. Chem. 272:27042-27052(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Schmidt O.G., von Holtum D., Gross S., Horsthemke B., Luedecke H.-J.;
RT   "The gene encoding the p40 subunit of the translation initiation
RT   factor eIF3 has 8 exons, maps to the Langer-Giedion syndrome region on
RT   chromosome 8q24, but is not the TRPS gene.";
RL   Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INTERACTION WITH RPS6KB1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=16286006; DOI=10.1016/j.cell.2005.10.024;
RA   Holz M.K., Ballif B.A., Gygi S.P., Blenis J.;
RT   "mTOR and S6K1 mediate assembly of the translation preinitiation
RT   complex through dynamic protein interchange and ordered
RT   phosphorylation events.";
RL   Cell 123:569-580(2005).
RN   [5]
RP   CHARACTERIZATION OF THE EIF-3 COMPLEX.
RX   PubMed=15703437; DOI=10.1261/rna.7215305;
RA   Kolupaeva V.G., Unbehaun A., Lomakin I.B., Hellen C.U.T.,
RA   Pestova T.V.;
RT   "Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits
RT   and its role in ribosomal dissociation and anti-association.";
RL   RNA 11:470-486(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Epithelium;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [7]
RP   IDENTIFICATION IN THE EIF-3 COMPLEX, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=16766523; DOI=10.1074/jbc.M605418200;
RA   LeFebvre A.K., Korneeva N.L., Trutschl M., Cvek U., Duzan R.D.,
RA   Bradley C.A., Hershey J.W.B., Rhoads R.E.;
RT   "Translation initiation factor eIF4G-1 binds to eIF3 through the eIF3e
RT   subunit.";
RL   J. Biol. Chem. 281:22917-22932(2006).
RN   [8]
RP   CHARACTERIZATION OF THE EIF-3 COMPLEX.
RX   PubMed=17581632; DOI=10.1038/sj.emboj.7601765;
RA   Masutani M., Sonenberg N., Yokoyama S., Imataka H.;
RT   "Reconstitution reveals the functional core of mammalian eIF3.";
RL   EMBO J. 26:3373-3383(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8; SER-10 AND THR-11,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Epithelium;
RX   PubMed=17924679; DOI=10.1021/pr070152u;
RA   Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT   "Improved titanium dioxide enrichment of phosphopeptides from HeLa
RT   cells and high confident phosphopeptide identification by cross-
RT   validation of MS/MS and MS/MS/MS spectra.";
RL   J. Proteome Res. 6:4150-4162(2007).
RN   [10]
RP   IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3
RP   COMPLEX, PHOSPHORYLATION AT SER-183, AND MASS SPECTROMETRY.
RX   PubMed=17322308; DOI=10.1074/mcp.M600399-MCP200;
RA   Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L.,
RA   Hershey J.W.B., Doudna J.A., Robinson C.V., Leary J.A.;
RT   "Structural characterization of the human eukaryotic initiation factor
RT   3 protein complex by mass spectrometry.";
RL   Mol. Cell. Proteomics 6:1135-1146(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, AND MASS
RP   SPECTROMETRY.
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [12]
RP   IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3
RP   COMPLEX, MASS SPECTROMETRY, AND INTERACTION WITH EIF3B; EIF3F AND
RP   EIF3M.
RX   PubMed=18599441; DOI=10.1073/pnas.0801313105;
RA   Zhou M., Sandercock A.M., Fraser C.S., Ridlova G., Stephens E.,
RA   Schenauer M.R., Yokoi-Fong T., Barsky D., Leary J.A., Hershey J.W.B.,
RA   Doudna J.A., Robinson C.V.;
RT   "Mass spectrometry reveals modularity and a complete subunit
RT   interaction map of the eukaryotic translation factor eIF3.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:18139-18144(2008).
RN   [13]
RP   IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
RN   [14]
RP   3D-STRUCTURE MODELING, AND ELECTRON MICROSCOPY.
RX   PubMed=16322461; DOI=10.1126/science.1118977;
RA   Siridechadilok B., Fraser C.S., Hall R.J., Doudna J.A., Nogales E.;
RT   "Structural roles for human translation factor eIF3 in initiation of
RT   protein synthesis.";
RL   Science 310:1513-1515(2005).
CC   -!- FUNCTION: Component of the eukaryotic translation initiation
CC       factor 3 (eIF-3) complex, which is required for several steps in
CC       the initiation of protein synthesis. The eIF-3 complex associates
CC       with the 40S ribosome and facilitates the recruitment of eIF-1,
CC       eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S
CC       preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA
CC       recruitment to the 43S PIC and scanning of the mRNA for AUG
CC       recognition. The eIF-3 complex is also required for disassembly
CC       and recycling of posttermination ribosomal complexes and
CC       subsequently prevents premature joining of the 40S and 60S
CC       ribosomal subunits prior to initiation.
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor
CC       3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B,
CC       EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K,
CC       EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable
CC       modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I;
CC       module B is composed of EIF3F, EIF3H, and EIF3M; and module C is
CC       composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module
CC       C binds EIF3B of module A and EIF3H of module B, thereby linking
CC       the three modules. EIF3J is a labile subunit that binds to the
CC       eIF-3 complex via EIF3B. The eIF-3 complex interacts with RPS6KB1
CC       under conditions of nutrient depletion. Mitogenic stimulation
CC       leads to binding and activation of a complex composed of FRAP1 and
CC       RAPTOR, leading to phosphorylation and release of RPS6KB1 and
CC       binding of EIF4B to eIF-3.
CC   -!- INTERACTION:
CC       Q9P2A4:ABI3; NbExp=2; IntAct=EBI-709735, EBI-742038;
CC       Q9NRI5:DISC1; NbExp=7; IntAct=EBI-709735, EBI-529989;
CC       O60739:EIF1B; NbExp=1; IntAct=EBI-709735, EBI-1043343;
CC       Q14152:EIF3A; NbExp=1; IntAct=EBI-709735, EBI-366617;
CC       Q14240:EIF4A2; NbExp=1; IntAct=EBI-709735, EBI-73473;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- MASS SPECTROMETRY: Mass=40010.4; Method=Unknown; Range=1-352;
CC       Source=PubMed:17322308;
CC   -!- MASS SPECTROMETRY: Mass=39842.6; Mass_error=0.4; Method=MALDI;
CC       Range=1-352; Source=PubMed:18599441;
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit H family.
CC   -!- SIMILARITY: Contains 1 MPN (JAB/Mov34) domain.
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DR   EMBL; U54559; AAD03465.1; -; mRNA.
DR   EMBL; AF092576; AAC84044.1; -; Genomic_DNA.
DR   EMBL; AF092569; AAC84044.1; JOINED; Genomic_DNA.
DR   EMBL; AF092570; AAC84044.1; JOINED; Genomic_DNA.
DR   EMBL; AF092571; AAC84044.1; JOINED; Genomic_DNA.
DR   EMBL; AF092572; AAC84044.1; JOINED; Genomic_DNA.
DR   EMBL; AF092573; AAC84044.1; JOINED; Genomic_DNA.
DR   EMBL; AF092574; AAC84044.1; JOINED; Genomic_DNA.
DR   EMBL; AF092575; AAC84044.1; JOINED; Genomic_DNA.
DR   EMBL; BC000386; AAH00386.1; -; mRNA.
DR   IPI; IPI00941359; -.
DR   RefSeq; NP_003747.1; -.
DR   UniGene; Hs.492599; -.
DR   DIP; DIP-33689N; -.
DR   IntAct; O15372; 50.
DR   STRING; O15372; -.
DR   MEROPS; M67.971; -.
DR   PhosphoSite; O15372; -.
DR   PRIDE; O15372; -.
DR   Ensembl; ENST00000276682; ENSP00000276682; ENSG00000147677; Homo sapiens.
DR   Ensembl; ENST00000411422; ENSP00000394044; ENSG00000147677; Homo sapiens.
DR   GeneID; 8667; -.
DR   KEGG; hsa:8667; -.
DR   UCSC; uc003yoa.1; human.
DR   CTD; 8667; -.
DR   GeneCards; GC08M117727; -.
DR   H-InvDB; HIX0007736; -.
DR   HGNC; HGNC:3273; EIF3H.
DR   HPA; HPA023117; -.
DR   HPA; HPA023553; -.
DR   MIM; 603912; gene.
DR   PharmGKB; PA27701; -.
DR   HOVERGEN; HBG000883; -.
DR   InParanoid; O15372; -.
DR   OrthoDB; EOG9H1DF9; -.
DR   PhylomeDB; O15372; -.
DR   Reactome; REACT_17015; Metabolism of proteins.
DR   Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR   Reactome; REACT_71; Gene Expression.
DR   NextBio; 32511; -.
DR   ArrayExpress; O15372; -.
DR   Bgee; O15372; -.
DR   CleanEx; HS_EIF3H; -.
DR   Genevestigator; O15372; -.
DR   GermOnline; ENSG00000147677; Homo sapiens.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0005852; C:eukaryotic translation initiation factor 3 ...; IDA:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006446; P:regulation of translational initiation; TAS:UniProtKB.
DR   GO; GO:0006413; P:translational initiation; IDA:UniProtKB.
DR   InterPro; IPR000555; Mov34_MPN_PAD1.
DR   Pfam; PF01398; Mov34; 1.
DR   SMART; SM00232; JAB_MPN; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; Initiation factor; Phosphoprotein;
KW   Protein biosynthesis.
FT   CHAIN         1    352       Eukaryotic translation initiation factor
FT                                3 subunit H.
FT                                /FTId=PRO_0000213961.
FT   DOMAIN       34    146       MPN.
FT   MOD_RES       8      8       Phosphothreonine.
FT   MOD_RES      10     10       Phosphoserine.
FT   MOD_RES      11     11       Phosphothreonine.
FT   MOD_RES     183    183       Phosphoserine.
FT   CONFLICT     73     73       E -> K (in Ref. 2; AAC84044).
SQ   SEQUENCE   352 AA;  39930 MW;  F3A6EFA0CEF587D0 CRC64;
     MASRKEGTGS TATSSSSTAG AAGKGKGKGG SGDSAVKQVQ IDGLVVLKII KHYQEEGQGT
     EVVQGVLLGL VVEDRLEITN CFPFPQHTED DADFDEVQYQ MEMMRSLRHV NIDHLHVGWY
     QSTYYGSFVT RALLDSQFSY QHAIEESVVL IYDPIKTAQG SLSLKAYRLT PKLMEVCKEK
     DFSPEALKKA NITFEYMFEE VPIVIKNSHL INVLMWELEK KSAVADKHEL LSLASSNHLG
     KNLQLLMDRV DEMSQDIVKY NTYMRNTSKQ QQQKHQYQQR RQQENMQRQS RGEPPLPEED
     LSKLFKPPQP PARMDSLLIA GQINTYCQNI KEFTAQNLGK LFMAQALQEY NN
//