Full text data of EIF3F
EIF3F
(EIF3S5)
[Confidence: low (only semi-automatic identification from reviews)]
Eukaryotic translation initiation factor 3 subunit F; eIF3f (Deubiquitinating enzyme eIF3f; 3.4.19.12; Eukaryotic translation initiation factor 3 subunit 5; eIF-3-epsilon; eIF3 p47)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Eukaryotic translation initiation factor 3 subunit F; eIF3f (Deubiquitinating enzyme eIF3f; 3.4.19.12; Eukaryotic translation initiation factor 3 subunit 5; eIF-3-epsilon; eIF3 p47)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O00303
ID EIF3F_HUMAN Reviewed; 357 AA.
AC O00303; A8K0S2; Q6IB45; Q8N978;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUL-1997, sequence version 1.
DT 22-JAN-2014, entry version 133.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit F;
DE Short=eIF3f;
DE AltName: Full=Deubiquitinating enzyme eIF3f;
DE EC=3.4.19.12;
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 5;
DE AltName: Full=eIF-3-epsilon;
DE AltName: Full=eIF3 p47;
GN Name=EIF3F; Synonyms=EIF3S5;
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 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 [LARGE SCALE MRNA].
RC TISSUE=Amygdala, and Brain;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP PHOSPHORYLATION AT SER-46.
RX PubMed=12446680; DOI=10.1074/jbc.M206427200;
RA Shi J., Feng Y., Goulet A.C., Vaillancourt R.R., Sachs N.A.,
RA Hershey J.W., Nelson M.A.;
RT "The p34cdc2-related cyclin-dependent kinase 11 interacts with the p47
RT subunit of eukaryotic initiation factor 3 during apoptosis.";
RL J. Biol. Chem. 278:5062-5071(2003).
RN [7]
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 [8]
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 [9]
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 [10]
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 [11]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3
RP COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2,
RP PHOSPHORYLATION AT SER-258, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP IDENTIFICATION BY 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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-238, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
RP INTERACTION WITH RNF139.
RX PubMed=20068067; DOI=10.1158/1541-7786.MCR-08-0491;
RA Lee J.P., Brauweiler A., Rudolph M., Hooper J.E., Drabkin H.A.,
RA Gemmill R.M.;
RT "The TRC8 ubiquitin ligase is sterol regulated and interacts with
RT lipid and protein biosynthetic pathways.";
RL Mol. Cancer Res. 8:93-106(2010).
RN [16]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3
RP COMPLEX, MASS SPECTROMETRY, AND INTERACTION WITH EIF3B; EIF3H 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 [17]
RP FUNCTION AS A DEUBIQUITINATING ENZYME, CATALYTIC ACTIVITY, AND
RP INTERACTION WITH DTX1.
RX PubMed=21124883; DOI=10.1371/journal.pbio.1000545;
RA Moretti J., Chastagner P., Gastaldello S., Heuss S.F., Dirac A.M.,
RA Bernards R., Masucci M.G., Israel A., Brou C.;
RT "The translation initiation factor 3f (eIF3f) exhibits a
RT deubiquitinase activity regulating Notch activation.";
RL PLoS Biol. 8:E1000545-E1000545(2010).
RN [18]
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [19]
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.,
RA Buerckstuemmer T., 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 [20]
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.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [21]
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 post-termination ribosomal complexes and
CC subsequently prevents premature joining of the 40S and 60S
CC ribosomal subunits prior to initiation.
CC -!- FUNCTION: Deubiquitinates activated NOTCH1, promoting its nuclear
CC import, thereby acting as a positive regulator of Notch signaling.
CC -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC thioester, amide, peptide and isopeptide bonds formed by the C-
CC terminal Gly of ubiquitin (a 76-residue protein attached to
CC proteins as an intracellular targeting signal).
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 MTOR and
CC RPTOR, leading to phosphorylation and release of RPS6KB1 and
CC binding of EIF4B to eIF-3. Interacts with RNF139; the interaction
CC leads to protein translation inhibitions in a ubiquitination-
CC dependent manner. Interacts with DTX1, the interaction is required
CC for deubiquitinating activity towards NOTCH1.
CC -!- INTERACTION:
CC P21127:CDK11B; NbExp=3; IntAct=EBI-711990, EBI-1298;
CC P55884:EIF3B; NbExp=3; IntAct=EBI-711990, EBI-366696;
CC Q969P5:FBXO32; NbExp=7; IntAct=EBI-711990, EBI-2932534;
CC Q9Q2G4:ORF (xeno); NbExp=3; IntAct=EBI-711990, EBI-6248094;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- DOMAIN: The MPN domain mediates deubiquitinating activity.
CC -!- PTM: Phosphorylation is enhanced upon serum stimulation.
CC Phosphorylated during apoptosis by caspase-processed CDK11.
CC -!- MASS SPECTROMETRY: Mass=37554.8; Method=Unknown; Range=1-357;
CC Source=PubMed:17322308;
CC -!- MASS SPECTROMETRY: Mass=37475.6; Mass_error=0.2; Method=MALDI;
CC Range=1-357; Source=PubMed:18599441;
CC -!- SIMILARITY: Belongs to the eIF-3 subunit F family.
CC -!- SIMILARITY: Contains 1 MPN (JAB/Mov34) domain.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/EIF3FID44407ch11p15.html";
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DR EMBL; U94855; AAD03467.1; -; mRNA.
DR EMBL; AK095574; BAC04577.1; -; mRNA.
DR EMBL; AK289637; BAF82326.1; -; mRNA.
DR EMBL; AK291354; BAF84043.1; -; mRNA.
DR EMBL; BT006894; AAP35540.1; -; mRNA.
DR EMBL; CR456959; CAG33240.1; -; mRNA.
DR EMBL; BC000490; AAH00490.1; -; mRNA.
DR RefSeq; NP_003745.1; NM_003754.2.
DR UniGene; Hs.516023; -.
DR ProteinModelPortal; O00303; -.
DR SMR; O00303; 92-293.
DR DIP; DIP-35580N; -.
DR IntAct; O00303; 22.
DR MINT; MINT-5000761; -.
DR STRING; 9606.ENSP00000310040; -.
DR ChEMBL; CHEMBL2062352; -.
DR MEROPS; M67.974; -.
DR PhosphoSite; O00303; -.
DR PaxDb; O00303; -.
DR PRIDE; O00303; -.
DR DNASU; 8665; -.
DR Ensembl; ENST00000309828; ENSP00000310040; ENSG00000175390.
DR Ensembl; ENST00000533626; ENSP00000431800; ENSG00000175390.
DR GeneID; 8665; -.
DR KEGG; hsa:8665; -.
DR UCSC; uc001mfw.3; human.
DR CTD; 8665; -.
DR GeneCards; GC11P007966; -.
DR HGNC; HGNC:3275; EIF3F.
DR HPA; HPA049250; -.
DR MIM; 603914; gene.
DR neXtProt; NX_O00303; -.
DR PharmGKB; PA162384806; -.
DR eggNOG; COG1310; -.
DR HOGENOM; HOG000241154; -.
DR HOVERGEN; HBG107843; -.
DR InParanoid; O00303; -.
DR KO; K03249; -.
DR OrthoDB; EOG77T152; -.
DR PhylomeDB; O00303; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_71; Gene Expression.
DR GeneWiki; EIF3F; -.
DR GenomeRNAi; 8665; -.
DR NextBio; 32503; -.
DR PRO; PR:O00303; -.
DR ArrayExpress; O00303; -.
DR Bgee; O00303; -.
DR CleanEx; HS_EIF3F; -.
DR Genevestigator; O00303; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-HAMAP.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-HAMAP.
DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:UniProtKB.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; TAS:UniProtKB.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IEA:UniProtKB-HAMAP.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0006446; P:regulation of translational initiation; IEA:UniProtKB-HAMAP.
DR HAMAP; MF_03005; eIF3f; 1; -.
DR InterPro; IPR027531; eIF3f.
DR InterPro; IPR000555; JAB_MPN_dom.
DR InterPro; IPR024969; Rpn11/EIF3F_C.
DR Pfam; PF01398; JAB; 1.
DR Pfam; PF13012; MitMem_reg; 1.
DR SMART; SM00232; JAB_MPN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Hydrolase;
KW Initiation factor; Phosphoprotein; Polymorphism; Protease;
KW Protein biosynthesis; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 357 Eukaryotic translation initiation factor
FT 3 subunit F.
FT /FTId=PRO_0000213964.
FT DOMAIN 87 196 MPN.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 46 46 Phosphoserine; by CDK11; in vitro.
FT MOD_RES 238 238 N6-acetyllysine.
FT MOD_RES 258 258 Phosphoserine.
FT VARIANT 39 39 P -> L (in dbSNP:rs1043738).
FT /FTId=VAR_029267.
FT VARIANT 172 172 W -> L (in dbSNP:rs1044058).
FT /FTId=VAR_014452.
FT CONFLICT 50 56 Missing (in Ref. 2; BAC04577).
SQ SEQUENCE 357 AA; 37564 MW; 8A70FC6E2BF07737 CRC64;
MATPAVPVSA PPATPTPVPA AAPASVPAPT PAPAAAPVPA AAPASSSDPA AAAAATAAPG
QTPASAQAPA QTPAPALPGP ALPGPFPGGR VVRLHPVILA SIVDSYERRN EGAARVIGTL
LGTVDKHSVE VTNCFSVPHN ESEDEVAVDM EFAKNMYELH KKVSPNELIL GWYATGHDIT
EHSVLIHEYY SREAPNPIHL TVDTSLQNGR MSIKAYVSTL MGVPGRTMGV MFTPLTVKYA
YYDTERIGVD LIMKTCFSPN RVIGLSSDLQ QVGGASARIQ DALSTVLQYA EDVLSGKVSA
DNTVGRFLMS LVNQVPKIVP DDFETMLNSN INDLLMVTYL ANLTQSQIAL NEKLVNL
//
ID EIF3F_HUMAN Reviewed; 357 AA.
AC O00303; A8K0S2; Q6IB45; Q8N978;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUL-1997, sequence version 1.
DT 22-JAN-2014, entry version 133.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit F;
DE Short=eIF3f;
DE AltName: Full=Deubiquitinating enzyme eIF3f;
DE EC=3.4.19.12;
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 5;
DE AltName: Full=eIF-3-epsilon;
DE AltName: Full=eIF3 p47;
GN Name=EIF3F; Synonyms=EIF3S5;
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 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 [LARGE SCALE MRNA].
RC TISSUE=Amygdala, and Brain;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP PHOSPHORYLATION AT SER-46.
RX PubMed=12446680; DOI=10.1074/jbc.M206427200;
RA Shi J., Feng Y., Goulet A.C., Vaillancourt R.R., Sachs N.A.,
RA Hershey J.W., Nelson M.A.;
RT "The p34cdc2-related cyclin-dependent kinase 11 interacts with the p47
RT subunit of eukaryotic initiation factor 3 during apoptosis.";
RL J. Biol. Chem. 278:5062-5071(2003).
RN [7]
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 [8]
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 [9]
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 [10]
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 [11]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3
RP COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2,
RP PHOSPHORYLATION AT SER-258, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP IDENTIFICATION BY 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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-238, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
RP INTERACTION WITH RNF139.
RX PubMed=20068067; DOI=10.1158/1541-7786.MCR-08-0491;
RA Lee J.P., Brauweiler A., Rudolph M., Hooper J.E., Drabkin H.A.,
RA Gemmill R.M.;
RT "The TRC8 ubiquitin ligase is sterol regulated and interacts with
RT lipid and protein biosynthetic pathways.";
RL Mol. Cancer Res. 8:93-106(2010).
RN [16]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3
RP COMPLEX, MASS SPECTROMETRY, AND INTERACTION WITH EIF3B; EIF3H 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 [17]
RP FUNCTION AS A DEUBIQUITINATING ENZYME, CATALYTIC ACTIVITY, AND
RP INTERACTION WITH DTX1.
RX PubMed=21124883; DOI=10.1371/journal.pbio.1000545;
RA Moretti J., Chastagner P., Gastaldello S., Heuss S.F., Dirac A.M.,
RA Bernards R., Masucci M.G., Israel A., Brou C.;
RT "The translation initiation factor 3f (eIF3f) exhibits a
RT deubiquitinase activity regulating Notch activation.";
RL PLoS Biol. 8:E1000545-E1000545(2010).
RN [18]
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [19]
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.,
RA Buerckstuemmer T., 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 [20]
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.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [21]
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 post-termination ribosomal complexes and
CC subsequently prevents premature joining of the 40S and 60S
CC ribosomal subunits prior to initiation.
CC -!- FUNCTION: Deubiquitinates activated NOTCH1, promoting its nuclear
CC import, thereby acting as a positive regulator of Notch signaling.
CC -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC thioester, amide, peptide and isopeptide bonds formed by the C-
CC terminal Gly of ubiquitin (a 76-residue protein attached to
CC proteins as an intracellular targeting signal).
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 MTOR and
CC RPTOR, leading to phosphorylation and release of RPS6KB1 and
CC binding of EIF4B to eIF-3. Interacts with RNF139; the interaction
CC leads to protein translation inhibitions in a ubiquitination-
CC dependent manner. Interacts with DTX1, the interaction is required
CC for deubiquitinating activity towards NOTCH1.
CC -!- INTERACTION:
CC P21127:CDK11B; NbExp=3; IntAct=EBI-711990, EBI-1298;
CC P55884:EIF3B; NbExp=3; IntAct=EBI-711990, EBI-366696;
CC Q969P5:FBXO32; NbExp=7; IntAct=EBI-711990, EBI-2932534;
CC Q9Q2G4:ORF (xeno); NbExp=3; IntAct=EBI-711990, EBI-6248094;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- DOMAIN: The MPN domain mediates deubiquitinating activity.
CC -!- PTM: Phosphorylation is enhanced upon serum stimulation.
CC Phosphorylated during apoptosis by caspase-processed CDK11.
CC -!- MASS SPECTROMETRY: Mass=37554.8; Method=Unknown; Range=1-357;
CC Source=PubMed:17322308;
CC -!- MASS SPECTROMETRY: Mass=37475.6; Mass_error=0.2; Method=MALDI;
CC Range=1-357; Source=PubMed:18599441;
CC -!- SIMILARITY: Belongs to the eIF-3 subunit F family.
CC -!- SIMILARITY: Contains 1 MPN (JAB/Mov34) domain.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/EIF3FID44407ch11p15.html";
CC -----------------------------------------------------------------------
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DR EMBL; U94855; AAD03467.1; -; mRNA.
DR EMBL; AK095574; BAC04577.1; -; mRNA.
DR EMBL; AK289637; BAF82326.1; -; mRNA.
DR EMBL; AK291354; BAF84043.1; -; mRNA.
DR EMBL; BT006894; AAP35540.1; -; mRNA.
DR EMBL; CR456959; CAG33240.1; -; mRNA.
DR EMBL; BC000490; AAH00490.1; -; mRNA.
DR RefSeq; NP_003745.1; NM_003754.2.
DR UniGene; Hs.516023; -.
DR ProteinModelPortal; O00303; -.
DR SMR; O00303; 92-293.
DR DIP; DIP-35580N; -.
DR IntAct; O00303; 22.
DR MINT; MINT-5000761; -.
DR STRING; 9606.ENSP00000310040; -.
DR ChEMBL; CHEMBL2062352; -.
DR MEROPS; M67.974; -.
DR PhosphoSite; O00303; -.
DR PaxDb; O00303; -.
DR PRIDE; O00303; -.
DR DNASU; 8665; -.
DR Ensembl; ENST00000309828; ENSP00000310040; ENSG00000175390.
DR Ensembl; ENST00000533626; ENSP00000431800; ENSG00000175390.
DR GeneID; 8665; -.
DR KEGG; hsa:8665; -.
DR UCSC; uc001mfw.3; human.
DR CTD; 8665; -.
DR GeneCards; GC11P007966; -.
DR HGNC; HGNC:3275; EIF3F.
DR HPA; HPA049250; -.
DR MIM; 603914; gene.
DR neXtProt; NX_O00303; -.
DR PharmGKB; PA162384806; -.
DR eggNOG; COG1310; -.
DR HOGENOM; HOG000241154; -.
DR HOVERGEN; HBG107843; -.
DR InParanoid; O00303; -.
DR KO; K03249; -.
DR OrthoDB; EOG77T152; -.
DR PhylomeDB; O00303; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_71; Gene Expression.
DR GeneWiki; EIF3F; -.
DR GenomeRNAi; 8665; -.
DR NextBio; 32503; -.
DR PRO; PR:O00303; -.
DR ArrayExpress; O00303; -.
DR Bgee; O00303; -.
DR CleanEx; HS_EIF3F; -.
DR Genevestigator; O00303; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-HAMAP.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-HAMAP.
DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:UniProtKB.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; TAS:UniProtKB.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IEA:UniProtKB-HAMAP.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0006446; P:regulation of translational initiation; IEA:UniProtKB-HAMAP.
DR HAMAP; MF_03005; eIF3f; 1; -.
DR InterPro; IPR027531; eIF3f.
DR InterPro; IPR000555; JAB_MPN_dom.
DR InterPro; IPR024969; Rpn11/EIF3F_C.
DR Pfam; PF01398; JAB; 1.
DR Pfam; PF13012; MitMem_reg; 1.
DR SMART; SM00232; JAB_MPN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Hydrolase;
KW Initiation factor; Phosphoprotein; Polymorphism; Protease;
KW Protein biosynthesis; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 357 Eukaryotic translation initiation factor
FT 3 subunit F.
FT /FTId=PRO_0000213964.
FT DOMAIN 87 196 MPN.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 46 46 Phosphoserine; by CDK11; in vitro.
FT MOD_RES 238 238 N6-acetyllysine.
FT MOD_RES 258 258 Phosphoserine.
FT VARIANT 39 39 P -> L (in dbSNP:rs1043738).
FT /FTId=VAR_029267.
FT VARIANT 172 172 W -> L (in dbSNP:rs1044058).
FT /FTId=VAR_014452.
FT CONFLICT 50 56 Missing (in Ref. 2; BAC04577).
SQ SEQUENCE 357 AA; 37564 MW; 8A70FC6E2BF07737 CRC64;
MATPAVPVSA PPATPTPVPA AAPASVPAPT PAPAAAPVPA AAPASSSDPA AAAAATAAPG
QTPASAQAPA QTPAPALPGP ALPGPFPGGR VVRLHPVILA SIVDSYERRN EGAARVIGTL
LGTVDKHSVE VTNCFSVPHN ESEDEVAVDM EFAKNMYELH KKVSPNELIL GWYATGHDIT
EHSVLIHEYY SREAPNPIHL TVDTSLQNGR MSIKAYVSTL MGVPGRTMGV MFTPLTVKYA
YYDTERIGVD LIMKTCFSPN RVIGLSSDLQ QVGGASARIQ DALSTVLQYA EDVLSGKVSA
DNTVGRFLMS LVNQVPKIVP DDFETMLNSN INDLLMVTYL ANLTQSQIAL NEKLVNL
//
MIM
603914
*RECORD*
*FIELD* NO
603914
*FIELD* TI
*603914 EUKARYOTIC TRANSLATION INITIATION FACTOR 3, SUBUNIT F; EIF3F
;;EIF3-p47;;
EUKARYOTIC TRANSLATION INITIATION FACTOR 3, SUBUNIT 5, FORMERLY; EIF3S5,
read moreFORMERLY
*FIELD* TX
DESCRIPTION
Eukaryotic initiation factor-3 (eIF3) is the largest of the eIFs and
consists of at least 10 nonidentical subunits, including p47 (EIF3F), in
mammals (Asano et al., 1997). For further background information on
eIF3, see p66 (EIF3S7; 603915).
CLONING
By searching EST databases with the partial protein sequences of rabbit
p66, p47, and p40 (603912), Asano et al. (1997) identified cDNAs
encoding the human homologs. Although the predicted 357-amino acid human
p47 protein has a calculated molecular mass of 37.5 kD, it migrates at
47 kD by SDS-PAGE. The authors attributed the anomalous migration to the
high proline content of the N-terminal region of p47. Sequence analysis
revealed that the N-terminal halves of p40 and p47 are similar to each
other and are related to the mouse Mov34 protein (157970). Northern blot
analysis revealed that p47 is expressed as a 1.3-kb mRNA in HeLa cells.
MAPPING
Hartz (2012) mapped the EIF3F gene to chromosome 11p15.4 based on an
alignment of the EIF3F sequence (GenBank GENBANK BC000490) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Asano, K.; Vornlocher, H.-P.; Richter-Cook, N. J.; Merrick, W.
C.; Hinnebusch, A. G.; Hershey, J. W. B.: Structure of cDNAs encoding
human eukaryotic initiation factor 3 subunits: possible roles in DNA
binding and macromolecular assembly. J. Biol. Chem. 272: 27042-27052,
1997.
2. Hartz, P. A.: Personal Communication. Baltimore, Md. 7/11/2012.
*FIELD* CN
Patricia A. Hartz - updated: 7/11/2012
*FIELD* CD
Rebekah S. Rasooly: 6/16/1999
*FIELD* ED
mgross: 07/18/2012
terry: 7/11/2012
mgross: 10/2/2007
alopez: 6/17/1999
*RECORD*
*FIELD* NO
603914
*FIELD* TI
*603914 EUKARYOTIC TRANSLATION INITIATION FACTOR 3, SUBUNIT F; EIF3F
;;EIF3-p47;;
EUKARYOTIC TRANSLATION INITIATION FACTOR 3, SUBUNIT 5, FORMERLY; EIF3S5,
read moreFORMERLY
*FIELD* TX
DESCRIPTION
Eukaryotic initiation factor-3 (eIF3) is the largest of the eIFs and
consists of at least 10 nonidentical subunits, including p47 (EIF3F), in
mammals (Asano et al., 1997). For further background information on
eIF3, see p66 (EIF3S7; 603915).
CLONING
By searching EST databases with the partial protein sequences of rabbit
p66, p47, and p40 (603912), Asano et al. (1997) identified cDNAs
encoding the human homologs. Although the predicted 357-amino acid human
p47 protein has a calculated molecular mass of 37.5 kD, it migrates at
47 kD by SDS-PAGE. The authors attributed the anomalous migration to the
high proline content of the N-terminal region of p47. Sequence analysis
revealed that the N-terminal halves of p40 and p47 are similar to each
other and are related to the mouse Mov34 protein (157970). Northern blot
analysis revealed that p47 is expressed as a 1.3-kb mRNA in HeLa cells.
MAPPING
Hartz (2012) mapped the EIF3F gene to chromosome 11p15.4 based on an
alignment of the EIF3F sequence (GenBank GENBANK BC000490) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Asano, K.; Vornlocher, H.-P.; Richter-Cook, N. J.; Merrick, W.
C.; Hinnebusch, A. G.; Hershey, J. W. B.: Structure of cDNAs encoding
human eukaryotic initiation factor 3 subunits: possible roles in DNA
binding and macromolecular assembly. J. Biol. Chem. 272: 27042-27052,
1997.
2. Hartz, P. A.: Personal Communication. Baltimore, Md. 7/11/2012.
*FIELD* CN
Patricia A. Hartz - updated: 7/11/2012
*FIELD* CD
Rebekah S. Rasooly: 6/16/1999
*FIELD* ED
mgross: 07/18/2012
terry: 7/11/2012
mgross: 10/2/2007
alopez: 6/17/1999