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Eukaryotic translation initiation factor 3 subunit F (eIF3f) (Deubiquitinating enzyme eIF3f) (EC 3.4.19.12) (Eukaryotic translation initiation factor 3 subunit 5) (eIF-3-epsilon) (eIF3 p47)

 EIF3F_HUMAN             Reviewed;         357 AA.
O00303; A8K0S2; Q6IB45; Q8N978;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
18-JUL-2018, entry version 178.
RecName: Full=Eukaryotic translation initiation factor 3 subunit F {ECO:0000255|HAMAP-Rule:MF_03005};
Short=eIF3f {ECO:0000255|HAMAP-Rule:MF_03005};
AltName: Full=Deubiquitinating enzyme eIF3f;
EC=3.4.19.12;
AltName: Full=Eukaryotic translation initiation factor 3 subunit 5 {ECO:0000255|HAMAP-Rule:MF_03005};
AltName: Full=eIF-3-epsilon {ECO:0000255|HAMAP-Rule:MF_03005};
AltName: Full=eIF3 p47 {ECO:0000255|HAMAP-Rule:MF_03005};
Name=EIF3F {ECO:0000255|HAMAP-Rule:MF_03005};
Synonyms=EIF3S5 {ECO:0000255|HAMAP-Rule:MF_03005};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=9341143; DOI=10.1074/jbc.272.43.27042;
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 RNA binding and macromolecular assembly.";
J. Biol. Chem. 272:27042-27052(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Amygdala, and Brain;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PHOSPHORYLATION AT SER-46.
PubMed=12446680; DOI=10.1074/jbc.M206427200;
Shi J., Feng Y., Goulet A.C., Vaillancourt R.R., Sachs N.A.,
Hershey J.W., Nelson M.A.;
"The p34cdc2-related cyclin-dependent kinase 11 interacts with the p47
subunit of eukaryotic initiation factor 3 during apoptosis.";
J. Biol. Chem. 278:5062-5071(2003).
[7]
INTERACTION WITH RPS6KB1, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16286006; DOI=10.1016/j.cell.2005.10.024;
Holz M.K., Ballif B.A., Gygi S.P., Blenis J.;
"mTOR and S6K1 mediate assembly of the translation preinitiation
complex through dynamic protein interchange and ordered
phosphorylation events.";
Cell 123:569-580(2005).
[8]
CHARACTERIZATION OF THE EIF-3 COMPLEX.
PubMed=15703437; DOI=10.1261/rna.7215305;
Kolupaeva V.G., Unbehaun A., Lomakin I.B., Hellen C.U.T.,
Pestova T.V.;
"Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits
and its role in ribosomal dissociation and anti-association.";
RNA 11:470-486(2005).
[9]
IDENTIFICATION IN THE EIF-3 COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=16766523; DOI=10.1074/jbc.M605418200;
LeFebvre A.K., Korneeva N.L., Trutschl M., Cvek U., Duzan R.D.,
Bradley C.A., Hershey J.W.B., Rhoads R.E.;
"Translation initiation factor eIF4G-1 binds to eIF3 through the eIF3e
subunit.";
J. Biol. Chem. 281:22917-22932(2006).
[10]
FUNCTION, AND CHARACTERIZATION OF THE EIF-3 COMPLEX.
PubMed=17581632; DOI=10.1038/sj.emboj.7601765;
Masutani M., Sonenberg N., Yokoyama S., Imataka H.;
"Reconstitution reveals the functional core of mammalian eIF3.";
EMBO J. 26:3373-3383(2007).
[11]
IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3
COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2,
PHOSPHORYLATION AT SER-258, AND MASS SPECTROMETRY.
PubMed=17322308; DOI=10.1074/mcp.M600399-MCP200;
Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L.,
Hershey J.W.B., Doudna J.A., Robinson C.V., Leary J.A.;
"Structural characterization of the human eukaryotic initiation factor
3 protein complex by mass spectrometry.";
Mol. Cell. Proteomics 6:1135-1146(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-238, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[15]
INTERACTION WITH RNF139.
PubMed=20068067; DOI=10.1158/1541-7786.MCR-08-0491;
Lee J.P., Brauweiler A., Rudolph M., Hooper J.E., Drabkin H.A.,
Gemmill R.M.;
"The TRC8 ubiquitin ligase is sterol regulated and interacts with
lipid and protein biosynthetic pathways.";
Mol. Cancer Res. 8:93-106(2010).
[16]
IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3
COMPLEX, MASS SPECTROMETRY, AND INTERACTION WITH EIF3B; EIF3H AND
EIF3M.
PubMed=18599441; DOI=10.1073/pnas.0801313105;
Zhou M., Sandercock A.M., Fraser C.S., Ridlova G., Stephens E.,
Schenauer M.R., Yokoi-Fong T., Barsky D., Leary J.A., Hershey J.W.B.,
Doudna J.A., Robinson C.V.;
"Mass spectrometry reveals modularity and a complete subunit
interaction map of the eukaryotic translation factor eIF3.";
Proc. Natl. Acad. Sci. U.S.A. 105:18139-18144(2008).
[17]
FUNCTION AS A DEUBIQUITINATING ENZYME, CATALYTIC ACTIVITY, AND
INTERACTION WITH DTX1.
PubMed=21124883; DOI=10.1371/journal.pbio.1000545;
Moretti J., Chastagner P., Gastaldello S., Heuss S.F., Dirac A.M.,
Bernards R., Masucci M.G., Israel A., Brou C.;
"The translation initiation factor 3f (eIF3f) exhibits a
deubiquitinase activity regulating Notch activation.";
PLoS Biol. 8:E1000545-E1000545(2010).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[23]
FUNCTION, AND IDENTIFICATION IN THE EIF-3 COMPLEX.
PubMed=25849773; DOI=10.1038/nature14267;
Lee A.S., Kranzusch P.J., Cate J.H.;
"eIF3 targets cell-proliferation messenger RNAs for translational
activation or repression.";
Nature 522:111-114(2015).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[25]
FUNCTION.
PubMed=27462815; DOI=10.1038/nature18954;
Lee A.S., Kranzusch P.J., Doudna J.A., Cate J.H.;
"eIF3d is an mRNA cap-binding protein that is required for specialized
translation initiation.";
Nature 536:96-99(2016).
[26]
3D-STRUCTURE MODELING, AND ELECTRON MICROSCOPY.
PubMed=16322461; DOI=10.1126/science.1118977;
Siridechadilok B., Fraser C.S., Hall R.J., Doudna J.A., Nogales E.;
"Structural roles for human translation factor eIF3 in initiation of
protein synthesis.";
Science 310:1513-1515(2005).
-!- FUNCTION: Component of the eukaryotic translation initiation
factor 3 (eIF-3) complex, which is required for several steps in
the initiation of protein synthesis (PubMed:17581632,
PubMed:25849773, PubMed:27462815). The eIF-3 complex associates
with the 40S ribosome and facilitates the recruitment of eIF-1,
eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-
initiation complex (43S PIC). The eIF-3 complex stimulates mRNA
recruitment to the 43S PIC and scanning of the mRNA for AUG
recognition. The eIF-3 complex is also required for disassembly
and recycling of post-termination ribosomal complexes and
subsequently prevents premature joining of the 40S and 60S
ribosomal subunits prior to initiation (PubMed:17581632). The eIF-
3 complex specifically targets and initiates translation of a
subset of mRNAs involved in cell proliferation, including cell
cycling, differentiation and apoptosis, and uses different modes
of RNA stem-loop binding to exert either translational activation
or repression (PubMed:25849773). {ECO:0000255|HAMAP-Rule:MF_03005,
ECO:0000269|PubMed:17581632, ECO:0000269|PubMed:25849773,
ECO:0000269|PubMed:27462815}.
-!- FUNCTION: Deubiquitinates activated NOTCH1, promoting its nuclear
import, thereby acting as a positive regulator of Notch signaling.
{ECO:0000269|PubMed:21124883}.
-!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
thioester, amide, peptide and isopeptide bonds formed by the C-
terminal Gly of ubiquitin (a 76-residue protein attached to
proteins as an intracellular targeting signal).
{ECO:0000269|PubMed:21124883}.
-!- SUBUNIT: Component of the eukaryotic translation initiation factor
3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B,
EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K,
EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable
modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I;
module B is composed of EIF3F, EIF3H, and EIF3M; and module C is
composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module
C binds EIF3B of module A and EIF3H of module B, thereby linking
the three modules. EIF3J is a labile subunit that binds to the
eIF-3 complex via EIF3B. The eIF-3 complex interacts with RPS6KB1
under conditions of nutrient depletion. Mitogenic stimulation
leads to binding and activation of a complex composed of MTOR and
RPTOR, leading to phosphorylation and release of RPS6KB1 and
binding of EIF4B to eIF-3. Interacts with RNF139; the interaction
leads to protein translation inhibitions in a ubiquitination-
dependent manner. Interacts with DTX1, the interaction is required
for deubiquitinating activity towards NOTCH1. {ECO:0000255|HAMAP-
Rule:MF_03005, ECO:0000269|PubMed:16286006,
ECO:0000269|PubMed:16766523, ECO:0000269|PubMed:17322308,
ECO:0000269|PubMed:18599441, ECO:0000269|PubMed:20068067,
ECO:0000269|PubMed:21124883, ECO:0000269|PubMed:25849773}.
-!- INTERACTION:
P21127:CDK11B; NbExp=3; IntAct=EBI-711990, EBI-1298;
Q14152:EIF3A; NbExp=15; IntAct=EBI-711990, EBI-366617;
P55884:EIF3B; NbExp=8; IntAct=EBI-711990, EBI-366696;
O15372:EIF3H; NbExp=6; IntAct=EBI-711990, EBI-709735;
Q7L2H7:EIF3M; NbExp=14; IntAct=EBI-711990, EBI-353901;
Q969P5:FBXO32; NbExp=7; IntAct=EBI-711990, EBI-2932534;
Q53GS7:GLE1; NbExp=2; IntAct=EBI-711990, EBI-1955541;
O15457:MSH4; NbExp=6; IntAct=EBI-711990, EBI-6092777;
Q9Q2G4:ORF (xeno); NbExp=3; IntAct=EBI-711990, EBI-6248094;
P78424:POU6F2; NbExp=4; IntAct=EBI-711990, EBI-12029004;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03005}.
-!- DOMAIN: The MPN domain mediates deubiquitinating activity.
-!- PTM: Phosphorylation is enhanced upon serum stimulation.
Phosphorylated during apoptosis by caspase-processed CDK11.
{ECO:0000269|PubMed:12446680, ECO:0000269|PubMed:17322308}.
-!- MASS SPECTROMETRY: Mass=37554.8; Method=Unknown; Range=1-357;
Evidence={ECO:0000269|PubMed:17322308};
-!- MASS SPECTROMETRY: Mass=37475.6; Mass_error=0.2; Method=MALDI;
Range=1-357; Evidence={ECO:0000269|PubMed:18599441};
-!- SIMILARITY: Belongs to the eIF-3 subunit F family.
{ECO:0000255|HAMAP-Rule:MF_03005}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/EIF3FID44407ch11p15.html";
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EMBL; U94855; AAD03467.1; -; mRNA.
EMBL; AK095574; BAC04577.1; -; mRNA.
EMBL; AK289637; BAF82326.1; -; mRNA.
EMBL; AK291354; BAF84043.1; -; mRNA.
EMBL; BT006894; AAP35540.1; -; mRNA.
EMBL; CR456959; CAG33240.1; -; mRNA.
EMBL; BC000490; AAH00490.1; -; mRNA.
CCDS; CCDS7785.1; -.
RefSeq; NP_003745.1; NM_003754.2.
UniGene; Hs.516023; -.
PDB; 3J8B; EM; -; F=1-257.
PDB; 3J8C; EM; -; F=1-257.
PDBsum; 3J8B; -.
PDBsum; 3J8C; -.
ProteinModelPortal; O00303; -.
SMR; O00303; -.
BioGrid; 114214; 100.
CORUM; O00303; -.
DIP; DIP-35580N; -.
IntAct; O00303; 71.
MINT; O00303; -.
STRING; 9606.ENSP00000310040; -.
ChEMBL; CHEMBL2062352; -.
MEROPS; M67.974; -.
iPTMnet; O00303; -.
PhosphoSitePlus; O00303; -.
SwissPalm; O00303; -.
BioMuta; EIF3F; -.
EPD; O00303; -.
MaxQB; O00303; -.
PaxDb; O00303; -.
PeptideAtlas; O00303; -.
PRIDE; O00303; -.
ProteomicsDB; 47830; -.
DNASU; 8665; -.
Ensembl; ENST00000309828; ENSP00000310040; ENSG00000175390.
Ensembl; ENST00000533626; ENSP00000431800; ENSG00000175390.
Ensembl; ENST00000626223; ENSP00000485772; ENSG00000280606.
Ensembl; ENST00000628056; ENSP00000486798; ENSG00000280606.
GeneID; 8665; -.
KEGG; hsa:8665; -.
UCSC; uc001mfw.5; human.
CTD; 8665; -.
DisGeNET; 8665; -.
EuPathDB; HostDB:ENSG00000175390.12; -.
GeneCards; EIF3F; -.
HGNC; HGNC:3275; EIF3F.
HPA; HPA049250; -.
MIM; 603914; gene.
neXtProt; NX_O00303; -.
OpenTargets; ENSG00000175390; -.
PharmGKB; PA162384806; -.
eggNOG; KOG2975; Eukaryota.
eggNOG; COG1310; LUCA.
GeneTree; ENSGT00530000063075; -.
HOGENOM; HOG000241154; -.
HOVERGEN; HBG107843; -.
InParanoid; O00303; -.
KO; K03249; -.
OMA; AVDMEYH; -.
OrthoDB; EOG091G0EMR; -.
PhylomeDB; O00303; -.
TreeFam; TF101517; -.
Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
Reactome; R-HSA-72649; Translation initiation complex formation.
Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
SIGNOR; O00303; -.
ChiTaRS; EIF3F; human.
GeneWiki; EIF3F; -.
GenomeRNAi; 8665; -.
PRO; PR:O00303; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000175390; -.
CleanEx; HS_EIF3F; -.
ExpressionAtlas; O00303; baseline and differential.
Genevisible; O00303; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:UniProtKB.
GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IBA:GO_Central.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IDA:FlyBase.
GO; GO:0003743; F:translation initiation factor activity; TAS:UniProtKB.
GO; GO:0031369; F:translation initiation factor binding; IBA:GO_Central.
GO; GO:0075522; P:IRES-dependent viral translational initiation; IDA:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; IDA:FlyBase.
GO; GO:0006413; P:translational initiation; IDA:UniProtKB.
CDD; cd08064; MPN_eIF3f; 1.
HAMAP; MF_03005; eIF3f; 1.
InterPro; IPR027531; eIF3f.
InterPro; IPR000555; JAMM/MPN+_dom.
InterPro; IPR037518; MPN.
InterPro; IPR024969; Rpn11/EIF3F_C.
PANTHER; PTHR10540:SF6; PTHR10540:SF6; 1.
Pfam; PF01398; JAB; 1.
Pfam; PF13012; MitMem_reg; 1.
SMART; SM00232; JAB_MPN; 1.
PROSITE; PS50249; MPN; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm; Hydrolase;
Initiation factor; Phosphoprotein; Polymorphism; Protease;
Protein biosynthesis; Reference proteome; Thiol protease;
Ubl conjugation pathway.
INIT_MET 1 1 Removed. {ECO:0000255|HAMAP-
Rule:MF_03005,
ECO:0000269|PubMed:17322308}.
CHAIN 2 357 Eukaryotic translation initiation factor
3 subunit F.
/FTId=PRO_0000213964.
DOMAIN 92 222 MPN. {ECO:0000255|PROSITE-
ProRule:PRU01182}.
MOD_RES 2 2 N-acetylalanine. {ECO:0000255|HAMAP-
Rule:MF_03005,
ECO:0000269|PubMed:17322308}.
MOD_RES 46 46 Phosphoserine; by CDK11; in vitro.
{ECO:0000255|HAMAP-Rule:MF_03005,
ECO:0000269|PubMed:12446680}.
MOD_RES 238 238 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 258 258 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000255|HAMAP-Rule:MF_03005,
ECO:0000269|PubMed:17322308}.
VARIANT 39 39 P -> L (in dbSNP:rs1043738).
/FTId=VAR_029267.
VARIANT 172 172 W -> L (in dbSNP:rs1044058).
/FTId=VAR_014452.
CONFLICT 50 56 Missing (in Ref. 2; BAC04577).
{ECO:0000305}.
STRAND 91 94 {ECO:0000244|PDB:3J8B}.
HELIX 96 109 {ECO:0000244|PDB:3J8B}.
STRAND 117 123 {ECO:0000244|PDB:3J8B}.
STRAND 125 136 {ECO:0000244|PDB:3J8B}.
STRAND 139 142 {ECO:0000244|PDB:3J8B}.
STRAND 145 148 {ECO:0000244|PDB:3J8B}.
HELIX 150 163 {ECO:0000244|PDB:3J8B}.
STRAND 167 174 {ECO:0000244|PDB:3J8B}.
HELIX 183 193 {ECO:0000244|PDB:3J8B}.
STRAND 194 196 {ECO:0000244|PDB:3J8B}.
STRAND 198 202 {ECO:0000244|PDB:3J8B}.
STRAND 208 210 {ECO:0000244|PDB:3J8B}.
STRAND 212 219 {ECO:0000244|PDB:3J8B}.
STRAND 231 239 {ECO:0000244|PDB:3J8B}.
HELIX 243 252 {ECO:0000244|PDB:3J8B}.
TURN 253 256 {ECO:0000244|PDB:3J8B}.
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


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