EIF3F_HUMAN
ID EIF3F_HUMAN Reviewed; 357 AA.
AC O00303; A8K0S2; Q6IB45; Q8N978;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit F {ECO:0000255|HAMAP-Rule:MF_03005};
DE Short=eIF3f {ECO:0000255|HAMAP-Rule:MF_03005};
DE AltName: Full=Deubiquitinating enzyme eIF3f;
DE EC=3.4.19.12;
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 5 {ECO:0000255|HAMAP-Rule:MF_03005};
DE AltName: Full=eIF-3-epsilon {ECO:0000255|HAMAP-Rule:MF_03005};
DE AltName: Full=eIF3 p47 {ECO:0000255|HAMAP-Rule:MF_03005};
GN Name=EIF3F {ECO:0000255|HAMAP-Rule:MF_03005};
GN Synonyms=EIF3S5 {ECO:0000255|HAMAP-Rule:MF_03005};
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 [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 subunits.
RT 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., 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 [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 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 project:
RT 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., Hershey J.W.,
RA 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 complex
RT through dynamic protein interchange and ordered 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., Pestova T.V.;
RT "Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits and
RT 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 FUNCTION, AND 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 COMPLEX,
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, PHOSPHORYLATION AT
RP 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., Hershey J.W.B.,
RA Doudna J.A., Robinson C.V., Leary J.A.;
RT "Structural characterization of the human eukaryotic initiation factor 3
RT protein complex by mass spectrometry.";
RL Mol. Cell. Proteomics 6:1135-1146(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA 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 lipid and
RT 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 COMPLEX,
RP MASS SPECTROMETRY, AND INTERACTION WITH EIF3B; EIF3H AND 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 interaction
RT 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 INTERACTION
RP 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 deubiquitinase
RT 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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT 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., 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 [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., 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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 [22]
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 [23]
RP FUNCTION, AND IDENTIFICATION IN THE EIF-3 COMPLEX.
RX PubMed=25849773; DOI=10.1038/nature14267;
RA Lee A.S., Kranzusch P.J., Cate J.H.;
RT "eIF3 targets cell-proliferation messenger RNAs for translational
RT activation or repression.";
RL Nature 522:111-114(2015).
RN [24]
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).
RN [25]
RP FUNCTION.
RX PubMed=27462815; DOI=10.1038/nature18954;
RA Lee A.S., Kranzusch P.J., Doudna J.A., Cate J.H.;
RT "eIF3d is an mRNA cap-binding protein that is required for specialized
RT translation initiation.";
RL Nature 536:96-99(2016).
RN [26]
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).
RN [27]
RP INVOLVEMENT IN MRT67, VARIANT MRT67 VAL-232, AND CHARACTERIZATION OF
RP VARIANT MRT67 VAL-232.
RX PubMed=30409806; DOI=10.1126/science.aar6731;
RG Deciphering Developmental Disorders Study;
RA Martin H.C., Jones W.D., McIntyre R., Sanchez-Andrade G., Sanderson M.,
RA Stephenson J.D., Jones C.P., Handsaker J., Gallone G., Bruntraeger M.,
RA McRae J.F., Prigmore E., Short P., Niemi M., Kaplanis J., Radford E.J.,
RA Akawi N., Balasubramanian M., Dean J., Horton R., Hulbert A., Johnson D.S.,
RA Johnson K., Kumar D., Lynch S.A., Mehta S.G., Morton J., Parker M.J.,
RA Splitt M., Turnpenny P.D., Vasudevan P.C., Wright M., Bassett A.,
RA Gerety S.S., Wright C.F., FitzPatrick D.R., Firth H.V., Hurles M.E.,
RA Barrett J.C.;
RT "Quantifying the contribution of recessive coding variation to
RT developmental disorders.";
RL Science 362:1161-1164(2018).
CC -!- FUNCTION: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex, which is required for several steps in the initiation
CC of protein synthesis (PubMed:17581632, PubMed:25849773,
CC PubMed:27462815). The eIF-3 complex associates with the 40S ribosome
CC and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-
CC tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The
CC eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning
CC of the mRNA for AUG recognition. The eIF-3 complex is also required for
CC disassembly and recycling of post-termination ribosomal complexes and
CC subsequently prevents premature joining of the 40S and 60S ribosomal
CC subunits prior to initiation (PubMed:17581632). The eIF-3 complex
CC specifically targets and initiates translation of a subset of mRNAs
CC involved in cell proliferation, including cell cycling, differentiation
CC and apoptosis, and uses different modes of RNA stem-loop binding to
CC exert either translational activation or repression (PubMed:25849773).
CC {ECO:0000255|HAMAP-Rule:MF_03005, ECO:0000269|PubMed:17581632,
CC ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:27462815}.
CC -!- FUNCTION: Deubiquitinates activated NOTCH1, promoting its nuclear
CC import, thereby acting as a positive regulator of Notch signaling.
CC {ECO:0000269|PubMed:21124883}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:21124883};
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C,
CC EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and
CC EIF3M. The eIF-3 complex appears to include 3 stable modules: module A
CC is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of
CC EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D,
CC EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and
CC EIF3H of module B, thereby linking the three modules. EIF3J is a labile
CC subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex
CC interacts with RPS6KB1 under conditions of nutrient depletion.
CC Mitogenic stimulation leads to binding and activation of a complex
CC composed of MTOR and RPTOR, leading to phosphorylation and release of
CC RPS6KB1 and binding of EIF4B to eIF-3. Interacts with RNF139; the
CC interaction leads to protein translation inhibitions in a
CC ubiquitination-dependent manner. Interacts with DTX1, the interaction
CC is required for deubiquitinating activity towards NOTCH1.
CC {ECO:0000255|HAMAP-Rule:MF_03005, ECO:0000269|PubMed:16286006,
CC ECO:0000269|PubMed:16766523, ECO:0000269|PubMed:17322308,
CC ECO:0000269|PubMed:18599441, ECO:0000269|PubMed:20068067,
CC ECO:0000269|PubMed:21124883, ECO:0000269|PubMed:25849773}.
CC -!- INTERACTION:
CC O00303; O95994: AGR2; NbExp=3; IntAct=EBI-711990, EBI-712648;
CC O00303; P54253: ATXN1; NbExp=4; IntAct=EBI-711990, EBI-930964;
CC O00303; P46379-2: BAG6; NbExp=3; IntAct=EBI-711990, EBI-10988864;
CC O00303; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-711990, EBI-747505;
CC O00303; Q7Z4U5-3: C6orf201; NbExp=3; IntAct=EBI-711990, EBI-18680706;
CC O00303; P55212: CASP6; NbExp=3; IntAct=EBI-711990, EBI-718729;
CC O00303; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-711990, EBI-744556;
CC O00303; A0A1B0GWI1: CCDC196; NbExp=5; IntAct=EBI-711990, EBI-10181422;
CC O00303; P21127: CDK11B; NbExp=3; IntAct=EBI-711990, EBI-1298;
CC O00303; P08123: COL1A2; NbExp=3; IntAct=EBI-711990, EBI-983038;
CC O00303; P99999: CYCS; NbExp=3; IntAct=EBI-711990, EBI-446479;
CC O00303; G5E9A7: DMWD; NbExp=3; IntAct=EBI-711990, EBI-10976677;
CC O00303; O14645: DNALI1; NbExp=3; IntAct=EBI-711990, EBI-395638;
CC O00303; P55884: EIF3B; NbExp=8; IntAct=EBI-711990, EBI-366696;
CC O00303; O00303: EIF3F; NbExp=3; IntAct=EBI-711990, EBI-711990;
CC O00303; O15372: EIF3H; NbExp=7; IntAct=EBI-711990, EBI-709735;
CC O00303; Q7L2H7: EIF3M; NbExp=19; IntAct=EBI-711990, EBI-353901;
CC O00303; A0A0C4DGQ7: EML2; NbExp=3; IntAct=EBI-711990, EBI-12112376;
CC O00303; Q8WU58: FAM222B; NbExp=3; IntAct=EBI-711990, EBI-2807642;
CC O00303; Q969P5: FBXO32; NbExp=7; IntAct=EBI-711990, EBI-2932534;
CC O00303; Q53GS7: GLE1; NbExp=2; IntAct=EBI-711990, EBI-1955541;
CC O00303; O14964: HGS; NbExp=3; IntAct=EBI-711990, EBI-740220;
CC O00303; P04792: HSPB1; NbExp=3; IntAct=EBI-711990, EBI-352682;
CC O00303; O43464: HTRA2; NbExp=3; IntAct=EBI-711990, EBI-517086;
CC O00303; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-711990, EBI-1055254;
CC O00303; O60333-2: KIF1B; NbExp=3; IntAct=EBI-711990, EBI-10975473;
CC O00303; O14901: KLF11; NbExp=3; IntAct=EBI-711990, EBI-948266;
CC O00303; P13473-2: LAMP2; NbExp=3; IntAct=EBI-711990, EBI-21591415;
CC O00303; Q9H000: MKRN2; NbExp=3; IntAct=EBI-711990, EBI-2341005;
CC O00303; O15457: MSH4; NbExp=6; IntAct=EBI-711990, EBI-6092777;
CC O00303; Q969H8: MYDGF; NbExp=3; IntAct=EBI-711990, EBI-718622;
CC O00303; Q9NP98: MYOZ1; NbExp=3; IntAct=EBI-711990, EBI-744402;
CC O00303; P35240-4: NF2; NbExp=3; IntAct=EBI-711990, EBI-1014514;
CC O00303; Q7Z3B4: NUP54; NbExp=3; IntAct=EBI-711990, EBI-741048;
CC O00303; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-711990, EBI-2811583;
CC O00303; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-711990, EBI-10302990;
CC O00303; Q16512: PKN1; NbExp=3; IntAct=EBI-711990, EBI-602382;
CC O00303; Q7Z3K3: POGZ; NbExp=3; IntAct=EBI-711990, EBI-1389308;
CC O00303; P78424: POU6F2; NbExp=6; IntAct=EBI-711990, EBI-12029004;
CC O00303; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-711990, EBI-5280197;
CC O00303; P60891: PRPS1; NbExp=3; IntAct=EBI-711990, EBI-749195;
CC O00303; P47224: RABIF; NbExp=5; IntAct=EBI-711990, EBI-713992;
CC O00303; Q13671: RIN1; NbExp=3; IntAct=EBI-711990, EBI-366017;
CC O00303; Q14D33: RTP5; NbExp=3; IntAct=EBI-711990, EBI-10217913;
CC O00303; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-711990, EBI-2623095;
CC O00303; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-711990, EBI-5235340;
CC O00303; P51687: SUOX; NbExp=3; IntAct=EBI-711990, EBI-3921347;
CC O00303; Q13148: TARDBP; NbExp=6; IntAct=EBI-711990, EBI-372899;
CC O00303; Q9Y5J6: TIMM10B; NbExp=3; IntAct=EBI-711990, EBI-1200382;
CC O00303; Q14119: VEZF1; NbExp=3; IntAct=EBI-711990, EBI-11980193;
CC O00303; O76024: WFS1; NbExp=3; IntAct=EBI-711990, EBI-720609;
CC O00303; A0A1U9X8X8; NbExp=3; IntAct=EBI-711990, EBI-17234977;
CC O00303; Q9Q2G4: ORF; Xeno; NbExp=3; IntAct=EBI-711990, EBI-6248094;
CC O00303; P11223: S; Xeno; NbExp=2; IntAct=EBI-711990, EBI-25497861;
CC O00303; P59594: S; Xeno; NbExp=5; IntAct=EBI-711990, EBI-15582614;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03005}.
CC -!- DOMAIN: The MPN domain mediates deubiquitinating activity.
CC -!- PTM: Phosphorylation is enhanced upon serum stimulation. Phosphorylated
CC during apoptosis by caspase-processed CDK11.
CC {ECO:0000269|PubMed:12446680, ECO:0000269|PubMed:17322308}.
CC -!- MASS SPECTROMETRY: Mass=37554.8; Method=Unknown;
CC Evidence={ECO:0000269|PubMed:17322308};
CC -!- MASS SPECTROMETRY: Mass=37475.6; Mass_error=0.2; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18599441};
CC -!- DISEASE: Intellectual developmental disorder, autosomal recessive 67
CC (MRT67) [MIM:618295]: A form of intellectual disability, a disorder
CC characterized by significantly below average general intellectual
CC functioning associated with impairments in adaptive behavior and
CC manifested during the developmental period. Some MRT67 patients
CC manifest seizures and sensorineural hearing loss.
CC {ECO:0000269|PubMed:30409806}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit F family. {ECO:0000255|HAMAP-
CC Rule:MF_03005}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC 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 CCDS; CCDS7785.1; -.
DR RefSeq; NP_003745.1; NM_003754.2.
DR PDB; 3J8B; EM; -; F=1-257.
DR PDB; 3J8C; EM; -; F=1-257.
DR PDB; 6YBD; EM; 3.30 A; 4=1-357.
DR PDB; 6ZMW; EM; 3.70 A; 4=1-357.
DR PDB; 6ZON; EM; 3.00 A; F=1-357.
DR PDB; 6ZP4; EM; 2.90 A; F=1-357.
DR PDB; 6ZVJ; EM; 3.80 A; F=89-357.
DR PDB; 7A09; EM; 3.50 A; F=1-357.
DR PDBsum; 3J8B; -.
DR PDBsum; 3J8C; -.
DR PDBsum; 6YBD; -.
DR PDBsum; 6ZMW; -.
DR PDBsum; 6ZON; -.
DR PDBsum; 6ZP4; -.
DR PDBsum; 6ZVJ; -.
DR PDBsum; 7A09; -.
DR AlphaFoldDB; O00303; -.
DR SMR; O00303; -.
DR BioGRID; 114214; 256.
DR ComplexPortal; CPX-6036; Eukaryotic translation initiation factor 3 complex.
DR CORUM; O00303; -.
DR DIP; DIP-35580N; -.
DR IntAct; O00303; 133.
DR MINT; O00303; -.
DR STRING; 9606.ENSP00000431800; -.
DR ChEMBL; CHEMBL2062352; -.
DR DrugBank; DB04216; Quercetin.
DR MEROPS; M67.974; -.
DR GlyGen; O00303; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O00303; -.
DR MetOSite; O00303; -.
DR PhosphoSitePlus; O00303; -.
DR SwissPalm; O00303; -.
DR BioMuta; EIF3F; -.
DR EPD; O00303; -.
DR jPOST; O00303; -.
DR MassIVE; O00303; -.
DR MaxQB; O00303; -.
DR PaxDb; O00303; -.
DR PeptideAtlas; O00303; -.
DR PRIDE; O00303; -.
DR ProteomicsDB; 47830; -.
DR Antibodypedia; 11428; 250 antibodies from 31 providers.
DR DNASU; 8665; -.
DR Ensembl; ENST00000533626.5; ENSP00000431800.1; ENSG00000175390.15.
DR Ensembl; ENST00000651655.1; ENSP00000499218.1; ENSG00000175390.15.
DR GeneID; 8665; -.
DR KEGG; hsa:8665; -.
DR MANE-Select; ENST00000651655.1; ENSP00000499218.1; NM_003754.3; NP_003745.1.
DR UCSC; uc001mfw.5; human.
DR CTD; 8665; -.
DR DisGeNET; 8665; -.
DR GeneCards; EIF3F; -.
DR HGNC; HGNC:3275; EIF3F.
DR HPA; ENSG00000175390; Low tissue specificity.
DR MalaCards; EIF3F; -.
DR MIM; 603914; gene.
DR MIM; 618295; phenotype.
DR neXtProt; NX_O00303; -.
DR OpenTargets; ENSG00000175390; -.
DR PharmGKB; PA162384806; -.
DR VEuPathDB; HostDB:ENSG00000175390; -.
DR eggNOG; KOG2975; Eukaryota.
DR GeneTree; ENSGT00950000183073; -.
DR HOGENOM; CLU_027018_0_1_1; -.
DR InParanoid; O00303; -.
DR OMA; MADTDSF; -.
DR OrthoDB; 1038775at2759; -.
DR PhylomeDB; O00303; -.
DR TreeFam; TF101517; -.
DR PathwayCommons; O00303; -.
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-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
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; O00303; -.
DR SIGNOR; O00303; -.
DR BioGRID-ORCS; 8665; 739 hits in 1083 CRISPR screens.
DR ChiTaRS; EIF3F; human.
DR GeneWiki; EIF3F; -.
DR GenomeRNAi; 8665; -.
DR Pharos; O00303; Tbio.
DR PRO; PR:O00303; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; O00303; protein.
DR Bgee; ENSG00000175390; Expressed in ganglionic eminence and 177 other tissues.
DR ExpressionAtlas; O00303; baseline and differential.
DR Genevisible; O00303; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:UniProtKB.
DR GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IDA:FlyBase.
DR GO; GO:0003743; F:translation initiation factor activity; TAS:UniProtKB.
DR GO; GO:0031369; F:translation initiation factor binding; IBA:GO_Central.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IC:ComplexPortal.
DR GO; GO:0075522; P:IRES-dependent viral translational initiation; IDA:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; IDA:FlyBase.
DR GO; GO:0006413; P:translational initiation; IDA:UniProtKB.
DR CDD; cd08064; MPN_eIF3f; 1.
DR HAMAP; MF_03005; eIF3f; 1.
DR InterPro; IPR027531; eIF3f.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR024969; Rpn11/EIF3F_C.
DR PANTHER; PTHR10540:SF16; PTHR10540:SF16; 1.
DR Pfam; PF01398; JAB; 1.
DR Pfam; PF13012; MitMem_reg; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR PROSITE; PS50249; MPN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Disease variant; Hydrolase;
KW Initiation factor; Intellectual disability; Phosphoprotein; Protease;
KW Protein biosynthesis; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03005,
FT ECO:0000269|PubMed:17322308"
FT CHAIN 2..357
FT /note="Eukaryotic translation initiation factor 3 subunit
FT F"
FT /id="PRO_0000213964"
FT DOMAIN 92..222
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..38
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03005,
FT ECO:0000269|PubMed:17322308"
FT MOD_RES 46
FT /note="Phosphoserine; by CDK11; in vitro"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03005,
FT ECO:0000269|PubMed:12446680"
FT MOD_RES 238
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03005,
FT ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 39
FT /note="P -> L (in dbSNP:rs1043738)"
FT /id="VAR_029267"
FT VARIANT 172
FT /note="W -> L (in dbSNP:rs1044058)"
FT /id="VAR_014452"
FT VARIANT 232
FT /note="F -> V (in MRT67; decreased protein abundance;
FT dbSNP:rs141976414)"
FT /evidence="ECO:0000269|PubMed:30409806"
FT /id="VAR_081783"
FT CONFLICT 50..56
FT /note="Missing (in Ref. 2; BAC04577)"
FT /evidence="ECO:0000305"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 96..105
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 106..111
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 150..163
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 168..176
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 181..193
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 245..254
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 266..289
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 290..293
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 295..300
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 301..305
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 306..314
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 320..352
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 353..355
FT /evidence="ECO:0007829|PDB:6YBD"
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
