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 27-MAR-2024, entry version 214. 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; 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="https://atlasgeneticsoncology.org/gene/44407/EIF3F"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7QP6; EM; 4.70 A; 4=1-357. DR PDB; 7QP7; EM; 3.70 A; 4=1-357. DR PDB; 8PPL; EM; 2.65 A; I4=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 PDBsum; 7QP6; -. DR PDBsum; 7QP7; -. DR PDBsum; 8PPL; -. DR AlphaFoldDB; O00303; -. DR EMDB; EMD-10769; -. DR EMDB; EMD-11302; -. DR EMDB; EMD-11325; -. DR EMDB; EMD-11335; -. DR EMDB; EMD-11458; -. DR EMDB; EMD-11602; -. DR EMDB; EMD-14113; -. DR EMDB; EMD-14114; -. DR EMDB; EMD-17805; -. DR SMR; O00303; -. DR BioGRID; 114214; 296. DR ComplexPortal; CPX-6036; Eukaryotic translation initiation factor 3 complex. DR CORUM; O00303; -. DR DIP; DIP-35580N; -. DR IntAct; O00303; 139. 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; 9606-ENSP00000431800; -. DR PeptideAtlas; O00303; -. DR ProteomicsDB; 47830; -. DR Pumba; O00303; -. DR Antibodypedia; 11428; 273 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 AGR; HGNC:3275; -. 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; TVSPMLD; -. DR OrthoDB; 231037at2759; -. 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; 771 hits in 1173 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 primordial germ cell in gonad and 179 other cell types or tissues. DR ExpressionAtlas; O00303; baseline and differential. 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:0045202; C:synapse; IEA:Ensembl. 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: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; NAS: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:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0006413; P:translational initiation; IDA:UniProtKB. DR CDD; cd08064; MPN_eIF3f; 1. DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1. DR HAMAP; MF_03005; eIF3f; 1. DR InterPro; IPR027531; eIF3f. DR InterPro; IPR024969; EIF3F/CSN6-like_C. DR InterPro; IPR000555; JAMM/MPN+_dom. DR InterPro; IPR037518; MPN. DR PANTHER; PTHR10540:SF6; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT F; 1. DR PANTHER; PTHR10540; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT F-RELATED; 1. DR Pfam; PF01398; JAB; 1. DR Pfam; PF13012; MitMem_reg; 1. DR SMART; SM00232; JAB_MPN; 1. DR PROSITE; PS50249; MPN; 1. DR Genevisible; O00303; HS. 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 //