ID EIF3C_HUMAN Reviewed; 913 AA. AC Q99613; A8K7Z0; B2RXG3; B4E1D5; H3BRV0; O00215; Q9BW98; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 27-MAR-2024, entry version 220. DE RecName: Full=Eukaryotic translation initiation factor 3 subunit C {ECO:0000255|HAMAP-Rule:MF_03002}; DE Short=eIF3c {ECO:0000255|HAMAP-Rule:MF_03002}; DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 8 {ECO:0000255|HAMAP-Rule:MF_03002}; DE AltName: Full=eIF3 p110 {ECO:0000255|HAMAP-Rule:MF_03002}; GN Name=EIF3C {ECO:0000255|HAMAP-Rule:MF_03002}; GN Synonyms=EIF3S8 {ECO:0000255|HAMAP-Rule:MF_03002}; 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 [GENOMIC DNA]. RX PubMed=8995409; DOI=10.1074/jbc.272.2.1101; RA Asano K., Kinzy T.G., Merrick W.C., Hershey J.W.B.; RT "Conservation and diversity of eukaryotic translation initiation factor RT eIF3."; RL J. Biol. Chem. 272:1101-1109(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10493829; DOI=10.1006/geno.1999.5927; RA Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J., RA Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X., RA Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C., RA Adams M.D.; RT "Genome duplications and other features in 12 Mb of DNA sequence from human RT chromosome 16p and 16q."; RL Genomics 60:295-308(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Liver, and Synovium; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, Lymph, and Placenta; 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 589-913 (ISOFORM 1). 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 [8] RP INTERACTION WITH EIF3B. RX PubMed=14519125; DOI=10.1046/j.1432-1033.2003.03807.x; RA Mayeur G.L., Fraser C.S., Peiretti F., Block K.L., Hershey J.W.B.; RT "Characterization of eIF3k: a newly discovered subunit of mammalian RT translation initiation factor eIF3."; RL Eur. J. Biochem. 270:4133-4139(2003). RN [9] RP INTERACTION WITH MTOR; RPTOR AND RPS6KB1. 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 [10] 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 [11] RP INTERACTION WITH IFIT1 AND IFIT2. RX PubMed=16023166; DOI=10.1016/j.virol.2005.06.011; RA Terenzi F., Pal S., Sen G.C.; RT "Induction and mode of action of the viral stress-inducible murine RT proteins, P56 and P54."; RL Virology 340:116-124(2005). RN [12] 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 [13] RP INTERACTION WITH IFIT2. RX PubMed=16973618; DOI=10.1074/jbc.m605771200; RA Terenzi F., Hui D.J., Merrick W.C., Sen G.C.; RT "Distinct induction patterns and functions of two closely related RT interferon-inducible human genes, ISG54 and ISG56."; RL J. Biol. Chem. 281:34064-34071(2006). RN [14] 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 [15] RP INTERACTION WITH EIF3E. RX PubMed=17468741; DOI=10.1038/sj.embor.7400955; RA Morris C., Wittmann J., Jaeck H.-M., Jalinot P.; RT "Human INT6/eIF3e is required for nonsense-mediated mRNA decay."; RL EMBO Rep. 8:596-602(2007). RN [16] RP IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX, RP PHOSPHORYLATION AT SER-9; SER-11; SER-13; SER-15; SER-16; SER-18; SER-39; RP SER-166; THR-524 AND SER-909, 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 [17] RP IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX, RP AND MASS SPECTROMETRY. 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 [18] RP IDENTIFICATION IN A HCV IRES-MEDIATED TRANSLATION COMPLEX. RX PubMed=19541769; DOI=10.1261/rna.1578409; RA Weinlich S., Huettelmaier S., Schierhorn A., Behrens S.-E., RA Ostareck-Lederer A., Ostareck D.H.; RT "IGF2BP1 enhances HCV IRES-mediated translation initiation via the 3'UTR."; RL RNA 15:1528-1542(2009). 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 INTERACTION WITH ALKBH4. RX PubMed=23145062; DOI=10.1371/journal.pone.0049045; RA Bjornstad L.G., Meza T.J., Otterlei M., Olafsrud S.M., Meza-Zepeda L.A., RA Falnes P.O.; RT "Human ALKBH4 interacts with proteins associated with transcription."; RL PLoS ONE 7:E49045-E49045(2012). RN [21] 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 [22] 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 [23] RP INTERACTION WITH BZW2/5MP1. RX PubMed=34260931; DOI=10.1016/j.celrep.2021.109376; RA Singh C.R., Glineburg M.R., Moore C., Tani N., Jaiswal R., Zou Y., Aube E., RA Gillaspie S., Thornton M., Cecil A., Hilgers M., Takasu A., Asano I., RA Asano M., Escalante C.R., Nakamura A., Todd P.K., Asano K.; RT "Human oncoprotein 5MP suppresses general and repeat-associated non-AUG RT translation via eIF3 by a common mechanism."; RL Cell Rep. 36:109376-109376(2021). RN [24] 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 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_03002, ECO:0000269|PubMed:17581632, CC ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:27462815}. 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. Identified in a HCV IRES- CC mediated translation complex, at least composed of EIF3C, IGF2BP1, RPS3 CC and HCV RNA-replicon. Interacts with ALKBH4, IFIT1 and IFIT2. Interacts CC with BZW2/5MP1 (PubMed:34260931). {ECO:0000255|HAMAP-Rule:MF_03002, CC ECO:0000269|PubMed:14519125, ECO:0000269|PubMed:16023166, CC ECO:0000269|PubMed:16286006, ECO:0000269|PubMed:16766523, CC ECO:0000269|PubMed:16973618, ECO:0000269|PubMed:17322308, CC ECO:0000269|PubMed:17468741, ECO:0000269|PubMed:18599441, CC ECO:0000269|PubMed:19541769, ECO:0000269|PubMed:23145062, CC ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:34260931}. CC -!- INTERACTION: CC Q99613; O00571: DDX3X; NbExp=3; IntAct=EBI-353741, EBI-353779; CC Q99613; P41567: EIF1; NbExp=2; IntAct=EBI-353741, EBI-726200; CC Q99613; P47813: EIF1AX; NbExp=2; IntAct=EBI-353741, EBI-1045377; CC Q99613; Q14152: EIF3A; NbExp=14; IntAct=EBI-353741, EBI-366617; CC Q99613; P60228: EIF3E; NbExp=14; IntAct=EBI-353741, EBI-347740; CC Q99613; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-353741, EBI-742388; CC Q99613; Q05086-2: UBE3A; NbExp=2; IntAct=EBI-353741, EBI-10175863; CC Q99613; Q9Q2G4: ORF; Xeno; NbExp=5; IntAct=EBI-353741, EBI-6248094; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03002}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q99613-1; Sequence=Displayed; CC Name=2; CC IsoId=Q99613-2; Sequence=VSP_055472; CC -!- PTM: Phosphorylated. Phosphorylation is enhanced upon serum CC stimulation. {ECO:0000255|HAMAP-Rule:MF_03002, CC ECO:0000269|PubMed:17322308}. CC -!- MASS SPECTROMETRY: Mass=106143.8; Method=Unknown; CC Evidence={ECO:0000269|PubMed:17322308}; CC -!- MASS SPECTROMETRY: Mass=106855; Mass_error=40; Method=MALDI; CC Evidence={ECO:0000269|PubMed:18599441}; CC -!- SIMILARITY: Belongs to the eIF-3 subunit C family. {ECO:0000255|HAMAP- CC Rule:MF_03002}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/44187/EIF3C"; 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; U46025; AAD03462.1; -; Genomic_DNA. DR EMBL; AC002544; AAC27426.1; -; Genomic_DNA. DR EMBL; U91326; AAC27674.1; -; Genomic_DNA. DR EMBL; AK000739; BAA91352.1; -; mRNA. DR EMBL; AK292155; BAF84844.1; -; mRNA. DR EMBL; AK303790; BAG64747.1; -; mRNA. DR EMBL; AC145285; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC000533; AAH00533.1; -; mRNA. DR EMBL; BC001571; AAH01571.1; -; mRNA. DR EMBL; BC071705; AAH71705.1; -; mRNA. DR EMBL; BC157842; AAI57843.1; -; mRNA. DR EMBL; BC157849; AAI57850.1; -; mRNA. DR EMBL; CH878380; EAW50492.1; -; Genomic_DNA. DR EMBL; BT007335; AAP35999.1; -; mRNA. DR CCDS; CCDS10638.1; -. [Q99613-1] DR CCDS; CCDS66993.1; -. [Q99613-2] DR RefSeq; NP_001032897.1; NM_001037808.2. [Q99613-1] DR RefSeq; NP_001186071.1; NM_001199142.1. [Q99613-1] DR RefSeq; NP_001254503.1; NM_001267574.2. [Q99613-1] DR RefSeq; NP_001273407.1; NM_001286478.1. [Q99613-2] DR RefSeq; NP_003743.1; NM_003752.4. [Q99613-1] DR PDB; 3J8B; EM; -; C=326-846. DR PDB; 3J8C; EM; -; C=326-846. DR PDB; 6YBD; EM; 3.30 A; y=1-913. DR PDB; 6YBW; EM; 3.10 A; y=1-913. DR PDB; 6ZMW; EM; 3.70 A; y=1-913. DR PDB; 6ZON; EM; 3.00 A; C=1-913. DR PDB; 6ZP4; EM; 2.90 A; C=1-913. DR PDB; 7A09; EM; 3.50 A; C=1-913. DR PDB; 7QP6; EM; 4.70 A; y=1-913. DR PDB; 7QP7; EM; 3.70 A; y=1-913. DR PDB; 8PPL; EM; 2.65 A; Iy=1-913. DR PDBsum; 3J8B; -. DR PDBsum; 3J8C; -. DR PDBsum; 6YBD; -. DR PDBsum; 6YBW; -. DR PDBsum; 6ZMW; -. DR PDBsum; 6ZON; -. DR PDBsum; 6ZP4; -. DR PDBsum; 7A09; -. DR PDBsum; 7QP6; -. DR PDBsum; 7QP7; -. DR PDBsum; 8PPL; -. DR AlphaFoldDB; Q99613; -. DR EMDB; EMD-10769; -. DR EMDB; EMD-10775; -. DR EMDB; EMD-11302; -. DR EMDB; EMD-11325; -. DR EMDB; EMD-11335; -. DR EMDB; EMD-11602; -. DR EMDB; EMD-14113; -. DR EMDB; EMD-14114; -. DR EMDB; EMD-17805; -. DR SMR; Q99613; -. DR BioGRID; 114212; 258. DR ComplexPortal; CPX-6036; Eukaryotic translation initiation factor 3 complex. DR CORUM; Q99613; -. DR DIP; DIP-32865N; -. DR IntAct; Q99613; 86. DR MINT; Q99613; -. DR STRING; 9606.ENSP00000332604; -. DR GlyGen; Q99613; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q99613; -. DR PhosphoSitePlus; Q99613; -. DR SwissPalm; Q99613; -. DR BioMuta; EIF3C; -. DR DMDM; 6685539; -. DR EPD; Q99613; -. DR jPOST; Q99613; -. DR MassIVE; Q99613; -. DR MaxQB; Q99613; -. DR PaxDb; 9606-ENSP00000332604; -. DR PeptideAtlas; Q99613; -. DR ProteomicsDB; 42171; -. DR ProteomicsDB; 78357; -. [Q99613-1] DR Pumba; Q99613; -. DR Antibodypedia; 26523; 284 antibodies from 26 providers. DR DNASU; 8663; -. DR Ensembl; ENST00000331666.11; ENSP00000332604.7; ENSG00000184110.15. [Q99613-1] DR Ensembl; ENST00000395587.5; ENSP00000378953.1; ENSG00000184110.15. [Q99613-1] DR Ensembl; ENST00000564243.5; ENSP00000456416.1; ENSG00000184110.15. [Q99613-2] DR Ensembl; ENST00000566501.5; ENSP00000457963.1; ENSG00000184110.15. [Q99613-1] DR Ensembl; ENST00000566866.5; ENSP00000457418.1; ENSG00000184110.15. [Q99613-1] DR GeneID; 8663; -. DR KEGG; hsa:8663; -. DR MANE-Select; ENST00000331666.11; ENSP00000332604.7; NM_003752.5; NP_003743.1. DR UCSC; uc002dqs.6; human. [Q99613-1] DR AGR; HGNC:3279; -. DR CTD; 8663; -. DR DisGeNET; 8663; -. DR GeneCards; EIF3C; -. DR HGNC; HGNC:3279; EIF3C. DR HPA; ENSG00000184110; Low tissue specificity. DR MIM; 603916; gene. DR neXtProt; NX_Q99613; -. DR OpenTargets; ENSG00000184110; -. DR PharmGKB; PA162384646; -. DR VEuPathDB; HostDB:ENSG00000184110; -. DR eggNOG; KOG1076; Eukaryota. DR GeneTree; ENSGT00390000017900; -. DR HOGENOM; CLU_004304_0_0_1; -. DR InParanoid; Q99613; -. DR OMA; ETNERAM; -. DR OrthoDB; 5482362at2759; -. DR PhylomeDB; Q99613; -. DR TreeFam; TF101520; -. DR PathwayCommons; Q99613; -. 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; Q99613; -. DR SIGNOR; Q99613; -. DR BioGRID-ORCS; 8663; 334 hits in 988 CRISPR screens. DR ChiTaRS; EIF3C; human. DR GeneWiki; EIF3C; -. DR GenomeRNAi; 8663; -. DR Pharos; Q99613; Tbio. DR PRO; PR:Q99613; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q99613; Protein. DR Bgee; ENSG00000184110; Expressed in right uterine tube and 136 other cell types or tissues. DR ExpressionAtlas; Q99613; 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:0043022; F:ribosome binding; IDA:MGI. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule. 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:1902416; P:positive regulation of mRNA binding; IPI:ParkinsonsUK-UCL. DR GO; GO:0045727; P:positive regulation of translation; IPI:ParkinsonsUK-UCL. DR GO; GO:0006413; P:translational initiation; IDA:UniProtKB. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR HAMAP; MF_03002; eIF3c; 1. DR InterPro; IPR027516; EIF3C. DR InterPro; IPR008905; EIF3C_N_dom. DR InterPro; IPR000717; PCI_dom. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR PANTHER; PTHR13937; EUKARYOTIC TRANSLATION INITATION FACTOR 3, SUBUNIT 8 EIF3S8 -RELATED; 1. DR PANTHER; PTHR13937:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT C-RELATED; 1. DR Pfam; PF05470; eIF-3c_N; 1. DR Pfam; PF01399; PCI; 1. DR SMART; SM00088; PINT; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR PROSITE; PS50250; PCI; 1. DR Genevisible; Q99613; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; KW Initiation factor; Phosphoprotein; Protein biosynthesis; KW Reference proteome. FT CHAIN 1..913 FT /note="Eukaryotic translation initiation factor 3 subunit FT C" FT /id="PRO_0000123525" FT DOMAIN 673..849 FT /note="PCI" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185" FT REGION 1..44 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 157..301 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 522..542 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 885..913 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..20 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 169..190 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 202..217 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 218..240 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 259..277 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 9 FT /note="Phosphoserine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03002, FT ECO:0000269|PubMed:17322308" FT MOD_RES 11 FT /note="Phosphoserine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03002, FT ECO:0000269|PubMed:17322308" FT MOD_RES 13 FT /note="Phosphoserine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03002, FT ECO:0000269|PubMed:17322308" FT MOD_RES 15 FT /note="Phosphoserine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03002, FT ECO:0000269|PubMed:17322308" FT MOD_RES 16 FT /note="Phosphoserine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03002, FT ECO:0000269|PubMed:17322308" FT MOD_RES 18 FT /note="Phosphoserine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03002, FT ECO:0000269|PubMed:17322308" FT MOD_RES 39 FT /note="Phosphoserine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03002, FT ECO:0000269|PubMed:17322308" FT MOD_RES 99 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8R1B4" FT MOD_RES 166 FT /note="Phosphoserine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03002, FT ECO:0000269|PubMed:17322308" FT MOD_RES 178 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8R1B4" FT MOD_RES 181 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8R1B4" FT MOD_RES 182 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8R1B4" FT MOD_RES 524 FT /note="Phosphothreonine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03002, FT ECO:0000269|PubMed:17322308" FT MOD_RES 643 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8R1B4" FT MOD_RES 909 FT /note="Phosphoserine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03002, FT ECO:0000269|PubMed:17322308" FT VAR_SEQ 120..129 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055472" FT CONFLICT 313..314 FT /note="EK -> VR (in Ref. 2; AAC27674)" FT /evidence="ECO:0000305" FT CONFLICT 737 FT /note="V -> A (in Ref. 3; BAG64747)" FT /evidence="ECO:0000305" FT HELIX 52..73 FT /evidence="ECO:0007829|PDB:6YBW" FT HELIX 76..93 FT /evidence="ECO:0007829|PDB:6YBW" FT TURN 94..96 FT /evidence="ECO:0007829|PDB:6YBW" FT HELIX 97..100 FT /evidence="ECO:0007829|PDB:6YBW" FT HELIX 104..120 FT /evidence="ECO:0007829|PDB:6YBW" FT HELIX 124..127 FT /evidence="ECO:0007829|PDB:6YBW" FT STRAND 131..133 FT /evidence="ECO:0007829|PDB:6YBW" FT HELIX 134..149 FT /evidence="ECO:0007829|PDB:6YBW" FT HELIX 150..152 FT /evidence="ECO:0007829|PDB:6YBW" FT HELIX 153..159 FT /evidence="ECO:0007829|PDB:6YBW" FT HELIX 265..277 FT /evidence="ECO:0007829|PDB:6YBW" FT HELIX 288..295 FT /evidence="ECO:0007829|PDB:6YBW" FT STRAND 303..305 FT /evidence="ECO:0007829|PDB:6YBW" FT STRAND 315..318 FT /evidence="ECO:0007829|PDB:6YBD" FT STRAND 321..323 FT /evidence="ECO:0007829|PDB:6YBD" FT HELIX 328..337 FT /evidence="ECO:0007829|PDB:6YBD" FT HELIX 347..363 FT /evidence="ECO:0007829|PDB:6YBD" FT HELIX 368..383 FT /evidence="ECO:0007829|PDB:6YBD" FT STRAND 385..387 FT /evidence="ECO:0007829|PDB:6YBD" FT STRAND 389..391 FT /evidence="ECO:0007829|PDB:6YBD" FT HELIX 395..414 FT /evidence="ECO:0007829|PDB:6YBD" FT TURN 420..423 FT /evidence="ECO:0007829|PDB:6YBD" FT STRAND 426..428 FT /evidence="ECO:0007829|PDB:6YBD" FT HELIX 444..460 FT /evidence="ECO:0007829|PDB:6YBD" FT HELIX 467..473 FT /evidence="ECO:0007829|PDB:6YBD" FT HELIX 476..492 FT /evidence="ECO:0007829|PDB:6YBD" FT HELIX 496..507 FT /evidence="ECO:0007829|PDB:6YBD" FT STRAND 509..512 FT /evidence="ECO:0007829|PDB:6YBD" FT HELIX 516..519 FT /evidence="ECO:0007829|PDB:6YBD" FT HELIX 544..557 FT /evidence="ECO:0007829|PDB:6YBD" FT HELIX 564..578 FT /evidence="ECO:0007829|PDB:6YBD" FT TURN 583..585 FT /evidence="ECO:0007829|PDB:6YBD" FT HELIX 586..592 FT /evidence="ECO:0007829|PDB:6YBD" FT TURN 595..597 FT /evidence="ECO:0007829|PDB:6YBD" FT HELIX 598..600 FT /evidence="ECO:0007829|PDB:6YBD" FT HELIX 603..621 FT /evidence="ECO:0007829|PDB:6YBD" FT TURN 622..624 FT /evidence="ECO:0007829|PDB:6YBD" FT HELIX 627..632 FT /evidence="ECO:0007829|PDB:6YBD" FT HELIX 634..637 FT /evidence="ECO:0007829|PDB:6YBD" FT HELIX 642..645 FT /evidence="ECO:0007829|PDB:6YBD" FT HELIX 652..654 FT /evidence="ECO:0007829|PDB:6YBD" FT HELIX 661..666 FT /evidence="ECO:0007829|PDB:6YBD" FT HELIX 679..699 FT /evidence="ECO:0007829|PDB:6YBD" FT TURN 700..702 FT /evidence="ECO:0007829|PDB:6YBD" FT STRAND 703..705 FT /evidence="ECO:0007829|PDB:6YBD" FT HELIX 713..722 FT /evidence="ECO:0007829|PDB:6YBD" FT HELIX 733..742 FT /evidence="ECO:0007829|PDB:6YBD" FT TURN 743..746 FT /evidence="ECO:0007829|PDB:6YBD" FT HELIX 750..756 FT /evidence="ECO:0007829|PDB:6YBD" FT HELIX 759..764 FT /evidence="ECO:0007829|PDB:6YBD" FT HELIX 766..768 FT /evidence="ECO:0007829|PDB:6YBD" FT STRAND 769..771 FT /evidence="ECO:0007829|PDB:6YBD" FT HELIX 772..794 FT /evidence="ECO:0007829|PDB:6YBD" FT TURN 796..798 FT /evidence="ECO:0007829|PDB:6YBD" FT STRAND 799..803 FT /evidence="ECO:0007829|PDB:6YBD" FT TURN 804..812 FT /evidence="ECO:0007829|PDB:6YBD" FT HELIX 815..824 FT /evidence="ECO:0007829|PDB:6YBD" FT STRAND 827..830 FT /evidence="ECO:0007829|PDB:6YBD" FT STRAND 832..835 FT /evidence="ECO:0007829|PDB:6YBD" FT TURN 836..839 FT /evidence="ECO:0007829|PDB:6YBD" FT STRAND 840..843 FT /evidence="ECO:0007829|PDB:6YBD" FT HELIX 852..859 FT /evidence="ECO:0007829|PDB:6YBD" SQ SEQUENCE 913 AA; 105344 MW; CE5029F4EB51C1AA CRC64; MSRFFTTGSD SESESSLSGE ELVTKPVGGN YGKQPLLLSE DEEDTKRVVR SAKDKRFEEL TNLIRTIRNA MKIRDVTKCL EEFELLGKAY GKAKSIVDKE GVPRFYIRIL ADLEDYLNEL WEDKEGKKKM NKNNAKALST LRQKIRKYNR DFESHITSYK QNPEQSADED AEKNEEDSEG SSDEDEDEDG VSAATFLKKK SEAPSGESRK FLKKMDDEDE DSEDSEDDED WDTGSTSSDS DSEEEEGKQT ALASRFLKKA PTTDEDKKAA EKKREDKAKK KHDRKSKRLD EEEEDNEGGE WERVRGGVPL VKEKPKMFAK GTEITHAVVI KKLNEILQAR GKKGTDRAAQ IELLQLLVQI AAENNLGEGV IVKIKFNIIA SLYDYNPNLA TYMKPEMWGK CLDCINELMD ILFANPNIFV GENILEESEN LHNADQPLRV RGCILTLVER MDEEFTKIMQ NTDPHSQEYV EHLKDEAQVC AIIERVQRYL EEKGTTEEVC RIYLLRILHT YYKFDYKAHQ RQLTPPEGSS KSEQDQAENE GEDSAVLMER LCKYIYAKDR TDRIRTCAIL CHIYHHALHS RWYQARDLML MSHLQDNIQH ADPPVQILYN RTMVQLGICA FRQGLTKDAH NALLDIQSSG RAKELLGQGL LLRSLQERNQ EQEKVERRRQ VPFHLHINLE LLECVYLVSA MLLEIPYMAA HESDARRRMI SKQFHHQLRV GERQPLLGPP ESMREHVVAA SKAMKMGDWK TCHSFIINEK MNGKVWDLFP EADKVRTMLV RKIQEESLRT YLFTYSSVYD SISMETLSDM FELDLPTVHS IISKMIINEE LMASLDQPTQ TVVMHRTEPT AQQNLALQLA EKLGSLVENN ERVFDHKQGT YGGYFRDQKD GYRKNEGYMR RGGYRQQQSQ TAY //