EIF3C_HUMAN
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 03-AUG-2022, entry version 211.
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.272.28.17668;
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="http://atlasgeneticsoncology.org/Genes/EIF3CID44187ch16p11.html";
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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 PDBsum; 3J8B; -.
DR PDBsum; 3J8C; -.
DR PDBsum; 6YBD; -.
DR PDBsum; 6YBW; -.
DR PDBsum; 6ZMW; -.
DR PDBsum; 6ZON; -.
DR PDBsum; 6ZP4; -.
DR PDBsum; 7A09; -.
DR AlphaFoldDB; Q99613; -.
DR SMR; Q99613; -.
DR BioGRID; 114212; 187.
DR ComplexPortal; CPX-6036; Eukaryotic translation initiation factor 3 complex.
DR CORUM; Q99613; -.
DR DIP; DIP-32865N; -.
DR IntAct; Q99613; 79.
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; Q99613; -.
DR PeptideAtlas; Q99613; -.
DR PRIDE; Q99613; -.
DR ProteomicsDB; 42171; -.
DR ProteomicsDB; 78357; -. [Q99613-1]
DR Antibodypedia; 26523; 261 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 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; NAGNESW; -.
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; 325 hits in 923 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 134 other tissues.
DR ExpressionAtlas; Q99613; baseline and differential.
DR Genevisible; Q99613; 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: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; IC: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; -; 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; PTHR13937; 1.
DR Pfam; PF05470; eIF-3c_N; 1.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50250; PCI; 1.
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
