ID EIF3K_HUMAN Reviewed; 218 AA. AC Q9UBQ5; A8K0I9; B7ZAM9; Q96IQ0; Q9Y6D1; DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 207. DE RecName: Full=Eukaryotic translation initiation factor 3 subunit K {ECO:0000255|HAMAP-Rule:MF_03010}; DE Short=eIF3k {ECO:0000255|HAMAP-Rule:MF_03010}; DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 12 {ECO:0000255|HAMAP-Rule:MF_03010}; DE AltName: Full=Muscle-specific gene M9 protein; DE AltName: Full=PLAC-24; DE AltName: Full=eIF-3 p25 {ECO:0000255|HAMAP-Rule:MF_03010}; DE AltName: Full=eIF-3 p28; GN Name=EIF3K {ECO:0000255|HAMAP-Rule:MF_03010}; GN Synonyms=EIF3S12 {ECO:0000255|HAMAP-Rule:MF_03010}; GN ORFNames=ARG134, HSPC029, MSTP001, PTD001; 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] (ISOFORM 1), PROTEIN SEQUENCE OF 21-31, RP IDENTIFICATION IN THE EIF-3 COMPLEX, INTERACTION WITH EIF3B; EIF3C; EIF3G RP AND EIF3J, TISSUE SPECIFICITY, AND BLOCKAGE OF N-TERMINUS. RC TISSUE=Cervix carcinoma; 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 [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Skeletal muscle; RA Nawa G., Miyoshi Y., Nakamura Y.; RT "Muscle specific gene M9."; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Pituitary tumor; RA Ye M., Song H., Peng Y., Huang Q., Dai M., Mao Y., Zhu H., Li G., Luo M., RA Hu R., Chen J.; RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Aorta; RA Hui R.T., Liu Y.Q., Liu B., Zhao B., Meng X.M., Sheng H., Xu Y.Y., RA Wang X.Y., Ye J., Song L., Gao Y., Wei Y.J., Zhang C.L., Zhang J., RA Chai M.Q., Chen J.Z., Sun Y.H., Zhou X.L., Jiang Y.X., Zhao X.W., Liu S., RA Cao H.Q., Zhao Y., Liu D.Q., Ding J.F., Liu L.S., Gao R.L., Wu Q.Y., RA Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S.; RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Stomach cancer; RA Yanqiu Z., Huazhang A., Fei L., Baojun C., Taidong Q., Kaichun W., Jie D., RA Daiming F.; RT "Gene cloning of human adenocarcinoma cell line."; RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Umbilical cord blood; RX PubMed=11042152; DOI=10.1101/gr.140200; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for 300 RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor RT cells."; RL Genome Res. 10:1546-1560(2000). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Cerebellum, and Spleen; 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [9] 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 [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Placenta, Skin, and Uterus; 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 [11] RP PROTEIN SEQUENCE OF 2-8; 21-31 AND 39-52, CLEAVAGE OF INITIATOR METHIONINE, RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Colon carcinoma; RA Bienvenut W.V., Zebisch A., Kolch W.; RL Submitted (DEC-2008) to UniProtKB. RN [12] RP INTERACTION WITH CCND3, AND SUBCELLULAR LOCATION. RX PubMed=15327989; DOI=10.1016/j.febslet.2004.07.071; RA Shen X., Yang Y., Liu W., Sun M., Jiang J., Zong H., Gu J.; RT "Identification of the p28 subunit of eukaryotic initiation factor 3(eIF3k) RT as a new interaction partner of cyclin D3."; RL FEBS Lett. 573:139-146(2004). RN [13] 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 [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [15] 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 [16] 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 [17] RP IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX, RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS RP 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217, 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 [19] 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 [20] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217, AND IDENTIFICATION BY RP 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 [22] 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 [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217, AND IDENTIFICATION BY RP 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 [24] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [25] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-28, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [27] 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 [28] 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 [29] 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 [30] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). RX PubMed=15180986; DOI=10.1074/jbc.m405158200; RA Wei Z., Zhang P., Zhou Z., Cheng Z., Wan M., Gong W.; RT "Crystal structure of human eIF3k, the first structure of eIF3 subunits."; RL J. Biol. Chem. 279:34983-34990(2004). 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_03010, 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. Interacts with CCND3, but not CC with CCND1 and CCND2. {ECO:0000255|HAMAP-Rule:MF_03010, CC ECO:0000269|PubMed:14519125, ECO:0000269|PubMed:15327989, CC ECO:0000269|PubMed:16766523, ECO:0000269|PubMed:17322308, CC ECO:0000269|PubMed:18599441, ECO:0000269|PubMed:25849773}. CC -!- INTERACTION: CC Q9UBQ5; O14645: DNALI1; NbExp=4; IntAct=EBI-354344, EBI-395638; CC Q9UBQ5; P55884: EIF3B; NbExp=4; IntAct=EBI-354344, EBI-366696; CC Q9UBQ5; P60228: EIF3E; NbExp=6; IntAct=EBI-354344, EBI-347740; CC Q9UBQ5; Q9Y262: EIF3L; NbExp=14; IntAct=EBI-354344, EBI-373519; CC Q9UBQ5; O14901: KLF11; NbExp=3; IntAct=EBI-354344, EBI-948266; CC Q9UBQ5; Q9Q2G4: ORF; Xeno; NbExp=5; IntAct=EBI-354344, EBI-6248094; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03010, CC ECO:0000269|PubMed:15327989}. Cytoplasm {ECO:0000255|HAMAP- CC Rule:MF_03010, ECO:0000269|PubMed:15327989}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9UBQ5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UBQ5-2; Sequence=VSP_055475; CC -!- TISSUE SPECIFICITY: Ubiquitous, with the highest levels of expression CC in brain, testis and kidney. {ECO:0000269|PubMed:14519125}. CC -!- MASS SPECTROMETRY: Mass=24970.6; Method=Unknown; CC Evidence={ECO:0000269|PubMed:17322308}; CC -!- MASS SPECTROMETRY: Mass=24971.1; Mass_error=0.2; Method=MALDI; CC Evidence={ECO:0000269|PubMed:18599441}; CC -!- SIMILARITY: Belongs to the eIF-3 subunit K family. {ECO:0000255|HAMAP- CC Rule:MF_03010}. 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; AY245432; AAP22070.1; -; mRNA. DR EMBL; AB019392; BAA76626.1; -; mRNA. DR EMBL; AF077051; AAD27784.1; -; mRNA. DR EMBL; AF109355; AAQ13503.1; -; mRNA. DR EMBL; AF315506; AAK01365.1; -; mRNA. DR EMBL; AF085358; AAD40193.1; -; mRNA. DR EMBL; AK289554; BAF82243.1; -; mRNA. DR EMBL; AK316344; BAH14715.1; -; mRNA. DR EMBL; AC008649; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471126; EAW56807.1; -; Genomic_DNA. DR EMBL; BC001031; AAH01031.1; -; mRNA. DR EMBL; BC007335; AAH07335.2; -; mRNA. DR EMBL; BC007559; AAH07559.1; -; mRNA. DR CCDS; CCDS12517.1; -. [Q9UBQ5-1] DR RefSeq; NP_037366.1; NM_013234.3. [Q9UBQ5-1] DR PDB; 1RZ4; X-ray; 2.10 A; A=1-218. DR PDB; 3J8B; EM; -; K=1-190. DR PDB; 3J8C; EM; -; K=1-190. DR PDB; 6FEC; EM; 6.30 A; 6=1-218. DR PDB; 6YBD; EM; 3.30 A; 3=1-218. DR PDB; 6ZMW; EM; 3.70 A; 3=1-218. DR PDB; 6ZON; EM; 3.00 A; K=1-218. DR PDB; 6ZP4; EM; 2.90 A; K=1-218. DR PDB; 6ZVJ; EM; 3.80 A; K=2-218. DR PDB; 7A09; EM; 3.50 A; K=1-218. DR PDB; 7QP6; EM; 4.70 A; 3=1-218. DR PDB; 7QP7; EM; 3.70 A; 3=1-218. DR PDB; 8PPL; EM; 2.65 A; I3=1-218. DR PDBsum; 1RZ4; -. DR PDBsum; 3J8B; -. DR PDBsum; 3J8C; -. DR PDBsum; 6FEC; -. 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; Q9UBQ5; -. 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 EMDB; EMD-4242; -. DR SMR; Q9UBQ5; -. DR BioGRID; 118148; 178. DR ComplexPortal; CPX-6036; Eukaryotic translation initiation factor 3 complex. DR CORUM; Q9UBQ5; -. DR DIP; DIP-32880N; -. DR IntAct; Q9UBQ5; 50. DR MINT; Q9UBQ5; -. DR STRING; 9606.ENSP00000248342; -. DR GlyGen; Q9UBQ5; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9UBQ5; -. DR PhosphoSitePlus; Q9UBQ5; -. DR SwissPalm; Q9UBQ5; -. DR BioMuta; EIF3K; -. DR DMDM; 23396628; -. DR EPD; Q9UBQ5; -. DR jPOST; Q9UBQ5; -. DR MassIVE; Q9UBQ5; -. DR MaxQB; Q9UBQ5; -. DR PaxDb; 9606-ENSP00000248342; -. DR PeptideAtlas; Q9UBQ5; -. DR ProteomicsDB; 7071; -. DR ProteomicsDB; 84032; -. [Q9UBQ5-1] DR Pumba; Q9UBQ5; -. DR TopDownProteomics; Q9UBQ5-1; -. [Q9UBQ5-1] DR Antibodypedia; 30132; 272 antibodies from 30 providers. DR DNASU; 27335; -. DR Ensembl; ENST00000248342.9; ENSP00000248342.3; ENSG00000178982.10. [Q9UBQ5-1] DR Ensembl; ENST00000545173.6; ENSP00000438145.1; ENSG00000178982.10. [Q9UBQ5-2] DR Ensembl; ENST00000635417.1; ENSP00000489379.1; ENSG00000282986.2. [Q9UBQ5-2] DR Ensembl; ENST00000635567.2; ENSP00000489438.1; ENSG00000282986.2. [Q9UBQ5-1] DR GeneID; 27335; -. DR KEGG; hsa:27335; -. DR MANE-Select; ENST00000248342.9; ENSP00000248342.3; NM_013234.4; NP_037366.1. DR UCSC; uc002oiz.2; human. [Q9UBQ5-1] DR AGR; HGNC:24656; -. DR CTD; 27335; -. DR DisGeNET; 27335; -. DR GeneCards; EIF3K; -. DR HGNC; HGNC:24656; EIF3K. DR HPA; ENSG00000178982; Low tissue specificity. DR MIM; 609596; gene. DR neXtProt; NX_Q9UBQ5; -. DR OpenTargets; ENSG00000178982; -. DR PharmGKB; PA162384923; -. DR VEuPathDB; HostDB:ENSG00000178982; -. DR eggNOG; KOG3252; Eukaryota. DR GeneTree; ENSGT00390000009409; -. DR HOGENOM; CLU_076723_1_0_1; -. DR InParanoid; Q9UBQ5; -. DR OMA; GDDLCAD; -. DR OrthoDB; 6606at2759; -. DR PhylomeDB; Q9UBQ5; -. DR TreeFam; TF314893; -. DR PathwayCommons; Q9UBQ5; -. 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; Q9UBQ5; -. DR SIGNOR; Q9UBQ5; -. DR BioGRID-ORCS; 27335; 140 hits in 1177 CRISPR screens. DR ChiTaRS; EIF3K; human. DR EvolutionaryTrace; Q9UBQ5; -. DR GeneWiki; EIF3K; -. DR GenomeRNAi; 27335; -. DR Pharos; Q9UBQ5; Tbio. DR PRO; PR:Q9UBQ5; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q9UBQ5; Protein. DR Bgee; ENSG00000178982; Expressed in apex of heart and 153 other cell types or tissues. DR ExpressionAtlas; Q9UBQ5; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. 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:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0043022; F:ribosome binding; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule. DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; NAS:ComplexPortal. DR GO; GO:0006446; P:regulation of translational initiation; IEA:InterPro. 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_03010; eIF3k; 1. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR033464; CSN8_PSD8_EIF3K. DR InterPro; IPR009374; eIF3k. DR InterPro; IPR000717; PCI_dom. DR InterPro; IPR016020; Transl_init_fac_sub12_N_euk. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR PANTHER; PTHR13022; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT 11; 1. DR PANTHER; PTHR13022:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT K; 1. DR Pfam; PF10075; CSN8_PSD8_EIF3K; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR PROSITE; PS50250; PCI; 1. DR Genevisible; Q9UBQ5; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; KW Direct protein sequencing; Initiation factor; Nucleus; Phosphoprotein; KW Protein biosynthesis; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03010, FT ECO:0000269|PubMed:17322308, ECO:0000269|Ref.11, FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT CHAIN 2..218 FT /note="Eukaryotic translation initiation factor 3 subunit FT K" FT /id="PRO_0000123546" FT DOMAIN 42..204 FT /note="PCI" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03010, FT ECO:0000269|PubMed:17322308, ECO:0000269|Ref.11, FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT MOD_RES 28 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 217 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT VAR_SEQ 210..218 FT /note="VSSIMASSQ -> EW (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055475" FT CONFLICT 119 FT /note="Q -> K (in Ref. 6; AAD40193)" FT /evidence="ECO:0000305" FT HELIX 3..16 FT /evidence="ECO:0007829|PDB:1RZ4" FT HELIX 18..21 FT /evidence="ECO:0007829|PDB:1RZ4" FT HELIX 23..25 FT /evidence="ECO:0007829|PDB:1RZ4" FT HELIX 26..39 FT /evidence="ECO:0007829|PDB:1RZ4" FT HELIX 44..56 FT /evidence="ECO:0007829|PDB:1RZ4" FT HELIX 58..60 FT /evidence="ECO:0007829|PDB:1RZ4" FT HELIX 63..75 FT /evidence="ECO:0007829|PDB:1RZ4" FT TURN 76..78 FT /evidence="ECO:0007829|PDB:1RZ4" FT HELIX 81..87 FT /evidence="ECO:0007829|PDB:1RZ4" FT HELIX 91..94 FT /evidence="ECO:0007829|PDB:1RZ4" FT HELIX 99..110 FT /evidence="ECO:0007829|PDB:1RZ4" FT HELIX 114..120 FT /evidence="ECO:0007829|PDB:1RZ4" FT HELIX 126..129 FT /evidence="ECO:0007829|PDB:1RZ4" FT HELIX 134..149 FT /evidence="ECO:0007829|PDB:1RZ4" FT STRAND 151..153 FT /evidence="ECO:0007829|PDB:1RZ4" FT HELIX 155..161 FT /evidence="ECO:0007829|PDB:1RZ4" FT HELIX 167..177 FT /evidence="ECO:0007829|PDB:1RZ4" FT STRAND 187..190 FT /evidence="ECO:0007829|PDB:6YBD" FT HELIX 192..195 FT /evidence="ECO:0007829|PDB:1RZ4" FT HELIX 207..214 FT /evidence="ECO:0007829|PDB:1RZ4" SQ SEQUENCE 218 AA; 25060 MW; 6B2CBBE8A9D1F28F CRC64; MAMFEQMRAN VGKLLKGIDR YNPENLATLE RYVETQAKEN AYDLEANLAV LKLYQFNPAF FQTTVTAQIL LKALTNLPHT DFTLCKCMID QAHQEERPIR QILYLGDLLE TCHFQAFWQA LDENMDLLEG ITGFEDSVRK FICHVVGITY QHIDRWLLAE MLGDLSDSQL KVWMSKYGWS ADESGQIFIC SQEESIKPKN IVEKIDFDSV SSIMASSQ //