EIF3K_HUMAN
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 03-AUG-2022, entry version 198.
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}.
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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 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 AlphaFoldDB; Q9UBQ5; -.
DR SMR; Q9UBQ5; -.
DR BioGRID; 118148; 115.
DR ComplexPortal; CPX-6036; Eukaryotic translation initiation factor 3 complex.
DR CORUM; Q9UBQ5; -.
DR DIP; DIP-32880N; -.
DR IntAct; Q9UBQ5; 46.
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; Q9UBQ5; -.
DR PeptideAtlas; Q9UBQ5; -.
DR PRIDE; Q9UBQ5; -.
DR ProteomicsDB; 7071; -.
DR ProteomicsDB; 84032; -. [Q9UBQ5-1]
DR TopDownProteomics; Q9UBQ5-1; -. [Q9UBQ5-1]
DR Antibodypedia; 30132; 245 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 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; WKHQGQG; -.
DR OrthoDB; 1576799at2759; -.
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; 132 hits in 1093 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 151 other tissues.
DR ExpressionAtlas; Q9UBQ5; baseline and differential.
DR Genevisible; Q9UBQ5; HS.
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; IC: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; -; 1.
DR Gene3D; 1.25.40.250; -; 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; PTHR13022; 1.
DR Pfam; PF10075; CSN8_PSD8_EIF3K; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50250; PCI; 1.
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
