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Eukaryotic translation initiation factor 3 subunit K (eIF3k) (Eukaryotic translation initiation factor 3 subunit 12) (Muscle-specific gene M9 protein) (PLAC-24) (eIF-3 p25) (eIF-3 p28)

 EIF3K_HUMAN             Reviewed;         218 AA.
Q9UBQ5; A8K0I9; B7ZAM9; Q96IQ0; Q9Y6D1;
19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-APR-2018, entry version 171.
RecName: Full=Eukaryotic translation initiation factor 3 subunit K {ECO:0000255|HAMAP-Rule:MF_03010};
Short=eIF3k {ECO:0000255|HAMAP-Rule:MF_03010};
AltName: Full=Eukaryotic translation initiation factor 3 subunit 12 {ECO:0000255|HAMAP-Rule:MF_03010};
AltName: Full=Muscle-specific gene M9 protein;
AltName: Full=PLAC-24;
AltName: Full=eIF-3 p25 {ECO:0000255|HAMAP-Rule:MF_03010};
AltName: Full=eIF-3 p28;
Name=EIF3K {ECO:0000255|HAMAP-Rule:MF_03010};
Synonyms=EIF3S12 {ECO:0000255|HAMAP-Rule:MF_03010};
ORFNames=ARG134, HSPC029, MSTP001, PTD001;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 21-31,
IDENTIFICATION IN THE EIF-3 COMPLEX, INTERACTION WITH EIF3B; EIF3C;
EIF3G AND EIF3J, TISSUE SPECIFICITY, AND BLOCKAGE OF N-TERMINUS.
TISSUE=Cervix carcinoma;
PubMed=14519125; DOI=10.1046/j.1432-1033.2003.03807.x;
Mayeur G.L., Fraser C.S., Peiretti F., Block K.L., Hershey J.W.B.;
"Characterization of eIF3k: a newly discovered subunit of mammalian
translation initiation factor eIF3.";
Eur. J. Biochem. 270:4133-4139(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Skeletal muscle;
Nawa G., Miyoshi Y., Nakamura Y.;
"Muscle specific gene M9.";
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Pituitary tumor;
Ye M., Song H., Peng Y., Huang Q., Dai M., Mao Y., Zhu H., Li G.,
Luo M., Hu R., Chen J.;
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Aorta;
Hui R.T., Liu Y.Q., Liu B., Zhao B., Meng X.M., Sheng H., Xu Y.Y.,
Wang X.Y., Ye J., Song L., Gao Y., Wei Y.J., Zhang C.L., Zhang J.,
Chai M.Q., Chen J.Z., Sun Y.H., Zhou X.L., Jiang Y.X., Zhao X.W.,
Liu S., Cao H.Q., Zhao Y., Liu D.Q., Ding J.F., Liu L.S., Gao R.L.,
Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S.;
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Stomach cancer;
Yanqiu Z., Huazhang A., Fei L., Baojun C., Taidong Q., Kaichun W.,
Jie D., Daiming F.;
"Gene cloning of human adenocarcinoma cell line.";
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Umbilical cord blood;
PubMed=11042152; DOI=10.1101/gr.140200;
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
"Cloning and functional analysis of cDNAs with open reading frames for
300 previously undefined genes expressed in CD34+ hematopoietic
stem/progenitor cells.";
Genome Res. 10:1546-1560(2000).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Cerebellum, and Spleen;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta, Skin, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
PROTEIN SEQUENCE OF 2-8; 21-31 AND 39-52, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Colon carcinoma;
Bienvenut W.V., Zebisch A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[12]
INTERACTION WITH CCND3, AND SUBCELLULAR LOCATION.
PubMed=15327989; DOI=10.1016/j.febslet.2004.07.071;
Shen X., Yang Y., Liu W., Sun M., Jiang J., Zong H., Gu J.;
"Identification of the p28 subunit of eukaryotic initiation factor
3(eIF3k) as a new interaction partner of cyclin D3.";
FEBS Lett. 573:139-146(2004).
[13]
CHARACTERIZATION OF THE EIF-3 COMPLEX.
PubMed=15703437; DOI=10.1261/rna.7215305;
Kolupaeva V.G., Unbehaun A., Lomakin I.B., Hellen C.U.T.,
Pestova T.V.;
"Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits
and its role in ribosomal dissociation and anti-association.";
RNA 11:470-486(2005).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[15]
IDENTIFICATION IN THE EIF-3 COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=16766523; DOI=10.1074/jbc.M605418200;
LeFebvre A.K., Korneeva N.L., Trutschl M., Cvek U., Duzan R.D.,
Bradley C.A., Hershey J.W.B., Rhoads R.E.;
"Translation initiation factor eIF4G-1 binds to eIF3 through the eIF3e
subunit.";
J. Biol. Chem. 281:22917-22932(2006).
[16]
FUNCTION, AND CHARACTERIZATION OF THE EIF-3 COMPLEX.
PubMed=17581632; DOI=10.1038/sj.emboj.7601765;
Masutani M., Sonenberg N., Yokoyama S., Imataka H.;
"Reconstitution reveals the functional core of mammalian eIF3.";
EMBO J. 26:3373-3383(2007).
[17]
IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3
COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
MASS SPECTROMETRY.
PubMed=17322308; DOI=10.1074/mcp.M600399-MCP200;
Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L.,
Hershey J.W.B., Doudna J.A., Robinson C.V., Leary J.A.;
"Structural characterization of the human eukaryotic initiation factor
3 protein complex by mass spectrometry.";
Mol. Cell. Proteomics 6:1135-1146(2007).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[19]
IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3
COMPLEX, AND MASS SPECTROMETRY.
PubMed=18599441; DOI=10.1073/pnas.0801313105;
Zhou M., Sandercock A.M., Fraser C.S., Ridlova G., Stephens E.,
Schenauer M.R., Yokoi-Fong T., Barsky D., Leary J.A., Hershey J.W.B.,
Doudna J.A., Robinson C.V.;
"Mass spectrometry reveals modularity and a complete subunit
interaction map of the eukaryotic translation factor eIF3.";
Proc. Natl. Acad. Sci. U.S.A. 105:18139-18144(2008).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[24]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[25]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-28, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[27]
FUNCTION, AND IDENTIFICATION IN THE EIF-3 COMPLEX.
PubMed=25849773; DOI=10.1038/nature14267;
Lee A.S., Kranzusch P.J., Cate J.H.;
"eIF3 targets cell-proliferation messenger RNAs for translational
activation or repression.";
Nature 522:111-114(2015).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[29]
FUNCTION.
PubMed=27462815; DOI=10.1038/nature18954;
Lee A.S., Kranzusch P.J., Doudna J.A., Cate J.H.;
"eIF3d is an mRNA cap-binding protein that is required for specialized
translation initiation.";
Nature 536:96-99(2016).
[30]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
PubMed=15180986; DOI=10.1074/jbc.M405158200;
Wei Z., Zhang P., Zhou Z., Cheng Z., Wan M., Gong W.;
"Crystal structure of human eIF3k, the first structure of eIF3
subunits.";
J. Biol. Chem. 279:34983-34990(2004).
-!- FUNCTION: Component of the eukaryotic translation initiation
factor 3 (eIF-3) complex, which is required for several steps in
the initiation of protein synthesis (PubMed:17581632,
PubMed:25849773, PubMed:27462815). The eIF-3 complex associates
with the 40S ribosome and facilitates the recruitment of eIF-1,
eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-
initiation complex (43S PIC). The eIF-3 complex stimulates mRNA
recruitment to the 43S PIC and scanning of the mRNA for AUG
recognition. The eIF-3 complex is also required for disassembly
and recycling of post-termination ribosomal complexes and
subsequently prevents premature joining of the 40S and 60S
ribosomal subunits prior to initiation (PubMed:17581632). The eIF-
3 complex specifically targets and initiates translation of a
subset of mRNAs involved in cell proliferation, including cell
cycling, differentiation and apoptosis, and uses different modes
of RNA stem-loop binding to exert either translational activation
or repression (PubMed:25849773). {ECO:0000255|HAMAP-Rule:MF_03010,
ECO:0000269|PubMed:17581632, ECO:0000269|PubMed:25849773,
ECO:0000269|PubMed:27462815}.
-!- SUBUNIT: Component of the eukaryotic translation initiation factor
3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B,
EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K,
EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable
modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I;
module B is composed of EIF3F, EIF3H, and EIF3M; and module C is
composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module
C binds EIF3B of module A and EIF3H of module B, thereby linking
the three modules. EIF3J is a labile subunit that binds to the
eIF-3 complex via EIF3B. The eIF-3 complex interacts with RPS6KB1
under conditions of nutrient depletion. Mitogenic stimulation
leads to binding and activation of a complex composed of MTOR and
RPTOR, leading to phosphorylation and release of RPS6KB1 and
binding of EIF4B to eIF-3. Interacts with CCND3, but not with
CCND1 and CCND2. {ECO:0000255|HAMAP-Rule:MF_03010,
ECO:0000269|PubMed:14519125, ECO:0000269|PubMed:15327989,
ECO:0000269|PubMed:16766523, ECO:0000269|PubMed:17322308,
ECO:0000269|PubMed:18599441, ECO:0000269|PubMed:25849773}.
-!- INTERACTION:
P30281:CCND3; NbExp=4; IntAct=EBI-354344, EBI-375013;
Q14152:EIF3A; NbExp=14; IntAct=EBI-354344, EBI-366617;
P55884:EIF3B; NbExp=4; IntAct=EBI-354344, EBI-366696;
P60228:EIF3E; NbExp=5; IntAct=EBI-354344, EBI-347740;
Q9Y262:EIF3L; NbExp=12; IntAct=EBI-354344, EBI-373519;
Q9Q2G4:ORF (xeno); NbExp=5; IntAct=EBI-354344, EBI-6248094;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03010,
ECO:0000269|PubMed:15327989}. Cytoplasm {ECO:0000255|HAMAP-
Rule:MF_03010, ECO:0000269|PubMed:15327989}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9UBQ5-1; Sequence=Displayed;
Name=2;
IsoId=Q9UBQ5-2; Sequence=VSP_055475;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous, with the highest levels of
expression in brain, testis and kidney.
{ECO:0000269|PubMed:14519125}.
-!- MASS SPECTROMETRY: Mass=24970.6; Method=Unknown; Range=1-218;
Evidence={ECO:0000269|PubMed:17322308};
-!- MASS SPECTROMETRY: Mass=24971.1; Mass_error=0.2; Method=MALDI;
Range=1-218; Evidence={ECO:0000269|PubMed:18599441};
-!- SIMILARITY: Belongs to the eIF-3 subunit K family.
{ECO:0000255|HAMAP-Rule:MF_03010}.
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EMBL; AY245432; AAP22070.1; -; mRNA.
EMBL; AB019392; BAA76626.1; -; mRNA.
EMBL; AF077051; AAD27784.1; -; mRNA.
EMBL; AF109355; AAQ13503.1; -; mRNA.
EMBL; AF315506; AAK01365.1; -; mRNA.
EMBL; AF085358; AAD40193.1; -; mRNA.
EMBL; AK289554; BAF82243.1; -; mRNA.
EMBL; AK316344; BAH14715.1; -; mRNA.
EMBL; AC008649; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471126; EAW56807.1; -; Genomic_DNA.
EMBL; BC001031; AAH01031.1; -; mRNA.
EMBL; BC007335; AAH07335.2; -; mRNA.
EMBL; BC007559; AAH07559.1; -; mRNA.
CCDS; CCDS12517.1; -. [Q9UBQ5-1]
RefSeq; NP_037366.1; NM_013234.3. [Q9UBQ5-1]
UniGene; Hs.314359; -.
PDB; 1RZ4; X-ray; 2.10 A; A=1-218.
PDB; 3J8B; EM; -; K=1-190.
PDB; 3J8C; EM; -; K=1-190.
PDB; 6FEC; EM; 6.30 A; 6=1-218.
PDBsum; 1RZ4; -.
PDBsum; 3J8B; -.
PDBsum; 3J8C; -.
PDBsum; 6FEC; -.
ProteinModelPortal; Q9UBQ5; -.
SMR; Q9UBQ5; -.
BioGrid; 118148; 61.
CORUM; Q9UBQ5; -.
DIP; DIP-32880N; -.
IntAct; Q9UBQ5; 34.
MINT; Q9UBQ5; -.
STRING; 9606.ENSP00000248342; -.
iPTMnet; Q9UBQ5; -.
PhosphoSitePlus; Q9UBQ5; -.
SwissPalm; Q9UBQ5; -.
BioMuta; EIF3K; -.
DMDM; 23396628; -.
EPD; Q9UBQ5; -.
PaxDb; Q9UBQ5; -.
PeptideAtlas; Q9UBQ5; -.
PRIDE; Q9UBQ5; -.
TopDownProteomics; Q9UBQ5-1; -. [Q9UBQ5-1]
DNASU; 27335; -.
Ensembl; ENST00000248342; ENSP00000248342; ENSG00000178982. [Q9UBQ5-1]
Ensembl; ENST00000545173; ENSP00000438145; ENSG00000178982. [Q9UBQ5-2]
Ensembl; ENST00000635417; ENSP00000489379; ENSG00000282986. [Q9UBQ5-2]
Ensembl; ENST00000635567; ENSP00000489438; ENSG00000282986. [Q9UBQ5-1]
GeneID; 27335; -.
KEGG; hsa:27335; -.
UCSC; uc002oiz.2; human. [Q9UBQ5-1]
CTD; 27335; -.
DisGeNET; 27335; -.
EuPathDB; HostDB:ENSG00000178982.9; -.
GeneCards; EIF3K; -.
HGNC; HGNC:24656; EIF3K.
HPA; HPA045446; -.
HPA; HPA054590; -.
MIM; 609596; gene.
neXtProt; NX_Q9UBQ5; -.
OpenTargets; ENSG00000178982; -.
PharmGKB; PA162384923; -.
eggNOG; KOG3252; Eukaryota.
eggNOG; ENOG410ZSE4; LUCA.
GeneTree; ENSGT00390000009409; -.
HOGENOM; HOG000008222; -.
HOVERGEN; HBG052081; -.
InParanoid; Q9UBQ5; -.
KO; K15028; -.
OMA; YVQDQAK; -.
OrthoDB; EOG091G0IXT; -.
PhylomeDB; Q9UBQ5; -.
TreeFam; TF314893; -.
Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
Reactome; R-HSA-72649; Translation initiation complex formation.
Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
ChiTaRS; EIF3K; human.
EvolutionaryTrace; Q9UBQ5; -.
GeneWiki; EIF3K; -.
GenomeRNAi; 27335; -.
PRO; PR:Q9UBQ5; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000178982; -.
CleanEx; HS_EIF3K; -.
ExpressionAtlas; Q9UBQ5; baseline and differential.
Genevisible; Q9UBQ5; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0043022; F:ribosome binding; IEA:InterPro.
GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
GO; GO:0006446; P:regulation of translational initiation; IEA:InterPro.
GO; GO:0006413; P:translational initiation; IDA:UniProtKB.
Gene3D; 1.10.10.10; -; 1.
Gene3D; 1.25.40.250; -; 1.
HAMAP; MF_03010; eIF3k; 1.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR033464; CSN8_PSD8_EIF3K.
InterPro; IPR009374; eIF3k.
InterPro; IPR016020; Transl_init_fac_sub12_N_euk.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
PANTHER; PTHR13022; PTHR13022; 1.
Pfam; PF10075; CSN8_PSD8_EIF3K; 1.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF48371; SSF48371; 1.
PROSITE; PS50250; PCI; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; Initiation factor; Nucleus;
Phosphoprotein; Protein biosynthesis; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000255|HAMAP-Rule:MF_03010,
ECO:0000269|PubMed:17322308,
ECO:0000269|Ref.11}.
CHAIN 2 218 Eukaryotic translation initiation factor
3 subunit K.
/FTId=PRO_0000123546.
DOMAIN 42 204 PCI. {ECO:0000255|PROSITE-
ProRule:PRU01185}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000255|HAMAP-Rule:MF_03010,
ECO:0000269|PubMed:17322308,
ECO:0000269|Ref.11}.
MOD_RES 28 28 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 217 217 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
VAR_SEQ 210 218 VSSIMASSQ -> EW (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055475.
CONFLICT 119 119 Q -> K (in Ref. 6; AAD40193).
{ECO:0000305}.
HELIX 3 16 {ECO:0000244|PDB:1RZ4}.
HELIX 18 21 {ECO:0000244|PDB:1RZ4}.
HELIX 23 25 {ECO:0000244|PDB:1RZ4}.
HELIX 26 39 {ECO:0000244|PDB:1RZ4}.
HELIX 44 56 {ECO:0000244|PDB:1RZ4}.
HELIX 58 60 {ECO:0000244|PDB:1RZ4}.
HELIX 63 75 {ECO:0000244|PDB:1RZ4}.
TURN 76 78 {ECO:0000244|PDB:1RZ4}.
HELIX 81 87 {ECO:0000244|PDB:1RZ4}.
HELIX 91 94 {ECO:0000244|PDB:1RZ4}.
HELIX 99 110 {ECO:0000244|PDB:1RZ4}.
HELIX 114 120 {ECO:0000244|PDB:1RZ4}.
HELIX 126 129 {ECO:0000244|PDB:1RZ4}.
HELIX 134 149 {ECO:0000244|PDB:1RZ4}.
STRAND 151 153 {ECO:0000244|PDB:1RZ4}.
HELIX 155 161 {ECO:0000244|PDB:1RZ4}.
HELIX 167 177 {ECO:0000244|PDB:1RZ4}.
HELIX 192 195 {ECO:0000244|PDB:1RZ4}.
HELIX 207 214 {ECO:0000244|PDB:1RZ4}.
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


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