Full text data of EIF3K
EIF3K
(EIF3S12)
[Confidence: low (only semi-automatic identification from reviews)]
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)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
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)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9UBQ5
ID EIF3K_HUMAN Reviewed; 218 AA.
AC Q9UBQ5; A8K0I9; Q96IQ0; Q9Y6D1;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 131.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit K;
DE Short=eIF3k;
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 12;
DE AltName: Full=Muscle-specific gene M9 protein;
DE AltName: Full=PLAC-24;
DE AltName: Full=eIF-3 p25;
DE AltName: Full=eIF-3 p28;
GN Name=EIF3K; Synonyms=EIF3S12;
GN ORFNames=ARG134, HSPC029, MSTP001, PTD001;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-31, IDENTIFICATION
RP IN THE EIF-3 COMPLEX, INTERACTION WITH EIF3B; EIF3C; EIF3G AND EIF3J,
RP 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].
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].
RC TISSUE=Pituitary tumor;
RA Ye M., Song H., Peng Y., Huang Q., Dai M., Mao Y., Zhu H., Li G.,
RA Luo M., Hu R., Chen J.;
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.,
RA Liu S., Cao H.Q., Zhao Y., Liu D.Q., Ding J.F., Liu L.S., Gao R.L.,
RA Wu Q.Y., 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].
RC TISSUE=Stomach cancer;
RA Yanqiu Z., Huazhang A., Fei L., Baojun C., Taidong Q., Kaichun W.,
RA Jie D., 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].
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
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP PROTEIN SEQUENCE OF 2-8; 21-31 AND 39-52, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Zebisch A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [11]
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
RT 3(eIF3k) as a new interaction partner of cyclin D3.";
RL FEBS Lett. 573:139-146(2004).
RN [12]
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.,
RA Pestova T.V.;
RT "Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits
RT and its role in ribosomal dissociation and anti-association.";
RL RNA 11:470-486(2005).
RN [13]
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [14]
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 [15]
RP 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 [16]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3
RP COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
RP MASS SPECTROMETRY.
RX PubMed=17322308; DOI=10.1074/mcp.M600399-MCP200;
RA Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L.,
RA Hershey J.W.B., Doudna J.A., Robinson C.V., Leary J.A.;
RT "Structural characterization of the human eukaryotic initiation factor
RT 3 protein complex by mass spectrometry.";
RL Mol. Cell. Proteomics 6:1135-1146(2007).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217, AND MASS
RP SPECTROMETRY.
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 [18]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3
RP COMPLEX, 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
RT interaction map of the eukaryotic translation factor eIF3.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18139-18144(2008).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [21]
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.,
RA Buerckstuemmer T., 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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [24]
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
RT subunits.";
RL J. Biol. Chem. 279:34983-34990(2004).
CC -!- FUNCTION: Component of the eukaryotic translation initiation
CC factor 3 (eIF-3) complex, which is required for several steps in
CC the initiation of protein synthesis. The eIF-3 complex associates
CC with the 40S ribosome and facilitates the recruitment of eIF-1,
CC eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S
CC preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA
CC recruitment to the 43S PIC and scanning of the mRNA for AUG
CC recognition. The eIF-3 complex is also required for disassembly
CC and recycling of post-termination ribosomal complexes and
CC subsequently prevents premature joining of the 40S and 60S
CC ribosomal subunits prior to initiation.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor
CC 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B,
CC EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K,
CC EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable
CC modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I;
CC module B is composed of EIF3F, EIF3H, and EIF3M; and module C is
CC composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module
CC C binds EIF3B of module A and EIF3H of module B, thereby linking
CC the three modules. EIF3J is a labile subunit that binds to the
CC eIF-3 complex via EIF3B. The eIF-3 complex interacts with RPS6KB1
CC under conditions of nutrient depletion. Mitogenic stimulation
CC leads to binding and activation of a complex composed of MTOR and
CC RPTOR, leading to phosphorylation and release of RPS6KB1 and
CC binding of EIF4B to eIF-3. Interacts with CCND3, but not with
CC CCND1 and CCND2.
CC -!- INTERACTION:
CC Q9Q2G4:ORF (xeno); NbExp=5; IntAct=EBI-354344, EBI-6248094;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm.
CC -!- TISSUE SPECIFICITY: Ubiquitous, with the highest levels of
CC expression in brain, testis and kidney.
CC -!- MASS SPECTROMETRY: Mass=24970.6; Method=Unknown; Range=1-218;
CC Source=PubMed:17322308;
CC -!- MASS SPECTROMETRY: Mass=24971.1; Mass_error=0.2; Method=MALDI;
CC Range=1-218; Source=PubMed:18599441;
CC -!- SIMILARITY: Belongs to the eIF-3 subunit K family.
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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; CH471126; EAW56807.1; -; Genomic_DNA.
DR EMBL; BC001031; AAH01031.1; -; mRNA.
DR EMBL; BC007335; AAH07335.2; -; mRNA.
DR EMBL; BC007559; AAH07559.1; -; mRNA.
DR RefSeq; NP_037366.1; NM_013234.2.
DR UniGene; Hs.314359; -.
DR PDB; 1RZ4; X-ray; 2.10 A; A=1-218.
DR PDBsum; 1RZ4; -.
DR ProteinModelPortal; Q9UBQ5; -.
DR SMR; Q9UBQ5; 2-216.
DR DIP; DIP-32880N; -.
DR IntAct; Q9UBQ5; 12.
DR MINT; MINT-5002042; -.
DR STRING; 9606.ENSP00000248342; -.
DR PhosphoSite; Q9UBQ5; -.
DR DMDM; 23396628; -.
DR PaxDb; Q9UBQ5; -.
DR PeptideAtlas; Q9UBQ5; -.
DR PRIDE; Q9UBQ5; -.
DR DNASU; 27335; -.
DR Ensembl; ENST00000248342; ENSP00000248342; ENSG00000178982.
DR GeneID; 27335; -.
DR KEGG; hsa:27335; -.
DR UCSC; uc002oiz.1; human.
DR CTD; 27335; -.
DR GeneCards; GC19P039109; -.
DR HGNC; HGNC:24656; EIF3K.
DR HPA; HPA045446; -.
DR MIM; 609596; gene.
DR neXtProt; NX_Q9UBQ5; -.
DR PharmGKB; PA162384923; -.
DR eggNOG; NOG311878; -.
DR HOGENOM; HOG000008222; -.
DR HOVERGEN; HBG052081; -.
DR InParanoid; Q9UBQ5; -.
DR KO; K15028; -.
DR OMA; GLERYNP; -.
DR PhylomeDB; Q9UBQ5; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; EIF3K; human.
DR EvolutionaryTrace; Q9UBQ5; -.
DR GeneWiki; EIF3K; -.
DR GenomeRNAi; 27335; -.
DR NextBio; 50392; -.
DR PRO; PR:Q9UBQ5; -.
DR ArrayExpress; Q9UBQ5; -.
DR Bgee; Q9UBQ5; -.
DR CleanEx; HS_EIF3K; -.
DR Genevestigator; Q9UBQ5; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-HAMAP.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-HAMAP.
DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-HAMAP.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IEA:UniProtKB-HAMAP.
DR GO; GO:0006446; P:regulation of translational initiation; IEA:UniProtKB-HAMAP.
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; IPR009374; eIF3k.
DR InterPro; IPR016020; Transl_init_fac_sub12_N_euk.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR PANTHER; PTHR13022; PTHR13022; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Initiation factor; Nucleus; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 218 Eukaryotic translation initiation factor
FT 3 subunit K.
FT /FTId=PRO_0000123546.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 217 217 Phosphoserine.
FT CONFLICT 119 119 Q -> K (in Ref. 6; AAD40193).
FT HELIX 3 16
FT HELIX 18 21
FT HELIX 23 25
FT HELIX 26 39
FT HELIX 44 56
FT HELIX 58 60
FT HELIX 63 75
FT TURN 76 78
FT HELIX 81 87
FT HELIX 91 94
FT HELIX 99 110
FT HELIX 114 120
FT HELIX 126 129
FT HELIX 134 149
FT STRAND 151 153
FT HELIX 155 161
FT HELIX 167 177
FT HELIX 192 195
FT HELIX 207 214
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
//
ID EIF3K_HUMAN Reviewed; 218 AA.
AC Q9UBQ5; A8K0I9; Q96IQ0; Q9Y6D1;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 131.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit K;
DE Short=eIF3k;
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 12;
DE AltName: Full=Muscle-specific gene M9 protein;
DE AltName: Full=PLAC-24;
DE AltName: Full=eIF-3 p25;
DE AltName: Full=eIF-3 p28;
GN Name=EIF3K; Synonyms=EIF3S12;
GN ORFNames=ARG134, HSPC029, MSTP001, PTD001;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-31, IDENTIFICATION
RP IN THE EIF-3 COMPLEX, INTERACTION WITH EIF3B; EIF3C; EIF3G AND EIF3J,
RP 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].
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].
RC TISSUE=Pituitary tumor;
RA Ye M., Song H., Peng Y., Huang Q., Dai M., Mao Y., Zhu H., Li G.,
RA Luo M., Hu R., Chen J.;
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.,
RA Liu S., Cao H.Q., Zhao Y., Liu D.Q., Ding J.F., Liu L.S., Gao R.L.,
RA Wu Q.Y., 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].
RC TISSUE=Stomach cancer;
RA Yanqiu Z., Huazhang A., Fei L., Baojun C., Taidong Q., Kaichun W.,
RA Jie D., 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].
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
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP PROTEIN SEQUENCE OF 2-8; 21-31 AND 39-52, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Zebisch A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [11]
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
RT 3(eIF3k) as a new interaction partner of cyclin D3.";
RL FEBS Lett. 573:139-146(2004).
RN [12]
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.,
RA Pestova T.V.;
RT "Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits
RT and its role in ribosomal dissociation and anti-association.";
RL RNA 11:470-486(2005).
RN [13]
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [14]
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 [15]
RP 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 [16]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3
RP COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
RP MASS SPECTROMETRY.
RX PubMed=17322308; DOI=10.1074/mcp.M600399-MCP200;
RA Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L.,
RA Hershey J.W.B., Doudna J.A., Robinson C.V., Leary J.A.;
RT "Structural characterization of the human eukaryotic initiation factor
RT 3 protein complex by mass spectrometry.";
RL Mol. Cell. Proteomics 6:1135-1146(2007).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217, AND MASS
RP SPECTROMETRY.
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 [18]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3
RP COMPLEX, 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
RT interaction map of the eukaryotic translation factor eIF3.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18139-18144(2008).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [21]
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.,
RA Buerckstuemmer T., 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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [24]
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
RT subunits.";
RL J. Biol. Chem. 279:34983-34990(2004).
CC -!- FUNCTION: Component of the eukaryotic translation initiation
CC factor 3 (eIF-3) complex, which is required for several steps in
CC the initiation of protein synthesis. The eIF-3 complex associates
CC with the 40S ribosome and facilitates the recruitment of eIF-1,
CC eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S
CC preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA
CC recruitment to the 43S PIC and scanning of the mRNA for AUG
CC recognition. The eIF-3 complex is also required for disassembly
CC and recycling of post-termination ribosomal complexes and
CC subsequently prevents premature joining of the 40S and 60S
CC ribosomal subunits prior to initiation.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor
CC 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B,
CC EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K,
CC EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable
CC modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I;
CC module B is composed of EIF3F, EIF3H, and EIF3M; and module C is
CC composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module
CC C binds EIF3B of module A and EIF3H of module B, thereby linking
CC the three modules. EIF3J is a labile subunit that binds to the
CC eIF-3 complex via EIF3B. The eIF-3 complex interacts with RPS6KB1
CC under conditions of nutrient depletion. Mitogenic stimulation
CC leads to binding and activation of a complex composed of MTOR and
CC RPTOR, leading to phosphorylation and release of RPS6KB1 and
CC binding of EIF4B to eIF-3. Interacts with CCND3, but not with
CC CCND1 and CCND2.
CC -!- INTERACTION:
CC Q9Q2G4:ORF (xeno); NbExp=5; IntAct=EBI-354344, EBI-6248094;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm.
CC -!- TISSUE SPECIFICITY: Ubiquitous, with the highest levels of
CC expression in brain, testis and kidney.
CC -!- MASS SPECTROMETRY: Mass=24970.6; Method=Unknown; Range=1-218;
CC Source=PubMed:17322308;
CC -!- MASS SPECTROMETRY: Mass=24971.1; Mass_error=0.2; Method=MALDI;
CC Range=1-218; Source=PubMed:18599441;
CC -!- SIMILARITY: Belongs to the eIF-3 subunit K family.
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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; CH471126; EAW56807.1; -; Genomic_DNA.
DR EMBL; BC001031; AAH01031.1; -; mRNA.
DR EMBL; BC007335; AAH07335.2; -; mRNA.
DR EMBL; BC007559; AAH07559.1; -; mRNA.
DR RefSeq; NP_037366.1; NM_013234.2.
DR UniGene; Hs.314359; -.
DR PDB; 1RZ4; X-ray; 2.10 A; A=1-218.
DR PDBsum; 1RZ4; -.
DR ProteinModelPortal; Q9UBQ5; -.
DR SMR; Q9UBQ5; 2-216.
DR DIP; DIP-32880N; -.
DR IntAct; Q9UBQ5; 12.
DR MINT; MINT-5002042; -.
DR STRING; 9606.ENSP00000248342; -.
DR PhosphoSite; Q9UBQ5; -.
DR DMDM; 23396628; -.
DR PaxDb; Q9UBQ5; -.
DR PeptideAtlas; Q9UBQ5; -.
DR PRIDE; Q9UBQ5; -.
DR DNASU; 27335; -.
DR Ensembl; ENST00000248342; ENSP00000248342; ENSG00000178982.
DR GeneID; 27335; -.
DR KEGG; hsa:27335; -.
DR UCSC; uc002oiz.1; human.
DR CTD; 27335; -.
DR GeneCards; GC19P039109; -.
DR HGNC; HGNC:24656; EIF3K.
DR HPA; HPA045446; -.
DR MIM; 609596; gene.
DR neXtProt; NX_Q9UBQ5; -.
DR PharmGKB; PA162384923; -.
DR eggNOG; NOG311878; -.
DR HOGENOM; HOG000008222; -.
DR HOVERGEN; HBG052081; -.
DR InParanoid; Q9UBQ5; -.
DR KO; K15028; -.
DR OMA; GLERYNP; -.
DR PhylomeDB; Q9UBQ5; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; EIF3K; human.
DR EvolutionaryTrace; Q9UBQ5; -.
DR GeneWiki; EIF3K; -.
DR GenomeRNAi; 27335; -.
DR NextBio; 50392; -.
DR PRO; PR:Q9UBQ5; -.
DR ArrayExpress; Q9UBQ5; -.
DR Bgee; Q9UBQ5; -.
DR CleanEx; HS_EIF3K; -.
DR Genevestigator; Q9UBQ5; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-HAMAP.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-HAMAP.
DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-HAMAP.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IEA:UniProtKB-HAMAP.
DR GO; GO:0006446; P:regulation of translational initiation; IEA:UniProtKB-HAMAP.
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; IPR009374; eIF3k.
DR InterPro; IPR016020; Transl_init_fac_sub12_N_euk.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR PANTHER; PTHR13022; PTHR13022; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Initiation factor; Nucleus; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 218 Eukaryotic translation initiation factor
FT 3 subunit K.
FT /FTId=PRO_0000123546.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 217 217 Phosphoserine.
FT CONFLICT 119 119 Q -> K (in Ref. 6; AAD40193).
FT HELIX 3 16
FT HELIX 18 21
FT HELIX 23 25
FT HELIX 26 39
FT HELIX 44 56
FT HELIX 58 60
FT HELIX 63 75
FT TURN 76 78
FT HELIX 81 87
FT HELIX 91 94
FT HELIX 99 110
FT HELIX 114 120
FT HELIX 126 129
FT HELIX 134 149
FT STRAND 151 153
FT HELIX 155 161
FT HELIX 167 177
FT HELIX 192 195
FT HELIX 207 214
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
//
MIM
609596
*RECORD*
*FIELD* NO
609596
*FIELD* TI
*609596 EUKARYOTIC TRANSLATION INITIATION FACTOR 3, SUBUNIT K; EIF3K
;;EIF3-p28;;
PLAC24;;
read moreEUKARYOTIC TRANSLATION INITIATION FACTOR 3, SUBUNIT 12, FORMERLY;
EIF3S12, FORMERLY
*FIELD* TX
DESCRIPTION
The 700-kD eukaryotic translation initiation factor-3 (eIF3) is the
largest eIF and contains at least 12 subunits, including EIF2S12. eIF3
plays an essential role in translation by binding directly to the 40S
ribosomal subunit and promoting formation of the 40S preinitiation
complex (Mayeur et al., 2003).
CLONING
Karki et al. (2002) isolated rat Eif3s12, which they called Plac24, by
screening rat brain cytosol for cytoplasmic dynein intermediate chain
(see 603772)-binding proteins. They obtained human EIF3S12 by searching
an EST database using the rat sequence. The predicted human protein
contains 218 amino acids. Northern blot analysis of human tissues showed
ubiquitous expression of a 1-kb EIF3S12 transcript, with highest levels
in heart and skeletal muscle. Western blot analysis detected EIF3S12
protein in all human tissues examined.
By searching an EST database using the peptide sequence of a 28-kD
protein purified from HeLa cell eIF3 complex as query, Mayeur et al.
(2003) identified human EIF3S12, which they called EIF3K. EIF3S12
encodes a 218-amino acid protein composed of approximately 10% leucine
residues. In vitro transcription/translation of EIF3S12 resulted in
labeled protein that comigrated with the 28-kD protein found in eIF3
complex. Northern blot analysis detected ubiquitous expression of a
1.1-kb EIF3S12 transcript in human cell lines and tissues, with highest
levels in brain, testis, and kidney.
GENE FUNCTION
Karki et al. (2002) found that EIF3S12 did not coimmunoprecipitate with
cytoplasmic dynein, indicating it is not a dynein subunit. However,
affinity column binding and yeast 2-hybrid experiments showed direct
binding between EIF3S12 and dynein intermediate chain.
Immunohistochemistry experiments localized EIF3S12 to perinuclear
cytoplasmic regions in isolated epithelial cells and fibroblasts. In
epithelial cells, EIF3S12 localized to the cell surface at sites of
cell-cell contact and colocalized with E-cadherin (CDH1; 192090) and
beta-catenin (CTNNB1; 116806). Disruption of the actin cytoskeleton or
overexpression of beta-catenin resulted in loss of EIF3S12 expression at
sites of cell-cell contact.
Using immunoprecipitation and isoelectric focusing, Mayeur et al. (2003)
showed that EIF3S12 associated with the eIF3 complex.
Immunoprecipitation of baculovirus-infected cells demonstrated that
EIF3S12 associated with 5 core eIF3 subunits, and GST pull-down
experiments revealed direct interactions between EIF3S12 and EIF3C
(EIF3S8; 603916), EIF3G (EIF3S4; 603913), and EIF3J (EIF3S1; 603910).
Cell fractionation experiments localized EIF3S12 in the region of the
40S ribosomal subunit.
By yeast 2-hybrid analysis, Shen et al. (2004) identified EIF3S12 as a
binding partner of cyclin D3 (CCND3; 123834). GST pull-down experiments
and transient transfections showed that EIF3S12 and cyclin D3 bound both
in vitro and in vivo, and EIF3S12 did not bind cyclin D1 (CCND1; 168461)
or D2 (CCND2; 123833). Immunofluorescence revealed EIF3S12 distributed
in the nucleus and cytoplasm in a pattern that overlapped with that of
cyclin D3.
GENE STRUCTURE
By genomic sequence analysis, Mayeur et al. (2003) determined that the
EIF3S12 gene contains 8 exons.
MAPPING
By genomic sequence analysis, Mayeur et al. (2003) mapped the EIF3S12
gene to chromosome 19q13.2.
*FIELD* RF
1. Karki, S.; Ligon, L. A.; DeSantis, J.; Tokito, M.; Holzbaur, E.
L. F.: PLAC-24 is a cytoplasmic dynein-binding protein that is recruited
to sites of cell-cell contact. Molec. Biol. Cell 13: 1722-1734,
2002.
2. Mayeur, G. L.; Fraser, C. S.; Peiretti, F.; Block, K. L.; Hershey,
J. W. B.: Characterization of elF3k: a newly discovered subunit of
mammalian translation initiation factor elF3. Europ. J. Biochem. 270:
4133-4139, 2003.
3. 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.
*FIELD* CD
Laura L. Baxter: 9/22/2005
*FIELD* ED
mgross: 10/02/2007
mgross: 9/22/2005
*RECORD*
*FIELD* NO
609596
*FIELD* TI
*609596 EUKARYOTIC TRANSLATION INITIATION FACTOR 3, SUBUNIT K; EIF3K
;;EIF3-p28;;
PLAC24;;
read moreEUKARYOTIC TRANSLATION INITIATION FACTOR 3, SUBUNIT 12, FORMERLY;
EIF3S12, FORMERLY
*FIELD* TX
DESCRIPTION
The 700-kD eukaryotic translation initiation factor-3 (eIF3) is the
largest eIF and contains at least 12 subunits, including EIF2S12. eIF3
plays an essential role in translation by binding directly to the 40S
ribosomal subunit and promoting formation of the 40S preinitiation
complex (Mayeur et al., 2003).
CLONING
Karki et al. (2002) isolated rat Eif3s12, which they called Plac24, by
screening rat brain cytosol for cytoplasmic dynein intermediate chain
(see 603772)-binding proteins. They obtained human EIF3S12 by searching
an EST database using the rat sequence. The predicted human protein
contains 218 amino acids. Northern blot analysis of human tissues showed
ubiquitous expression of a 1-kb EIF3S12 transcript, with highest levels
in heart and skeletal muscle. Western blot analysis detected EIF3S12
protein in all human tissues examined.
By searching an EST database using the peptide sequence of a 28-kD
protein purified from HeLa cell eIF3 complex as query, Mayeur et al.
(2003) identified human EIF3S12, which they called EIF3K. EIF3S12
encodes a 218-amino acid protein composed of approximately 10% leucine
residues. In vitro transcription/translation of EIF3S12 resulted in
labeled protein that comigrated with the 28-kD protein found in eIF3
complex. Northern blot analysis detected ubiquitous expression of a
1.1-kb EIF3S12 transcript in human cell lines and tissues, with highest
levels in brain, testis, and kidney.
GENE FUNCTION
Karki et al. (2002) found that EIF3S12 did not coimmunoprecipitate with
cytoplasmic dynein, indicating it is not a dynein subunit. However,
affinity column binding and yeast 2-hybrid experiments showed direct
binding between EIF3S12 and dynein intermediate chain.
Immunohistochemistry experiments localized EIF3S12 to perinuclear
cytoplasmic regions in isolated epithelial cells and fibroblasts. In
epithelial cells, EIF3S12 localized to the cell surface at sites of
cell-cell contact and colocalized with E-cadherin (CDH1; 192090) and
beta-catenin (CTNNB1; 116806). Disruption of the actin cytoskeleton or
overexpression of beta-catenin resulted in loss of EIF3S12 expression at
sites of cell-cell contact.
Using immunoprecipitation and isoelectric focusing, Mayeur et al. (2003)
showed that EIF3S12 associated with the eIF3 complex.
Immunoprecipitation of baculovirus-infected cells demonstrated that
EIF3S12 associated with 5 core eIF3 subunits, and GST pull-down
experiments revealed direct interactions between EIF3S12 and EIF3C
(EIF3S8; 603916), EIF3G (EIF3S4; 603913), and EIF3J (EIF3S1; 603910).
Cell fractionation experiments localized EIF3S12 in the region of the
40S ribosomal subunit.
By yeast 2-hybrid analysis, Shen et al. (2004) identified EIF3S12 as a
binding partner of cyclin D3 (CCND3; 123834). GST pull-down experiments
and transient transfections showed that EIF3S12 and cyclin D3 bound both
in vitro and in vivo, and EIF3S12 did not bind cyclin D1 (CCND1; 168461)
or D2 (CCND2; 123833). Immunofluorescence revealed EIF3S12 distributed
in the nucleus and cytoplasm in a pattern that overlapped with that of
cyclin D3.
GENE STRUCTURE
By genomic sequence analysis, Mayeur et al. (2003) determined that the
EIF3S12 gene contains 8 exons.
MAPPING
By genomic sequence analysis, Mayeur et al. (2003) mapped the EIF3S12
gene to chromosome 19q13.2.
*FIELD* RF
1. Karki, S.; Ligon, L. A.; DeSantis, J.; Tokito, M.; Holzbaur, E.
L. F.: PLAC-24 is a cytoplasmic dynein-binding protein that is recruited
to sites of cell-cell contact. Molec. Biol. Cell 13: 1722-1734,
2002.
2. Mayeur, G. L.; Fraser, C. S.; Peiretti, F.; Block, K. L.; Hershey,
J. W. B.: Characterization of elF3k: a newly discovered subunit of
mammalian translation initiation factor elF3. Europ. J. Biochem. 270:
4133-4139, 2003.
3. 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.
*FIELD* CD
Laura L. Baxter: 9/22/2005
*FIELD* ED
mgross: 10/02/2007
mgross: 9/22/2005