Full text data of EIF3C
EIF3C
(EIF3S8)
[Confidence: low (only semi-automatic identification from reviews)]
Eukaryotic translation initiation factor 3 subunit C; eIF3c (Eukaryotic translation initiation factor 3 subunit 8; eIF3 p110)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Eukaryotic translation initiation factor 3 subunit C; eIF3c (Eukaryotic translation initiation factor 3 subunit 8; eIF3 p110)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q99613
ID EIF3C_HUMAN Reviewed; 913 AA.
AC Q99613; A8K7Z0; B2RXG3; O00215; Q9BW98;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1997, sequence version 1.
DT 22-JAN-2014, entry version 146.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit C;
DE Short=eIF3c;
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 8;
DE AltName: Full=eIF3 p110;
GN Name=EIF3C; Synonyms=EIF3S8;
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 [GENOMIC DNA].
RX PubMed=8995409; DOI=10.1074/jbc.272.28.17668;
RA Asano K., Kinzy T.G., Merrick W.C., Hershey J.W.B.;
RT "Conservation and diversity of eukaryotic translation initiation
RT factor eIF3.";
RL J. Biol. Chem. 272:1101-1109(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10493829; DOI=10.1006/geno.1999.5927;
RA Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R.,
RA Fuhrmann J., Mason T., Crosby M.L., Barnstead M., Cronin L.,
RA Mays A.D., Cao Y., Xu R.X., Kang H.-L., Mitchell S., Eichler E.E.,
RA Harris P.C., Venter J.C., Adams M.D.;
RT "Genome duplications and other features in 12 Mb of DNA sequence from
RT human chromosome 16p and 16q.";
RL Genomics 60:295-308(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Synovium;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Lymph, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 589-913.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP INTERACTION WITH EIF3B.
RX PubMed=14519125; DOI=10.1046/j.1432-1033.2003.03807.x;
RA Mayeur G.L., Fraser C.S., Peiretti F., Block K.L., Hershey J.W.B.;
RT "Characterization of eIF3k: a newly discovered subunit of mammalian
RT translation initiation factor eIF3.";
RL Eur. J. Biochem. 270:4133-4139(2003).
RN [8]
RP INTERACTION WITH MTOR; RPTOR AND RPS6KB1.
RX PubMed=16286006; DOI=10.1016/j.cell.2005.10.024;
RA Holz M.K., Ballif B.A., Gygi S.P., Blenis J.;
RT "mTOR and S6K1 mediate assembly of the translation preinitiation
RT complex through dynamic protein interchange and ordered
RT phosphorylation events.";
RL Cell 123:569-580(2005).
RN [9]
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 [10]
RP INTERACTION WITH IFIT1 AND IFIT2.
RX PubMed=16023166; DOI=10.1016/j.virol.2005.06.011;
RA Terenzi F., Pal S., Sen G.C.;
RT "Induction and mode of action of the viral stress-inducible murine
RT proteins, P56 and P54.";
RL Virology 340:116-124(2005).
RN [11]
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 [12]
RP INTERACTION WITH IFIT2.
RX PubMed=16973618; DOI=10.1074/jbc.M605771200;
RA Terenzi F., Hui D.J., Merrick W.C., Sen G.C.;
RT "Distinct induction patterns and functions of two closely related
RT interferon-inducible human genes, ISG54 and ISG56.";
RL J. Biol. Chem. 281:34064-34071(2006).
RN [13]
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 [14]
RP INTERACTION WITH EIF3E.
RX PubMed=17468741; DOI=10.1038/sj.embor.7400955;
RA Morris C., Wittmann J., Jaeck H.-M., Jalinot P.;
RT "Human INT6/eIF3e is required for nonsense-mediated mRNA decay.";
RL EMBO Rep. 8:596-602(2007).
RN [15]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3
RP COMPLEX, PHOSPHORYLATION AT SER-9; SER-11; SER-13; SER-15; SER-16;
RP SER-18; SER-39; SER-166; THR-524 AND SER-909, AND MASS SPECTROMETRY.
RX PubMed=17322308; DOI=10.1074/mcp.M600399-MCP200;
RA Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L.,
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 [16]
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 [17]
RP IDENTIFICATION IN A HCV IRES-MEDIATED TRANSLATION COMPLEX.
RX PubMed=19541769; DOI=10.1261/rna.1578409;
RA Weinlich S., Huettelmaier S., Schierhorn A., Behrens S.-E.,
RA Ostareck-Lederer A., Ostareck D.H.;
RT "IGF2BP1 enhances HCV IRES-mediated translation initiation via the
RT 3'UTR.";
RL RNA 15:1528-1542(2009).
RN [18]
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 [19]
RP INTERACTION WITH ALKBH4.
RX PubMed=23145062; DOI=10.1371/journal.pone.0049045;
RA Bjornstad L.G., Meza T.J., Otterlei M., Olafsrud S.M.,
RA Meza-Zepeda L.A., Falnes P.O.;
RT "Human ALKBH4 interacts with proteins associated with transcription.";
RL PLoS ONE 7:E49045-E49045(2012).
RN [20]
RP 3D-STRUCTURE MODELING, AND ELECTRON MICROSCOPY.
RX PubMed=16322461; DOI=10.1126/science.1118977;
RA Siridechadilok B., Fraser C.S., Hall R.J., Doudna J.A., Nogales E.;
RT "Structural roles for human translation factor eIF3 in initiation of
RT protein synthesis.";
RL Science 310:1513-1515(2005).
CC -!- FUNCTION: Component of the eukaryotic translation initiation
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. Identified in a HCV IRES-mediated
CC translation complex, at least composed of EIF3C, IGF2BP1, RPS3 and
CC HCV RNA-replicon. Interacts with ALKBH4, IFIT1 and IFIT2.
CC -!- INTERACTION:
CC O00571:DDX3X; NbExp=3; IntAct=EBI-353741, EBI-353779;
CC Q9Q2G4:ORF (xeno); NbExp=5; IntAct=EBI-353741, EBI-6248094;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- PTM: Phosphorylated. Phosphorylation is enhanced upon serum
CC stimulation.
CC -!- MASS SPECTROMETRY: Mass=106143.8; Method=Unknown; Range=1-913;
CC Source=PubMed:17322308;
CC -!- MASS SPECTROMETRY: Mass=106855; Mass_error=40; Method=MALDI;
CC Range=1-913; Source=PubMed:18599441;
CC -!- SIMILARITY: Belongs to the eIF-3 subunit C family.
CC -!- SIMILARITY: Contains 1 PCI domain.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org//Genes/EIF3CID44187ch16p11.html";
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DR EMBL; U46025; AAD03462.1; -; Genomic_DNA.
DR EMBL; AC002544; AAC27426.1; -; Genomic_DNA.
DR EMBL; U91326; AAC27674.1; -; Genomic_DNA.
DR EMBL; AK000739; BAA91352.1; -; mRNA.
DR EMBL; AK292155; BAF84844.1; -; mRNA.
DR EMBL; BC000533; AAH00533.1; -; mRNA.
DR EMBL; BC001571; AAH01571.1; -; mRNA.
DR EMBL; BC071705; AAH71705.1; -; mRNA.
DR EMBL; BC157842; AAI57843.1; -; mRNA.
DR EMBL; BC157849; AAI57850.1; -; mRNA.
DR EMBL; CH878380; EAW50492.1; -; Genomic_DNA.
DR EMBL; BT007335; AAP35999.1; -; mRNA.
DR RefSeq; NP_001032897.1; NM_001037808.2.
DR RefSeq; NP_001186071.1; NM_001199142.1.
DR RefSeq; NP_001254503.1; NM_001267574.2.
DR RefSeq; NP_001273407.1; NM_001286478.1.
DR RefSeq; NP_003743.1; NM_003752.4.
DR RefSeq; XP_005255703.1; XM_005255646.1.
DR UniGene; Hs.567374; -.
DR ProteinModelPortal; Q99613; -.
DR DIP; DIP-32865N; -.
DR IntAct; Q99613; 23.
DR MINT; MINT-5000313; -.
DR STRING; 9606.ENSP00000332604; -.
DR PhosphoSite; Q99613; -.
DR DMDM; 6685539; -.
DR PaxDb; Q99613; -.
DR PeptideAtlas; Q99613; -.
DR PRIDE; Q99613; -.
DR DNASU; 8663; -.
DR Ensembl; ENST00000331666; ENSP00000332604; ENSG00000184110.
DR Ensembl; ENST00000395587; ENSP00000378953; ENSG00000184110.
DR Ensembl; ENST00000566501; ENSP00000457963; ENSG00000184110.
DR Ensembl; ENST00000566866; ENSP00000457418; ENSG00000184110.
DR GeneID; 8663; -.
DR KEGG; hsa:8663; -.
DR UCSC; uc002dpg.5; human.
DR CTD; 8663; -.
DR GeneCards; GC16P028700; -.
DR H-InvDB; HIX0038592; -.
DR HGNC; HGNC:3279; EIF3C.
DR HPA; CAB034045; -.
DR MIM; 603916; gene.
DR neXtProt; NX_Q99613; -.
DR PharmGKB; PA162384646; -.
DR eggNOG; NOG305883; -.
DR HOGENOM; HOG000029414; -.
DR HOVERGEN; HBG035174; -.
DR InParanoid; Q99613; -.
DR KO; K03252; -.
DR OMA; EEGKQTV; -.
DR OrthoDB; EOG7DC23R; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; EIF3CL; human.
DR GeneWiki; EIF3C; -.
DR GenomeRNAi; 8663; -.
DR NextBio; 32493; -.
DR PRO; PR:Q99613; -.
DR ArrayExpress; Q99613; -.
DR Bgee; Q99613; -.
DR CleanEx; HS_EIF3C; -.
DR CleanEx; HS_EIF3CL; -.
DR Genevestigator; Q99613; -.
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: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 HAMAP; MF_03002; eIF3c; 1; -.
DR InterPro; IPR027516; EIF3C.
DR InterPro; IPR008905; EIF3C_N_dom.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR Pfam; PF05470; eIF-3c_N; 2.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; Initiation factor; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1 913 Eukaryotic translation initiation factor
FT 3 subunit C.
FT /FTId=PRO_0000123525.
FT DOMAIN 712 846 PCI.
FT COMPBIAS 164 189 Asp/Glu-rich (acidic).
FT COMPBIAS 243 246 Poly-Glu.
FT COMPBIAS 291 294 Poly-Glu.
FT MOD_RES 9 9 Phosphoserine.
FT MOD_RES 11 11 Phosphoserine.
FT MOD_RES 13 13 Phosphoserine.
FT MOD_RES 15 15 Phosphoserine.
FT MOD_RES 16 16 Phosphoserine.
FT MOD_RES 18 18 Phosphoserine.
FT MOD_RES 39 39 Phosphoserine.
FT MOD_RES 166 166 Phosphoserine.
FT MOD_RES 524 524 Phosphothreonine.
FT MOD_RES 909 909 Phosphoserine.
FT CONFLICT 313 314 EK -> VR (in Ref. 2; AAC27674).
SQ SEQUENCE 913 AA; 105344 MW; CE5029F4EB51C1AA CRC64;
MSRFFTTGSD SESESSLSGE ELVTKPVGGN YGKQPLLLSE DEEDTKRVVR SAKDKRFEEL
TNLIRTIRNA MKIRDVTKCL EEFELLGKAY GKAKSIVDKE GVPRFYIRIL ADLEDYLNEL
WEDKEGKKKM NKNNAKALST LRQKIRKYNR DFESHITSYK QNPEQSADED AEKNEEDSEG
SSDEDEDEDG VSAATFLKKK SEAPSGESRK FLKKMDDEDE DSEDSEDDED WDTGSTSSDS
DSEEEEGKQT ALASRFLKKA PTTDEDKKAA EKKREDKAKK KHDRKSKRLD EEEEDNEGGE
WERVRGGVPL VKEKPKMFAK GTEITHAVVI KKLNEILQAR GKKGTDRAAQ IELLQLLVQI
AAENNLGEGV IVKIKFNIIA SLYDYNPNLA TYMKPEMWGK CLDCINELMD ILFANPNIFV
GENILEESEN LHNADQPLRV RGCILTLVER MDEEFTKIMQ NTDPHSQEYV EHLKDEAQVC
AIIERVQRYL EEKGTTEEVC RIYLLRILHT YYKFDYKAHQ RQLTPPEGSS KSEQDQAENE
GEDSAVLMER LCKYIYAKDR TDRIRTCAIL CHIYHHALHS RWYQARDLML MSHLQDNIQH
ADPPVQILYN RTMVQLGICA FRQGLTKDAH NALLDIQSSG RAKELLGQGL LLRSLQERNQ
EQEKVERRRQ VPFHLHINLE LLECVYLVSA MLLEIPYMAA HESDARRRMI SKQFHHQLRV
GERQPLLGPP ESMREHVVAA SKAMKMGDWK TCHSFIINEK MNGKVWDLFP EADKVRTMLV
RKIQEESLRT YLFTYSSVYD SISMETLSDM FELDLPTVHS IISKMIINEE LMASLDQPTQ
TVVMHRTEPT AQQNLALQLA EKLGSLVENN ERVFDHKQGT YGGYFRDQKD GYRKNEGYMR
RGGYRQQQSQ TAY
//
ID EIF3C_HUMAN Reviewed; 913 AA.
AC Q99613; A8K7Z0; B2RXG3; O00215; Q9BW98;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1997, sequence version 1.
DT 22-JAN-2014, entry version 146.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit C;
DE Short=eIF3c;
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 8;
DE AltName: Full=eIF3 p110;
GN Name=EIF3C; Synonyms=EIF3S8;
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 [GENOMIC DNA].
RX PubMed=8995409; DOI=10.1074/jbc.272.28.17668;
RA Asano K., Kinzy T.G., Merrick W.C., Hershey J.W.B.;
RT "Conservation and diversity of eukaryotic translation initiation
RT factor eIF3.";
RL J. Biol. Chem. 272:1101-1109(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10493829; DOI=10.1006/geno.1999.5927;
RA Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R.,
RA Fuhrmann J., Mason T., Crosby M.L., Barnstead M., Cronin L.,
RA Mays A.D., Cao Y., Xu R.X., Kang H.-L., Mitchell S., Eichler E.E.,
RA Harris P.C., Venter J.C., Adams M.D.;
RT "Genome duplications and other features in 12 Mb of DNA sequence from
RT human chromosome 16p and 16q.";
RL Genomics 60:295-308(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Synovium;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Lymph, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 589-913.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP INTERACTION WITH EIF3B.
RX PubMed=14519125; DOI=10.1046/j.1432-1033.2003.03807.x;
RA Mayeur G.L., Fraser C.S., Peiretti F., Block K.L., Hershey J.W.B.;
RT "Characterization of eIF3k: a newly discovered subunit of mammalian
RT translation initiation factor eIF3.";
RL Eur. J. Biochem. 270:4133-4139(2003).
RN [8]
RP INTERACTION WITH MTOR; RPTOR AND RPS6KB1.
RX PubMed=16286006; DOI=10.1016/j.cell.2005.10.024;
RA Holz M.K., Ballif B.A., Gygi S.P., Blenis J.;
RT "mTOR and S6K1 mediate assembly of the translation preinitiation
RT complex through dynamic protein interchange and ordered
RT phosphorylation events.";
RL Cell 123:569-580(2005).
RN [9]
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 [10]
RP INTERACTION WITH IFIT1 AND IFIT2.
RX PubMed=16023166; DOI=10.1016/j.virol.2005.06.011;
RA Terenzi F., Pal S., Sen G.C.;
RT "Induction and mode of action of the viral stress-inducible murine
RT proteins, P56 and P54.";
RL Virology 340:116-124(2005).
RN [11]
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 [12]
RP INTERACTION WITH IFIT2.
RX PubMed=16973618; DOI=10.1074/jbc.M605771200;
RA Terenzi F., Hui D.J., Merrick W.C., Sen G.C.;
RT "Distinct induction patterns and functions of two closely related
RT interferon-inducible human genes, ISG54 and ISG56.";
RL J. Biol. Chem. 281:34064-34071(2006).
RN [13]
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 [14]
RP INTERACTION WITH EIF3E.
RX PubMed=17468741; DOI=10.1038/sj.embor.7400955;
RA Morris C., Wittmann J., Jaeck H.-M., Jalinot P.;
RT "Human INT6/eIF3e is required for nonsense-mediated mRNA decay.";
RL EMBO Rep. 8:596-602(2007).
RN [15]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3
RP COMPLEX, PHOSPHORYLATION AT SER-9; SER-11; SER-13; SER-15; SER-16;
RP SER-18; SER-39; SER-166; THR-524 AND SER-909, AND MASS SPECTROMETRY.
RX PubMed=17322308; DOI=10.1074/mcp.M600399-MCP200;
RA Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L.,
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 [16]
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 [17]
RP IDENTIFICATION IN A HCV IRES-MEDIATED TRANSLATION COMPLEX.
RX PubMed=19541769; DOI=10.1261/rna.1578409;
RA Weinlich S., Huettelmaier S., Schierhorn A., Behrens S.-E.,
RA Ostareck-Lederer A., Ostareck D.H.;
RT "IGF2BP1 enhances HCV IRES-mediated translation initiation via the
RT 3'UTR.";
RL RNA 15:1528-1542(2009).
RN [18]
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 [19]
RP INTERACTION WITH ALKBH4.
RX PubMed=23145062; DOI=10.1371/journal.pone.0049045;
RA Bjornstad L.G., Meza T.J., Otterlei M., Olafsrud S.M.,
RA Meza-Zepeda L.A., Falnes P.O.;
RT "Human ALKBH4 interacts with proteins associated with transcription.";
RL PLoS ONE 7:E49045-E49045(2012).
RN [20]
RP 3D-STRUCTURE MODELING, AND ELECTRON MICROSCOPY.
RX PubMed=16322461; DOI=10.1126/science.1118977;
RA Siridechadilok B., Fraser C.S., Hall R.J., Doudna J.A., Nogales E.;
RT "Structural roles for human translation factor eIF3 in initiation of
RT protein synthesis.";
RL Science 310:1513-1515(2005).
CC -!- FUNCTION: Component of the eukaryotic translation initiation
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. Identified in a HCV IRES-mediated
CC translation complex, at least composed of EIF3C, IGF2BP1, RPS3 and
CC HCV RNA-replicon. Interacts with ALKBH4, IFIT1 and IFIT2.
CC -!- INTERACTION:
CC O00571:DDX3X; NbExp=3; IntAct=EBI-353741, EBI-353779;
CC Q9Q2G4:ORF (xeno); NbExp=5; IntAct=EBI-353741, EBI-6248094;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- PTM: Phosphorylated. Phosphorylation is enhanced upon serum
CC stimulation.
CC -!- MASS SPECTROMETRY: Mass=106143.8; Method=Unknown; Range=1-913;
CC Source=PubMed:17322308;
CC -!- MASS SPECTROMETRY: Mass=106855; Mass_error=40; Method=MALDI;
CC Range=1-913; Source=PubMed:18599441;
CC -!- SIMILARITY: Belongs to the eIF-3 subunit C family.
CC -!- SIMILARITY: Contains 1 PCI domain.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org//Genes/EIF3CID44187ch16p11.html";
CC -----------------------------------------------------------------------
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DR EMBL; U46025; AAD03462.1; -; Genomic_DNA.
DR EMBL; AC002544; AAC27426.1; -; Genomic_DNA.
DR EMBL; U91326; AAC27674.1; -; Genomic_DNA.
DR EMBL; AK000739; BAA91352.1; -; mRNA.
DR EMBL; AK292155; BAF84844.1; -; mRNA.
DR EMBL; BC000533; AAH00533.1; -; mRNA.
DR EMBL; BC001571; AAH01571.1; -; mRNA.
DR EMBL; BC071705; AAH71705.1; -; mRNA.
DR EMBL; BC157842; AAI57843.1; -; mRNA.
DR EMBL; BC157849; AAI57850.1; -; mRNA.
DR EMBL; CH878380; EAW50492.1; -; Genomic_DNA.
DR EMBL; BT007335; AAP35999.1; -; mRNA.
DR RefSeq; NP_001032897.1; NM_001037808.2.
DR RefSeq; NP_001186071.1; NM_001199142.1.
DR RefSeq; NP_001254503.1; NM_001267574.2.
DR RefSeq; NP_001273407.1; NM_001286478.1.
DR RefSeq; NP_003743.1; NM_003752.4.
DR RefSeq; XP_005255703.1; XM_005255646.1.
DR UniGene; Hs.567374; -.
DR ProteinModelPortal; Q99613; -.
DR DIP; DIP-32865N; -.
DR IntAct; Q99613; 23.
DR MINT; MINT-5000313; -.
DR STRING; 9606.ENSP00000332604; -.
DR PhosphoSite; Q99613; -.
DR DMDM; 6685539; -.
DR PaxDb; Q99613; -.
DR PeptideAtlas; Q99613; -.
DR PRIDE; Q99613; -.
DR DNASU; 8663; -.
DR Ensembl; ENST00000331666; ENSP00000332604; ENSG00000184110.
DR Ensembl; ENST00000395587; ENSP00000378953; ENSG00000184110.
DR Ensembl; ENST00000566501; ENSP00000457963; ENSG00000184110.
DR Ensembl; ENST00000566866; ENSP00000457418; ENSG00000184110.
DR GeneID; 8663; -.
DR KEGG; hsa:8663; -.
DR UCSC; uc002dpg.5; human.
DR CTD; 8663; -.
DR GeneCards; GC16P028700; -.
DR H-InvDB; HIX0038592; -.
DR HGNC; HGNC:3279; EIF3C.
DR HPA; CAB034045; -.
DR MIM; 603916; gene.
DR neXtProt; NX_Q99613; -.
DR PharmGKB; PA162384646; -.
DR eggNOG; NOG305883; -.
DR HOGENOM; HOG000029414; -.
DR HOVERGEN; HBG035174; -.
DR InParanoid; Q99613; -.
DR KO; K03252; -.
DR OMA; EEGKQTV; -.
DR OrthoDB; EOG7DC23R; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; EIF3CL; human.
DR GeneWiki; EIF3C; -.
DR GenomeRNAi; 8663; -.
DR NextBio; 32493; -.
DR PRO; PR:Q99613; -.
DR ArrayExpress; Q99613; -.
DR Bgee; Q99613; -.
DR CleanEx; HS_EIF3C; -.
DR CleanEx; HS_EIF3CL; -.
DR Genevestigator; Q99613; -.
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: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 HAMAP; MF_03002; eIF3c; 1; -.
DR InterPro; IPR027516; EIF3C.
DR InterPro; IPR008905; EIF3C_N_dom.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR Pfam; PF05470; eIF-3c_N; 2.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; Initiation factor; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1 913 Eukaryotic translation initiation factor
FT 3 subunit C.
FT /FTId=PRO_0000123525.
FT DOMAIN 712 846 PCI.
FT COMPBIAS 164 189 Asp/Glu-rich (acidic).
FT COMPBIAS 243 246 Poly-Glu.
FT COMPBIAS 291 294 Poly-Glu.
FT MOD_RES 9 9 Phosphoserine.
FT MOD_RES 11 11 Phosphoserine.
FT MOD_RES 13 13 Phosphoserine.
FT MOD_RES 15 15 Phosphoserine.
FT MOD_RES 16 16 Phosphoserine.
FT MOD_RES 18 18 Phosphoserine.
FT MOD_RES 39 39 Phosphoserine.
FT MOD_RES 166 166 Phosphoserine.
FT MOD_RES 524 524 Phosphothreonine.
FT MOD_RES 909 909 Phosphoserine.
FT CONFLICT 313 314 EK -> VR (in Ref. 2; AAC27674).
SQ SEQUENCE 913 AA; 105344 MW; CE5029F4EB51C1AA CRC64;
MSRFFTTGSD SESESSLSGE ELVTKPVGGN YGKQPLLLSE DEEDTKRVVR SAKDKRFEEL
TNLIRTIRNA MKIRDVTKCL EEFELLGKAY GKAKSIVDKE GVPRFYIRIL ADLEDYLNEL
WEDKEGKKKM NKNNAKALST LRQKIRKYNR DFESHITSYK QNPEQSADED AEKNEEDSEG
SSDEDEDEDG VSAATFLKKK SEAPSGESRK FLKKMDDEDE DSEDSEDDED WDTGSTSSDS
DSEEEEGKQT ALASRFLKKA PTTDEDKKAA EKKREDKAKK KHDRKSKRLD EEEEDNEGGE
WERVRGGVPL VKEKPKMFAK GTEITHAVVI KKLNEILQAR GKKGTDRAAQ IELLQLLVQI
AAENNLGEGV IVKIKFNIIA SLYDYNPNLA TYMKPEMWGK CLDCINELMD ILFANPNIFV
GENILEESEN LHNADQPLRV RGCILTLVER MDEEFTKIMQ NTDPHSQEYV EHLKDEAQVC
AIIERVQRYL EEKGTTEEVC RIYLLRILHT YYKFDYKAHQ RQLTPPEGSS KSEQDQAENE
GEDSAVLMER LCKYIYAKDR TDRIRTCAIL CHIYHHALHS RWYQARDLML MSHLQDNIQH
ADPPVQILYN RTMVQLGICA FRQGLTKDAH NALLDIQSSG RAKELLGQGL LLRSLQERNQ
EQEKVERRRQ VPFHLHINLE LLECVYLVSA MLLEIPYMAA HESDARRRMI SKQFHHQLRV
GERQPLLGPP ESMREHVVAA SKAMKMGDWK TCHSFIINEK MNGKVWDLFP EADKVRTMLV
RKIQEESLRT YLFTYSSVYD SISMETLSDM FELDLPTVHS IISKMIINEE LMASLDQPTQ
TVVMHRTEPT AQQNLALQLA EKLGSLVENN ERVFDHKQGT YGGYFRDQKD GYRKNEGYMR
RGGYRQQQSQ TAY
//
MIM
603916
*RECORD*
*FIELD* NO
603916
*FIELD* TI
*603916 EUKARYOTIC TRANSLATION INITIATION FACTOR 3, SUBUNIT C; EIF3C
;;EIF3-p110;;
read moreEUKARYOTIC TRANSLATION INITIATION FACTOR 3, SUBUNIT 8, FORMERLY; EIF3S8,
FORMERLY
*FIELD* TX
DESCRIPTION
Eukaryotic initiation factor-3 (eIF3) is the largest of the eIFs and
consists of at least 10 nonidentical subunits, including EIF2C (Asano et
al., 1997).
CLONING
Asano et al. (1997) demonstrated that the 115-kD component of HeLa cell
eIF3 is actually composed of 2 proteins, p116 (PRT1; 603917) and p110.
By screening a HeLa cell expression library with antibodies against the
115-kD band, these authors identified cDNAs encoding p110. The predicted
913-amino acid p110 protein has a pI of 5.8 and is unrelated to p116.
p110 shares 31% identity to the S. cerevisiae Nip1 protein, which is
thought to be involved in nuclear import and the initiation phase of
protein synthesis. Asano et al. (1997) found that the p116, p110, and
p36 (603911) subunits localize on 40S ribosomes in cells active in
translation and coimmunoprecipitate with p170 (602039), indicating that
these proteins are integral components of eIF3. Northern blot analysis
revealed that p110 is expressed as a 3-kb mRNA.
GENE FUNCTION
By reciprocal yeast 2-hybrid and coimmunoprecipitation analyses of the
human STS26T malignant schwannoma cell line, Scoles et al. (2006) showed
that isoforms 1 and 2 of schwannomin (NF2; 607379) interacted with
EIF3C. Mutation analysis revealed that the FERM domain of schwannomin
interacted with the C-terminal half of EIF3C. Immunofluorescence
microscopy of STS26T cells showed that the 2 proteins partly colocalized
at punctate perinuclear structures and at some membranous structures.
Overexpression of EIF3C in STS26T cells elevated cell proliferation, and
schwannomin countered this effect. Western blot analysis revealed an
inverse abundance of schwannomin and EIF3C in human meningiomas.
MAPPING
Gross (2011) mapped the EIF3C gene to chromosome 16p11.2 based on an
alignment of the EIF3C sequence (GenBank GENBANK BC000533) with the
genomic sequence (GRCh37). A nearly identical copy of EIF3C, designated
EIF3CL, also maps to chromosome 16p11.2.
*FIELD* RF
1. Asano, K.; Kinzy, T. G.; Merrick, W. C.; Hershey, J. W. B.: Conservation
and diversity of eukaryotic translation initiation factor eIF3. J.
Biol. Chem. 272: 1101-1109, 1997.
2. Gross, M. B.: Personal Communication. Baltimore, Md. 5/20/2011.
3. Scoles, D. R.; Yong, W. H.; Qin, Y.; Wawrowsky, K.; Pulst, S. M.
: Schwannomin inhibits tumorigenesis through direct interaction with
the eukaryotic initiation factor subunit c (elF3c). Hum. Molec. Genet. 15:
1059-1070, 2006.
*FIELD* CN
Matthew B. Gross - updated: 05/20/2011
Patricia A. Hartz - updated: 4/28/2011
*FIELD* CD
Rebekah S. Rasooly: 6/16/1999
*FIELD* ED
mgross: 05/20/2011
mgross: 5/19/2011
terry: 4/28/2011
mgross: 10/2/2007
cwells: 9/17/2003
alopez: 6/17/1999
*RECORD*
*FIELD* NO
603916
*FIELD* TI
*603916 EUKARYOTIC TRANSLATION INITIATION FACTOR 3, SUBUNIT C; EIF3C
;;EIF3-p110;;
read moreEUKARYOTIC TRANSLATION INITIATION FACTOR 3, SUBUNIT 8, FORMERLY; EIF3S8,
FORMERLY
*FIELD* TX
DESCRIPTION
Eukaryotic initiation factor-3 (eIF3) is the largest of the eIFs and
consists of at least 10 nonidentical subunits, including EIF2C (Asano et
al., 1997).
CLONING
Asano et al. (1997) demonstrated that the 115-kD component of HeLa cell
eIF3 is actually composed of 2 proteins, p116 (PRT1; 603917) and p110.
By screening a HeLa cell expression library with antibodies against the
115-kD band, these authors identified cDNAs encoding p110. The predicted
913-amino acid p110 protein has a pI of 5.8 and is unrelated to p116.
p110 shares 31% identity to the S. cerevisiae Nip1 protein, which is
thought to be involved in nuclear import and the initiation phase of
protein synthesis. Asano et al. (1997) found that the p116, p110, and
p36 (603911) subunits localize on 40S ribosomes in cells active in
translation and coimmunoprecipitate with p170 (602039), indicating that
these proteins are integral components of eIF3. Northern blot analysis
revealed that p110 is expressed as a 3-kb mRNA.
GENE FUNCTION
By reciprocal yeast 2-hybrid and coimmunoprecipitation analyses of the
human STS26T malignant schwannoma cell line, Scoles et al. (2006) showed
that isoforms 1 and 2 of schwannomin (NF2; 607379) interacted with
EIF3C. Mutation analysis revealed that the FERM domain of schwannomin
interacted with the C-terminal half of EIF3C. Immunofluorescence
microscopy of STS26T cells showed that the 2 proteins partly colocalized
at punctate perinuclear structures and at some membranous structures.
Overexpression of EIF3C in STS26T cells elevated cell proliferation, and
schwannomin countered this effect. Western blot analysis revealed an
inverse abundance of schwannomin and EIF3C in human meningiomas.
MAPPING
Gross (2011) mapped the EIF3C gene to chromosome 16p11.2 based on an
alignment of the EIF3C sequence (GenBank GENBANK BC000533) with the
genomic sequence (GRCh37). A nearly identical copy of EIF3C, designated
EIF3CL, also maps to chromosome 16p11.2.
*FIELD* RF
1. Asano, K.; Kinzy, T. G.; Merrick, W. C.; Hershey, J. W. B.: Conservation
and diversity of eukaryotic translation initiation factor eIF3. J.
Biol. Chem. 272: 1101-1109, 1997.
2. Gross, M. B.: Personal Communication. Baltimore, Md. 5/20/2011.
3. Scoles, D. R.; Yong, W. H.; Qin, Y.; Wawrowsky, K.; Pulst, S. M.
: Schwannomin inhibits tumorigenesis through direct interaction with
the eukaryotic initiation factor subunit c (elF3c). Hum. Molec. Genet. 15:
1059-1070, 2006.
*FIELD* CN
Matthew B. Gross - updated: 05/20/2011
Patricia A. Hartz - updated: 4/28/2011
*FIELD* CD
Rebekah S. Rasooly: 6/16/1999
*FIELD* ED
mgross: 05/20/2011
mgross: 5/19/2011
terry: 4/28/2011
mgross: 10/2/2007
cwells: 9/17/2003
alopez: 6/17/1999