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Eukaryotic translation initiation factor 3 subunit A (eIF3a) (Eukaryotic translation initiation factor 3 subunit 10) (eIF-3-theta) (eIF3 p167) (eIF3 p180) (eIF3 p185)

 EIF3A_HUMAN             Reviewed;        1382 AA.
Q14152; B1AMV5; B4DYS1; F5H335; O00653; Q15778;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-APR-2018, entry version 180.
RecName: Full=Eukaryotic translation initiation factor 3 subunit A {ECO:0000255|HAMAP-Rule:MF_03000};
Short=eIF3a {ECO:0000255|HAMAP-Rule:MF_03000};
AltName: Full=Eukaryotic translation initiation factor 3 subunit 10 {ECO:0000255|HAMAP-Rule:MF_03000};
AltName: Full=eIF-3-theta {ECO:0000255|HAMAP-Rule:MF_03000};
AltName: Full=eIF3 p167;
AltName: Full=eIF3 p180;
AltName: Full=eIF3 p185;
Name=EIF3A {ECO:0000255|HAMAP-Rule:MF_03000};
Synonyms=EIF3S10 {ECO:0000255|HAMAP-Rule:MF_03000}, KIAA0139;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND SUBCELLULAR
LOCATION.
TISSUE=Lymphoblastoma;
PubMed=9150439; DOI=10.1089/dna.1997.16.515;
Scholler J.K., Kanner S.B.;
"The human p167 gene encodes a unique structural protein that contains
centrosomin A homology and associates with a multicomponent complex.";
DNA Cell Biol. 16:515-531(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Keratinocyte, and Liver;
PubMed=9054404; DOI=10.1074/jbc.272.11.7106;
Johnson K.R., Merrick W.C., Zoll W.L., Zhu Y.;
"Identification of cDNA clones for the large subunit of eukaryotic
translation initiation factor 3. Comparison of homologues from human,
Nicotiana tabacum, Caenorhabditis elegans, and Saccharomyces
cerevisiae.";
J. Biol. Chem. 272:7106-7113(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Myelomonocyte;
PubMed=8590280; DOI=10.1093/dnares/2.4.167;
Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. IV.
The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 2:167-174(1995).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
LYS-386.
TISSUE=Testis;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
PROTEIN SEQUENCE OF 2-13; 15-36; 69-75; 85-91; 144-151; 173-183;
252-264; 279-298; 309-317; 322-335; 341-351; 368-388; 439-469;
490-546; 582-589; 624-632; 694-711; 719-740; 776-782; 817-824;
838-847; 850-856; 862-868; 877-885; 1071-1080; 1122-1130; 1142-1150
AND 1358-1366, CLEAVAGE OF INITIATOR METHIONINE, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=Hepatoma, and Mammary carcinoma;
Bienvenut W.V., Boldt K., von Kriegsheim A.F., Matallanas D.,
Cooper W.N., Kolch W.;
Submitted (JUL-2007) to UniProtKB.
[8]
FUNCTION, AND INTERACTION WITH EIF3B AND KRT7.
PubMed=11169732;
DOI=10.1002/1097-4644(20010315)80:4<483::AID-JCB1002>3.0.CO;2-B;
Lin L., Holbro T., Alonso G., Gerosa D., Burger M.M.;
"Molecular interaction between human tumor marker protein p150, the
largest subunit of eIF3, and intermediate filament protein K7.";
J. Cell. Biochem. 80:483-490(2001).
[9]
INTERACTION WITH EIF3B.
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).
[10]
INTERACTION WITH EIF3B.
PubMed=14688252; DOI=10.1074/jbc.M312745200;
Fraser C.S., Lee J.Y., Mayeur G.L., Bushell M., Doudna J.A.,
Hershey J.W.B.;
"The j-subunit of human translation initiation factor eIF3 is required
for the stable binding of eIF3 and its subcomplexes to 40 S ribosomal
subunits in vitro.";
J. Biol. Chem. 279:8946-8956(2004).
[11]
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).
[12]
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).
[13]
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).
[14]
INTERACTION WITH EIF3E.
PubMed=17468741; DOI=10.1038/sj.embor.7400955;
Morris C., Wittmann J., Jaeck H.-M., Jalinot P.;
"Human INT6/eIF3e is required for nonsense-mediated mRNA decay.";
EMBO Rep. 8:596-602(2007).
[15]
FUNCTION (MICROBIAL INFECTION).
PubMed=18056426; DOI=10.1101/gad.439507;
Poyry T.A., Kaminski A., Connell E.J., Fraser C.S., Jackson R.J.;
"The mechanism of an exceptional case of reinitiation after
translation of a long ORF reveals why such events do not generally
occur in mammalian mRNA translation.";
Genes Dev. 21:3149-3162(2007).
[16]
IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3
COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, PHOSPHORYLATION AT SER-881;
SER-1198; SER-1336 AND SER-1364, 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).
[17]
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).
[18]
IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3
COMPLEX, AND IDENTIFICATION BY 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).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-68, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-882, 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-492; SER-584; SER-881;
SER-882; SER-895; SER-949; SER-1028; SER-1188; SER-1198; SER-1262 AND
SER-1336, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[24]
FUNCTION (MICROBIAL INFECTION).
PubMed=23766293; DOI=10.1093/nar/gkt510;
Sun C., Querol-Audi J., Mortimer S.A., Arias-Palomo E., Doudna J.A.,
Nogales E., Cate J.H.;
"Two RNA-binding motifs in eIF3 direct HCV IRES-dependent
translation.";
Nucleic Acids Res. 41:7512-7521(2013).
[25]
FUNCTION (MICROBIAL INFECTION).
PubMed=24357634; DOI=10.1002/embj.201386124;
Sweeney T.R., Abaeva I.S., Pestova T.V., Hellen C.U.;
"The mechanism of translation initiation on Type 1 picornavirus
IRESs.";
EMBO J. 33:76-92(2014).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-882, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[27]
FUNCTION, IDENTIFICATION IN THE EIF-3 COMPLEX, AND RNA-BINDING.
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, AND RNA-BINDING.
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]
3D-STRUCTURE MODELING, AND ELECTRON MICROSCOPY.
PubMed=16322461; DOI=10.1126/science.1118977;
Siridechadilok B., Fraser C.S., Hall R.J., Doudna J.A., Nogales E.;
"Structural roles for human translation factor eIF3 in initiation of
protein synthesis.";
Science 310:1513-1515(2005).
-!- FUNCTION: RNA-binding 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). 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, PubMed:11169732). 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, PubMed:27462815). {ECO:0000255|HAMAP-
Rule:MF_03000, ECO:0000269|PubMed:11169732,
ECO:0000269|PubMed:17581632, ECO:0000269|PubMed:25849773,
ECO:0000269|PubMed:27462815}.
-!- FUNCTION: (Microbial infection) Essential for the initiation of
translation on type-1 viral ribosomal entry sites (IRESs), like
for HCV, PV, EV71 or BEV translation (PubMed:23766293,
PubMed:24357634). {ECO:0000269|PubMed:23766293,
ECO:0000269|PubMed:24357634}.
-!- FUNCTION: (Microbial infection) In case of FCV infection, plays a
role in the ribosomal termination-reinitiation event leading to
the translation of VP2 (PubMed:18056426).
{ECO:0000269|PubMed:18056426}.
-!- SUBUNIT: Interacts with EIF4G1 (By similarity). 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, EIF3L and EIF3K. 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. Also interacts with KRT7 and PIWIL2. {ECO:0000250,
ECO:0000269|PubMed:11169732, ECO:0000269|PubMed:14519125,
ECO:0000269|PubMed:14688252, ECO:0000269|PubMed:16766523,
ECO:0000269|PubMed:17322308, ECO:0000269|PubMed:17468741,
ECO:0000269|PubMed:18599441, ECO:0000269|PubMed:25849773}.
-!- INTERACTION:
P41567:EIF1; NbExp=2; IntAct=EBI-366617, EBI-726200;
P47813:EIF1AX; NbExp=2; IntAct=EBI-366617, EBI-1045377;
P55884:EIF3B; NbExp=9; IntAct=EBI-366617, EBI-366696;
Q99613:EIF3C; NbExp=14; IntAct=EBI-366617, EBI-353741;
O15371:EIF3D; NbExp=6; IntAct=EBI-366617, EBI-353818;
P60228:EIF3E; NbExp=15; IntAct=EBI-366617, EBI-347740;
O00303:EIF3F; NbExp=15; IntAct=EBI-366617, EBI-711990;
Q9DCH4:Eif3f (xeno); NbExp=4; IntAct=EBI-366617, EBI-1634316;
O15372:EIF3H; NbExp=15; IntAct=EBI-366617, EBI-709735;
Q13347:EIF3I; NbExp=4; IntAct=EBI-366617, EBI-354047;
Q9UBQ5:EIF3K; NbExp=14; IntAct=EBI-366617, EBI-354344;
Q9Y262:EIF3L; NbExp=14; IntAct=EBI-366617, EBI-373519;
Q7L2H7:EIF3M; NbExp=14; IntAct=EBI-366617, EBI-353901;
P23588:EIF4B; NbExp=3; IntAct=EBI-366617, EBI-970310;
P08729:KRT7; NbExp=3; IntAct=EBI-366617, EBI-297833;
Q9Q2G4:ORF (xeno); NbExp=5; IntAct=EBI-366617, EBI-6248094;
Q92900-2:UPF1; NbExp=5; IntAct=EBI-366617, EBI-373492;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03000,
ECO:0000269|PubMed:9150439}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q14152-1; Sequence=Displayed;
Name=2;
IsoId=Q14152-2; Sequence=VSP_055471;
Note=No experimental confirmation available.;
-!- PTM: Phosphorylated. Phosphorylation is enhanced upon serum
stimulation. {ECO:0000255|HAMAP-Rule:MF_03000,
ECO:0000269|PubMed:17322308}.
-!- MASS SPECTROMETRY: Mass=166758.3; Method=Unknown; Range=1-1382;
Evidence={ECO:0000269|PubMed:17322308};
-!- SIMILARITY: Belongs to the eIF-3 subunit A family.
{ECO:0000255|HAMAP-Rule:MF_03000}.
-!- SEQUENCE CAUTION:
Sequence=BAA09488.2; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/EIF3AID40425ch10q26.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U58046; AAB41584.1; -; mRNA.
EMBL; U58047; AAB41586.1; -; Genomic_DNA.
EMBL; U78311; AAB80695.1; -; mRNA.
EMBL; D50929; BAA09488.2; ALT_INIT; mRNA.
EMBL; AK302575; BAG63833.1; -; mRNA.
EMBL; AL355598; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471066; EAW49408.1; -; Genomic_DNA.
CCDS; CCDS7608.1; -. [Q14152-1]
RefSeq; NP_003741.1; NM_003750.2. [Q14152-1]
UniGene; Hs.523299; -.
UniGene; Hs.713331; -.
PDB; 3J8B; EM; -; A=1-494.
PDB; 3J8C; EM; -; A=1-494.
PDBsum; 3J8B; -.
PDBsum; 3J8C; -.
ProteinModelPortal; Q14152; -.
SMR; Q14152; -.
BioGrid; 114210; 123.
CORUM; Q14152; -.
DIP; DIP-31114N; -.
IntAct; Q14152; 73.
MINT; Q14152; -.
STRING; 9606.ENSP00000358140; -.
MoonProt; Q14152; -.
iPTMnet; Q14152; -.
PhosphoSitePlus; Q14152; -.
SwissPalm; Q14152; -.
BioMuta; EIF3A; -.
DMDM; 6685537; -.
UCD-2DPAGE; Q14152; -.
EPD; Q14152; -.
MaxQB; Q14152; -.
PaxDb; Q14152; -.
PeptideAtlas; Q14152; -.
PRIDE; Q14152; -.
Ensembl; ENST00000369144; ENSP00000358140; ENSG00000107581. [Q14152-1]
Ensembl; ENST00000541549; ENSP00000438178; ENSG00000107581. [Q14152-1]
GeneID; 8661; -.
KEGG; hsa:8661; -.
UCSC; uc001ldu.4; human. [Q14152-1]
CTD; 8661; -.
DisGeNET; 8661; -.
EuPathDB; HostDB:ENSG00000107581.12; -.
GeneCards; EIF3A; -.
H-InvDB; HIX0170434; -.
HGNC; HGNC:3271; EIF3A.
HPA; HPA038315; -.
HPA; HPA038316; -.
MIM; 602039; gene.
neXtProt; NX_Q14152; -.
OpenTargets; ENSG00000107581; -.
PharmGKB; PA27699; -.
eggNOG; KOG2072; Eukaryota.
eggNOG; ENOG410XQ37; LUCA.
GeneTree; ENSGT00730000111063; -.
HOGENOM; HOG000246822; -.
HOVERGEN; HBG006128; -.
InParanoid; Q14152; -.
KO; K03254; -.
OMA; QDRDEND; -.
OrthoDB; EOG091G01VW; -.
PhylomeDB; Q14152; -.
TreeFam; TF101522; -.
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; EIF3A; human.
GeneWiki; EIF3A; -.
GenomeRNAi; 8661; -.
PRO; PR:Q14152; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000107581; -.
CleanEx; HS_EIF3A; -.
Genevisible; Q14152; HS.
GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:UniProtKB.
GO; GO:0071540; C:eukaryotic translation initiation factor 3 complex, eIF3e; IBA:GO_Central.
GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IBA:GO_Central.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005874; C:microtubule; IEA:Ensembl.
GO; GO:0043614; C:multi-eIF complex; IBA:GO_Central.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
GO; GO:0030971; F:receptor tyrosine kinase binding; IEA:Ensembl.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0005198; F:structural molecule activity; NAS:UniProtKB.
GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IDA:UniProtKB.
GO; GO:0075522; P:IRES-dependent viral translational initiation; IDA:UniProtKB.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:0002188; P:translation reinitiation; IBA:GO_Central.
GO; GO:0006413; P:translational initiation; TAS:Reactome.
GO; GO:0075525; P:viral translational termination-reinitiation; IDA:UniProtKB.
HAMAP; MF_03000; eIF3a; 1.
InterPro; IPR027512; EIF3A.
InterPro; IPR000717; PCI_dom.
Pfam; PF01399; PCI; 1.
SMART; SM00088; PINT; 1.
PROSITE; PS50250; PCI; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Coiled coil;
Complete proteome; Cytoplasm; Direct protein sequencing;
Initiation factor; Phosphoprotein; Polymorphism; Protein biosynthesis;
Reference proteome; Repeat; RNA-binding.
INIT_MET 1 1 Removed. {ECO:0000255|HAMAP-
Rule:MF_03000,
ECO:0000269|PubMed:17322308,
ECO:0000269|Ref.7}.
CHAIN 2 1382 Eukaryotic translation initiation factor
3 subunit A.
/FTId=PRO_0000123537.
DOMAIN 315 498 PCI. {ECO:0000255|PROSITE-
ProRule:PRU01185}.
REPEAT 925 934 1.
REPEAT 935 942 2; truncated.
REPEAT 943 952 3.
REPEAT 953 962 4.
REPEAT 963 972 5.
REPEAT 973 982 6.
REPEAT 983 992 7.
REPEAT 993 1002 8.
REPEAT 1003 1012 9.
REPEAT 1013 1022 10.
REPEAT 1023 1032 11.
REPEAT 1033 1042 12.
REPEAT 1043 1052 13.
REPEAT 1054 1063 14.
REPEAT 1064 1073 15.
REPEAT 1074 1083 16.
REPEAT 1084 1093 17.
REPEAT 1094 1103 18.
REPEAT 1104 1113 19.
REPEAT 1114 1123 20.
REPEAT 1124 1133 21.
REPEAT 1134 1143 22.
REPEAT 1144 1152 23; truncated.
REPEAT 1153 1162 24.
REPEAT 1163 1172 25; approximate.
REGION 664 835 Interaction with EIF3B.
REGION 925 1172 25 X 10 AA approximate tandem repeats of
[DE]-[DE]-[DE]-R-[SEVGFPILV]-[HPSN]-
[RSW]-[RL]-[DRGTIHN]-[EPMANLGDT].
COILED 82 120 {ECO:0000255|HAMAP-Rule:MF_03000}.
COMPBIAS 576 875 Glu-rich.
COMPBIAS 925 1294 Asp-rich.
MOD_RES 68 68 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 492 492 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 584 584 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 881 881 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000255|HAMAP-Rule:MF_03000,
ECO:0000269|PubMed:17322308}.
MOD_RES 882 882 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 895 895 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 949 949 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1028 1028 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1188 1188 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1198 1198 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000255|HAMAP-Rule:MF_03000,
ECO:0000269|PubMed:17322308}.
MOD_RES 1262 1262 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1336 1336 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000255|HAMAP-Rule:MF_03000,
ECO:0000269|PubMed:17322308}.
MOD_RES 1364 1364 Phosphoserine. {ECO:0000255|HAMAP-
Rule:MF_03000,
ECO:0000269|PubMed:17322308}.
VAR_SEQ 1 34 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055471.
VARIANT 386 386 E -> K (in dbSNP:rs967185).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_024438.
VARIANT 694 694 K -> N (in dbSNP:rs431898).
/FTId=VAR_048921.
VARIANT 993 993 D -> E (in dbSNP:rs532138).
/FTId=VAR_048922.
CONFLICT 520 520 R -> G (in Ref. 4; BAG63833).
{ECO:0000305}.
CONFLICT 983 983 D -> G (in Ref. 4; BAG63833).
{ECO:0000305}.
CONFLICT 1272 1272 D -> G (in Ref. 4; BAG63833).
{ECO:0000305}.
HELIX 10 20 {ECO:0000244|PDB:3J8B}.
HELIX 24 35 {ECO:0000244|PDB:3J8B}.
HELIX 38 40 {ECO:0000244|PDB:3J8B}.
HELIX 47 60 {ECO:0000244|PDB:3J8B}.
HELIX 64 78 {ECO:0000244|PDB:3J8B}.
HELIX 84 107 {ECO:0000244|PDB:3J8B}.
HELIX 147 164 {ECO:0000244|PDB:3J8B}.
HELIX 168 170 {ECO:0000244|PDB:3J8B}.
HELIX 171 187 {ECO:0000244|PDB:3J8B}.
HELIX 191 213 {ECO:0000244|PDB:3J8B}.
HELIX 223 242 {ECO:0000244|PDB:3J8B}.
HELIX 246 262 {ECO:0000244|PDB:3J8B}.
HELIX 269 286 {ECO:0000244|PDB:3J8B}.
HELIX 289 305 {ECO:0000244|PDB:3J8B}.
STRAND 306 309 {ECO:0000244|PDB:3J8B}.
HELIX 312 327 {ECO:0000244|PDB:3J8B}.
HELIX 336 342 {ECO:0000244|PDB:3J8B}.
STRAND 346 348 {ECO:0000244|PDB:3J8B}.
HELIX 354 358 {ECO:0000244|PDB:3J8B}.
HELIX 367 375 {ECO:0000244|PDB:3J8B}.
HELIX 377 381 {ECO:0000244|PDB:3J8B}.
HELIX 385 395 {ECO:0000244|PDB:3J8B}.
HELIX 400 416 {ECO:0000244|PDB:3J8B}.
HELIX 420 425 {ECO:0000244|PDB:3J8B}.
HELIX 428 446 {ECO:0000244|PDB:3J8B}.
STRAND 448 451 {ECO:0000244|PDB:3J8B}.
HELIX 452 458 {ECO:0000244|PDB:3J8B}.
HELIX 464 476 {ECO:0000244|PDB:3J8B}.
STRAND 483 485 {ECO:0000244|PDB:3J8B}.
TURN 486 489 {ECO:0000244|PDB:3J8B}.
STRAND 490 492 {ECO:0000244|PDB:3J8B}.
SEQUENCE 1382 AA; 166569 MW; 485C01B28D67EBBA CRC64;
MPAYFQRPEN ALKRANEFLE VGKKQPALDV LYDVMKSKKH RTWQKIHEPI MLKYLELCVD
LRKSHLAKEG LYQYKNICQQ VNIKSLEDVV RAYLKMAEEK TEAAKEESQQ MVLDIEDLDN
IQTPESVLLS AVSGEDTQDR TDRLLLTPWV KFLWESYRQC LDLLRNNSRV ERLYHDIAQQ
AFKFCLQYTR KAEFRKLCDN LRMHLSQIQR HHNQSTAINL NNPESQSMHL ETRLVQLDSA
ISMELWQEAF KAVEDIHGLF SLSKKPPKPQ LMANYYNKVS TVFWKSGNAL FHASTLHRLY
HLSREMRKNL TQDEMQRMST RVLLATLSIP ITPERTDIAR LLDMDGIIVE KQRRLATLLG
LQAPPTRIGL INDMVRFNVL QYVVPEVKDL YNWLEVEFNP LKLCERVTKV LNWVREQPEK
EPELQQYVPQ LQNNTILRLL QQVSQIYQSI EFSRLTSLVP FVDAFQLERA IVDAARHCDL
QVRIDHTSRT LSFGSDLNYA TREDAPIGPH LQSMPSEQIR NQLTAMSSVL AKALEVIKPA
HILQEKEEQH QLAVTAYLKN SRKEHQRILA RRQTIEERKE RLESLNIQRE KEELEQREAE
LQKVRKAEEE RLRQEAKERE KERILQEHEQ IKKKTVRERL EQIKKTELGA KAFKDIDIED
LEELDPDFIM AKQVEQLEKE KKELQERLKN QEKKIDYFER AKRLEEIPLI KSAYEEQRIK
DMDLWEQQEE ERITTMQLER EKALEHKNRM SRMLEDRDLF VMRLKAARQS VYEEKLKQFE
ERLAEERHNR LEERKRQRKE ERRITYYREK EEEEQRRAEE QMLKEREERE RAERAKREEE
LREYQERVKK LEEVERKKRQ RELEIEERER RREEERRLGD SSLSRKDSRW GDRDSEGTWR
KGPEADSEWR RGPPEKEWRR GEGRDEDRSH RRDEERPRRL GDDEDREPSL RPDDDRVPRR
GMDDDRGPRR GPEEDRFSRR GADDDRPSWR NTDDDRPPRR IADEDRGNWR HADDDRPPRR
GLDEDRGSWR TADEDRGPRR GMDDDRGPRR GGADDERSSW RNADDDRGPR RGLDDDRGPR
RGMDDDRGPR RGMDDDRGPR RGMDDDRGPR RGLDDDRGPW RNADDDRIPR RGAEDDRGPW
RNMDDDRLSR RADDDRFPRR GDDSRPGPWR PLVKPGGWRE KEKAREESWG PPRESRPSEE
REWDREKERD RDNQDREEND KDPERERDRE RDVDREDRFR RPRDEGGWRR GPAEESSSWR
DSSRRDDRDR DDRRRERDDR RDLRERRDLR DDRDRRGPPL RSEREEVSSW RRADDRKDDR
VEERDPPRRV PPPALSRDRE RDRDREREGE KEKASWRAEK DRESLRRTKN ETDEDGWTTV
RR


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