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Eukaryotic translation initiation factor 3 subunit B (eIF3b) (Eukaryotic translation initiation factor 3 subunit 9) (Prt1 homolog) (hPrt1) (eIF-3-eta) (eIF3 p110) (eIF3 p116)

 EIF3B_HUMAN             Reviewed;         814 AA.
P55884; A4D208; Q2NL77; Q9UMF9;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
16-DEC-2008, sequence version 3.
10-OCT-2018, entry version 188.
RecName: Full=Eukaryotic translation initiation factor 3 subunit B {ECO:0000255|HAMAP-Rule:MF_03001};
Short=eIF3b {ECO:0000255|HAMAP-Rule:MF_03001};
AltName: Full=Eukaryotic translation initiation factor 3 subunit 9 {ECO:0000255|HAMAP-Rule:MF_03001};
AltName: Full=Prt1 homolog;
Short=hPrt1;
AltName: Full=eIF-3-eta {ECO:0000255|HAMAP-Rule:MF_03001};
AltName: Full=eIF3 p110 {ECO:0000255|HAMAP-Rule:MF_03001};
AltName: Full=eIF3 p116;
Name=EIF3B {ECO:0000255|HAMAP-Rule:MF_03001};
Synonyms=EIF3S9 {ECO:0000255|HAMAP-Rule:MF_03001};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND VARIANT PRO-64.
TISSUE=Skeletal muscle;
PubMed=9388245; DOI=10.1074/jbc.272.49.30975;
Chaudhuri J., Chakrabarti A., Maitra U.;
"Biochemical characterization of mammalian translation initiation
factor 3 (eIF3). Molecular cloning reveals that p110 subunit is the
mammalian homologue of Saccharomyces cerevisiae protein Prt1.";
J. Biol. Chem. 272:30975-30983(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT PRO-64.
TISSUE=Placenta;
PubMed=8995410; DOI=10.1074/jbc.272.20.12994;
Methot N., Rom E., Olsen H., Sonenberg N.;
"The human homologue of the yeast Prt1 protein is an integral part of
the eukaryotic initiation factor 3 complex and interacts with p170.";
J. Biol. Chem. 272:1110-1116(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
PRO-64.
TISSUE=Brain, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
INTERACTION WITH EIF3E.
PubMed=11457827; DOI=10.1074/jbc.M102161200;
Shalev A., Valasek L., Pise-Masison C.A., Radonovich M., Phan L.,
Clayton J., He H., Brady J.N., Hinnebusch A.G., Asano K.;
"Saccharomyces cerevisiae protein Pci8p and human protein eIF3e/Int-6
interact with the eIF3 core complex by binding to cognate eIF3b
subunits.";
J. Biol. Chem. 276:34948-34957(2001).
[8]
INTERACTION WITH EIF3A.
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 EIF3A; EIF3C; EIF3G; EIF3I AND EIF3K.
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 EIF3A; EIF3G; EIF3I AND EIF3J.
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]
INTERACTION WITH EIF4B; MTOR; RPTOR AND RPS6KB1.
PubMed=16286006; DOI=10.1016/j.cell.2005.10.024;
Holz M.K., Ballif B.A., Gygi S.P., Blenis J.;
"mTOR and S6K1 mediate assembly of the translation preinitiation
complex through dynamic protein interchange and ordered
phosphorylation events.";
Cell 123:569-580(2005).
[12]
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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-154 AND
SER-164, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[14]
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).
[15]
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).
[16]
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).
[17]
INTERACTION WITH EIF3A; EIF3C; EIF3E AND UPF2.
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).
[18]
IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3
COMPLEX, ACETYLATION AT MET-1, PHOSPHORYLATION AT SER-83; SER-85;
SER-119; SER-125; SER-152; SER-154 AND SER-164, 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).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78; SER-81; SER-83;
SER-85 AND SER-239, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[21]
IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3
COMPLEX, INTERACTION WITH EIF3E; EIF3F; EIF3H; EIF3L AND EIF3M, AND
MASS SPECTROMETRY.
PubMed=18599441; DOI=10.1073/pnas.0801313105;
Zhou M., Sandercock A.M., Fraser C.S., Ridlova G., Stephens E.,
Schenauer M.R., Yokoi-Fong T., Barsky D., Leary J.A., Hershey J.W.B.,
Doudna J.A., Robinson C.V.;
"Mass spectrometry reveals modularity and a complete subunit
interaction map of the eukaryotic translation factor eIF3.";
Proc. Natl. Acad. Sci. U.S.A. 105:18139-18144(2008).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-154 AND
SER-164, 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).
[24]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-209; LYS-288 AND LYS-364,
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).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-154; SER-164
AND SER-239, 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).
[26]
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).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125 AND SER-154, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[28]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[29]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, 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).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, 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).
[32]
INTERACTION WITH HNRPD, AND RNA-BINDING.
PubMed=24423872; DOI=10.1093/nar/gkt1379;
Lee K.H., Kim S.H., Kim H.J., Kim W., Lee H.R., Jung Y., Choi J.H.,
Hong K.Y., Jang S.K., Kim K.T.;
"AUF1 contributes to Cryptochrome1 mRNA degradation and rhythmic
translation.";
Nucleic Acids Res. 42:3590-3606(2014).
[33]
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).
[34]
INTERACTION WITH METTL3.
PubMed=27117702; DOI=10.1016/j.molcel.2016.03.021;
Lin S., Choe J., Du P., Triboulet R., Gregory R.I.;
"The m(6)A methyltransferase METTL3 promotes translation in human
cancer cells.";
Mol. Cell 62:335-345(2016).
[35]
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).
[36]
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).
[37]
STRUCTURE BY NMR OF 170-274, AND INTERACTION WITH EIF3J.
PubMed=17190833; DOI=10.1074/jbc.M610860200;
ElAntak L., Tzakos A.G., Locker N., Lukavsky P.J.;
"Structure of eIF3b RNA recognition motif and its interaction with
eIF3j: structural insights into the recruitment of eIF3b to the 40 S
ribosomal subunit.";
J. Biol. Chem. 282:8165-8174(2007).
-!- 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:9388245,
PubMed:17581632, PubMed:25849773, PubMed:27462815). The eIF-3
complex associates with the 40S ribosome and facilitates the
recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5
to form the 43S pre-initiation complex (43S PIC). The eIF-3
complex stimulates mRNA recruitment to the 43S PIC and scanning of
the mRNA for AUG recognition. The eIF-3 complex is also required
for disassembly and recycling of post-termination ribosomal
complexes and subsequently prevents premature joining of the 40S
and 60S ribosomal subunits prior to initiation (PubMed:9388245,
PubMed:17581632). The eIF-3 complex specifically targets and
initiates translation of a subset of mRNAs involved in cell
proliferation, including cell cycling, differentiation and
apoptosis, and uses different modes of RNA stem-loop binding to
exert either translational activation or repression
(PubMed:25849773). {ECO:0000255|HAMAP-Rule:MF_03001,
ECO:0000269|PubMed:17581632, ECO:0000269|PubMed:25849773,
ECO:0000269|PubMed:27462815, ECO:0000269|PubMed:9388245}.
-!- 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: Component of the eukaryotic translation initiation factor
3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B,
EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K,
EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable
modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I;
module B is composed of EIF3F, EIF3H, and EIF3M; and module C is
composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module
C binds EIF3B of module A and EIF3H of module B, thereby linking
the three modules. EIF3J is a labile subunit that binds to the
eIF-3 complex via EIF3B. The eIF-3 complex interacts with RPS6KB1
under conditions of nutrient depletion. Mitogenic stimulation
leads to binding and activation of a complex composed of MTOR and
RPTOR, leading to phosphorylation and release of RPS6KB1 and
binding of EIF4B to eIF-3. Also interacts with UPF2 and HNRPD.
Interacts with METTL3 (PubMed:27117702). {ECO:0000255|HAMAP-
Rule:MF_03001, ECO:0000269|PubMed:11169732,
ECO:0000269|PubMed:11457827, ECO:0000269|PubMed:14519125,
ECO:0000269|PubMed:14688252, ECO:0000269|PubMed:16286006,
ECO:0000269|PubMed:16766523, ECO:0000269|PubMed:17190833,
ECO:0000269|PubMed:17322308, ECO:0000269|PubMed:17468741,
ECO:0000269|PubMed:18599441, ECO:0000269|PubMed:24423872,
ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:27117702}.
-!- INTERACTION:
O00571:DDX3X; NbExp=5; IntAct=EBI-366696, EBI-353779;
Q14152:EIF3A; NbExp=9; IntAct=EBI-366696, EBI-366617;
P60228:EIF3E; NbExp=6; IntAct=EBI-366696, EBI-347740;
O00303:EIF3F; NbExp=8; IntAct=EBI-366696, EBI-711990;
O75821:EIF3G; NbExp=9; IntAct=EBI-366696, EBI-366632;
O15372:EIF3H; NbExp=6; IntAct=EBI-366696, EBI-709735;
Q13347:EIF3I; NbExp=7; IntAct=EBI-366696, EBI-354047;
O75822:EIF3J; NbExp=5; IntAct=EBI-366696, EBI-366647;
Q9UBQ5:EIF3K; NbExp=4; IntAct=EBI-366696, EBI-354344;
Q9Y262:EIF3L; NbExp=3; IntAct=EBI-366696, EBI-373519;
Q7L2H7:EIF3M; NbExp=4; IntAct=EBI-366696, EBI-353901;
P23443:RPS6KB1; NbExp=3; IntAct=EBI-366696, EBI-1775921;
Q9J0X9:UL54 (xeno); NbExp=4; IntAct=EBI-366696, EBI-7967856;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03001}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P55884-1; Sequence=Displayed;
Name=2;
IsoId=P55884-2; Sequence=VSP_017274;
-!- DOMAIN: The RRM domain mediates interaction with EIF3J.
-!- PTM: Phosphorylated. Phosphorylation is enhanced upon serum
stimulation. {ECO:0000255|HAMAP-Rule:MF_03001,
ECO:0000269|PubMed:17322308}.
-!- MASS SPECTROMETRY: Mass=93093.7; Method=Unknown; Range=1-814;
Evidence={ECO:0000269|PubMed:17322308};
-!- MASS SPECTROMETRY: Mass=92561; Mass_error=43.5; Method=MALDI;
Range=1-814; Evidence={ECO:0000269|PubMed:18599441};
-!- SIMILARITY: Belongs to the eIF-3 subunit B family.
{ECO:0000255|HAMAP-Rule:MF_03001}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; U78525; AAC99479.1; -; mRNA.
EMBL; U62583; AAB42010.1; -; mRNA.
EMBL; AC004971; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC004840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH236953; EAL23951.1; -; Genomic_DNA.
EMBL; CH471144; EAW87237.1; -; Genomic_DNA.
EMBL; BC001173; AAH01173.1; -; mRNA.
EMBL; BC110865; AAI10866.1; -; mRNA.
CCDS; CCDS5332.1; -. [P55884-1]
PIR; T09582; T09582.
RefSeq; NP_001032360.1; NM_001037283.1. [P55884-1]
RefSeq; NP_003742.2; NM_003751.3. [P55884-1]
RefSeq; XP_011513901.1; XM_011515599.1. [P55884-1]
RefSeq; XP_011513902.1; XM_011515600.1. [P55884-1]
RefSeq; XP_016868241.1; XM_017012752.1.
UniGene; Hs.371001; -.
PDB; 2KRB; NMR; -; A=184-264.
PDB; 2NLW; NMR; -; A=170-274.
PDB; 5K1H; EM; 4.90 A; B=170-745.
PDBsum; 2KRB; -.
PDBsum; 2NLW; -.
PDBsum; 5K1H; -.
ProteinModelPortal; P55884; -.
SMR; P55884; -.
BioGrid; 114211; 89.
CORUM; P55884; -.
DIP; DIP-31113N; -.
IntAct; P55884; 59.
MINT; P55884; -.
STRING; 9606.ENSP00000354125; -.
iPTMnet; P55884; -.
PhosphoSitePlus; P55884; -.
SwissPalm; P55884; -.
BioMuta; EIF3B; -.
DMDM; 218512094; -.
EPD; P55884; -.
MaxQB; P55884; -.
PaxDb; P55884; -.
PeptideAtlas; P55884; -.
PRIDE; P55884; -.
ProteomicsDB; 56875; -.
ProteomicsDB; 56876; -. [P55884-2]
Ensembl; ENST00000360876; ENSP00000354125; ENSG00000106263. [P55884-1]
Ensembl; ENST00000397011; ENSP00000380206; ENSG00000106263. [P55884-1]
GeneID; 8662; -.
KEGG; hsa:8662; -.
UCSC; uc003slx.4; human. [P55884-1]
CTD; 8662; -.
DisGeNET; 8662; -.
EuPathDB; HostDB:ENSG00000106263.17; -.
GeneCards; EIF3B; -.
H-InvDB; HIX0006430; -.
HGNC; HGNC:3280; EIF3B.
HPA; CAB017562; -.
HPA; HPA048983; -.
MIM; 603917; gene.
neXtProt; NX_P55884; -.
OpenTargets; ENSG00000106263; -.
PharmGKB; PA162384603; -.
eggNOG; KOG2314; Eukaryota.
eggNOG; COG5354; LUCA.
GeneTree; ENSGT00550000074913; -.
HOGENOM; HOG000265546; -.
HOVERGEN; HBG006127; -.
InParanoid; P55884; -.
KO; K03253; -.
OMA; NFAWEPK; -.
OrthoDB; EOG091G02V5; -.
PhylomeDB; P55884; -.
TreeFam; TF101521; -.
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; EIF3B; human.
EvolutionaryTrace; P55884; -.
GeneWiki; EIF3B; -.
GenomeRNAi; 8662; -.
PRO; PR:P55884; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000106263; Expressed in 231 organ(s), highest expression level in testis.
CleanEx; HS_EIF3B; -.
ExpressionAtlas; P55884; baseline and differential.
Genevisible; P55884; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:UniProtKB.
GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0045202; C:synapse; IEA:Ensembl.
GO; GO:0032947; F:protein-containing complex scaffold activity; TAS:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0003743; F:translation initiation factor activity; IDA:UniProtKB.
GO; GO:0031369; F:translation initiation factor binding; IEA:InterPro.
GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
GO; GO:0075522; P:IRES-dependent viral translational initiation; IDA:UniProtKB.
GO; GO:0006446; P:regulation of translational initiation; IDA:UniProtKB.
GO; GO:0006413; P:translational initiation; IDA:UniProtKB.
GO; GO:0075525; P:viral translational termination-reinitiation; IDA:UniProtKB.
CDD; cd12278; RRM_eIF3B; 1.
Gene3D; 2.130.10.10; -; 2.
Gene3D; 3.30.70.330; -; 1.
HAMAP; MF_03001; eIF3b; 1.
InterPro; IPR011400; EIF3B.
InterPro; IPR034363; eIF3B_RRM.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
InterPro; IPR013979; TIF_beta_prop-like.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
PANTHER; PTHR14068; PTHR14068; 1.
Pfam; PF08662; eIF2A; 1.
Pfam; PF00076; RRM_1; 1.
PIRSF; PIRSF036424; eIF3b; 1.
SMART; SM00360; RRM; 1.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50102; RRM; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Initiation factor; Phosphoprotein; Polymorphism;
Protein biosynthesis; Reference proteome; Repeat; RNA-binding;
WD repeat.
CHAIN 1 814 Eukaryotic translation initiation factor
3 subunit B.
/FTId=PRO_0000123531.
DOMAIN 185 268 RRM. {ECO:0000255|HAMAP-Rule:MF_03001}.
REPEAT 285 324 WD 1.
REPEAT 325 365 WD 2.
REPEAT 366 425 WD 3.
REPEAT 426 489 WD 4.
REPEAT 490 553 WD 5.
REPEAT 554 598 WD 6.
REPEAT 599 642 WD 7.
REPEAT 643 685 WD 8.
REGION 124 413 Sufficient for interaction with EIF3E.
REGION 170 274 Sufficient for interaction with EIF3J.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000255|HAMAP-Rule:MF_03001,
ECO:0000269|PubMed:17322308}.
MOD_RES 78 78 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 81 81 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 83 83 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000255|HAMAP-Rule:MF_03001,
ECO:0000269|PubMed:17322308}.
MOD_RES 85 85 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000255|HAMAP-Rule:MF_03001,
ECO:0000269|PubMed:17322308}.
MOD_RES 119 119 Phosphoserine. {ECO:0000255|HAMAP-
Rule:MF_03001,
ECO:0000269|PubMed:17322308}.
MOD_RES 125 125 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569,
ECO:0000255|HAMAP-Rule:MF_03001,
ECO:0000269|PubMed:17322308}.
MOD_RES 152 152 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000255|HAMAP-Rule:MF_03001,
ECO:0000269|PubMed:17322308}.
MOD_RES 154 154 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000255|HAMAP-Rule:MF_03001,
ECO:0000269|PubMed:17322308}.
MOD_RES 164 164 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000255|HAMAP-Rule:MF_03001,
ECO:0000269|PubMed:17322308}.
MOD_RES 209 209 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 239 239 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 288 288 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 364 364 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VAR_SEQ 812 814 NQE -> IRSDLEHCAQPCVLWSRGRPAGSRVTPASSLCSL
ALDCDCAWILPLRHIFVPFSPWCLQWGI (in isoform
2). {ECO:0000303|PubMed:8995410}.
/FTId=VSP_017274.
VARIANT 64 64 S -> P (in dbSNP:rs9690787).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:8995410,
ECO:0000269|PubMed:9388245}.
/FTId=VAR_047972.
VARIANT 793 793 D -> E (in dbSNP:rs1063257).
/FTId=VAR_047973.
CONFLICT 115 116 ER -> AG (in Ref. 2; AAB42010).
{ECO:0000305}.
STRAND 186 191 {ECO:0000244|PDB:2KRB}.
TURN 197 199 {ECO:0000244|PDB:2KRB}.
HELIX 200 212 {ECO:0000244|PDB:2KRB}.
STRAND 217 221 {ECO:0000244|PDB:2KRB}.
STRAND 232 239 {ECO:0000244|PDB:2KRB}.
HELIX 240 247 {ECO:0000244|PDB:2KRB}.
STRAND 250 252 {ECO:0000244|PDB:2KRB}.
STRAND 256 259 {ECO:0000244|PDB:2KRB}.
STRAND 260 264 {ECO:0000244|PDB:2NLW}.
SEQUENCE 814 AA; 92482 MW; C687A986EDAE0F5E CRC64;
MQDAENVAVP EAAEERAEPG QQQPAAEPPP AEGLLRPAGP GAPEAAGTEA SSEEVGIAEA
GPESEVRTEP AAEAEAASGP SESPSPPAAE ELPGSHAEPP VPAQGEAPGE QARDERSDSR
AQAVSEDAGG NEGRAAEAEP RALENGDADE PSFSDPEDFV DDVSEEELLG DVLKDRPQEA
DGIDSVIVVD NVPQVGPDRL EKLKNVIHKI FSKFGKITND FYPEEDGKTK GYIFLEYASP
AHAVDAVKNA DGYKLDKQHT FRVNLFTDFD KYMTISDEWD IPEKQPFKDL GNLRYWLEEA
ECRDQYSVIF ESGDRTSIFW NDVKDPVSIE ERARWTETYV RWSPKGTYLA TFHQRGIALW
GGEKFKQIQR FSHQGVQLID FSPCERYLVT FSPLMDTQDD PQAIIIWDIL TGHKKRGFHC
ESSAHWPIFK WSHDGKFFAR MTLDTLSIYE TPSMGLLDKK SLKISGIKDF SWSPGGNIIA
FWVPEDKDIP ARVTLMQLPT RQEIRVRNLF NVVDCKLHWQ KNGDYLCVKV DRTPKGTQGV
VTNFEIFRMR EKQVPVDVVE MKETIIAFAW EPNGSKFAVL HGEAPRISVS FYHVKNNGKI
ELIKMFDKQQ ANTIFWSPQG QFVVLAGLRS MNGALAFVDT SDCTVMNIAE HYMASDVEWD
PTGRYVVTSV SWWSHKVDNA YWLWTFQGRL LQKNNKDRFC QLLWRPRPPT LLSQEQIKQI
KKDLKKYSKI FEQKDRLSQS KASKELVERR RTMMEDFRKY RKMAQELYME QKNERLELRG
GVDTDELDSN VDDWEEETIE FFVTEEIIPL GNQE


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