IF4B_HUMAN
ID IF4B_HUMAN Reviewed; 611 AA.
AC P23588; B4DS13; Q4G0E3; Q53HQ2; Q6GPH5; Q6IB46; Q8WYK5;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Eukaryotic translation initiation factor 4B;
DE Short=eIF-4B;
GN Name=EIF4B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2390971; DOI=10.1002/j.1460-2075.1990.tb07466.x;
RA Milburn S.C., Hershey J.W.B., Davies M.V., Kelleher K., Kaufman R.J.;
RT "Cloning and expression of eukaryotic initiation factor 4B cDNA: sequence
RT determination identifies a common RNA recognition motif.";
RL EMBO J. 9:2783-2790(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Cervix carcinoma;
RA Yokoyama K.;
RT "Human eukaryotic initiation factor 4B.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Adipose tissue;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, Testis, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 71-87; 118-135; 168-182; 189-225; 235-242; 340-372;
RP 380-398; 473-486 AND 512-537, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Calvo F., Kolch W.;
RL Submitted (MAR-2008) to UniProtKB.
RN [10]
RP CHARACTERIZATION.
RX PubMed=8139536; DOI=10.1128/mcb.14.4.2307-2316.1994;
RA Methot N., Pause A., Hershey J.W., Sonenberg N.;
RT "The translation initiation factor eIF-4B contains an RNA-binding region
RT that is distinct and independent from its ribonucleoprotein consensus
RT sequence.";
RL Mol. Cell. Biol. 14:2307-2316(1994).
RN [11]
RP CHARACTERIZATION.
RX PubMed=8816444; DOI=10.1128/mcb.16.10.5328;
RA Methot N., Song M.S., Sonenberg N.;
RT "A region rich in aspartic acid, arginine, tyrosine, and glycine (DRYG)
RT mediates eukaryotic initiation factor 4B (eIF4B) self-association and
RT interaction with eIF3.";
RL Mol. Cell. Biol. 16:5328-5334(1996).
RN [12]
RP PHOSPHORYLATION AT SER-422.
RX PubMed=15071500; DOI=10.1038/sj.emboj.7600193;
RA Raught B., Peiretti F., Gingras A.C., Livingstone M., Shahbazian D.,
RA Mayeur G.L., Polakiewicz R.D., Sonenberg N., Hershey J.W.;
RT "Phosphorylation of eucaryotic translation initiation factor 4B Ser422 is
RT modulated by S6 kinases.";
RL EMBO J. 23:1761-1769(2004).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406 AND SER-445, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [14]
RP PHOSPHORYLATION AT SER-422.
RX PubMed=16763566; DOI=10.1038/sj.emboj.7601166;
RA Shahbazian D., Roux P.P., Mieulet V., Cohen M.S., Raught B., Taunton J.,
RA Hershey J.W., Blenis J., Pende M., Sonenberg N.;
RT "The mTOR/PI3K and MAPK pathways converge on eIF4B to control its
RT phosphorylation and activity.";
RL EMBO J. 25:2781-2791(2006).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-219; SER-283; SER-459
RP AND SER-597, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-597, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-586, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-192; SER-219;
RP SER-406; SER-422; SER-445; SER-498; SER-504 AND SER-597, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [22]
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., Buerckstuemmer T.,
RA 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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406; THR-412; SER-418;
RP SER-425; SER-445; SER-498; SER-504 AND SER-597, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-192; SER-207;
RP SER-219; SER-359; SER-406; SER-409; SER-422 AND SER-597, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-422; SER-425; SER-459;
RP SER-462; SER-498 AND SER-504, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [26]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-343, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [27]
RP STRUCTURE BY NMR OF 88-178.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RNA binding domain of eukaryotic initiation
RT factor 4B.";
RL Submitted (NOV-2004) to the PDB data bank.
RN [28]
RP VARIANT ARG-203.
RX PubMed=21248752; DOI=10.1038/nature09639;
RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H.,
RA Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J.,
RA Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M.,
RA Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L.,
RA Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J.,
RA Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A.,
RA Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K.,
RA Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.;
RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene
RT PBRM1 in renal carcinoma.";
RL Nature 469:539-542(2011).
CC -!- FUNCTION: Required for the binding of mRNA to ribosomes. Functions in
CC close association with EIF4-F and EIF4-A. Binds near the 5'-terminal
CC cap of mRNA in presence of EIF-4F and ATP. Promotes the ATPase activity
CC and the ATP-dependent RNA unwinding activity of both EIF4-A and EIF4-F.
CC -!- SUBUNIT: Self-associates and interacts with EIF3 p170 subunit.
CC -!- INTERACTION:
CC P23588; Q86V38: ATN1; NbExp=3; IntAct=EBI-970310, EBI-11954292;
CC P23588; P02489: CRYAA; NbExp=3; IntAct=EBI-970310, EBI-6875961;
CC P23588; Q92876: KLK6; NbExp=3; IntAct=EBI-970310, EBI-2432309;
CC P23588; P53350: PLK1; NbExp=3; IntAct=EBI-970310, EBI-476768;
CC P23588; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-970310, EBI-717399;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P23588-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P23588-2; Sequence=VSP_057351;
CC -!- PTM: Phosphorylated at Ser-422 by RPS6KA1 and RPS6KB1; phosphorylation
CC enhances the affinity of EIF4B for the EIF3 complex.
CC {ECO:0000269|PubMed:15071500, ECO:0000269|PubMed:16763566}.
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DR EMBL; X55733; CAA39265.1; -; Genomic_DNA.
DR EMBL; AB076839; BAB82380.1; -; mRNA.
DR EMBL; AK299526; BAG61475.1; -; mRNA.
DR EMBL; CR456958; CAG33239.1; -; mRNA.
DR EMBL; AK222528; BAD96248.1; -; mRNA.
DR EMBL; AC068888; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW96657.1; -; Genomic_DNA.
DR EMBL; BC073139; AAH73139.1; -; mRNA.
DR EMBL; BC073154; AAH73154.1; -; mRNA.
DR EMBL; BC098437; AAH98437.1; -; mRNA.
DR CCDS; CCDS41788.1; -. [P23588-1]
DR CCDS; CCDS86303.1; -. [P23588-2]
DR PIR; S12566; S12566.
DR RefSeq; NP_001317583.1; NM_001330654.1. [P23588-2]
DR RefSeq; NP_001408.2; NM_001417.6. [P23588-1]
DR PDB; 1WI8; NMR; -; A=88-178.
DR PDB; 2J76; NMR; -; E=77-176.
DR PDB; 6FEC; EM; 6.30 A; u=1-611.
DR PDBsum; 1WI8; -.
DR PDBsum; 2J76; -.
DR PDBsum; 6FEC; -.
DR AlphaFoldDB; P23588; -.
DR BMRB; P23588; -.
DR SMR; P23588; -.
DR BioGRID; 108291; 246.
DR IntAct; P23588; 64.
DR MINT; P23588; -.
DR STRING; 9606.ENSP00000388806; -.
DR ChEMBL; CHEMBL3308928; -.
DR GlyGen; P23588; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; P23588; -.
DR PhosphoSitePlus; P23588; -.
DR SwissPalm; P23588; -.
DR BioMuta; EIF4B; -.
DR DMDM; 205371761; -.
DR EPD; P23588; -.
DR jPOST; P23588; -.
DR MassIVE; P23588; -.
DR MaxQB; P23588; -.
DR PaxDb; P23588; -.
DR PeptideAtlas; P23588; -.
DR PRIDE; P23588; -.
DR ProteomicsDB; 4987; -.
DR ProteomicsDB; 54135; -. [P23588-1]
DR Antibodypedia; 3427; 833 antibodies from 42 providers.
DR DNASU; 1975; -.
DR Ensembl; ENST00000262056.14; ENSP00000262056.9; ENSG00000063046.18. [P23588-1]
DR Ensembl; ENST00000416762.7; ENSP00000412530.3; ENSG00000063046.18. [P23588-2]
DR GeneID; 1975; -.
DR KEGG; hsa:1975; -.
DR MANE-Select; ENST00000262056.14; ENSP00000262056.9; NM_001417.7; NP_001408.2.
DR UCSC; uc001sbh.5; human. [P23588-1]
DR CTD; 1975; -.
DR DisGeNET; 1975; -.
DR GeneCards; EIF4B; -.
DR HGNC; HGNC:3285; EIF4B.
DR HPA; ENSG00000063046; Low tissue specificity.
DR MIM; 603928; gene.
DR neXtProt; NX_P23588; -.
DR OpenTargets; ENSG00000063046; -.
DR PharmGKB; PA27713; -.
DR VEuPathDB; HostDB:ENSG00000063046; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000153336; -.
DR HOGENOM; CLU_031798_0_0_1; -.
DR InParanoid; P23588; -.
DR PhylomeDB; P23588; -.
DR TreeFam; TF101525; -.
DR PathwayCommons; P23588; -.
DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-HSA-166208; mTORC1-mediated signalling.
DR Reactome; R-HSA-429947; Deadenylation of mRNA.
DR Reactome; R-HSA-72649; Translation initiation complex formation.
DR Reactome; R-HSA-72662; Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
DR Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR SignaLink; P23588; -.
DR SIGNOR; P23588; -.
DR BioGRID-ORCS; 1975; 420 hits in 1078 CRISPR screens.
DR ChiTaRS; EIF4B; human.
DR EvolutionaryTrace; P23588; -.
DR GeneWiki; EIF4B; -.
DR GenomeRNAi; 1975; -.
DR Pharos; P23588; Tbio.
DR PRO; PR:P23588; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P23588; protein.
DR Bgee; ENSG00000063046; Expressed in calcaneal tendon and 219 other tissues.
DR ExpressionAtlas; P23588; baseline and differential.
DR Genevisible; P23588; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; TAS:ProtInc.
DR GO; GO:0043024; F:ribosomal small subunit binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0033592; F:RNA strand annealing activity; IBA:GO_Central.
DR GO; GO:0034057; F:RNA strand-exchange activity; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; TAS:ProtInc.
DR GO; GO:0097010; P:eukaryotic translation initiation factor 4F complex assembly; IBA:GO_Central.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IBA:GO_Central.
DR GO; GO:0006446; P:regulation of translational initiation; TAS:ProtInc.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR033107; EIF-4B.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR23236:SF42; PTHR23236:SF42; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW Initiation factor; Isopeptide bond; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; RNA-binding; Ubl conjugation.
FT CHAIN 1..611
FT /note="Eukaryotic translation initiation factor 4B"
FT /id="PRO_0000081616"
FT DOMAIN 96..173
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..477
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..582
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 365
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BGD9"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 412
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 422
FT /note="Phosphoserine; by RPS6KA1 and RPS6KB1"
FT /evidence="ECO:0000269|PubMed:15071500,
FT ECO:0000269|PubMed:16763566, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 497
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BGD9"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 500
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BGD9"
FT MOD_RES 504
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 506
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BGD9"
FT MOD_RES 586
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 597
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT CROSSLNK 343
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 121..159
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057351"
FT VARIANT 203
FT /note="P -> R (found in a renal cell carcinoma case;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:21248752"
FT /id="VAR_064710"
FT CONFLICT 164
FT /note="R -> K (in Ref. 5; BAD96248)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="R -> C (in Ref. 8; AAH98437)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="K -> E (in Ref. 1; CAA39265)"
FT /evidence="ECO:0000305"
FT CONFLICT 391..392
FT /note="LD -> WN (in Ref. 1; CAA39265)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="L -> Q (in Ref. 8; AAH73154)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="K -> R (in Ref. 5; BAD96248)"
FT /evidence="ECO:0000305"
FT CONFLICT 611
FT /note="E -> D (in Ref. 4; CAG33239)"
FT /evidence="ECO:0000305"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:1WI8"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:1WI8"
FT HELIX 109..115
FT /evidence="ECO:0007829|PDB:1WI8"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:1WI8"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:1WI8"
FT TURN 130..133
FT /evidence="ECO:0007829|PDB:2J76"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:1WI8"
FT HELIX 147..154
FT /evidence="ECO:0007829|PDB:1WI8"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:1WI8"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:1WI8"
SQ SEQUENCE 611 AA; 69151 MW; 31CEFEA865FB10D2 CRC64;
MAASAKKKNK KGKTISLTDF LAEDGGTGGG STYVSKPVSW ADETDDLEGD VSTTWHSNDD
DVYRAPPIDR SILPTAPRAA REPNIDRSRL PKSPPYTAFL GNLPYDVTEE SIKEFFRGLN
ISAVRLPREP SNPERLKGFG YAEFEDLDSL LSALSLNEES LGNRRIRVDV ADQAQDKDRD
DRSFGRDRNR DSDKTDTDWR ARPATDSFDD YPPRRGDDSF GDKYRDRYDS DRYRDGYRDG
YRDGPRRDMD RYGGRDRYDD RGSRDYDRGY DSRIGSGRRA FGSGYRRDDD YRGGGDRYED
RYDRRDDRSW SSRDDYSRDD YRRDDRGPPQ RPKLNLKPRS TPKEDDSSAS TSQSTRAASI
FGGAKPVDTA AREREVEERL QKEQEKLQRQ LDEPKLERRP RERHPSWRSE ETQERERSRT
GSESSQTGTS TTSSRNARRR ESEKSLENET LNKEEDCHSP TSKPPKPDQP LKVMPAPPPK
ENAWVKRSSN PPARSQSSDT EQQSPTSGGG KVAPAQPSEE GPGRKDENKV DGMNAPKGQT
GNSSRGPGDG GNRDHWKESD RKDGKKDQDS RSAPEPKKPE ENPASKFSSA SKYAALSVDG
EDENEGEDYA E
