EIF3L_HUMAN
ID EIF3L_HUMAN Reviewed; 564 AA.
AC Q9Y262; B2RDG6; B4DYB2; G8JLH4; Q53HQ1; Q53HT4; Q5QTR1; Q5TI15; Q6ICD2;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit L {ECO:0000255|HAMAP-Rule:MF_03011};
DE Short=eIF3l {ECO:0000255|HAMAP-Rule:MF_03011};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 6-interacting protein {ECO:0000255|HAMAP-Rule:MF_03011};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit E-interacting protein {ECO:0000255|HAMAP-Rule:MF_03011};
GN Name=EIF3L {ECO:0000255|HAMAP-Rule:MF_03011};
GN Synonyms=EIF3EIP {ECO:0000255|HAMAP-Rule:MF_03011},
GN EIF3S6IP {ECO:0000255|HAMAP-Rule:MF_03011};
GN ORFNames=HSPC021, HSPC025, MSTP005;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Aorta;
RA Hui R.T., Liu Y.Q., Liu B., Zhao B., Meng X.M., Sheng H., Xu Y.Y.,
RA Wang X.Y., Ye J., Song L., Gao Y., Wei Y.J., Zhang C.L., Zhang J.,
RA Chai M.Q., Chen J.Z., Sun Y.H., Zhou X.L., Jiang Y.X., Zhao X.W., Liu S.,
RA Cao H.Q., Zhao Y., Liu D.Q., Ding J.F., Liu L.S., Gao R.L., Wu Q.Y.,
RA Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S.;
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis;
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 [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=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
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=Brain, Cervix, and Colon;
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 INTERACTION WITH EIF3E.
RX PubMed=11590142; DOI=10.1074/jbc.m104966200;
RA Morris-Desbois C., Rety S., Ferro M., Garin J., Jalinot P.;
RT "The human protein HSPC021 interacts with Int-6 and is associated with
RT eukaryotic translation initiation factor 3.";
RL J. Biol. Chem. 276:45988-45995(2001).
RN [10]
RP INTERACTION WITH RRN3.
RX PubMed=12393749; DOI=10.1093/embo-reports/kvf212;
RA Yuan X., Zhao J., Zentgraf H., Hoffmann-Rohrer U., Grummt I.;
RT "Multiple interactions between RNA polymerase I, TIF-IA and TAF(I) subunits
RT regulate preinitiation complex assembly at the ribosomal gene promoter.";
RL EMBO Rep. 3:1082-1087(2002).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [12]
RP CHARACTERIZATION OF THE EIF-3 COMPLEX.
RX PubMed=15703437; DOI=10.1261/rna.7215305;
RA Kolupaeva V.G., Unbehaun A., Lomakin I.B., Hellen C.U.T., Pestova T.V.;
RT "Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits and
RT its role in ribosomal dissociation and anti-association.";
RL RNA 11:470-486(2005).
RN [13]
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 [14]
RP FUNCTION, AND 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 [15]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=18056426; DOI=10.1101/gad.439507;
RA Poyry T.A., Kaminski A., Connell E.J., Fraser C.S., Jackson R.J.;
RT "The mechanism of an exceptional case of reinitiation after translation of
RT a long ORF reveals why such events do not generally occur in mammalian mRNA
RT translation.";
RL Genes Dev. 21:3149-3162(2007).
RN [16]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX,
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND MASS
RP SPECTROMETRY.
RX PubMed=17322308; DOI=10.1074/mcp.m600399-mcp200;
RA Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L., Hershey J.W.B.,
RA Doudna J.A., Robinson C.V., Leary J.A.;
RT "Structural characterization of the human eukaryotic initiation factor 3
RT protein complex by mass spectrometry.";
RL Mol. Cell. Proteomics 6:1135-1146(2007).
RN [17]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX,
RP MASS SPECTROMETRY, AND INTERACTION WITH EIF3B.
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 interaction
RT map of the eukaryotic translation factor eIF3.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18139-18144(2008).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-465 AND LYS-549, AND
RP IDENTIFICATION BY MASS 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 [20]
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 [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [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 [23]
RP FUNCTION, AND IDENTIFICATION IN THE EIF-3 COMPLEX.
RX PubMed=25849773; DOI=10.1038/nature14267;
RA Lee A.S., Kranzusch P.J., Cate J.H.;
RT "eIF3 targets cell-proliferation messenger RNAs for translational
RT activation or repression.";
RL Nature 522:111-114(2015).
RN [24]
RP FUNCTION.
RX PubMed=27462815; DOI=10.1038/nature18954;
RA Lee A.S., Kranzusch P.J., Doudna J.A., Cate J.H.;
RT "eIF3d is an mRNA cap-binding protein that is required for specialized
RT translation initiation.";
RL Nature 536:96-99(2016).
RN [25]
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 factor 3
CC (eIF-3) complex, which is required for several steps in the initiation
CC of protein synthesis (PubMed:17581632, PubMed:25849773,
CC PubMed:27462815). The eIF-3 complex associates with the 40S ribosome
CC and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-
CC tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The
CC eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning
CC of the mRNA for AUG recognition. The eIF-3 complex is also required for
CC disassembly and recycling of post-termination ribosomal complexes and
CC subsequently prevents premature joining of the 40S and 60S ribosomal
CC subunits prior to initiation (PubMed:17581632). The eIF-3 complex
CC specifically targets and initiates translation of a subset of mRNAs
CC involved in cell proliferation, including cell cycling, differentiation
CC and apoptosis, and uses different modes of RNA stem-loop binding to
CC exert either translational activation or repression (PubMed:25849773).
CC {ECO:0000255|HAMAP-Rule:MF_03011, ECO:0000269|PubMed:17581632,
CC ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:27462815}.
CC -!- FUNCTION: (Microbial infection) In case of FCV infection, plays a role
CC in the ribosomal termination-reinitiation event leading to the
CC translation of VP2 (PubMed:18056426). {ECO:0000269|PubMed:18056426}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C,
CC EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and
CC EIF3M. The eIF-3 complex appears to include 3 stable modules: module A
CC is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of
CC EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D,
CC EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and
CC EIF3H of module B, thereby linking the three modules. EIF3J is a labile
CC subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex
CC interacts with RPS6KB1 under conditions of nutrient depletion.
CC Mitogenic stimulation leads to binding and activation of a complex
CC composed of MTOR and RPTOR, leading to phosphorylation and release of
CC RPS6KB1 and binding of EIF4B to eIF-3. Interacts with RRN3.
CC {ECO:0000255|HAMAP-Rule:MF_03011, ECO:0000269|PubMed:25849773}.
CC -!- INTERACTION:
CC Q9Y262; P55884: EIF3B; NbExp=3; IntAct=EBI-373519, EBI-366696;
CC Q9Y262; P60228: EIF3E; NbExp=7; IntAct=EBI-373519, EBI-347740;
CC Q9Y262; Q9UBQ5: EIF3K; NbExp=14; IntAct=EBI-373519, EBI-354344;
CC Q9Y262; O14901: KLF11; NbExp=3; IntAct=EBI-373519, EBI-948266;
CC Q9Y262; Q6NYC8: PPP1R18; NbExp=3; IntAct=EBI-373519, EBI-2557469;
CC Q9Y262; Q9Q2G4: ORF; Xeno; NbExp=5; IntAct=EBI-373519, EBI-6248094;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03011}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y262-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y262-2; Sequence=VSP_045881;
CC -!- MASS SPECTROMETRY: Mass=66637.9; Method=Unknown;
CC Evidence={ECO:0000269|PubMed:17322308};
CC -!- MASS SPECTROMETRY: Mass=66640.2; Mass_error=0.5; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18599441};
CC -!- SIMILARITY: Belongs to the eIF-3 subunit L family. {ECO:0000255|HAMAP-
CC Rule:MF_03011}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAG30322.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF077207; AAD27002.1; -; mRNA.
DR EMBL; AF083243; AAD39841.1; -; mRNA.
DR EMBL; AF109359; AAQ13507.1; -; mRNA.
DR EMBL; CR456436; CAG30322.1; ALT_INIT; mRNA.
DR EMBL; AK302346; BAG63674.1; -; mRNA.
DR EMBL; AK315533; BAG37913.1; -; mRNA.
DR EMBL; AK222496; BAD96216.1; -; mRNA.
DR EMBL; AK222529; BAD96249.1; -; mRNA.
DR EMBL; AL022311; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z97630; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW60198.1; -; Genomic_DNA.
DR EMBL; BC001101; AAH01101.1; -; mRNA.
DR EMBL; BC007510; AAH07510.1; -; mRNA.
DR EMBL; BC029265; AAH29265.1; -; mRNA.
DR CCDS; CCDS13960.1; -. [Q9Y262-1]
DR CCDS; CCDS56230.1; -. [Q9Y262-2]
DR RefSeq; NP_001229852.1; NM_001242923.1. [Q9Y262-2]
DR RefSeq; NP_057175.1; NM_016091.3. [Q9Y262-1]
DR PDB; 3J8B; EM; -; L=1-515.
DR PDB; 3J8C; EM; -; L=1-515.
DR PDB; 6FEC; EM; 6.30 A; 7=1-564.
DR PDB; 6YBD; EM; 3.30 A; 5=1-564.
DR PDB; 6ZMW; EM; 3.70 A; 5=1-564.
DR PDB; 6ZON; EM; 3.00 A; L=1-564.
DR PDB; 6ZP4; EM; 2.90 A; L=1-564.
DR PDB; 6ZVJ; EM; 3.80 A; L=181-552.
DR PDB; 7A09; EM; 3.50 A; L=1-564.
DR PDBsum; 3J8B; -.
DR PDBsum; 3J8C; -.
DR PDBsum; 6FEC; -.
DR PDBsum; 6YBD; -.
DR PDBsum; 6ZMW; -.
DR PDBsum; 6ZON; -.
DR PDBsum; 6ZP4; -.
DR PDBsum; 6ZVJ; -.
DR PDBsum; 7A09; -.
DR AlphaFoldDB; Q9Y262; -.
DR SMR; Q9Y262; -.
DR BioGRID; 119516; 159.
DR ComplexPortal; CPX-6036; Eukaryotic translation initiation factor 3 complex.
DR CORUM; Q9Y262; -.
DR DIP; DIP-31172N; -.
DR IntAct; Q9Y262; 85.
DR MINT; Q9Y262; -.
DR STRING; 9606.ENSP00000485663; -.
DR GlyGen; Q9Y262; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y262; -.
DR MetOSite; Q9Y262; -.
DR PhosphoSitePlus; Q9Y262; -.
DR SwissPalm; Q9Y262; -.
DR BioMuta; EIF3L; -.
DR DMDM; 23396631; -.
DR EPD; Q9Y262; -.
DR jPOST; Q9Y262; -.
DR MassIVE; Q9Y262; -.
DR MaxQB; Q9Y262; -.
DR PaxDb; Q9Y262; -.
DR PeptideAtlas; Q9Y262; -.
DR PRIDE; Q9Y262; -.
DR ProteomicsDB; 34230; -.
DR ProteomicsDB; 85666; -. [Q9Y262-1]
DR TopDownProteomics; Q9Y262-1; -. [Q9Y262-1]
DR Antibodypedia; 221; 151 antibodies from 25 providers.
DR DNASU; 51386; -.
DR Ensembl; ENST00000381683.10; ENSP00000371099.4; ENSG00000100129.18. [Q9Y262-2]
DR Ensembl; ENST00000624234.3; ENSP00000485663.1; ENSG00000100129.18. [Q9Y262-1]
DR Ensembl; ENST00000652021.1; ENSP00000499067.1; ENSG00000100129.18. [Q9Y262-1]
DR GeneID; 51386; -.
DR KEGG; hsa:51386; -.
DR MANE-Select; ENST00000652021.1; ENSP00000499067.1; NM_016091.4; NP_057175.1.
DR UCSC; uc003auf.3; human. [Q9Y262-1]
DR CTD; 51386; -.
DR DisGeNET; 51386; -.
DR GeneCards; EIF3L; -.
DR HGNC; HGNC:18138; EIF3L.
DR HPA; ENSG00000100129; Low tissue specificity.
DR MIM; 619197; gene.
DR neXtProt; NX_Q9Y262; -.
DR OpenTargets; ENSG00000100129; -.
DR PharmGKB; PA27706; -.
DR VEuPathDB; HostDB:ENSG00000100129; -.
DR eggNOG; KOG3677; Eukaryota.
DR GeneTree; ENSGT00390000000411; -.
DR HOGENOM; CLU_029210_0_1_1; -.
DR InParanoid; Q9Y262; -.
DR OMA; AGWFIRN; -.
DR OrthoDB; 393910at2759; -.
DR PhylomeDB; Q9Y262; -.
DR TreeFam; TF101523; -.
DR PathwayCommons; Q9Y262; -.
DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-HSA-72649; Translation initiation complex formation.
DR Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
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; Q9Y262; -.
DR SIGNOR; Q9Y262; -.
DR BioGRID-ORCS; 51386; 257 hits in 1085 CRISPR screens.
DR ChiTaRS; EIF3L; human.
DR GeneWiki; EIF3EIP; -.
DR GenomeRNAi; 51386; -.
DR Pharos; Q9Y262; Tbio.
DR PRO; PR:Q9Y262; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9Y262; protein.
DR Bgee; ENSG00000100129; Expressed in cortical plate and 101 other tissues.
DR ExpressionAtlas; Q9Y262; baseline and differential.
DR Genevisible; Q9Y262; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:UniProtKB.
DR GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IC:ComplexPortal.
DR GO; GO:0006413; P:translational initiation; IDA:UniProtKB.
DR GO; GO:0075525; P:viral translational termination-reinitiation; IDA:UniProtKB.
DR HAMAP; MF_03011; eIF3l; 1.
DR InterPro; IPR019382; eIF3l.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR13242; PTHR13242; 1.
DR Pfam; PF10255; Paf67; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Initiation factor; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03011,
FT ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..564
FT /note="Eukaryotic translation initiation factor 3 subunit
FT L"
FT /id="PRO_0000084162"
FT DOMAIN 331..537
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03011,
FT ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 465
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 549
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 146..193
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045881"
FT CONFLICT 353
FT /note="T -> I (in Ref. 2; AAQ13507)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="M -> V (in Ref. 5; BAD96249)"
FT /evidence="ECO:0000305"
FT CONFLICT 432
FT /note="H -> Y (in Ref. 5; BAD96216)"
FT /evidence="ECO:0000305"
FT CONFLICT 434
FT /note="N -> D (in Ref. 5; BAD96249)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="F -> L (in Ref. 4; BAG63674)"
FT /evidence="ECO:0000305"
FT CONFLICT 528
FT /note="I -> T (in Ref. 4; BAG63674)"
FT /evidence="ECO:0000305"
FT CONFLICT 558
FT /note="K -> R (in Ref. 4; BAG63674)"
FT /evidence="ECO:0000305"
FT HELIX 184..206
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 209..217
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 224..246
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 253..267
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 275..289
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 298..302
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 312..325
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 329..334
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 336..341
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 358..374
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 383..385
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 388..400
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 406..416
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 439..461
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 468..470
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 472..480
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 491..496
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 499..501
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 504..506
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 508..510
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 513..515
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 527..548
FT /evidence="ECO:0007829|PDB:6YBD"
SQ SEQUENCE 564 AA; 66727 MW; ECBD32192D96E3FE CRC64;
MSYPADDYES EAAYDPYAYP SDYDMHTGDP KQDLAYERQY EQQTYQVIPE VIKNFIQYFH
KTVSDLIDQK VYELQASRVS SDVIDQKVYE IQDIYENSWT KLTERFFKNT PWPEAEAIAP
QVGNDAVFLI LYKELYYRHI YAKVSGGPSL EQRFESYYNY CNLFNYILNA DGPAPLELPN
QWLWDIIDEF IYQFQSFSQY RCKTAKKSEE EIDFLRSNPK IWNVHSVLNV LHSLVDKSNI
NRQLEVYTSG GDPESVAGEY GRHSLYKMLG YFSLVGLLRL HSLLGDYYQA IKVLENIELN
KKSMYSRVPE CQVTTYYYVG FAYLMMRRYQ DAIRVFANIL LYIQRTKSMF QRTTYKYEMI
NKQNEQMHAL LAIALTMYPM RIDESIHLQL REKYGDKMLR MQKGDPQVYE ELFSYSCPKF
LSPVVPNYDN VHPNYHKEPF LQQLKVFSDE VQQQAQLSTI RSFLKLYTTM PVAKLAGFLD
LTEQEFRIQL LVFKHKMKNL VWTSGISALD GEFQSASEVD FYIDKDMIHI ADTKVARRYG
DFFIRQIHKF EELNRTLKKM GQRP
