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 27-MAR-2024, entry version 198. 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}, EIF3S6IP GN {ECO:0000255|HAMAP-Rule:MF_03011}; 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7QP6; EM; 4.70 A; 5=1-564. DR PDB; 7QP7; EM; 3.70 A; 5=1-564. DR PDB; 8PPL; EM; 2.65 A; I5=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 PDBsum; 7QP6; -. DR PDBsum; 7QP7; -. DR PDBsum; 8PPL; -. DR AlphaFoldDB; Q9Y262; -. DR EMDB; EMD-10769; -. DR EMDB; EMD-11302; -. DR EMDB; EMD-11325; -. DR EMDB; EMD-11335; -. DR EMDB; EMD-11458; -. DR EMDB; EMD-11602; -. DR EMDB; EMD-14113; -. DR EMDB; EMD-14114; -. DR EMDB; EMD-17805; -. DR EMDB; EMD-4242; -. DR SMR; Q9Y262; -. DR BioGRID; 119516; 245. DR ComplexPortal; CPX-6036; Eukaryotic translation initiation factor 3 complex. DR CORUM; Q9Y262; -. DR DIP; DIP-31172N; -. DR IntAct; Q9Y262; 90. DR MINT; Q9Y262; -. DR STRING; 9606.ENSP00000499067; -. 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; 9606-ENSP00000485663; -. DR PeptideAtlas; Q9Y262; -. DR PRIDE; Q9Y262; -. DR ProteomicsDB; 34230; -. DR ProteomicsDB; 85666; -. [Q9Y262-1] DR Pumba; Q9Y262; -. DR TopDownProteomics; Q9Y262-1; -. [Q9Y262-1] DR Antibodypedia; 221; 182 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 AGR; HGNC:18138; -. 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; 46475at2759; -. 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; 265 hits in 1161 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 103 other cell types or tissues. DR ExpressionAtlas; Q9Y262; baseline and differential. 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:0045202; C:synapse; 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; NAS: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; EUKARYOTIC TRANSLATION INITIATION FACTOR 3; 1. DR PANTHER; PTHR13242:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT L; 1. DR Pfam; PF10255; Paf67; 1. DR SUPFAM; SSF48452; TPR-like; 1. DR PROSITE; PS50250; PCI; 1. DR Genevisible; Q9Y262; HS. 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 //