LARP1_HUMAN
ID LARP1_HUMAN Reviewed; 1096 AA.
AC Q6PKG0; O94836; Q8N4M2; Q8NB73; Q9UFD7;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=La-related protein 1;
DE AltName: Full=La ribonucleoprotein domain family member 1;
GN Name=LARP1; Synonyms=KIAA0731, LARP;
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 2).
RC TISSUE=Cervix, and Placenta;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-816 (ISOFORM 1).
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 [3]
RP PROTEIN SEQUENCE OF 2-26; 115-123; 167-185; 252-265; 357-366; 410-422;
RP 429-473; 524-539; 579-597; 643-654; 695-703; 718-778; 904-924; 937-944;
RP 949-964 AND 1004-1017, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP ALA-2, PHOSPHORYLATION AT THR-526 AND SER-774, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma, Colon carcinoma, and Mammary carcinoma;
RA Bienvenut W.V., Calvo F., Matallanas D., Cooper W.N., Kolch W.,
RA Heiserich L., Boulahbel H., Gottlieb E.;
RL Submitted (FEB-2008) to UniProtKB.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 123-1096 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 538-1096.
RC TISSUE=Mammary cancer;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-521; THR-526;
RP SER-627; SER-766 AND SER-774, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-845, AND IDENTIFICATION BY
RP 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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17693683; DOI=10.1074/mcp.m700120-mcp200;
RA Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J.,
RA Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
RT "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
RT network: indicating the involvement of ribonucleoside-diphosphate reductase
RT M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal
RT transduction.";
RL Mol. Cell. Proteomics 6:1952-1967(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND SER-90, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-627, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-143; SER-165;
RP SER-517; SER-521; THR-526; SER-627; SER-631; THR-649; THR-724; SER-774;
RP SER-824 AND SER-851, 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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; THR-526 AND SER-774, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-90; SER-627; SER-631;
RP THR-724 AND SER-824, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-892 AND LYS-1017, 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 [18]
RP RNA-BINDING, FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN A
RP COMPLEX WITH MRNA; PABPC1; EIF4E AND EIF4G1.
RX PubMed=20430826; DOI=10.1093/nar/gkq294;
RA Burrows C., Abd Latip N., Lam S.J., Carpenter L., Sawicka K., Tzolovsky G.,
RA Gabra H., Bushell M., Glover D.M., Willis A.E., Blagden S.P.;
RT "The RNA binding protein Larp1 regulates cell division, apoptosis and cell
RT migration.";
RL Nucleic Acids Res. 38:5542-5553(2010).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143; SER-220; THR-376;
RP SER-521; THR-526; SER-548; SER-627; SER-631; THR-649; SER-766 AND SER-774,
RP AND IDENTIFICATION 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 [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-143; SER-215;
RP SER-220; SER-521; THR-526; SER-548; SER-627; SER-631; SER-766; SER-774 AND
RP TYR-777, AND IDENTIFICATION BY MASS 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 [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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 [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [24]
RP RNA-BINDING, FUNCTION, AND INTERACTION WITH PABPC1.
RX PubMed=23711370; DOI=10.1016/j.febslet.2013.05.035;
RA Aoki K., Adachi S., Homoto M., Kusano H., Koike K., Natsume T.;
RT "LARP1 specifically recognizes the 3' terminus of poly(A) mRNA.";
RL FEBS Lett. 587:2173-2178(2013).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-143; THR-376;
RP SER-517; SER-521; THR-526; SER-548; SER-591; SER-627; THR-649; SER-766;
RP SER-774; THR-785; THR-788; SER-824 AND SER-1089, AND IDENTIFICATION BY MASS
RP 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 [26]
RP INDUCTION.
RX PubMed=24159927; DOI=10.1186/1479-5876-11-272;
RA Xie C., Huang L., Xie S., Xie D., Zhang G., Wang P., Peng L., Gao Z.;
RT "LARP1 predict the prognosis for early-stage and AFP-normal hepatocellular
RT carcinoma.";
RL J. Transl. Med. 11:272-272(2013).
RN [27]
RP FUNCTION, RNA-BINDING, INTERACTION WITH RPTOR; EIF4A1 AND PABPC1,
RP SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=24532714; DOI=10.1101/gad.231407.113;
RA Tcherkezian J., Cargnello M., Romeo Y., Huttlin E.L., Lavoie G., Gygi S.P.,
RA Roux P.P.;
RT "Proteomic analysis of cap-dependent translation identifies LARP1 as a key
RT regulator of 5'TOP mRNA translation.";
RL Genes Dev. 28:357-371(2014).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-90; SER-627; SER-631;
RP THR-649; SER-766 AND SER-1040, 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 [29]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-311, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [30]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION (MICROBIAL INFECTION), AND
RP IDENTIFICATION IN A COMPLEX WITH PABPC1 AND SHFL.
RX PubMed=26735137; DOI=10.1371/journal.ppat.1005357;
RA Suzuki Y., Chin W.X., Han Q., Ichiyama K., Lee C.H., Eyo Z.W., Ebina H.,
RA Takahashi H., Takahashi C., Tan B.H., Hishiki T., Ohba K., Matsuyama T.,
RA Koyanagi Y., Tan Y.J., Sawasaki T., Chu J.J., Vasudevan S.G., Sano K.,
RA Yamamoto N.;
RT "Characterization of RyDEN (C19orf66) as an interferon-stimulated cellular
RT inhibitor against dengue virus replication.";
RL PLoS Pathog. 12:E1005357-E1005357(2016).
RN [31]
RP FUNCTION, INTERACTION WITH PABPC1; RPTOR AND THE MTORC1 COMPLEX,
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP OF 497-SER--PRO-507; PHE-505; 966-PHE--ILE-970 AND PHE-966.
RX PubMed=25940091; DOI=10.1074/jbc.m114.621730;
RA Fonseca B.D., Zakaria C., Jia J.J., Graber T.E., Svitkin Y., Tahmasebi S.,
RA Healy D., Hoang H.D., Jensen J.M., Diao I.T., Lussier A., Dajadian C.,
RA Padmanabhan N., Wang W., Matta-Camacho E., Hearnden J., Smith E.M.,
RA Tsukumo Y., Yanagiya A., Morita M., Petroulakis E., Gonzalez J.L.,
RA Hernandez G., Alain T., Damgaard C.K.;
RT "La-related protein 1 (LARP1) represses terminal oligopyrimidine (TOP) mRNA
RT translation downstream of mTOR complex 1 (mTORC1).";
RL J. Biol. Chem. 290:15996-16020(2015).
RN [32]
RP FUNCTION, INTERACTION WITH RPTOR; PABPC1; EIF4E AND EIF4G1, SUBCELLULAR
RP LOCATION, PHOSPHORYLATION AT SER-766; THR-769; THR-770; THR-782; THR-785;
RP THR-797; SER-824; SER-847; SER-851; SER-861; THR-865; SER-868 AND SER-1058,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF SER-766; THR-769;
RP SER-847 AND SER-1058.
RX PubMed=28650797; DOI=10.7554/elife.25237;
RA Hong S., Freeberg M.A., Han T., Kamath A., Yao Y., Fukuda T., Suzuki T.,
RA Kim J.K., Inoki K.;
RT "LARP1 functions as a molecular switch for mTORC1-mediated translation of
RT an essential class of mRNAs.";
RL Elife 6:0-0(2017).
RN [33]
RP FUNCTION.
RX PubMed=28673543; DOI=10.1016/j.molcel.2017.06.005;
RA Gentilella A., Moron-Duran F.D., Fuentes P., Zweig-Rocha G.,
RA Riano-Canalias F., Pelletier J., Ruiz M., Turon G., Castano J., Tauler A.,
RA Bueno C., Menendez P., Kozma S.C., Thomas G.;
RT "Autogenous Control of 5'TOP mRNA Stability by 40S Ribosomes.";
RL Mol. Cell 67:55-70(2017).
RN [34]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-260; LYS-311; LYS-531 AND
RP LYS-703, AND IDENTIFICATION BY MASS 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 [35]
RP FUNCTION, INTERACTION WITH PABPC1 AND RPTOR, DOMAIN, AND MUTAGENESIS OF
RP TYR-960.
RX PubMed=29244122; DOI=10.1093/nar/gkx1237;
RA Philippe L., Vasseur J.J., Debart F., Thoreen C.C.;
RT "La-related protein 1 (LARP1) repression of TOP mRNA translation is
RT mediated through its cap-binding domain and controlled by an adjacent
RT regulatory region.";
RL Nucleic Acids Res. 46:1457-1469(2018).
RN [36] {ECO:0007744|PDB:4ZC4, ECO:0007744|PDB:5C0V}
RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 873-1023, FUNCTION, DOMAIN,
RP RNA-BINDING, AND MUTAGENESIS OF ARG-917 AND TYR-960.
RX PubMed=26206669; DOI=10.1093/nar/gkv748;
RA Lahr R.M., Mack S.M., Heroux A., Blagden S.P., Bousquet-Antonelli C.,
RA Deragon J.M., Berman A.J.;
RT "The La-related protein 1-specific domain repurposes HEAT-like repeats to
RT directly bind a 5'TOP sequence.";
RL Nucleic Acids Res. 43:8077-8088(2015).
RN [37] {ECO:0007744|PDB:5V4R, ECO:0007744|PDB:5V7C, ECO:0007744|PDB:5V87}
RP X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 873-1023 IN COMPLEX WITH RNA
RP 7-METHYLGUANOSINE CAP, FUNCTION, DOMAIN, AND MUTAGENESIS OF ARG-917;
RP TYR-960; GLU-963 AND TYR-999.
RX PubMed=28379136; DOI=10.7554/elife.24146;
RA Lahr R.M., Fonseca B.D., Ciotti G.E., Al-Ashtal H.A., Jia J.J.,
RA Niklaus M.R., Blagden S.P., Alain T., Berman A.J.;
RT "La-related protein 1 (LARP1) binds the mRNA cap, blocking eIF4F assembly
RT on TOP mRNAs.";
RL Elife 6:0-0(2017).
CC -!- FUNCTION: RNA-binding protein that regulates the translation of
CC specific target mRNA species downstream of the mTORC1 complex, in
CC function of growth signals and nutrient availability (PubMed:20430826,
CC PubMed:23711370, PubMed:24532714, PubMed:25940091, PubMed:28650797,
CC PubMed:28673543, PubMed:29244122). Interacts on the one hand with the
CC 3' poly-A tails that are present in all mRNA molecules, and on the
CC other hand with the 7-methylguanosine cap structure of mRNAs containing
CC a 5' terminal oligopyrimidine (5'TOP) motif, which is present in mRNAs
CC encoding ribosomal proteins and several components of the translation
CC machinery (PubMed:23711370, PubMed:25940091, PubMed:28650797,
CC PubMed:29244122, PubMed:26206669, PubMed:28379136). The interaction
CC with the 5' end of mRNAs containing a 5'TOP motif leads to
CC translational repression by preventing the binding of EIF4G1
CC (PubMed:25940091, PubMed:28650797, PubMed:29244122, PubMed:28379136).
CC When mTORC1 is activated, LARP1 is phosphorylated and dissociates from
CC the 5' untranslated region (UTR) of mRNA (PubMed:25940091,
CC PubMed:28650797). Does not prevent binding of EIF4G1 to mRNAs that lack
CC a 5'TOP motif (PubMed:28379136). Interacts with the free 40S ribosome
CC subunit and with ribosomes, both monosomes and polysomes
CC (PubMed:20430826, PubMed:24532714, PubMed:25940091, PubMed:28673543).
CC Under normal nutrient availability, interacts primarily with the 3'
CC untranslated region (UTR) of mRNAs encoding ribosomal proteins and
CC increases protein synthesis (PubMed:23711370, PubMed:28650797).
CC Associates with actively translating ribosomes and stimulates
CC translation of mRNAs containing a 5'TOP motif, thereby regulating
CC protein synthesis, and as a consequence, cell growth and proliferation
CC (PubMed:20430826, PubMed:24532714). Stabilizes mRNAs species with a
CC 5'TOP motif, which is required to prevent apoptosis (PubMed:20430826,
CC PubMed:23711370, PubMed:25940091, PubMed:28673543).
CC {ECO:0000269|PubMed:20430826, ECO:0000269|PubMed:23711370,
CC ECO:0000269|PubMed:24532714, ECO:0000269|PubMed:25940091,
CC ECO:0000269|PubMed:26206669, ECO:0000269|PubMed:28379136,
CC ECO:0000269|PubMed:28650797, ECO:0000269|PubMed:28673543,
CC ECO:0000269|PubMed:29244122}.
CC -!- FUNCTION: (Microbial infection) Positively regulates the replication of
CC dengue virus (DENV). {ECO:0000269|PubMed:26735137}.
CC -!- SUBUNIT: Interacts with PABPC1/PABP (PubMed:20430826, PubMed:24532714,
CC PubMed:25940091, PubMed:23711370, PubMed:28650797). Interacts with
CC EIF4A1 (PubMed:24532714). Interacts with RPTOR (PubMed:24532714,
CC PubMed:25940091, PubMed:28650797). Recruited to the active mTORC1
CC complex via interaction with RPTOR (PubMed:25940091, PubMed:28650797).
CC Inhibition of mTORC1 activity strongly reduces interaction with RPTOR
CC and the mTORC1 complex (PubMed:25940091, PubMed:28650797). Identified
CC in a complex with mRNA, PABPC1, EIF4E and EIF4G1 (PubMed:20430826,
CC PubMed:28650797). Found in a complex with PABPC1 and SHFL
CC (PubMed:26735137). {ECO:0000269|PubMed:20430826,
CC ECO:0000269|PubMed:23711370, ECO:0000269|PubMed:24532714,
CC ECO:0000269|PubMed:25940091, ECO:0000269|PubMed:26735137,
CC ECO:0000269|PubMed:28650797}.
CC -!- INTERACTION:
CC Q6PKG0; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-1052114, EBI-749265;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20430826,
CC ECO:0000269|PubMed:24532714, ECO:0000269|PubMed:28650797}. Cytoplasmic
CC granule {ECO:0000269|PubMed:24532714, ECO:0000269|PubMed:25940091}.
CC Note=Colocalizes with RPTOR and PABPC1 in cytoplasmic granules that
CC resemble stress granules. {ECO:0000269|PubMed:24532714,
CC ECO:0000269|PubMed:25940091}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6PKG0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PKG0-3; Sequence=VSP_015114, VSP_015115;
CC -!- INDUCTION: Up-regulated in a number of hepatocellular carcinoma cell
CC lines and liver cancer lesions, as well as in patients with
CC hepatocellular carcinoma with a lower survival rate (at protein level).
CC {ECO:0000269|PubMed:24159927}.
CC -!- DOMAIN: The C-terminal region mediates interaction with the mRNA and
CC polysomes (PubMed:24532714, PubMed:26206669, PubMed:28379136). It is
CC required for translational repression of mRNAs with a 5'TOP motif
CC (PubMed:29244122). {ECO:0000269|PubMed:24532714,
CC ECO:0000269|PubMed:26206669, ECO:0000269|PubMed:28379136,
CC ECO:0000269|PubMed:29244122}.
CC -!- DOMAIN: The N-terminal region mediates interaction with PABPC1.
CC {ECO:0000269|PubMed:29244122}.
CC -!- PTM: Phosphorylated on multiple Ser and Thr residues in response to
CC active mTORC1. Phosphorylation is important for interaction with RPTOR
CC and the mTORC1 complex. Phosphorylation promotes dissociation from the
CC 5'UTR of mRNA molecules with a 5'TOP motif.
CC {ECO:0000269|PubMed:28650797}.
CC -!- SIMILARITY: Belongs to the LARP family. {ECO:0000305}.
CC -!- CAUTION: Conflicting results are reported regarding the interaction
CC with PABPC1. Some studies found that the interaction depends on the
CC presence of mRNA (PubMed:23711370, PubMed:28650797). Others found that
CC the interaction is direct and does not depend on the presence of mRNA
CC (PubMed:20430826, PubMed:24532714, PubMed:25940091).
CC {ECO:0000269|PubMed:20430826, ECO:0000269|PubMed:23711370,
CC ECO:0000269|PubMed:24532714, ECO:0000269|PubMed:25940091,
CC ECO:0000269|PubMed:28650797}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH33856.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA34451.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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DR EMBL; BC001460; AAH01460.2; -; mRNA.
DR EMBL; BC033856; AAH33856.1; ALT_INIT; mRNA.
DR EMBL; AK091465; BAC03668.1; -; mRNA.
DR EMBL; AB018274; BAA34451.1; ALT_SEQ; mRNA.
DR EMBL; AL133034; CAB61364.1; -; mRNA.
DR CCDS; CCDS4328.1; -. [Q6PKG0-3]
DR PIR; T42646; T42646.
DR RefSeq; NP_056130.2; NM_015315.4. [Q6PKG0-3]
DR RefSeq; XP_005268461.1; XM_005268404.3.
DR PDB; 4ZC4; X-ray; 1.86 A; A/B/C/D=873-1023.
DR PDB; 5C0V; X-ray; 2.20 A; A/B/C/D=873-1023.
DR PDB; 5V4R; X-ray; 1.77 A; A/B=873-1023.
DR PDB; 5V7C; X-ray; 2.59 A; B=873-1023.
DR PDB; 5V87; X-ray; 1.69 A; A/B=873-1023.
DR PDB; 6PW3; X-ray; 2.34 A; A/B/C/D=873-1023.
DR PDBsum; 4ZC4; -.
DR PDBsum; 5C0V; -.
DR PDBsum; 5V4R; -.
DR PDBsum; 5V7C; -.
DR PDBsum; 5V87; -.
DR PDBsum; 6PW3; -.
DR AlphaFoldDB; Q6PKG0; -.
DR SMR; Q6PKG0; -.
DR BioGRID; 116947; 307.
DR CORUM; Q6PKG0; -.
DR IntAct; Q6PKG0; 166.
DR MINT; Q6PKG0; -.
DR STRING; 9606.ENSP00000336721; -.
DR CarbonylDB; Q6PKG0; -.
DR GlyGen; Q6PKG0; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; Q6PKG0; -.
DR PhosphoSitePlus; Q6PKG0; -.
DR SwissPalm; Q6PKG0; -.
DR BioMuta; LARP1; -.
DR DMDM; 73621135; -.
DR EPD; Q6PKG0; -.
DR jPOST; Q6PKG0; -.
DR MassIVE; Q6PKG0; -.
DR MaxQB; Q6PKG0; -.
DR PaxDb; Q6PKG0; -.
DR PeptideAtlas; Q6PKG0; -.
DR PRIDE; Q6PKG0; -.
DR ProteomicsDB; 67242; -. [Q6PKG0-1]
DR ProteomicsDB; 67243; -. [Q6PKG0-3]
DR Antibodypedia; 28316; 146 antibodies from 27 providers.
DR DNASU; 23367; -.
DR Ensembl; ENST00000336314.9; ENSP00000336721.4; ENSG00000155506.19. [Q6PKG0-3]
DR Ensembl; ENST00000518297.6; ENSP00000428589.2; ENSG00000155506.19. [Q6PKG0-1]
DR GeneID; 23367; -.
DR KEGG; hsa:23367; -.
DR MANE-Select; ENST00000518297.6; ENSP00000428589.2; NM_033551.3; NP_291029.2.
DR UCSC; uc003lvo.4; human. [Q6PKG0-1]
DR CTD; 23367; -.
DR DisGeNET; 23367; -.
DR GeneCards; LARP1; -.
DR HGNC; HGNC:29531; LARP1.
DR HPA; ENSG00000155506; Low tissue specificity.
DR MIM; 612059; gene.
DR neXtProt; NX_Q6PKG0; -.
DR OpenTargets; ENSG00000155506; -.
DR PharmGKB; PA142671564; -.
DR VEuPathDB; HostDB:ENSG00000155506; -.
DR eggNOG; KOG2590; Eukaryota.
DR GeneTree; ENSGT00940000159577; -.
DR HOGENOM; CLU_003957_1_0_1; -.
DR InParanoid; Q6PKG0; -.
DR OMA; GGHFDYQ; -.
DR OrthoDB; 258488at2759; -.
DR PhylomeDB; Q6PKG0; -.
DR TreeFam; TF314516; -.
DR PathwayCommons; Q6PKG0; -.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR SignaLink; Q6PKG0; -.
DR SIGNOR; Q6PKG0; -.
DR BioGRID-ORCS; 23367; 128 hits in 1097 CRISPR screens.
DR ChiTaRS; LARP1; human.
DR GeneWiki; LARP1; -.
DR GenomeRNAi; 23367; -.
DR Pharos; Q6PKG0; Tbio.
DR PRO; PR:Q6PKG0; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q6PKG0; protein.
DR Bgee; ENSG00000155506; Expressed in superior vestibular nucleus and 216 other tissues.
DR ExpressionAtlas; Q6PKG0; baseline and differential.
DR Genevisible; Q6PKG0; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0008190; F:eukaryotic initiation factor 4E binding; IPI:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:UniProtKB.
DR GO; GO:0043024; F:ribosomal small subunit binding; IDA:UniProtKB.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000339; F:RNA cap binding; IDA:UniProtKB.
DR GO; GO:0008494; F:translation activator activity; IMP:UniProtKB.
DR GO; GO:0031369; F:translation initiation factor binding; IDA:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IMP:UniProtKB.
DR GO; GO:0072752; P:cellular response to rapamycin; IMP:UniProtKB.
DR GO; GO:0048255; P:mRNA stabilization; IMP:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IMP:UniProtKB.
DR GO; GO:0045947; P:negative regulation of translational initiation; IMP:UniProtKB.
DR GO; GO:0016239; P:positive regulation of macroautophagy; IMP:BHF-UCL.
DR GO; GO:0045727; P:positive regulation of translation; IBA:GO_Central.
DR GO; GO:0045948; P:positive regulation of translational initiation; IMP:CACAO.
DR GO; GO:0045070; P:positive regulation of viral genome replication; IMP:UniProtKB.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IDA:FlyBase.
DR GO; GO:1990928; P:response to amino acid starvation; IMP:UniProtKB.
DR GO; GO:0031929; P:TOR signaling; IMP:UniProtKB.
DR GO; GO:0038202; P:TORC1 signaling; IMP:UniProtKB.
DR GO; GO:0006413; P:translational initiation; IMP:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR006607; DM15.
DR InterPro; IPR045180; La_dom_prot.
DR InterPro; IPR006630; La_HTH.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR22792; PTHR22792; 1.
DR Pfam; PF05383; La; 1.
DR SMART; SM00684; DM15; 3.
DR SMART; SM00715; LA; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50961; HTH_LA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Isopeptide bond; Methylation; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; Repressor; RNA-binding;
KW Translation regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..1096
FT /note="La-related protein 1"
FT /id="PRO_0000207609"
FT DOMAIN 397..487
FT /note="HTH La-type RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00332"
FT REGION 1..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..573
FT /note="Required for interaction with PABPC1"
FT /evidence="ECO:0000269|PubMed:29244122"
FT REGION 511..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..1096
FT /note="Required for interaction with RPTOR and for
FT repression of mRNAs with a 5'TOP motif"
FT /evidence="ECO:0000269|PubMed:29244122"
FT REGION 759..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 873..1023
FT /note="Interaction with mRNA"
FT /evidence="ECO:0000269|PubMed:20430826,
FT ECO:0000269|PubMed:26206669"
FT REGION 956..999
FT /note="Interaction with 7-methylguanosine mRNA cap
FT structure"
FT /evidence="ECO:0000269|PubMed:28379136,
FT ECO:0007744|PDB:5V87"
FT REGION 1026..1096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..802
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..861
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1096
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17693683, ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 223
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZQ58"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZQ58"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZQ58"
FT MOD_RES 240
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZQ58"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZQ58"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZQ58"
FT MOD_RES 376
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 526
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 548
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 631
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:24275569"
FT MOD_RES 649
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 724
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 766
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:28650797,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 769
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:28650797"
FT MOD_RES 770
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:28650797"
FT MOD_RES 774
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 777
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 782
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:28650797"
FT MOD_RES 785
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:28650797,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 788
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 797
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:28650797"
FT MOD_RES 824
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:28650797,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 845
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243"
FT MOD_RES 847
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:28650797"
FT MOD_RES 851
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:28650797,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 853
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZQ58"
FT MOD_RES 861
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:28650797"
FT MOD_RES 865
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZQ58,
FT ECO:0000269|PubMed:28650797"
FT MOD_RES 868
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:28650797"
FT MOD_RES 892
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1017
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1040
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1058
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:28650797"
FT MOD_RES 1089
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 260
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 311
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 531
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 703
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..77
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015114"
FT VAR_SEQ 78..144
FT /note="PLQLPGAEGPAISDGEEGGGEPGAGGGAAGAAGAGRRDFVEAPPPKVNPWTK
FT NALPPVLTTVNGQSP -> MLWRVLLSKRPPFPHPELDFQEAPIPSCPGRLPGRKNSVA
FT LAAAPRKEPTGDREKPLPFPVLAPFSN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015115"
FT MUTAGEN 497..507
FT /note="Missing: Strongly reduced interaction with PABPC1."
FT /evidence="ECO:0000269|PubMed:25940091"
FT MUTAGEN 505
FT /note="F->A: Strongly reduced interaction with PABPC1."
FT /evidence="ECO:0000269|PubMed:25940091"
FT MUTAGEN 766
FT /note="S->A: Loss of phosphorylation by MTOR; when
FT associated with A-769. Decreased interaction with RPTOR and
FT impaired dissociation from the 5'UTR of mRNA molecules;
FT when associated with A-769; A-847 and A-1058."
FT /evidence="ECO:0000269|PubMed:28650797"
FT MUTAGEN 769
FT /note="T->A: Loss of phosphorylation by MTOR; when
FT associated with A-766. Decreased interaction with RPTOR and
FT impaired dissociation from the 5'UTR of mRNA molecules;
FT when associated with A-766; A-847 and A-1058."
FT /evidence="ECO:0000269|PubMed:28650797"
FT MUTAGEN 847
FT /note="S->A: Strongly reduced phosphorylation mediated by
FT Akt and RPS6KB1. Decreased interaction with RPTOR and
FT impaired dissociation from the 5'UTR of mRNA molecules;
FT when associated with A-766; A-769 and A-1058."
FT /evidence="ECO:0000269|PubMed:28650797"
FT MUTAGEN 917
FT /note="R->E: Abolishes RNA binding. Abolishes inhibition of
FT EIF4G1 binding to mRNA molecules with a 5'TOP motif; when
FT associated with A-960."
FT /evidence="ECO:0000269|PubMed:26206669,
FT ECO:0000269|PubMed:28379136"
FT MUTAGEN 960
FT /note="Y->A: Abolishes RNA binding. Abolishes translational
FT repression of mRNAs with a 5'TOP motif. Abolishes
FT inhibition of EIF4G1 binding to mRNA molecules with a 5'TOP
FT motif; when associated with E-917."
FT /evidence="ECO:0000269|PubMed:26206669,
FT ECO:0000269|PubMed:28379136, ECO:0000269|PubMed:29244122"
FT MUTAGEN 963
FT /note="E->R: Strongly decreased RNA binding."
FT /evidence="ECO:0000269|PubMed:28379136"
FT MUTAGEN 966..970
FT /note="Missing: Loss of interaction with RPTOR."
FT /evidence="ECO:0000269|PubMed:25940091"
FT MUTAGEN 966
FT /note="F->A: No effect on interaction with RPTOR."
FT /evidence="ECO:0000269|PubMed:25940091"
FT MUTAGEN 999
FT /note="Y->A: Strongly decreased RNA binding."
FT /evidence="ECO:0000269|PubMed:28379136"
FT MUTAGEN 1058
FT /note="S->A: Strongly reduced phosphorylation mediated by
FT AKT and RPS6KB1. Decreased interaction with RPTOR and
FT impaired dissociation from the 5'UTR of mRNA molecules;
FT when associated with A-766; A-769 and A-847."
FT /evidence="ECO:0000269|PubMed:28650797"
FT CONFLICT 778..780
FT /note="RNT -> TRP (in Ref. 1; AAH33856)"
FT /evidence="ECO:0000305"
FT CONFLICT 979
FT /note="V -> L (in Ref. 5; CAB61364)"
FT /evidence="ECO:0000305"
FT HELIX 875..880
FT /evidence="ECO:0007829|PDB:5V87"
FT TURN 882..884
FT /evidence="ECO:0007829|PDB:5V4R"
FT HELIX 887..904
FT /evidence="ECO:0007829|PDB:5V87"
FT TURN 906..908
FT /evidence="ECO:0007829|PDB:6PW3"
FT HELIX 910..925
FT /evidence="ECO:0007829|PDB:5V87"
FT HELIX 929..945
FT /evidence="ECO:0007829|PDB:5V87"
FT HELIX 949..964
FT /evidence="ECO:0007829|PDB:5V87"
FT HELIX 968..983
FT /evidence="ECO:0007829|PDB:5V87"
FT HELIX 988..999
FT /evidence="ECO:0007829|PDB:5V87"
FT HELIX 1001..1004
FT /evidence="ECO:0007829|PDB:5C0V"
FT HELIX 1009..1017
FT /evidence="ECO:0007829|PDB:5V87"
SQ SEQUENCE 1096 AA; 123510 MW; CA3E9D30BBC101B7 CRC64;
MATQVEPLLP GGATLLQAEE HGGLVRKKPP PAPEGKGEPG PNDVRGGEPD GSARRPRPPC
AKPHKEGTGQ QERESPRPLQ LPGAEGPAIS DGEEGGGEPG AGGGAAGAAG AGRRDFVEAP
PPKVNPWTKN ALPPVLTTVN GQSPPEHSAP AKVVRAAVPK QRKGSKVGDF GDAINWPTPG
EIAHKSVQPQ SHKPQPTRKL PPKKDMKEQE KGEGSDSKES PKTKSDESGE EKNGDEDCQR
GGQKKKGNKH KWVPLQIDMK PEVPREKLAS RPTRPPEPRH IPANRGEIKG SESATYVPVA
PPTPAWQPEI KPEPAWHDQD ETSSVKSDGA GGARASFRGR GRGRGRGRGR GRGGTRTHFD
YQFGYRKFDG VEGPRTPKYM NNITYYFDNV SSTELYSVDQ ELLKDYIKRQ IEYYFSVDNL
ERDFFLRRKM DADGFLPITL IASFHRVQAL TTDISLIFAA LKDSKVVEIV DEKVRRREEP
EKWPLPPIVD YSQTDFSQLL NCPEFVPRQH YQKETESAPG SPRAVTPVPT KTEEVSNLKT
LPKGLSASLP DLDSENWIEV KKRPRPSPAR PKKSEESRFS HLTSLPQQLP SQQLMSKDQD
EQEELDFLFD EEMEQMDGRK NTFTAWSDEE SDYEIDDRDV NKILIVTQTP HYMRRHPGGD
RTGNHTSRAK MSAELAKVIN DGLFYYEQDL WAEKFEPEYS QIKQEVENFK KVNMISREQF
DTLTPEPPVD PNQEVPPGPP RFQQVPTDAL ANKLFGAPEP STIARSLPTT VPESPNYRNT
RTPRTPRTPQ LKDSSQTSRF YPVVKEGRTL DAKMPRKRKT RHSSNPPLES HVGWVMDSRE
HRPRTASISS SPSEGTPTVG SYGCTPQSLP KFQHPSHELL KENGFTQHVY HKYRRRCLNE
RKRLGIGQSQ EMNTLFRFWS FFLRDHFNKK MYEEFKQLAL EDAKEGYRYG LECLFRYYSY
GLEKKFRLDI FKDFQEETVK DYEAGQLYGL EKFWAFLKYS KAKNLDIDPK LQEYLGKFRR
LEDFRVDPPM GEEGNHKRHS VVAGGGGGEG RKRCPSQSSS RPAAMISQPP TPPTGQPVRE
DAKWTSQHSN TQTLGK
