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La-related protein 1 (La ribonucleoprotein domain family member 1)

 LARP1_HUMAN             Reviewed;        1096 AA.
Q6PKG0; O94836; Q8N4M2; Q8NB73; Q9UFD7;
16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
16-AUG-2005, sequence version 2.
05-DEC-2018, entry version 152.
RecName: Full=La-related protein 1;
AltName: Full=La ribonucleoprotein domain family member 1;
Name=LARP1; Synonyms=KIAA0731, LARP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Cervix, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-816 (ISOFORM 1).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
PROTEIN SEQUENCE OF 2-26; 115-123; 167-185; 252-265; 357-366; 410-422;
429-473; 524-539; 579-597; 643-654; 695-703; 718-778; 904-924;
937-944; 949-964 AND 1004-1017, CLEAVAGE OF INITIATOR METHIONINE,
ACETYLATION AT ALA-2, PHOSPHORYLATION AT THR-526 AND SER-774, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Cervix carcinoma, Colon carcinoma, and Mammary carcinoma;
Bienvenut W.V., Calvo F., Matallanas D., Cooper W.N., Kolch W.,
Heiserich L., Boulahbel H., Gottlieb E.;
Submitted (FEB-2008) to UniProtKB.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 123-1096 (ISOFORM 1).
TISSUE=Brain;
PubMed=9872452; DOI=10.1093/dnares/5.5.277;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XI.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 5:277-286(1998).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 538-1096.
TISSUE=Mammary cancer;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-521; THR-526;
SER-627; SER-766 AND SER-774, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-845, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa
cells and high confident phosphopeptide identification by cross-
validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17693683; DOI=10.1074/mcp.M700120-MCP200;
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,
Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
network: indicating the involvement of ribonucleoside-diphosphate
reductase M2 subunit phosphorylation at residue serine 20 in canonical
Wnt signal transduction.";
Mol. Cell. Proteomics 6:1952-1967(2007).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND SER-90, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-627, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-143; SER-165;
SER-517; SER-521; THR-526; SER-627; SER-631; THR-649; THR-724;
SER-774; SER-824 AND SER-851, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; THR-526 AND SER-774,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-90; SER-627;
SER-631; THR-724 AND SER-824, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-892 AND LYS-1017, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[18]
RNA-BINDING, FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH
EIF4E AND PABPC1.
PubMed=20430826; DOI=10.1093/nar/gkq294;
Burrows C., Abd Latip N., Lam S.J., Carpenter L., Sawicka K.,
Tzolovsky G., Gabra H., Bushell M., Glover D.M., Willis A.E.,
Blagden S.P.;
"The RNA binding protein Larp1 regulates cell division, apoptosis and
cell migration.";
Nucleic Acids Res. 38:5542-5553(2010).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143; SER-220; THR-376;
SER-521; THR-526; SER-548; SER-627; SER-631; THR-649; SER-766 AND
SER-774, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-143; SER-215;
SER-220; SER-521; THR-526; SER-548; SER-627; SER-631; SER-766; SER-774
AND TYR-777, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[23]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[24]
RNA-BINDING, AND FUNCTION.
PubMed=23711370; DOI=10.1016/j.febslet.2013.05.035;
Aoki K., Adachi S., Homoto M., Kusano H., Koike K., Natsume T.;
"LARP1 specifically recognizes the 3' terminus of poly(A) mRNA.";
FEBS Lett. 587:2173-2178(2013).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-143; THR-376;
SER-517; SER-521; THR-526; SER-548; SER-591; SER-627; THR-649;
SER-766; SER-774; THR-785; THR-788; SER-824 AND SER-1089, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[26]
INDUCTION.
PubMed=24159927; DOI=10.1186/1479-5876-11-272;
Xie C., Huang L., Xie S., Xie D., Zhang G., Wang P., Peng L., Gao Z.;
"LARP1 predict the prognosis for early-stage and AFP-normal
hepatocellular carcinoma.";
J. Transl. Med. 11:272-272(2013).
[27]
FUNCTION, RNA-BINDING, INTERACTION WITH PABPC1, AND SUBCELLULAR
LOCATION.
PubMed=24532714; DOI=10.1101/gad.231407.113;
Tcherkezian J., Cargnello M., Romeo Y., Huttlin E.L., Lavoie G.,
Gygi S.P., Roux P.P.;
"Proteomic analysis of cap-dependent translation identifies LARP1 as a
key regulator of 5'TOP mRNA translation.";
Genes Dev. 28:357-371(2014).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-90; SER-627;
SER-631; THR-649; SER-766 AND SER-1040, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[29]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-311, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[30]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND IDENTIFICATION IN A
COMPLEX WITH PABPC1 AND RYDEN.
PubMed=26735137; DOI=10.1371/journal.ppat.1005357;
Suzuki Y., Chin W.X., Han Q., Ichiyama K., Lee C.H., Eyo Z.W.,
Ebina H., Takahashi H., Takahashi C., Tan B.H., Hishiki T., Ohba K.,
Matsuyama T., Koyanagi Y., Tan Y.J., Sawasaki T., Chu J.J.,
Vasudevan S.G., Sano K., Yamamoto N.;
"Characterization of RyDEN (C19orf66) as an interferon-stimulated
cellular inhibitor against dengue virus replication.";
PLoS Pathog. 12:E1005357-E1005357(2016).
[31]
FUNCTION, INTERACTION WITH PABPC1; RPTOR AND THE MTORC1 COMPLEX, AND
SUBCELLULAR LOCATION.
PubMed=25940091; DOI=10.1074/jbc.M114.621730;
Fonseca B.D., Zakaria C., Jia J.J., Graber T.E., Svitkin Y.,
Tahmasebi S., Healy D., Hoang H.D., Jensen J.M., Diao I.T.,
Lussier A., Dajadian C., Padmanabhan N., Wang W., Matta-Camacho E.,
Hearnden J., Smith E.M., Tsukumo Y., Yanagiya A., Morita M.,
Petroulakis E., Gonzalez J.L., Hernandez G., Alain T., Damgaard C.K.;
"La-related protein 1 (LARP1) represses terminal oligopyrimidine (TOP)
mRNA translation downstream of mTOR complex 1 (mTORC1).";
J. Biol. Chem. 290:15996-16020(2015).
[32]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-260; LYS-311; LYS-531 AND
LYS-703, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[33] {ECO:0000244|PDB:4ZC4, ECO:0000244|PDB:5C0V}
X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 873-1023, FUNCTION,
RNA-BINDING, AND MUTAGENESIS OF ARG-917 AND TYR-960.
PubMed=26206669; DOI=10.1093/nar/gkv748;
Lahr R.M., Mack S.M., Heroux A., Blagden S.P., Bousquet-Antonelli C.,
Deragon J.M., Berman A.J.;
"The La-related protein 1-specific domain repurposes HEAT-like repeats
to directly bind a 5'TOP sequence.";
Nucleic Acids Res. 43:8077-8088(2015).
-!- FUNCTION: RNA-binding protein that promotes translation of
specific classes of mRNAs downstream of the mTORC1 complex
(PubMed:24532714, PubMed:25940091). Associates with the mRNA 5'cap
in an MTOR-dependent manner and associates with mRNAs containing a
5' terminal oligopyrimidine (5'TOP) motif, which is present in
mRNAs encoding for ribosomal proteins and several components of
the translation machinery (PubMed:24532714, PubMed:25940091,
PubMed:26206669). Associates with actively translating ribosomes
via interaction with PABPC1/PABP and stimulates translation of
mRNAs containing a 5'TOP, thereby regulating cell growth and
proliferation (PubMed:20430826, PubMed:25940091). Positively
regulates the replication of dengue virus (DENV)
(PubMed:26735137). {ECO:0000269|PubMed:20430826,
ECO:0000269|PubMed:24532714, ECO:0000269|PubMed:26206669,
ECO:0000269|PubMed:26735137}.
-!- SUBUNIT: Interacts with PABPC1/PABP (PubMed:20430826,
PubMed:24532714, PubMed:25940091). Associates with the mTORC1
complex via interaction with RPTOR (PubMed:25940091). Interacts
with EIF4E (PubMed:20430826). Found in a complex with PABPC1 and
RYDEN (PubMed:26735137). {ECO:0000269|PubMed:20430826,
ECO:0000269|PubMed:24532714, ECO:0000269|PubMed:25940091,
ECO:0000269|PubMed:26735137}.
-!- INTERACTION:
Q8N6L0:CCDC155; NbExp=3; IntAct=EBI-1052114, EBI-749265;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20430826,
ECO:0000269|PubMed:24532714}. Cytoplasmic granule
{ECO:0000269|PubMed:25940091}. Note=Colocalizes with RPTOR and
PABPC1 in cytoplasmic granules that resemble stress granules.
{ECO:0000269|PubMed:25940091}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q6PKG0-1; Sequence=Displayed;
Name=2;
IsoId=Q6PKG0-3; Sequence=VSP_015114, VSP_015115;
-!- INDUCTION: Up-regulated in a number of hepatocellular carcinoma
cell lines and liver cancer lesions, as well as in patients with
hepatocellular carcinoma with a lower survival rate (at protein
level). {ECO:0000269|PubMed:24159927}.
-!- SIMILARITY: Belongs to the LARP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH33856.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAA34451.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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EMBL; BC001460; AAH01460.2; -; mRNA.
EMBL; BC033856; AAH33856.1; ALT_INIT; mRNA.
EMBL; AK091465; BAC03668.1; -; mRNA.
EMBL; AB018274; BAA34451.1; ALT_SEQ; mRNA.
EMBL; AL133034; CAB61364.1; -; mRNA.
CCDS; CCDS4328.1; -. [Q6PKG0-3]
PIR; T42646; T42646.
RefSeq; NP_056130.2; NM_015315.4. [Q6PKG0-3]
RefSeq; XP_005268461.1; XM_005268404.3. [Q6PKG0-1]
UniGene; Hs.292078; -.
PDB; 4ZC4; X-ray; 1.86 A; A/B/C/D=873-1023.
PDB; 5C0V; X-ray; 2.20 A; A/B/C/D=873-1023.
PDB; 5V4R; X-ray; 1.77 A; A/B=873-1023.
PDB; 5V7C; X-ray; 2.59 A; B=873-1023.
PDB; 5V87; X-ray; 1.69 A; A/B=873-1023.
PDBsum; 4ZC4; -.
PDBsum; 5C0V; -.
PDBsum; 5V4R; -.
PDBsum; 5V7C; -.
PDBsum; 5V87; -.
ProteinModelPortal; Q6PKG0; -.
SMR; Q6PKG0; -.
BioGrid; 116947; 143.
CORUM; Q6PKG0; -.
IntAct; Q6PKG0; 62.
MINT; Q6PKG0; -.
STRING; 9606.ENSP00000336721; -.
CarbonylDB; Q6PKG0; -.
iPTMnet; Q6PKG0; -.
PhosphoSitePlus; Q6PKG0; -.
SwissPalm; Q6PKG0; -.
DMDM; 73621135; -.
EPD; Q6PKG0; -.
MaxQB; Q6PKG0; -.
PaxDb; Q6PKG0; -.
PeptideAtlas; Q6PKG0; -.
PRIDE; Q6PKG0; -.
ProteomicsDB; 67242; -.
ProteomicsDB; 67243; -. [Q6PKG0-3]
DNASU; 23367; -.
Ensembl; ENST00000336314; ENSP00000336721; ENSG00000155506. [Q6PKG0-3]
GeneID; 23367; -.
KEGG; hsa:23367; -.
UCSC; uc003lvo.4; human. [Q6PKG0-1]
CTD; 23367; -.
DisGeNET; 23367; -.
EuPathDB; HostDB:ENSG00000155506.16; -.
GeneCards; LARP1; -.
HGNC; HGNC:29531; LARP1.
HPA; CAB015222; -.
HPA; HPA051397; -.
HPA; HPA054819; -.
MIM; 612059; gene.
neXtProt; NX_Q6PKG0; -.
OpenTargets; ENSG00000155506; -.
PharmGKB; PA142671564; -.
eggNOG; KOG2590; Eukaryota.
eggNOG; COG5193; LUCA.
GeneTree; ENSGT00940000159577; -.
HOGENOM; HOG000113283; -.
HOVERGEN; HBG054322; -.
InParanoid; Q6PKG0; -.
KO; K18757; -.
OMA; RAKMSSE; -.
OrthoDB; EOG091G02X0; -.
PhylomeDB; Q6PKG0; -.
TreeFam; TF314516; -.
ChiTaRS; LARP1; human.
GeneWiki; LARP1; -.
GenomeRNAi; 23367; -.
PMAP-CutDB; Q6PKG0; -.
PRO; PR:Q6PKG0; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000155506; Expressed in 251 organ(s), highest expression level in female gonad.
CleanEx; HS_LARP1; -.
ExpressionAtlas; Q6PKG0; baseline and differential.
Genevisible; Q6PKG0; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
GO; GO:0008190; F:eukaryotic initiation factor 4E binding; IPI:UniProtKB.
GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0000339; F:RNA cap binding; IDA:UniProtKB.
GO; GO:0008494; F:translation activator activity; IMP:UniProtKB.
GO; GO:0031369; F:translation initiation factor binding; IDA:UniProtKB.
GO; GO:0008283; P:cell proliferation; IMP:UniProtKB.
GO; GO:0072752; P:cellular response to rapamycin; IMP:UniProtKB.
GO; GO:0048255; P:mRNA stabilization; IMP:UniProtKB.
GO; GO:0017148; P:negative regulation of translation; IMP:UniProtKB.
GO; GO:0016239; P:positive regulation of macroautophagy; IMP:BHF-UCL.
GO; GO:0045070; P:positive regulation of viral genome replication; IMP:UniProtKB.
GO; GO:1990928; P:response to amino acid starvation; IMP:UniProtKB.
GO; GO:0031929; P:TOR signaling; IMP:UniProtKB.
GO; GO:0038202; P:TORC1 signaling; IMP:UniProtKB.
GO; GO:0006413; P:translational initiation; IMP:UniProtKB.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR006607; DM15.
InterPro; IPR006630; La_HTH.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF05383; La; 1.
SMART; SM00684; DM15; 3.
SMART; SM00715; LA; 1.
SUPFAM; SSF46785; SSF46785; 1.
PROSITE; PS50961; HTH_LA; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; Isopeptide bond; Methylation;
Phosphoprotein; Protein biosynthesis; Reference proteome; Repressor;
RNA-binding; Translation regulation; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.3}.
CHAIN 2 1096 La-related protein 1.
/FTId=PRO_0000207609.
DOMAIN 397 487 HTH La-type RNA-binding.
{ECO:0000255|PROSITE-ProRule:PRU00332}.
REGION 873 1023 Interaction with mRNA.
{ECO:0000269|PubMed:26206669}.
COMPBIAS 1044 1050 Poly-Gly.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.3}.
MOD_RES 75 75 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:24275569}.
MOD_RES 90 90 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:17693683,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 143 143 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 165 165 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 215 215 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 220 220 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 223 223 Phosphothreonine.
{ECO:0000250|UniProtKB:Q6ZQ58}.
MOD_RES 225 225 Phosphoserine.
{ECO:0000250|UniProtKB:Q6ZQ58}.
MOD_RES 228 228 Phosphoserine.
{ECO:0000250|UniProtKB:Q6ZQ58}.
MOD_RES 240 240 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q6ZQ58}.
MOD_RES 324 324 Phosphoserine.
{ECO:0000250|UniProtKB:Q6ZQ58}.
MOD_RES 327 327 Phosphoserine.
{ECO:0000250|UniProtKB:Q6ZQ58}.
MOD_RES 376 376 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 517 517 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 521 521 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 526 526 Phosphothreonine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|Ref.3}.
MOD_RES 548 548 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 591 591 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 627 627 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 631 631 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 649 649 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 724 724 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 766 766 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 774 774 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|Ref.3}.
MOD_RES 777 777 Phosphotyrosine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 785 785 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 788 788 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 824 824 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 845 845 Phosphothreonine.
{ECO:0000244|PubMed:16964243}.
MOD_RES 851 851 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 853 853 Phosphoserine.
{ECO:0000250|UniProtKB:Q6ZQ58}.
MOD_RES 865 865 Phosphothreonine.
{ECO:0000250|UniProtKB:Q6ZQ58}.
MOD_RES 868 868 Phosphoserine.
{ECO:0000250|UniProtKB:Q6ZQ58}.
MOD_RES 892 892 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1017 1017 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1040 1040 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1089 1089 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 260 260 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 311 311 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 531 531 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 703 703 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 77 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_015114.
VAR_SEQ 78 144 PLQLPGAEGPAISDGEEGGGEPGAGGGAAGAAGAGRRDFVE
APPPKVNPWTKNALPPVLTTVNGQSP -> MLWRVLLSKRP
PFPHPELDFQEAPIPSCPGRLPGRKNSVALAAAPRKEPTGD
REKPLPFPVLAPFSN (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_015115.
MUTAGEN 917 917 R->E: Abolishes RNA binding.
{ECO:0000269|PubMed:26206669}.
MUTAGEN 960 960 Y->A: Abolishes RNA binding.
{ECO:0000269|PubMed:26206669}.
CONFLICT 778 780 RNT -> TRP (in Ref. 1; AAH33856).
{ECO:0000305}.
CONFLICT 979 979 V -> L (in Ref. 5; CAB61364).
{ECO:0000305}.
HELIX 875 880 {ECO:0000244|PDB:5V87}.
TURN 882 884 {ECO:0000244|PDB:5V4R}.
HELIX 887 904 {ECO:0000244|PDB:5V87}.
HELIX 910 925 {ECO:0000244|PDB:5V87}.
HELIX 929 945 {ECO:0000244|PDB:5V87}.
HELIX 949 964 {ECO:0000244|PDB:5V87}.
HELIX 968 983 {ECO:0000244|PDB:5V87}.
HELIX 988 999 {ECO:0000244|PDB:5V87}.
HELIX 1001 1004 {ECO:0000244|PDB:5C0V}.
HELIX 1009 1017 {ECO:0000244|PDB:5V87}.
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


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