LARP4_HUMAN
ID LARP4_HUMAN Reviewed; 724 AA.
AC Q71RC2; A8K6T1; E9PDG5; G3XAA8; G5E976; Q5CZ97; Q6ZV14; Q96NF9;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=La-related protein 4;
DE AltName: Full=La ribonucleoprotein domain family member 4;
GN Name=LARP4; ORFNames=PP13296;
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] (ISOFORMS 1 AND 2), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 10-724 (ISOFORM 4).
RC TISSUE=Placenta, and Tongue;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT THR-502.
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC TISSUE=Bone marrow, and Cervix;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [6]
RP PROTEIN SEQUENCE OF 1-11; 166-178; 205-216 AND 494-503, ACETYLATION AT
RP MET-1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E.;
RL Submitted (JUL-2007) to UniProtKB.
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-722, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
RP IDENTIFICATION BY 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392; SER-583 AND SER-722, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-583 AND SER-722, AND
RP 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 [15]
RP FUNCTION.
RX PubMed=21834987; DOI=10.1186/1741-7007-9-54;
RA Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V.,
RA Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.;
RT "Identification and characterization of a set of conserved and new
RT regulators of cytoskeletal organisation, cell morphology and migration.";
RL BMC Biol. 9:54-54(2011).
RN [16]
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-583; SER-647 AND THR-649, AND
RP 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392; SER-505; SER-583;
RP SER-597 AND SER-722, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-578; THR-579 AND SER-722, AND
RP IDENTIFICATION BY 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 [20]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-368 AND ARG-686, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [21]
RP FUNCTION, AND SUBCELLULAR LOCATIONINTERACTION WITH PABPC1.
RX PubMed=27615744; DOI=10.1002/cm.21336;
RA Seetharaman S., Flemyng E., Shen J., Conte M.R., Ridley A.J.;
RT "The RNA-binding protein LARP4 regulates cancer cell migration and
RT invasion.";
RL Cytoskeleton 73:680-690(2016).
RN [22]
RP STRUCTURE BY NMR OF 112-199.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the La domain of c-mpl binding protein.";
RL Submitted (NOV-2005) to the PDB data bank.
RN [23]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 13-26 IN COMPLEX WITH PABPC1,
RP INTERACTION WITH PABPC1 AND RACK1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP LEU-15 AND TRP-22.
RX PubMed=21098120; DOI=10.1128/mcb.01162-10;
RA Yang R., Gaidamakov S.A., Xie J., Lee J., Martino L., Kozlov G.,
RA Crawford A.K., Russo A.N., Conte M.R., Gehring K., Maraia R.J.;
RT "La-related protein 4 binds poly(A), interacts with the poly(A)-binding
RT protein MLLE domain via a variant PAM2w motif, and can promote mRNA
RT stability.";
RL Mol. Cell. Biol. 31:542-556(2011).
CC -!- FUNCTION: RNA binding protein that binds to the poly-A tract of mRNA
CC molecules (PubMed:21098120). Associates with the 40S ribosomal subunit
CC and with polysomes (PubMed:21098120). Plays a role in the regulation of
CC mRNA translation (PubMed:21098120). Plays a role in the regulation of
CC cell morphology and cytoskeletal organization (PubMed:21834987,
CC PubMed:27615744). {ECO:0000269|PubMed:21098120,
CC ECO:0000269|PubMed:21834987, ECO:0000269|PubMed:27615744}.
CC -!- SUBUNIT: Interacts (via N-terminal region) with PABPC1
CC (PubMed:27615744, PubMed:21098120). Interacts with RACK1
CC (PubMed:21098120). {ECO:0000269|PubMed:21098120,
CC ECO:0000269|PubMed:27615744}.
CC -!- INTERACTION:
CC Q71RC2; Q5S007: LRRK2; NbExp=3; IntAct=EBI-2878091, EBI-5323863;
CC Q71RC2; P06748: NPM1; NbExp=2; IntAct=EBI-2878091, EBI-78579;
CC Q71RC2-6; O14503: BHLHE40; NbExp=3; IntAct=EBI-10255841, EBI-711810;
CC Q71RC2-6; O43186: CRX; NbExp=3; IntAct=EBI-10255841, EBI-748171;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, Stress granule
CC {ECO:0000269|PubMed:21098120}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:21098120, ECO:0000269|PubMed:27615744}.
CC Note=Localized throughout the cytosol. Partially localized in stress
CC granules in response to arsenite treatment.
CC {ECO:0000269|PubMed:21098120}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q71RC2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q71RC2-2; Sequence=VSP_033811, VSP_014611, VSP_014612;
CC Name=3;
CC IsoId=Q71RC2-3; Sequence=VSP_033811;
CC Name=4;
CC IsoId=Q71RC2-4; Sequence=VSP_033812;
CC Name=5;
CC IsoId=Q71RC2-5; Sequence=VSP_045677;
CC Name=6;
CC IsoId=Q71RC2-6; Sequence=VSP_046780;
CC Name=7;
CC IsoId=Q71RC2-7; Sequence=VSP_046781;
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC86052.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK055521; BAB70940.1; -; mRNA.
DR EMBL; AK125113; BAC86052.1; ALT_INIT; mRNA.
DR EMBL; AK291746; BAF84435.1; -; mRNA.
DR EMBL; AF370416; AAQ15252.1; -; mRNA.
DR EMBL; BX647457; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CR936626; CAI56769.1; -; mRNA.
DR EMBL; AC090058; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471111; EAW58146.1; -; Genomic_DNA.
DR EMBL; CH471111; EAW58148.1; -; Genomic_DNA.
DR CCDS; CCDS41782.1; -. [Q71RC2-1]
DR CCDS; CCDS44879.2; -. [Q71RC2-3]
DR CCDS; CCDS44880.1; -. [Q71RC2-5]
DR CCDS; CCDS53789.1; -. [Q71RC2-7]
DR CCDS; CCDS53790.1; -. [Q71RC2-6]
DR CCDS; CCDS81690.1; -. [Q71RC2-4]
DR RefSeq; NP_001164279.1; NM_001170808.1. [Q71RC2-6]
DR RefSeq; NP_001317344.1; NM_001330415.1. [Q71RC2-4]
DR RefSeq; NP_443111.4; NM_052879.4. [Q71RC2-1]
DR RefSeq; NP_954658.2; NM_199188.2. [Q71RC2-3]
DR RefSeq; NP_954660.1; NM_199190.2. [Q71RC2-5]
DR RefSeq; XP_005268670.1; XM_005268613.2.
DR RefSeq; XP_011536140.1; XM_011537838.2.
DR RefSeq; XP_011536141.1; XM_011537839.2.
DR RefSeq; XP_011536142.1; XM_011537840.2.
DR RefSeq; XP_011536143.1; XM_011537841.2.
DR RefSeq; XP_016874240.1; XM_017018751.1.
DR RefSeq; XP_016874241.1; XM_017018752.1.
DR RefSeq; XP_016874242.1; XM_017018753.1.
DR RefSeq; XP_016874243.1; XM_017018754.1.
DR PDB; 2CQK; NMR; -; A=113-200.
DR PDB; 3PKN; X-ray; 1.80 A; B=13-26.
DR PDB; 6I9B; NMR; -; A=111-287.
DR PDBsum; 2CQK; -.
DR PDBsum; 3PKN; -.
DR PDBsum; 6I9B; -.
DR AlphaFoldDB; Q71RC2; -.
DR SMR; Q71RC2; -.
DR BioGRID; 125238; 161.
DR ELM; Q71RC2; -.
DR IntAct; Q71RC2; 38.
DR MINT; Q71RC2; -.
DR STRING; 9606.ENSP00000381490; -.
DR GlyGen; Q71RC2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q71RC2; -.
DR MetOSite; Q71RC2; -.
DR PhosphoSitePlus; Q71RC2; -.
DR BioMuta; LARP4; -.
DR DMDM; 189047131; -.
DR EPD; Q71RC2; -.
DR jPOST; Q71RC2; -.
DR MassIVE; Q71RC2; -.
DR MaxQB; Q71RC2; -.
DR PaxDb; Q71RC2; -.
DR PeptideAtlas; Q71RC2; -.
DR PRIDE; Q71RC2; -.
DR ProteomicsDB; 19660; -.
DR ProteomicsDB; 33696; -.
DR ProteomicsDB; 33856; -.
DR ProteomicsDB; 68610; -. [Q71RC2-1]
DR ProteomicsDB; 68611; -. [Q71RC2-2]
DR ProteomicsDB; 68612; -. [Q71RC2-3]
DR ProteomicsDB; 68613; -. [Q71RC2-4]
DR Antibodypedia; 26215; 160 antibodies from 24 providers.
DR DNASU; 113251; -.
DR Ensembl; ENST00000293618.12; ENSP00000293618.8; ENSG00000161813.23. [Q71RC2-6]
DR Ensembl; ENST00000347328.9; ENSP00000340901.5; ENSG00000161813.23. [Q71RC2-5]
DR Ensembl; ENST00000398473.7; ENSP00000381490.2; ENSG00000161813.23. [Q71RC2-1]
DR Ensembl; ENST00000429001.7; ENSP00000415464.3; ENSG00000161813.23. [Q71RC2-4]
DR Ensembl; ENST00000518444.5; ENSP00000429077.1; ENSG00000161813.23. [Q71RC2-3]
DR Ensembl; ENST00000522085.5; ENSP00000429781.1; ENSG00000161813.23. [Q71RC2-7]
DR GeneID; 113251; -.
DR KEGG; hsa:113251; -.
DR MANE-Select; ENST00000398473.7; ENSP00000381490.2; NM_052879.5; NP_443111.4.
DR UCSC; uc001rwm.4; human. [Q71RC2-1]
DR CTD; 113251; -.
DR DisGeNET; 113251; -.
DR GeneCards; LARP4; -.
DR HGNC; HGNC:24320; LARP4.
DR HPA; ENSG00000161813; Low tissue specificity.
DR MIM; 618657; gene.
DR neXtProt; NX_Q71RC2; -.
DR OpenTargets; ENSG00000161813; -.
DR PharmGKB; PA142671566; -.
DR VEuPathDB; HostDB:ENSG00000161813; -.
DR eggNOG; KOG2590; Eukaryota.
DR eggNOG; KOG2591; Eukaryota.
DR GeneTree; ENSGT00940000154409; -.
DR HOGENOM; CLU_025110_0_0_1; -.
DR InParanoid; Q71RC2; -.
DR OMA; SYKTNVA; -.
DR OrthoDB; 263288at2759; -.
DR PhylomeDB; Q71RC2; -.
DR TreeFam; TF321960; -.
DR PathwayCommons; Q71RC2; -.
DR SignaLink; Q71RC2; -.
DR BioGRID-ORCS; 113251; 65 hits in 1043 CRISPR screens.
DR ChiTaRS; LARP4; human.
DR EvolutionaryTrace; Q71RC2; -.
DR GeneWiki; LARP4; -.
DR GenomeRNAi; 113251; -.
DR Pharos; Q71RC2; Tbio.
DR PRO; PR:Q71RC2; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q71RC2; protein.
DR Bgee; ENSG00000161813; Expressed in secondary oocyte and 208 other tissues.
DR ExpressionAtlas; Q71RC2; baseline and differential.
DR Genevisible; Q71RC2; HS.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:FlyBase.
DR GO; GO:0008143; F:poly(A) binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; IMP:UniProtKB.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IDA:FlyBase.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IMP:UniProtKB.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR CDD; cd12707; RRM_LARP4; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR IDEAL; IID00571; -.
DR InterPro; IPR045180; La_dom_prot.
DR InterPro; IPR006630; La_HTH.
DR InterPro; IPR034903; LARP4_RRM.
DR InterPro; IPR035979; RBD_domain_sf.
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; SM00715; LA; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50961; HTH_LA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Methylation; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; RNA-binding.
FT CHAIN 1..724
FT /note="La-related protein 4"
FT /id="PRO_0000207611"
FT DOMAIN 113..202
FT /note="HTH La-type RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00332"
FT DOMAIN 203..281
FT /note="RRM"
FT REGION 13..22
FT /note="Interaction with PABPC1"
FT /evidence="ECO:0000269|PubMed:21098120"
FT REGION 111..303
FT /note="Interaction with the poly-A tract of mRNA"
FT /evidence="ECO:0000269|PubMed:21098120"
FT REGION 374..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..674
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330"
FT MOD_RES 368
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 578
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 579
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 583
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 597
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 649
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 686
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 722
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT VAR_SEQ 7
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15498874"
FT /id="VSP_033811"
FT VAR_SEQ 55
FT /note="E -> EVSVFNT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_033812"
FT VAR_SEQ 97..194
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014611"
FT VAR_SEQ 269..339
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_045677"
FT VAR_SEQ 374..444
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_046780"
FT VAR_SEQ 446..724
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_046781"
FT VAR_SEQ 593..612
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014612"
FT VARIANT 351
FT /note="F -> L (in dbSNP:rs17124706)"
FT /id="VAR_055936"
FT VARIANT 502
FT /note="N -> T (in dbSNP:rs17124715)"
FT /evidence="ECO:0000269|PubMed:15498874"
FT /id="VAR_055937"
FT MUTAGEN 15
FT /note="L->A: Nearly abolishes interaction with PABPC1; when
FT associated with A-22."
FT /evidence="ECO:0000269|PubMed:21098120"
FT MUTAGEN 22
FT /note="W->A: Nearly abolishes interaction with PABPC1; when
FT associated with A-15."
FT /evidence="ECO:0000269|PubMed:21098120"
FT CONFLICT 422
FT /note="E -> G (in Ref. 3; BX647457)"
FT /evidence="ECO:0000305"
FT CONFLICT 529
FT /note="D -> G (in Ref. 3; BX647457)"
FT /evidence="ECO:0000305"
FT CONFLICT 639
FT /note="R -> Q (in Ref. 1; BAF84435)"
FT /evidence="ECO:0000305"
FT HELIX 116..130
FT /evidence="ECO:0007829|PDB:2CQK"
FT HELIX 133..138
FT /evidence="ECO:0007829|PDB:2CQK"
FT HELIX 140..145
FT /evidence="ECO:0007829|PDB:2CQK"
FT HELIX 154..159
FT /evidence="ECO:0007829|PDB:2CQK"
FT HELIX 161..166
FT /evidence="ECO:0007829|PDB:2CQK"
FT HELIX 170..179
FT /evidence="ECO:0007829|PDB:2CQK"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:2CQK"
FT STRAND 187..194
FT /evidence="ECO:0007829|PDB:2CQK"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:6I9B"
FT HELIX 212..219
FT /evidence="ECO:0007829|PDB:6I9B"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:6I9B"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:6I9B"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:6I9B"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:6I9B"
FT HELIX 245..258
FT /evidence="ECO:0007829|PDB:6I9B"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:6I9B"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:6I9B"
SQ SEQUENCE 724 AA; 80596 MW; 93B8C2D8CB3CDAEF CRC64;
MLLFVEQVAS KGTGLNPNAK VWQEIAPGNT DATPVTHGTE SSWHEIAATS GAHPEGNAEL
SEDICKEYEV MYSSSCETTR NTTGIEESTD GMILGPEDLS YQIYDVSGES NSAVSTEDLK
ECLKKQLEFC FSRENLSKDL YLISQMDSDQ FIPIWTVANM EEIKKLTTDP DLILEVLRSS
PMVQVDEKGE KVRPSHKRCI VILREIPETT PIEEVKGLFK SENCPKVISC EFAHNSNWYI
TFQSDTDAQQ AFKYLREEVK TFQGKPIMAR IKAINTFFAK NGYRLMDSSI YSHPIQTQAQ
YASPVFMQPV YNPHQQYSVY SIVPQSWSPN PTPYFETPLA PFPNGSFVNG FNSPGSYKTN
AAAMNMGRPF QKNRVKPQFR SSGGSEHSTE GSVSLGDGQL NRYSSRNFPA ERHNPTVTGH
QEQTYLQKET STLQVEQNGD YGRGRRTLFR GRRRREDDRI SRPHPSTAES KAPTPKFDLL
ASNFPPLPGS SSRMPGELVL ENRMSDVVKG VYKEKDNEEL TISCPVPADE QTECTSAQQL
NMSTSSPCAA ELTALSTTQQ EKDLIEDSSV QKDGLNQTTI PVSPPSTTKP SRASTASPCN
NNINAATAVA LQEPRKLSYA EVCQKPPKEP SSVLVQPLRE LRSNVVSPTK NEDNGAPENS
VEKPHEKPEA RASKDYSGFR GNIIPRGAAG KIREQRRQFS HRAIPQGVTR RNGKEQYVPP
RSPK
