LAR4B_HUMAN
ID LAR4B_HUMAN Reviewed; 738 AA.
AC Q92615; A7MD20; Q5T3R3; Q5T3R4; Q5T3R5; Q68CY4;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 3.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=La-related protein 4B;
DE AltName: Full=La ribonucleoprotein domain family member 4B;
DE AltName: Full=La ribonucleoprotein domain family member 5;
DE AltName: Full=La-related protein 5;
GN Name=LARP4B; Synonyms=KIAA0217, LARP5;
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].
RC TISSUE=Brain;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI. The
RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Trachea;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 495-738.
RC TISSUE=Fetal kidney;
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434 AND THR-566, AND
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 [9]
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 [10]
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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-424; SER-434; SER-451;
RP SER-524; SER-727 AND SER-736, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [13]
RP IDENTIFICATION BY MASS 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-424; THR-518 AND SER-524, AND
RP IDENTIFICATION BY 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 [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-724, AND IDENTIFICATION BY MASS
RP 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 [16]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PABPC1 AND RACK1.
RX PubMed=20573744; DOI=10.1261/rna.2146910;
RA Schaffler K., Schulz K., Hirmer A., Wiesner J., Grimm M., Sickmann A.,
RA Fischer U.;
RT "A stimulatory role for the La-related protein 4B in translation.";
RL RNA 16:1488-1499(2010).
RN [17]
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 [18]
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 [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451; SER-488; SER-524;
RP SER-556; SER-568; SER-601; SER-664 AND SER-718, 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-601, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [22]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-404 AND ARG-419, 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 [23] {ECO:0007744|PDB:3PTH}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 55-69 IN COMPLEX WITH PABPC1.
RA Grimm C., Pelz J.P.;
RT "LARP4B binds to the PABC1 MLLE domain via a variant PAM2 motif.";
RL Submitted (DEC-2010) to the PDB data bank.
CC -!- FUNCTION: Stimulates mRNA translation. {ECO:0000269|PubMed:20573744}.
CC -!- SUBUNIT: Interacts with PABPC1 (PubMed:20573744, Ref.23). Interacts
CC with RACK1 (PubMed:20573744). Associates with polysomes via the 40S
CC ribosomal subunit (PubMed:20573744). {ECO:0000269|PubMed:20573744,
CC ECO:0000269|Ref.23}.
CC -!- INTERACTION:
CC Q92615; P0C7T5: ATXN1L; NbExp=3; IntAct=EBI-1052558, EBI-8624731;
CC Q92615; Q9Y5Z0: BACE2; NbExp=3; IntAct=EBI-1052558, EBI-11282723;
CC Q92615; P46379-2: BAG6; NbExp=3; IntAct=EBI-1052558, EBI-10988864;
CC Q92615; P02489: CRYAA; NbExp=3; IntAct=EBI-1052558, EBI-6875961;
CC Q92615; Q01658: DR1; NbExp=3; IntAct=EBI-1052558, EBI-750300;
CC Q92615; P41091: EIF2S3; NbExp=3; IntAct=EBI-1052558, EBI-1054228;
CC Q92615; O75460-2: ERN1; NbExp=3; IntAct=EBI-1052558, EBI-25852368;
CC Q92615; Q9Y624: F11R; NbExp=3; IntAct=EBI-1052558, EBI-742600;
CC Q92615; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-1052558, EBI-10226858;
CC Q92615; Q9Y5Q9: GTF3C3; NbExp=3; IntAct=EBI-1052558, EBI-1054873;
CC Q92615; P54652: HSPA2; NbExp=3; IntAct=EBI-1052558, EBI-356991;
CC Q92615; P42858: HTT; NbExp=3; IntAct=EBI-1052558, EBI-466029;
CC Q92615; O14901: KLF11; NbExp=3; IntAct=EBI-1052558, EBI-948266;
CC Q92615; Q92876: KLK6; NbExp=3; IntAct=EBI-1052558, EBI-2432309;
CC Q92615; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-1052558, EBI-716006;
CC Q92615; P28331-2: NDUFS1; NbExp=3; IntAct=EBI-1052558, EBI-6190702;
CC Q92615; Q8N2W9: PIAS4; NbExp=3; IntAct=EBI-1052558, EBI-473160;
CC Q92615; P63244: RACK1; NbExp=5; IntAct=EBI-1052558, EBI-296739;
CC Q92615; P49591: SARS1; NbExp=3; IntAct=EBI-1052558, EBI-1053431;
CC Q92615; P14927: UQCRB; NbExp=3; IntAct=EBI-1052558, EBI-743128;
CC Q92615; E9KL35; NbExp=3; IntAct=EBI-1052558, EBI-8456500;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:20573744}.
CC Note=Localized in cytoplasmic mRNP granules containing untranslated
CC mRNAs in response to arsenite treatment. {ECO:0000269|PubMed:20573744}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13207.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D86971; BAA13207.2; ALT_INIT; mRNA.
DR EMBL; AK292946; BAF85635.1; -; mRNA.
DR EMBL; AL359878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL157709; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471072; EAW86530.1; -; Genomic_DNA.
DR EMBL; BC131630; AAI31631.1; -; mRNA.
DR EMBL; BC152443; AAI52444.1; -; mRNA.
DR EMBL; CR749653; CAH18446.1; -; mRNA.
DR CCDS; CCDS31131.1; -.
DR RefSeq; NP_055970.1; NM_015155.2.
DR PDB; 3PTH; X-ray; 1.70 A; B=55-69.
DR PDBsum; 3PTH; -.
DR AlphaFoldDB; Q92615; -.
DR SMR; Q92615; -.
DR BioGRID; 116795; 217.
DR ELM; Q92615; -.
DR IntAct; Q92615; 69.
DR MINT; Q92615; -.
DR STRING; 9606.ENSP00000482767; -.
DR GlyGen; Q92615; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; Q92615; -.
DR PhosphoSitePlus; Q92615; -.
DR BioMuta; LARP4B; -.
DR DMDM; 134034150; -.
DR EPD; Q92615; -.
DR jPOST; Q92615; -.
DR MassIVE; Q92615; -.
DR MaxQB; Q92615; -.
DR PaxDb; Q92615; -.
DR PeptideAtlas; Q92615; -.
DR PRIDE; Q92615; -.
DR ProteomicsDB; 75363; -.
DR Antibodypedia; 52530; 50 antibodies from 15 providers.
DR DNASU; 23185; -.
DR Ensembl; ENST00000316157.8; ENSP00000326128.3; ENSG00000107929.16.
DR GeneID; 23185; -.
DR KEGG; hsa:23185; -.
DR MANE-Select; ENST00000316157.8; ENSP00000326128.3; NM_015155.3; NP_055970.1.
DR UCSC; uc031ptb.1; human.
DR CTD; 23185; -.
DR DisGeNET; 23185; -.
DR GeneCards; LARP4B; -.
DR HGNC; HGNC:28987; LARP4B.
DR HPA; ENSG00000107929; Low tissue specificity.
DR MIM; 616513; gene.
DR neXtProt; NX_Q92615; -.
DR OpenTargets; ENSG00000107929; -.
DR PharmGKB; PA165548762; -.
DR VEuPathDB; HostDB:ENSG00000107929; -.
DR eggNOG; KOG2591; Eukaryota.
DR GeneTree; ENSGT00940000157755; -.
DR HOGENOM; CLU_025110_0_0_1; -.
DR InParanoid; Q92615; -.
DR OMA; LEFCLSX; -.
DR OrthoDB; 263288at2759; -.
DR PhylomeDB; Q92615; -.
DR TreeFam; TF321960; -.
DR PathwayCommons; Q92615; -.
DR SignaLink; Q92615; -.
DR SIGNOR; Q92615; -.
DR BioGRID-ORCS; 23185; 19 hits in 1087 CRISPR screens.
DR ChiTaRS; LARP4B; human.
DR GenomeRNAi; 23185; -.
DR Pharos; Q92615; Tbio.
DR PRO; PR:Q92615; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q92615; protein.
DR Bgee; ENSG00000107929; Expressed in apex of heart and 195 other tissues.
DR ExpressionAtlas; Q92615; baseline and differential.
DR Genevisible; Q92615; HS.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0042788; C:polysomal ribosome; IDA:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:FlyBase.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:1905870; P:positive regulation of 3'-UTR-mediated mRNA stabilization; IMP:FlyBase.
DR GO; GO:0045727; P:positive regulation of translation; IMP:UniProtKB.
DR CDD; cd12706; RRM_LARP5; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR045180; La_dom_prot.
DR InterPro; IPR006630; La_HTH.
DR InterPro; IPR034900; LARP5_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
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; Cytoplasm; Methylation; Phosphoprotein;
KW Reference proteome; RNA-binding; Translation regulation.
FT CHAIN 1..738
FT /note="La-related protein 4B"
FT /id="PRO_0000281139"
FT DOMAIN 150..239
FT /note="HTH La-type RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00332"
FT DOMAIN 240..307
FT /note="RRM"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..621
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..695
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..738
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6A0A2"
FT MOD_RES 404
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 419
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 493
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q6A0A2"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6A0A2"
FT MOD_RES 518
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 556
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 566
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243"
FT MOD_RES 568
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 601
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 718
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 724
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 727
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 732
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6A0A2"
FT MOD_RES 736
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
SQ SEQUENCE 738 AA; 80552 MW; A0E5D44ECA58265D CRC64;
MTSDQDAKVV AEPQTQRVQE GKDSAHLMNG PISQTTSQTS SIPPLSQVPA TKVSELNPNA
EVWGAPVLHL EASSAADGVS AAWEEVAGHH ADRGPQGSDA NGDGDQGHEN AALPDPQESD
PADMNALALG PSEYDSLPEN SETGGNESQP DSQEDPREVL KKTLEFCLSR ENLASDMYLI
SQMDSDQYVP ITTVANLDHI KKLSTDVDLI VEVLRSLPLV QVDEKGEKVR PNQNRCIVIL
REISESTPVE EVEALFKGDN LPKFINCEFA YNDNWFITFE TEADAQQAYK YLREEVKTFQ
GKPIKARIKA KAIAINTFLP KNGFRPLDVS LYAQQRYATS FYFPPMYSPQ QQFPLYSLIT
PQTWSATHSY LDPPLVTPFP NTGFINGFTS PAFKPAASPL TSLRQYPPRS RNPSKSHLRH
AIPSAERGPG LLESPSIFNF TADRLINGVR SPQTRQAGQT RTRIQNPSAY AKREAGPGRV
EPGSLESSPG LGRGRKNSFG YRKKREEKFT SSQTQSPTPP KPPSPSFELG LSSFPPLPGA
AGNLKTEDLF ENRLSSLIIG PSKERTLSAD ASVNTLPVVV SREPSVPASC AVSATYERSP
SPAHLPDDPK VAEKQRETHS VDRLPSALTA TACKSVQVNG AATELRKPSY AEICQRTSKE
PPSSPLQPQK EQKPNTVGCG KEEKKLAEPA ERYREPPALK STPGAPRDQR RPAGGRPSPS
AMGKRLSREQ STPPKSPQ
