GenomeNet

Database: UniProt
Entry: Q15717
LinkDB: Q15717
Original site: Q15717 
ID   ELAV1_HUMAN             Reviewed;         326 AA.
AC   Q15717; B4DVB8; Q53XN6; Q9BTT1;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2002, sequence version 2.
DT   10-FEB-2021, entry version 209.
DE   RecName: Full=ELAV-like protein 1;
DE   AltName: Full=Hu-antigen R;
DE            Short=HuR {ECO:0000303|PubMed:8626503};
GN   Name=ELAVL1; Synonyms=HUR;
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 [MRNA] (ISOFORM 1), FUNCTION, RNA-BINDING, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=8626503; DOI=10.1074/jbc.271.14.8144;
RA   Ma W.-J., Cheng S., Campbell C., Wright A., Furneaux H.M.;
RT   "Cloning and characterization of HuR, a ubiquitously expressed Elav-like
RT   protein.";
RL   J. Biol. Chem. 271:8144-8151(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Small intestine;
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=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Cervix;
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   INTERACTION WITH ANP32A.
RX   PubMed=11729309; DOI=10.1126/science.1064693;
RA   Gallouzi I.-E., Steitz J.A.;
RT   "Delineation of mRNA export pathways by the use of cell-permeable
RT   peptides.";
RL   Science 294:1895-1901(2001).
RN   [8]
RP   METHYLATION AT ARG-217.
RX   PubMed=12237300; DOI=10.1074/jbc.m206187200;
RA   Li H., Park S., Kilburn B., Jelinek M.A., Henschen-Edman A., Aswad D.W.,
RA   Stallcup M.R., Laird-Offringa I.A.;
RT   "Lipopolysaccharide-induced methylation of HuR, an mRNA-stabilizing
RT   protein, by CARM1. Coactivator-associated arginine methyltransferase.";
RL   J. Biol. Chem. 277:44623-44630(2002).
RN   [9]
RP   FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, AND PHOSPHORYLATION BY
RP   MAPKAPK2.
RX   PubMed=14517288; DOI=10.1128/mcb.23.20.7177-7188.2003;
RA   Tran H., Maurer F., Nagamine Y.;
RT   "Stabilization of urokinase and urokinase receptor mRNAs by HuR is linked
RT   to its cytoplasmic accumulation induced by activated mitogen-activated
RT   protein kinase-activated protein kinase 2.";
RL   Mol. Cell. Biol. 23:7177-7188(2003).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Lymphoblast;
RX   PubMed=14654843; DOI=10.1038/nature02166;
RA   Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT   "Proteomic characterization of the human centrosome by protein correlation
RT   profiling.";
RL   Nature 426:570-574(2003).
RN   [11]
RP   INTERACTION WITH DHX36 AND ILF3, AND RNA-BINDING.
RX   PubMed=14731398; DOI=10.1016/s1097-2765(03)00481-7;
RA   Tran H., Schilling M., Wirbelauer C., Hess D., Nagamine Y.;
RT   "Facilitation of mRNA deadenylation and decay by the exosome-bound, DExH
RT   protein RHAU.";
RL   Mol. Cell 13:101-111(2004).
RN   [12]
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   [13]
RP   INTERACTION WITH AGO1 AND AGO2.
RX   PubMed=17932509; DOI=10.1038/sj.embor.7401088;
RA   Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M.,
RA   Urlaub H., Meister G.;
RT   "Proteomic and functional analysis of Argonaute-containing mRNA-protein
RT   complexes in human cells.";
RL   EMBO Rep. 8:1052-1060(2007).
RN   [14]
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   [15]
RP   FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=17632515; DOI=10.1038/nchembio.2007.14;
RA   Meisner N.C., Hintersteiner M., Mueller K., Bauer R., Seifert J.M.,
RA   Naegeli H.U., Ottl J., Oberer L., Guenat C., Moss S., Harrer N.,
RA   Woisetschlaeger M., Buehler C., Uhl V., Auer M.;
RT   "Identification and mechanistic characterization of low-molecular-weight
RT   inhibitors for HuR.";
RL   Nat. Chem. Biol. 3:508-515(2007).
RN   [16]
RP   INTERACTION WITH PLEKHN1.
RX   PubMed=18191643; DOI=10.1016/j.bbamcr.2007.12.009;
RA   Sano E., Shono S., Tashiro K., Konishi H., Yamauchi E., Taniguchi H.;
RT   "Novel tyrosine phosphorylated and cardiolipin-binding protein CLPABP
RT   functions as mitochondrial RNA granule.";
RL   Biochim. Biophys. Acta 1783:1036-1047(2008).
RN   [17]
RP   INTERACTION WITH HNRNPL.
RX   PubMed=18161049; DOI=10.1002/hep.22036;
RA   Matsui K., Nishizawa M., Ozaki T., Kimura T., Hashimoto I., Yamada M.,
RA   Kaibori M., Kamiyama Y., Ito S., Okumura T.;
RT   "Natural antisense transcript stabilizes inducible nitric oxide synthase
RT   messenger RNA in rat hepatocytes.";
RL   Hepatology 47:686-697(2008).
RN   [18]
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   [19]
RP   RNA-BINDING, FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-158;
RP   SER-221 AND SER-318, AND MUTAGENESIS OF SER-158; SER-221 AND SER-318.
RX   PubMed=18285462; DOI=10.1128/mcb.01530-07;
RA   Doller A., Akool E.-S., Huwiler A., Mueller R., Radeke H.H.,
RA   Pfeilschifter J., Eberhardt W.;
RT   "Posttranslational modification of the AU-rich element binding protein HuR
RT   by protein kinase Cdelta elicits angiotensin II-induced stabilization and
RT   nuclear export of cyclooxygenase 2 mRNA.";
RL   Mol. Cell. Biol. 28:2608-2625(2008).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, AND IDENTIFICATION BY
RP   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   [21]
RP   RNA-BINDING.
RX   PubMed=19561594; DOI=10.1038/nbt.1550;
RA   Ray D., Kazan H., Chan E.T., Pena Castillo L., Chaudhry S., Talukder S.,
RA   Blencowe B.J., Morris Q., Hughes T.R.;
RT   "Rapid and systematic analysis of the RNA recognition specificities of RNA-
RT   binding proteins.";
RL   Nat. Biotechnol. 27:667-670(2009).
RN   [22]
RP   FUNCTION, IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR LOCATION, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=19029303; DOI=10.1261/rna.1175909;
RA   Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A.,
RA   Buchmeier S., Wahle E., Huettelmaiery S.;
RT   "Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs.";
RL   RNA 15:104-115(2009).
RN   [23]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, 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   [24]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, AND IDENTIFICATION BY
RP   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   [25]
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   [26]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP   ANALYSIS] AT SER-2 AND SER-202, CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP   SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [27]
RP   INTERACTION WITH IGF2BP1; IGF2BP2 AND IGF2BP3.
RX   PubMed=23640942; DOI=10.1515/hsz-2013-0111;
RA   Wachter K., Kohn M., Stohr N., Huttelmaier S.;
RT   "Subcellular localization and RNP formation of IGF2BPs (IGF2 mRNA-binding
RT   proteins) is modulated by distinct RNA-binding domains.";
RL   Biol. Chem. 394:1077-1090(2013).
RN   [28]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100; SER-197 AND SER-202, AND
RP   IDENTIFICATION BY MASS 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   [29]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-217, AND IDENTIFICATION BY MASS
RP   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   [30]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [31]
RP   INTERACTION WITH PLEKHN1.
RX   PubMed=27616329; DOI=10.1016/j.bbalip.2016.09.006;
RA   Nishino T., Matsunaga R., Jikihara H., Uchida M., Maeda A., Qi G., Abe T.,
RA   Kiyonari H., Tashiro S., Inagaki-Ohara K., Shimamoto F., Konishi H.;
RT   "Antagonizing effect of CLPABP on the function of HuR as a regulator of
RT   ARE-containing leptin mRNA stability and the effect of its depletion on
RT   obesity in old male mouse.";
RL   Biochim. Biophys. Acta 1861:1816-1827(2016).
RN   [32]
RP   INTERACTION WITH SHFL.
RX   PubMed=27974568; DOI=10.1128/jvi.01606-16;
RA   Balinsky C.A., Schmeisser H., Wells A.I., Ganesan S., Jin T., Singh K.,
RA   Zoon K.C.;
RT   "IRAV (FLJ11286), an Interferon-Stimulated Gene with Antiviral Activity
RT   against Dengue Virus, Interacts with MOV10.";
RL   J. Virol. 91:0-0(2017).
RN   [33]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-191, AND IDENTIFICATION BY MASS
RP   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   [34]
RP   FUNCTION.
RX   PubMed=29180010; DOI=10.1016/j.bbrc.2017.11.112;
RA   Maeda A., Uchida M., Nishikawa S., Nishino T., Konishi H.;
RT   "Role of N-myristoylation in stability and subcellular localization of the
RT   CLPABP protein.";
RL   Biochem. Biophys. Res. Commun. 495:1249-1256(2018).
RN   [35]
RP   FUNCTION, AND INTERACTION WITH YBX1.
RX   PubMed=31358969; DOI=10.1038/s41556-019-0361-y;
RA   Chen X., Li A., Sun B.F., Yang Y., Han Y.N., Yuan X., Chen R.X., Wei W.S.,
RA   Liu Y., Gao C.C., Chen Y.S., Zhang M., Ma X.D., Liu Z.W., Luo J.H., Lyu C.,
RA   Wang H.L., Ma J., Zhao Y.L., Zhou F.J., Huang Y., Xie D., Yang Y.G.;
RT   "5-methylcytosine promotes pathogenesis of bladder cancer through
RT   stabilizing mRNAs.";
RL   Nat. Cell Biol. 21:978-990(2019).
RN   [36]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 18-99, AND SUBUNIT.
RX   PubMed=20219472; DOI=10.1016/j.jmb.2010.02.043;
RA   Benoit R.M., Meisner N.C., Kallen J., Graff P., Hemmig R., Cebe R.,
RA   Ostermeier C., Widmer H., Auer M.;
RT   "The X-ray crystal structure of the first RNA recognition motif and site-
RT   directed mutagenesis suggest a possible HuR redox sensing mechanism.";
RL   J. Mol. Biol. 397:1231-1244(2010).
RN   [37]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 18-186 OF APOPROTEIN AND IN
RP   COMPLEX WITH RNA, FUNCTION, RNA-BINDING, AND DOMAIN.
RX   PubMed=23519412; DOI=10.1107/s0907444912047828;
RA   Wang H., Zeng F., Liu Q., Liu H., Liu Z., Niu L., Teng M., Li X.;
RT   "The structure of the ARE-binding domains of Hu antigen R (HuR) undergoes
RT   conformational changes during RNA binding.";
RL   Acta Crystallogr. D 69:373-380(2013).
CC   -!- FUNCTION: RNA-binding protein that binds to the 3'-UTR region of mRNAs
CC       and increases their stability (PubMed:14517288, PubMed:18285462,
CC       PubMed:31358969). Involved in embryonic stem cells (ESCs)
CC       differentiation: preferentially binds mRNAs that are not methylated by
CC       N6-methyladenosine (m6A), stabilizing them, promoting ESCs
CC       differentiation (By similarity). Binds to poly-U elements and AU-rich
CC       elements (AREs) in the 3'-UTR of target mRNAs (PubMed:8626503,
CC       PubMed:17632515, PubMed:18285462, PubMed:23519412, PubMed:14731398).
CC       Binds avidly to the AU-rich element in FOS and IL3/interleukin-3 mRNAs.
CC       In the case of the FOS AU-rich element, binds to a core element of 27
CC       nucleotides that contain AUUUA, AUUUUA, and AUUUUUA motifs. Binds
CC       preferentially to the 5'-UUUU[AG]UUU-3' motif in vitro
CC       (PubMed:8626503). With ZNF385A, binds the 3'-UTR of p53/TP53 mRNA to
CC       control their nuclear export induced by CDKN2A. Hence, may regulate
CC       p53/TP53 expression and mediate in part the CDKN2A anti-proliferative
CC       activity. May also bind with ZNF385A the CCNB1 mRNA (By similarity).
CC       Increases the stability of the leptin mRNA harboring an AU-rich element
CC       (ARE) in its 3' UTR (PubMed:29180010). {ECO:0000250|UniProtKB:P70372,
CC       ECO:0000269|PubMed:14517288, ECO:0000269|PubMed:14731398,
CC       ECO:0000269|PubMed:17632515, ECO:0000269|PubMed:18285462,
CC       ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:23519412,
CC       ECO:0000269|PubMed:29180010, ECO:0000269|PubMed:31358969,
CC       ECO:0000269|PubMed:8626503}.
CC   -!- SUBUNIT: Monomer and homodimer (in vitro) (PubMed:17632515,
CC       PubMed:20219472). Interacts with ANP32A (PubMed:11729309). Interacts
CC       with ZNF385A; the interaction is indirect and mRNA-dependent and may
CC       regulate p53/TP53 expression (By similarity). Identified in a mRNP
CC       complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1,
CC       ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1
CC       (PubMed:19029303). Interacts with AGO1 and AGO2 (PubMed:17932509).
CC       Interacts with IGF2BP2 and IGF2BP3 (PubMed:23640942). Interacts with
CC       HNRNPL (PubMed:18161049). Interacts with DHX36; this interaction occurs
CC       in a RNA-dependent manner (PubMed:14731398). Interacts with ILF3; this
CC       interaction occurs in a RNA-dependent manner (PubMed:14731398).
CC       Interacts with PLEKHN1 (PubMed:18191643, PubMed:27616329). Interacts
CC       with SHFL; the interaction increases in presence of RNA
CC       (PubMed:27974568). Interacts with YBX1; interaction recruits ELAVL1 on
CC       C5-methylcytosine (m5C)-containing mRNAs, thereby promoting mRNA
CC       stability (PubMed:31358969). {ECO:0000250|UniProtKB:P70372,
CC       ECO:0000269|PubMed:11729309, ECO:0000269|PubMed:14731398,
CC       ECO:0000269|PubMed:17632515, ECO:0000269|PubMed:17932509,
CC       ECO:0000269|PubMed:18161049, ECO:0000269|PubMed:18191643,
CC       ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:20219472,
CC       ECO:0000269|PubMed:23640942, ECO:0000269|PubMed:27616329,
CC       ECO:0000269|PubMed:27974568}.
CC   -!- INTERACTION:
CC       Q15717; P54253: ATXN1; NbExp=7; IntAct=EBI-374260, EBI-930964;
CC       Q15717; O00560: SDCBP; NbExp=3; IntAct=EBI-374260, EBI-727004;
CC       Q15717; Q13148: TARDBP; NbExp=7; IntAct=EBI-374260, EBI-372899;
CC       Q15717; P0CG48: UBC; NbExp=4; IntAct=EBI-374260, EBI-3390054;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14517288,
CC       ECO:0000269|PubMed:17632515, ECO:0000269|PubMed:18285462,
CC       ECO:0000269|PubMed:19029303}. Nucleus {ECO:0000269|PubMed:14517288,
CC       ECO:0000269|PubMed:17632515, ECO:0000269|PubMed:18285462}. Cytoplasm,
CC       Stress granule {ECO:0000250|UniProtKB:P70372}. Note=Translocates into
CC       the cytoplasm following phosphorylation by MAPKAPK2 (PubMed:14517288).
CC       Likewise, phosphorylation by PRKCD promotes translocation from the
CC       nucleus into the cytoplasm, where it is associated with free and
CC       cytoskeleton-bound polysomes (PubMed:18285462).Localizes to the stress
CC       granules in the presence of PLEKHN1 (By similarity).
CC       {ECO:0000250|UniProtKB:P70372, ECO:0000269|PubMed:14517288,
CC       ECO:0000269|PubMed:18285462}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q15717-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q15717-2; Sequence=VSP_056148;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Detected in brain, liver, thymus and
CC       muscle. {ECO:0000269|PubMed:8626503}.
CC   -!- DOMAIN: The first RRM (RNA recognition motif) domain is essential for
CC       binding to AU-rich elements. {ECO:0000269|PubMed:23519412}.
CC   -!- PTM: Phosphorylated by MAPKAPK2 (PubMed:14517288). Phosphorylated by
CC       PRKCD (PubMed:18285462). {ECO:0000269|PubMed:14517288,
CC       ECO:0000269|PubMed:18285462}.
CC   -!- PTM: Methylated at Arg-217 by CARM1 in macrophages in response to LPS
CC       challenge. {ECO:0000269|PubMed:12237300}.
CC   -!- SIMILARITY: Belongs to the RRM elav family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/ELAVL1ID44237ch19p13.html";
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DR   EMBL; U38175; AAB41913.1; -; mRNA.
DR   EMBL; BT009793; AAP88795.1; -; mRNA.
DR   EMBL; AK301013; BAG62630.1; -; mRNA.
DR   EMBL; AC008975; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC010336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471139; EAW68949.1; -; Genomic_DNA.
DR   EMBL; BC003376; AAH03376.1; -; mRNA.
DR   CCDS; CCDS12193.1; -. [Q15717-1]
DR   RefSeq; NP_001410.2; NM_001419.2. [Q15717-1]
DR   PDB; 3HI9; X-ray; 2.00 A; A/B/C/D=18-99.
DR   PDB; 4ED5; X-ray; 2.00 A; A/B=18-186.
DR   PDB; 4EGL; X-ray; 2.90 A; A=18-186.
DR   PDB; 4FXV; X-ray; 1.90 A; A/B/C/D=20-99.
DR   PDB; 5SZW; NMR; -; A=1-99.
DR   PDB; 6G2K; X-ray; 2.01 A; A/B/C=243-326.
DR   PDB; 6GC5; X-ray; 1.90 A; A/B/C/D=241-326.
DR   PDB; 6GD1; X-ray; 2.01 A; A/B=243-326.
DR   PDB; 6GD2; X-ray; 1.90 A; A/B/C=243-326.
DR   PDB; 6GD3; X-ray; 1.35 A; A/B/C=243-326.
DR   PDBsum; 3HI9; -.
DR   PDBsum; 4ED5; -.
DR   PDBsum; 4EGL; -.
DR   PDBsum; 4FXV; -.
DR   PDBsum; 5SZW; -.
DR   PDBsum; 6G2K; -.
DR   PDBsum; 6GC5; -.
DR   PDBsum; 6GD1; -.
DR   PDBsum; 6GD2; -.
DR   PDBsum; 6GD3; -.
DR   SMR; Q15717; -.
DR   BioGRID; 108309; 1831.
DR   CORUM; Q15717; -.
DR   DIP; DIP-31291N; -.
DR   IntAct; Q15717; 79.
DR   MINT; Q15717; -.
DR   STRING; 9606.ENSP00000385269; -.
DR   BindingDB; Q15717; -.
DR   ChEMBL; CHEMBL1250379; -.
DR   iPTMnet; Q15717; -.
DR   MetOSite; Q15717; -.
DR   PhosphoSitePlus; Q15717; -.
DR   SwissPalm; Q15717; -.
DR   BioMuta; ELAVL1; -.
DR   DMDM; 20981691; -.
DR   CPTAC; CPTAC-923; -.
DR   EPD; Q15717; -.
DR   jPOST; Q15717; -.
DR   MassIVE; Q15717; -.
DR   MaxQB; Q15717; -.
DR   PaxDb; Q15717; -.
DR   PeptideAtlas; Q15717; -.
DR   PRIDE; Q15717; -.
DR   ProteomicsDB; 60716; -. [Q15717-1]
DR   Antibodypedia; 3933; 466 antibodies.
DR   DNASU; 1994; -.
DR   Ensembl; ENST00000407627; ENSP00000385269; ENSG00000066044. [Q15717-1]
DR   Ensembl; ENST00000596459; ENSP00000472197; ENSG00000066044. [Q15717-1]
DR   GeneID; 1994; -.
DR   KEGG; hsa:1994; -.
DR   UCSC; uc002mjb.4; human. [Q15717-1]
DR   CTD; 1994; -.
DR   DisGeNET; 1994; -.
DR   GeneCards; ELAVL1; -.
DR   HGNC; HGNC:3312; ELAVL1.
DR   HPA; ENSG00000066044; Low tissue specificity.
DR   MIM; 603466; gene.
DR   neXtProt; NX_Q15717; -.
DR   OpenTargets; ENSG00000066044; -.
DR   PharmGKB; PA27740; -.
DR   VEuPathDB; HostDB:ENSG00000066044.13; -.
DR   eggNOG; KOG0145; Eukaryota.
DR   GeneTree; ENSGT00940000155528; -.
DR   HOGENOM; CLU_026186_2_2_1; -.
DR   InParanoid; Q15717; -.
DR   OMA; WQKHVTS; -.
DR   OrthoDB; 614259at2759; -.
DR   PhylomeDB; Q15717; -.
DR   TreeFam; TF313377; -.
DR   PathwayCommons; Q15717; -.
DR   Reactome; R-HSA-450520; HuR (ELAVL1) binds and stabilizes mRNA.
DR   Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR   SIGNOR; Q15717; -.
DR   BioGRID-ORCS; 1994; 135 hits in 884 CRISPR screens.
DR   ChiTaRS; ELAVL1; human.
DR   EvolutionaryTrace; Q15717; -.
DR   GeneWiki; ELAVL1; -.
DR   GenomeRNAi; 1994; -.
DR   Pharos; Q15717; Tchem.
DR   PRO; PR:Q15717; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q15717; protein.
DR   Bgee; ENSG00000066044; Expressed in endothelial cell and 245 other tissues.
DR   ExpressionAtlas; Q15717; baseline and differential.
DR   Genevisible; Q15717; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0098794; C:postsynapse; IEA:Ensembl.
DR   GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR   GO; GO:0017091; F:AU-rich element binding; IDA:UniProtKB.
DR   GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR   GO; GO:0035198; F:miRNA binding; IDA:UniProtKB.
DR   GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IDA:UniProtKB.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR   GO; GO:0003729; F:mRNA binding; TAS:ProtInc.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR   GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR   GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; IDA:UniProtKB.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
DR   GO; GO:0048255; P:mRNA stabilization; IDA:UniProtKB.
DR   GO; GO:0060965; P:negative regulation of gene silencing by miRNA; IMP:UniProtKB.
DR   GO; GO:0045727; P:positive regulation of translation; IDA:MGI.
DR   GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR   GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl.
DR   GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
DR   GO; GO:2000036; P:regulation of stem cell population maintenance; ISS:UniProtKB.
DR   CDD; cd12650; RRM1_Hu; 1.
DR   CDD; cd12773; RRM2_HuR; 1.
DR   Gene3D; 3.30.70.330; -; 3.
DR   InterPro; IPR006548; ELAD_HU_SF.
DR   InterPro; IPR034775; ELAV/Hu_RRM1.
DR   InterPro; IPR002343; Hud_Sxl_RNA.
DR   InterPro; IPR034996; HuR_RRM2.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   Pfam; PF00076; RRM_1; 3.
DR   PRINTS; PR00961; HUDSXLRNA.
DR   SMART; SM00360; RRM; 3.
DR   SUPFAM; SSF54928; SSF54928; 2.
DR   TIGRFAMs; TIGR01661; ELAV_HUD_SF; 1.
DR   PROSITE; PS50102; RRM; 3.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW   Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; RNA-binding; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000244|PubMed:21406692"
FT   CHAIN           2..326
FT                   /note="ELAV-like protein 1"
FT                   /id="PRO_0000081577"
FT   DOMAIN          20..98
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          106..186
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          244..322
FT                   /note="RRM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000244|PubMed:21406692"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:21406692"
FT   MOD_RES         100
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         158
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000305|PubMed:18285462"
FT   MOD_RES         197
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         202
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:23186163"
FT   MOD_RES         206
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P70372"
FT   MOD_RES         217
FT                   /note="Asymmetric dimethylarginine; by CARM1; alternate"
FT                   /evidence="ECO:0000269|PubMed:12237300"
FT   MOD_RES         217
FT                   /note="Omega-N-methylarginine; alternate"
FT                   /evidence="ECO:0000244|PubMed:24129315"
FT   MOD_RES         221
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000305|PubMed:18285462"
FT   MOD_RES         318
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000305|PubMed:18285462"
FT   CROSSLNK        191
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:28112733"
FT   VAR_SEQ         1
FT                   /note="M -> MGSGGRSAQVSTGQRAWLLPCRFLKNTM (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056148"
FT   MUTAGEN         158
FT                   /note="S->A: Decreases phosphorylation by PRKCD."
FT                   /evidence="ECO:0000269|PubMed:18285462"
FT   MUTAGEN         221
FT                   /note="S->A: Decreases phosphorylation by PRKCD. Nearly
FT                   abolishes phosphorylation by PRKCD and translocation from
FT                   the nucleus into the cytoplasm; when associated with A-
FT                   318."
FT                   /evidence="ECO:0000269|PubMed:18285462"
FT   MUTAGEN         318
FT                   /note="S->A: Decreases phosphorylation by PRKCD. Nearly
FT                   abolishes phosphorylation by PRKCD and translocation from
FT                   the nucleus into the cytoplasm; when associated with A-
FT                   221."
FT                   /evidence="ECO:0000269|PubMed:18285462"
FT   CONFLICT        180
FT                   /note="T -> A (in Ref. 1; AAB41913)"
FT                   /evidence="ECO:0000305"
FT   TURN            7..10
FT                   /evidence="ECO:0000244|PDB:5SZW"
FT   STRAND          20..26
FT                   /evidence="ECO:0000244|PDB:4FXV"
FT   HELIX           33..41
FT                   /evidence="ECO:0000244|PDB:4FXV"
FT   STRAND          46..53
FT                   /evidence="ECO:0000244|PDB:4FXV"
FT   STRAND          55..57
FT                   /evidence="ECO:0000244|PDB:4FXV"
FT   STRAND          60..70
FT                   /evidence="ECO:0000244|PDB:4FXV"
FT   HELIX           71..81
FT                   /evidence="ECO:0000244|PDB:4FXV"
FT   STRAND          92..95
FT                   /evidence="ECO:0000244|PDB:4FXV"
FT   HELIX           101..103
FT                   /evidence="ECO:0000244|PDB:4ED5"
FT   STRAND          107..111
FT                   /evidence="ECO:0000244|PDB:4ED5"
FT   HELIX           119..126
FT                   /evidence="ECO:0000244|PDB:4ED5"
FT   HELIX           127..129
FT                   /evidence="ECO:0000244|PDB:4ED5"
FT   STRAND          132..139
FT                   /evidence="ECO:0000244|PDB:4ED5"
FT   TURN            141..143
FT                   /evidence="ECO:0000244|PDB:4ED5"
FT   STRAND          146..156
FT                   /evidence="ECO:0000244|PDB:4ED5"
FT   HELIX           157..167
FT                   /evidence="ECO:0000244|PDB:4ED5"
FT   STRAND          180..183
FT                   /evidence="ECO:0000244|PDB:4ED5"
FT   STRAND          244..249
FT                   /evidence="ECO:0000244|PDB:6GD3"
FT   HELIX           257..264
FT                   /evidence="ECO:0000244|PDB:6GD3"
FT   HELIX           265..267
FT                   /evidence="ECO:0000244|PDB:6GD3"
FT   STRAND          270..277
FT                   /evidence="ECO:0000244|PDB:6GD3"
FT   TURN            279..281
FT                   /evidence="ECO:0000244|PDB:6GD3"
FT   STRAND          283..293
FT                   /evidence="ECO:0000244|PDB:6GD3"
FT   HELIX           295..305
FT                   /evidence="ECO:0000244|PDB:6GD3"
FT   STRAND          316..318
FT                   /evidence="ECO:0000244|PDB:6GD3"
SQ   SEQUENCE   326 AA;  36092 MW;  0B86143805264DEF CRC64;
     MSNGYEDHMA EDCRGDIGRT NLIVNYLPQN MTQDELRSLF SSIGEVESAK LIRDKVAGHS
     LGYGFVNYVT AKDAERAINT LNGLRLQSKT IKVSYARPSS EVIKDANLYI SGLPRTMTQK
     DVEDMFSRFG RIINSRVLVD QTTGLSRGVA FIRFDKRSEA EEAITSFNGH KPPGSSEPIT
     VKFAANPNQN KNVALLSQLY HSPARRFGGP VHHQAQRFRF SPMGVDHMSG LSGVNVPGNA
     SSGWCIFIYN LGQDADEGIL WQMFGPFGAV TNVKVIRDFN TNKCKGFGFV TMTNYEEAAM
     AIASLNGYRL GDKILQVSFK TNKSHK
//
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