GENTAUR Molecular Products.

 PQBP1_HUMAN             Reviewed;         265 AA.
 O60828; C9JQA1; Q4VY25; Q4VY26; Q4VY27; Q4VY29; Q4VY30; Q4VY34;
 Q4VY35; Q4VY36; Q4VY37; Q4VY38; Q9GZP2; Q9GZU4; Q9GZZ4;
 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
 01-AUG-1998, sequence version 1.
 20-JUN-2018, entry version 164.
 RecName: Full=Polyglutamine-binding protein 1 {ECO:0000303|PubMed:10332029, ECO:0000303|PubMed:11163963};
          Short=PQBP-1 {ECO:0000303|PubMed:10332029, ECO:0000303|PubMed:11163963};
 AltName: Full=38 kDa nuclear protein containing a WW domain {ECO:0000303|PubMed:10198427};
          Short=Npw38 {ECO:0000303|PubMed:10198427};
 AltName: Full=Polyglutamine tract-binding protein 1 {ECO:0000303|PubMed:10332029};
 Name=PQBP1 {ECO:0000303|PubMed:10332029, ECO:0000303|PubMed:11163963,
 ECO:0000312|HGNC:HGNC:9330};
 Synonyms=NPW38 {ECO:0000303|PubMed:10198427}; ORFNames=JM26;
 Homo sapiens (Human).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
 Catarrhini; Hominidae; Homo.
 NCBI_TaxID=9606;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH
 POU3F2; HTT AND AR, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
 TISSUE=Brain;
 PubMed=10332029; DOI=10.1093/hmg/8.6.977;
 Waragai M., Lammers C.-H., Takeuchi S., Imafuku I., Udagawa Y.,
 Kanazawa I., Kawabata M., Mouradian M.M., Okazawa H.;
 "PQBP-1, a novel polyglutamine tract binding protein, inhibits
 transcription activation by Brn-2 and affects cell survival.";
 Hum. Mol. Genet. 8:977-987(1999).
 [2]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
 LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF TRP-52; TYR-64;
 TYR-65; TRP-66; TRP-75 AND PRO-78.
 TISSUE=Gastric adenocarcinoma;
 PubMed=10198427; DOI=10.1093/nar/27.9.1957;
 Komuro A., Saeki M., Kato S.;
 "Npw38, a novel nuclear protein possessing a WW domain capable of
 activating basal transcription.";
 Nucleic Acids Res. 27:1957-1965(1999).
 [3]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 3; 4 AND 7).
 PubMed=11163963; DOI=10.1016/S0378-1119(00)00437-6;
 Iwamoto K., Huang Y.-T., Ueda S.;
 "Genomic organization and alternative transcripts of the human PQBP-1
 gene.";
 Gene 259:69-73(2000).
 [4]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 8; 9 AND 10).
 TISSUE=Adrenal gland, Kidney, Small intestine, and Thymus;
 Eades T.L., Huckle E.L., Ross M.T.;
 "Detailed sampling of cloned cDNA samples identifies additional PQBP1
 transcript variants.";
 Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
 [5]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
 Strom T.M., Nyakatura G., Hellebrand H., Drescher B., Rosenthal A.,
 Meindl A.;
 "Transcription map in Xp11.23.";
 Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
 [6]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 PubMed=15772651; DOI=10.1038/nature03440;
 Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
 Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
 Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
 Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
 Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
 Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
 Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
 Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
 Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
 Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
 Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
 Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
 Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
 Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
 Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
 Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
 Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
 Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
 Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
 Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
 Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
 Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
 Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
 Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
 Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
 Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
 Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
 de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
 Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
 Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
 Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
 Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
 McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
 Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
 Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
 Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
 Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
 Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
 Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
 Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
 Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
 Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
 Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
 Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
 Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
 Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
 Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
 Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
 Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
 Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
 Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
 Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
 Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
 "The DNA sequence of the human X chromosome.";
 Nature 434:325-337(2005).
 [7]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
 TISSUE=Lung;
 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).
 [8]
 PROTEIN SEQUENCE OF 2-10 AND 229-243, CLEAVAGE OF INITIATOR
 METHIONINE, AND IDENTIFICATION BY MASS SPECTROMETRY.
 TISSUE=Ovarian carcinoma;
 Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
 Submitted (DEC-2008) to UniProtKB.
 [9]
 INTERACTION WITH POU3F2.
 PubMed=9875212; DOI=10.1006/bbrc.1998.9725;
 Imafuku I., Waragai M., Takeuchi S., Kanazawa I., Kawabata M.,
 Mouradian M.M., Okazawa H.;
 "Polar amino acid-rich sequences bind to polyglutamine tracts.";
 Biochem. Biophys. Res. Commun. 253:16-20(1998).
 [10]
 INTERACTION WITH TXNL4A.
 PubMed=10873650; DOI=10.1006/bbrc.2000.2992;
 Waragai M., Junn E., Kajikawa M., Takeuchi S., Kanazawa I.,
 Shibata M., Mouradian M.M., Okazawa H.;
 "PQBP-1/Npw38, a nuclear protein binding to the polyglutamine tract,
 interacts with U5-15kD/dim1p via the carboxyl-terminal domain.";
 Biochem. Biophys. Res. Commun. 273:592-595(2000).
 [11]
 FUNCTION, INTERACTION WITH ATXN1 AND RNA POLYMERASE II LARGE SUBUNIT,
 AND SUBCELLULAR LOCATION.
 PubMed=12062018; DOI=10.1016/S0896-6273(02)00697-9;
 Okazawa H., Rich T., Chang A., Lin X., Waragai M., Kajikawa M.,
 Enokido Y., Komuro A., Kato S., Shibata M., Hatanaka H.,
 Mouradian M.M., Sudol M., Kanazawa I.;
 "Interaction between mutant ataxin-1 and PQBP-1 affects transcription
 and cell death.";
 Neuron 34:701-713(2002).
 [12]
 INVOLVEMENT IN RENS1.
 PubMed=14634649; DOI=10.1038/ng1264;
 Kalscheuer V.M., Freude K., Musante L., Jensen L.R., Yntema H.G.,
 Gecz J., Sefiani A., Hoffmann K., Moser B., Haas S., Gurok U.,
 Haesler S., Aranda B., Nshedjan A., Tzschach A., Hartmann N.,
 Roloff T.C., Shoichet S., Hagens O., Tao J., Van Bokhoven H.,
 Turner G., Chelly J., Moraine C., Fryns J.-P., Nuber U.,
 Hoeltzenbein M., Scharff C., Scherthan H., Lenzner S., Hamel B.C.J.,
 Schweiger S., Ropers H.-H.;
 "Mutations in the polyglutamine binding protein 1 gene cause X-linked
 mental retardation.";
 Nat. Genet. 35:313-315(2003).
 [13]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, 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]
 DOMAIN, CIRCULAR DICHROISM, NMR, AND INTERACTION WITH TXNL4A.
 PubMed=19303059; DOI=10.1016/j.bbapap.2009.03.001;
 Takahashi M., Mizuguchi M., Shinoda H., Aizawa T., Demura M.,
 Okazawa H., Kawano K.;
 "Polyglutamine tract binding protein-1 is an intrinsically
 unstructured protein.";
 Biochim. Biophys. Acta 1794:936-943(2009).
 [15]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, 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).
 [16]
 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).
 [17]
 INVOLVEMENT IN RENS1.
 PubMed=21315190; DOI=10.1016/j.ejmg.2011.01.010;
 Rejeb I., Ben Jemaa L., Abaied L., Kraoua L., Saillour Y., Maazoul F.,
 Chelly J., Chaabouni H.;
 "A novel frame shift mutation in the PQBP1 gene identified in a
 Tunisian family with X-linked mental retardation.";
 Eur. J. Med. Genet. 54:241-246(2011).
 [18]
 FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CAPRIN1; DDX1;
 SFPQ AND KHSRP.
 PubMed=21933836; DOI=10.1093/hmg/ddr430;
 Kunde S.A., Musante L., Grimme A., Fischer U., Mueller E.,
 Wanker E.E., Kalscheuer V.M.;
 "The X-chromosome-linked intellectual disability protein PQBP1 is a
 component of neuronal RNA granules and regulates the appearance of
 stress granules.";
 Hum. Mol. Genet. 20:4916-4931(2011).
 [19]
 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).
 [20]
 FUNCTION, INTERACTION WITH SF3B1 AND WBP11, SUBUNIT, SUBCELLULAR
 LOCATION, AND CHARACTERIZATION OF VARIANT RENS1 CYS-65.
 PubMed=23512658; DOI=10.1101/gad.212308.112;
 Wang Q., Moore M.J., Adelmant G., Marto J.A., Silver P.A.;
 "PQBP1, a factor linked to intellectual disability, affects
 alternative splicing associated with neurite outgrowth.";
 Genes Dev. 27:615-626(2013).
 [21]
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=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).
 [22]
 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).
 [23]
 FUNCTION, INTERACTION WITH CGAS, AND CHARACTERIZATION OF VARIANT RENS1
 CYS-65.
 PubMed=26046437; DOI=10.1016/j.cell.2015.04.050;
 Yoh S.M., Schneider M., Seifried J., Soonthornvacharin S., Akleh R.E.,
 Olivieri K.C., De Jesus P.D., Ruan C., de Castro E., Ruiz P.A.,
 Germanaud D., des Portes V., Garcia-Sastre A., Koenig R., Chanda S.K.;
 "PQBP1 is a proximal sensor of the cGAS-dependent innate response to
 HIV-1.";
 Cell 161:1293-1305(2015).
 [24]
 INTERACTION WITH TXNL4A AND WBP11.
 PubMed=27314904; DOI=10.1002/1873-3468.12256;
 Mizuguchi M., Obita T., Kajiyama A., Kozakai Y., Nakai T.,
 Nabeshima Y., Okazawa H.;
 "Allosteric modulation of the binding affinity between PQBP1 and the
 spliceosomal protein U5-15kD.";
 FEBS Lett. 590:2221-2231(2016).
 [25]
 REVIEW.
 PubMed=28627366; DOI=10.1016/j.neuint.2017.06.005;
 Okazawa H.;
 "PQBP1, an intrinsically disordered/denatured protein at the crossroad
 of intellectual disability and neurodegenerative diseases.";
 Neurochem. Int. 0:0-0(2017).
 [26]
 X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 223-265 IN COMPLEXES WITH
 TXNL4A AND CD2BP2, INTERACTION WITH TXNL4A AND CD2BP2, DOMAIN, AND
 MUTAGENESIS OF TYR-245; PRO-248; VAL-251; LEU-252; ARG-253 AND
 ASN-255.
 PubMed=24781215; DOI=10.1038/ncomms4822;
 Mizuguchi M., Obita T., Serita T., Kojima R., Nabeshima Y.,
 Okazawa H.;
 "Mutations in the PQBP1 gene prevent its interaction with the
 spliceosomal protein U5-15 kD.";
 Nat. Commun. 5:3822-3822(2014).
 [27]
 VARIANT RENS1 CYS-65.
 PubMed=16740914; DOI=10.1136/jmg.2005.037556;
 Lubs H., Abidi F.E., Echeverri R., Holloway L., Meindl A.,
 Stevenson R.E., Schwartz C.E.;
 "Golabi-Ito-Hall syndrome results from a missense mutation in the WW
 domain of the PQBP1 gene.";
 J. Med. Genet. 43:E30-E30(2006).
 [28]
 VARIANT [LARGE SCALE ANALYSIS] TRP-224.
 PubMed=16959974; DOI=10.1126/science.1133427;
 Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
 Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
 Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
 Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
 Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
 Vogelstein B., Kinzler K.W., Velculescu V.E.;
 "The consensus coding sequences of human breast and colorectal
 cancers.";
 Science 314:268-274(2006).
 [29]
 CHARACTERIZATION OF VARIANT RENS1 CYS-65, INTERACTION WITH WBP11 AND
 ATN1, DOMAIN, AND FUNCTION.
 PubMed=20410308; DOI=10.1074/jbc.M109.084525;
 Tapia V.E., Nicolaescu E., McDonald C.B., Musi V., Oka T.,
 Inayoshi Y., Satteson A.C., Mazack V., Humbert J., Gaffney C.J.,
 Beullens M., Schwartz C.E., Landgraf C., Volkmer R., Pastore A.,
 Farooq A., Bollen M., Sudol M.;
 "Y65C missense mutation in the WW domain of the Golabi-Ito-Hall
 syndrome protein PQBP1 affects its binding activity and deregulates
 pre-mRNA splicing.";
 J. Biol. Chem. 285:19391-19401(2010).
 [30]
 VARIANT LEU-244.
 PubMed=26637798; DOI=10.1016/j.neuron.2015.11.009;
 D'Gama A.M., Pochareddy S., Li M., Jamuar S.S., Reiff R.E., Lam A.T.,
 Sestan N., Walsh C.A.;
 "Targeted DNA Sequencing from Autism Spectrum Disorder Brains
 Implicates Multiple Genetic Mechanisms.";
 Neuron 88:910-917(2015).
 -!- FUNCTION: Intrinsically disordered protein that acts as a
     scaffold, and which is involved in different processes, such as
     pre-mRNA splicing, transcription regulation, innate immunity and
     neuron development (PubMed:10198427, PubMed:10332029,
     PubMed:12062018, PubMed:20410308, PubMed:23512658). Interacts with
     splicing-related factors via the intrinsically disordered region
     and regulates alternative splicing of target pre-mRNA species
     (PubMed:10332029, PubMed:12062018, PubMed:23512658,
     PubMed:20410308). May suppress the ability of POU3F2 to
     transactivate the DRD1 gene in a POU3F2 dependent manner. Can
     activate transcription directly or via association with the
     transcription machinery (PubMed:10198427). May be involved in
     ATXN1 mutant-induced cell death (PubMed:12062018). The interaction
     with ATXN1 mutant reduces levels of phosphorylated RNA polymerase
     II large subunit (PubMed:12062018). Involved in the assembly of
     cytoplasmic stress granule, possibly by participating to the
     transport of neuronal RNA granules (PubMed:21933836). Also acts as
     an innate immune sensor of infection by retroviruses, such as HIV,
     by detecting the presence of reverse-transcribed DNA in the
     cytosol (PubMed:26046437). Directly binds retroviral reverse-
     transcribed DNA in the cytosol and interacts with CGAS, leading to
     activate the cGAS-STING signaling pathway, triggering type-I
     interferon production (PubMed:26046437).
     {ECO:0000269|PubMed:10198427, ECO:0000269|PubMed:10332029,
     ECO:0000269|PubMed:12062018, ECO:0000269|PubMed:20410308,
     ECO:0000269|PubMed:21933836, ECO:0000269|PubMed:23512658,
     ECO:0000269|PubMed:26046437}.
 -!- SUBUNIT: Interacts with POU3F2/Brn-2, ATXN1, TXNL4A, HTT and AR
     (PubMed:10332029, PubMed:10873650, PubMed:19303059,
     PubMed:24781215). Interaction with ATXN1 correlates positively
     with the length of the polyglutamine tract (PubMed:12062018).
     Interacts with RNA polymerase II large subunit in a
     phosphorylation-dependent manner (PubMed:12062018). Forms a
     ternary complex with ATXN1 mutant and phosphorylated RNA
     polymerase II (PubMed:12062018). Interacts (via C-terminus) with
     TXNL4A and CD2BP2 (PubMed:10873650, PubMed:19303059,
     PubMed:24781215). Interacts (via WW domain) with ATN1 and SF3B1,
     and may interact with additional splice factors (PubMed:23512658,
     PubMed:20410308). Interacts (via WW domain) with WBP11; Leading to
     reduce interaction between PQBP1 and TXNL4A (PubMed:23512658,
     PubMed:20410308, PubMed:27314904). Interacts with CAPRIN1
     (PubMed:21933836). Interacts with DDX1 (PubMed:21933836).
     Interacts with SFPQ (PubMed:21933836). Interacts with KHSRP
     (PubMed:21933836). {ECO:0000269|PubMed:10332029,
     ECO:0000269|PubMed:10873650, ECO:0000269|PubMed:12062018,
     ECO:0000269|PubMed:19303059, ECO:0000269|PubMed:20410308,
     ECO:0000269|PubMed:21933836, ECO:0000269|PubMed:23512658,
     ECO:0000269|PubMed:24781215, ECO:0000269|PubMed:27314904,
     ECO:0000269|PubMed:9875212}.
 -!- INTERACTION:
     Q08379:GOLGA2; NbExp=6; IntAct=EBI-713867, EBI-618309;
     Q9BRK4:LZTS2; NbExp=6; IntAct=EBI-713867, EBI-741037;
     Q15691:MAPRE1; NbExp=5; IntAct=EBI-713867, EBI-1004115;
     Q9Y2W2:WBP11; NbExp=11; IntAct=EBI-713867, EBI-714455;
 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10198427,
     ECO:0000269|PubMed:10332029, ECO:0000269|PubMed:12062018,
     ECO:0000269|PubMed:23512658}. Nucleus speckle
     {ECO:0000250|UniProtKB:Q91VJ5}. Cytoplasmic granule
     {ECO:0000269|PubMed:21933836}. Note=Colocalizes with SRSF2 in
     nuclear speckles (By similarity). Colocalized with POU3F2
     (PubMed:10332029). Colocalized with ATXN1 in nuclear inclusion
     bodies (PubMed:12062018). Localizes to cytoplasmic stress granules
     (PubMed:21933836). {ECO:0000250|UniProtKB:Q91VJ5,
     ECO:0000269|PubMed:10332029, ECO:0000269|PubMed:12062018,
     ECO:0000269|PubMed:21933836}.
 -!- ALTERNATIVE PRODUCTS:
     Event=Alternative splicing; Named isoforms=10;
     Name=1; Synonyms=PQBP-1;
       IsoId=O60828-1; Sequence=Displayed;
     Name=2;
       IsoId=O60828-2; Sequence=VSP_015909;
     Name=3; Synonyms=PQBP-1b/c;
       IsoId=O60828-3; Sequence=VSP_015908, VSP_015910;
     Name=4; Synonyms=PQBP-1d;
       IsoId=O60828-4; Sequence=VSP_015903;
     Name=5;
       IsoId=O60828-5; Sequence=VSP_015900;
     Name=6;
       IsoId=O60828-6; Sequence=VSP_015906, VSP_015907;
     Name=7;
       IsoId=O60828-7; Sequence=VSP_015904, VSP_015905;
     Name=8; Synonyms=PQBP-1a;
       IsoId=O60828-8; Sequence=VSP_015896, VSP_015902;
     Name=9;
       IsoId=O60828-9; Sequence=VSP_015899, VSP_015901;
     Name=10;
       IsoId=O60828-10; Sequence=VSP_015897, VSP_015898;
 -!- TISSUE SPECIFICITY: Widely expressed with high level in heart,
     skeletal muscle, pancreas, spleen, thymus, prostate, ovary, small
     intestine and peripheral blood leukocytes.
     {ECO:0000269|PubMed:10198427, ECO:0000269|PubMed:10332029}.
 -!- DOMAIN: The WW domain may play a role as a transcriptional
     activator directly or via association with the transcription
     machinery. The WW domain mediates interaction with WBP11, ATN1,
     SF3B1 and the C-terminal domain of the RNA polymerase II large
     subunit. {ECO:0000269|PubMed:20410308,
     ECO:0000269|PubMed:24781215}.
 -!- DOMAIN: Except for the WW domain, the protein is intrinsically
     disordered. {ECO:0000269|PubMed:19303059,
     ECO:0000269|PubMed:24781215}.
 -!- DISEASE: Renpenning syndrome 1 (RENS1) [MIM:309500]: A X-linked
     mental retardation syndrome characterized by mental retardation,
     microcephaly, short stature, and small testes. The craniofacies
     tends to be narrow and tall with upslanting palpebral fissures,
     abnormal nasal configuration, cupped ears, and short philtrum. The
     nose may appear long or bulbous, with overhanging columella. Less
     consistent manifestations include ocular colobomas, cardiac
     malformations, cleft palate, and anal anomalies.
     {ECO:0000269|PubMed:14634649, ECO:0000269|PubMed:16740914,
     ECO:0000269|PubMed:20410308, ECO:0000269|PubMed:21315190,
     ECO:0000269|PubMed:23512658, ECO:0000269|PubMed:26046437}.
     Note=The disease is caused by mutations affecting the gene
     represented in this entry.
 -----------------------------------------------------------------------
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 Distributed under the Creative Commons Attribution (CC BY 4.0) License
 -----------------------------------------------------------------------
 EMBL; AJ242829; CAB44309.1; -; mRNA.
 EMBL; AB016533; BAA76400.1; -; mRNA.
 EMBL; AB041832; BAB16702.1; -; Genomic_DNA.
 EMBL; AB041832; BAB16703.1; -; Genomic_DNA.
 EMBL; AB041832; BAB16704.1; -; Genomic_DNA.
 EMBL; AB041832; BAB16705.1; -; Genomic_DNA.
 EMBL; AB041833; BAB16706.1; -; mRNA.
 EMBL; AB041834; BAB16707.1; -; mRNA.
 EMBL; AB041835; BAB16708.1; -; mRNA.
 EMBL; AB041836; BAB16709.1; -; mRNA.
 EMBL; AJ973593; CAJ00537.1; -; mRNA.
 EMBL; AJ973594; CAJ00538.1; -; mRNA.
 EMBL; AJ973595; CAJ00539.1; -; mRNA.
 EMBL; AJ973596; CAJ00540.1; -; mRNA.
 EMBL; AJ973597; CAJ00541.1; -; mRNA.
 EMBL; AJ973598; CAJ00542.1; -; mRNA.
 EMBL; AJ973599; CAJ00543.1; -; mRNA.
 EMBL; AJ973600; CAJ00544.1; -; mRNA.
 EMBL; AJ973601; CAJ00545.1; -; mRNA.
 EMBL; AJ973602; CAJ00546.1; -; mRNA.
 EMBL; AJ973603; CAJ00547.1; -; mRNA.
 EMBL; AJ973605; CAJ00548.1; -; mRNA.
 EMBL; AJ973606; CAJ00549.1; -; mRNA.
 EMBL; AJ973607; CAJ00550.1; -; mRNA.
 EMBL; AJ005893; CAA06750.1; -; mRNA.
 EMBL; AC233300; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; BC012358; AAH12358.1; -; mRNA.
 CCDS; CCDS14309.1; -. [O60828-1]
 CCDS; CCDS55412.1; -. [O60828-4]
 RefSeq; NP_001027553.1; NM_001032381.1. [O60828-1]
 RefSeq; NP_001027554.1; NM_001032382.1. [O60828-1]
 RefSeq; NP_001027555.1; NM_001032383.1. [O60828-1]
 RefSeq; NP_001027556.1; NM_001032384.1. [O60828-1]
 RefSeq; NP_001161461.1; NM_001167989.1. [O60828-2]
 RefSeq; NP_001161462.1; NM_001167990.1.
 RefSeq; NP_001161464.1; NM_001167992.1. [O60828-5]
 RefSeq; NP_005701.1; NM_005710.2. [O60828-1]
 RefSeq; NP_652766.1; NM_144495.2. [O60828-4]
 RefSeq; XP_005272628.1; XM_005272571.3. [O60828-2]
 RefSeq; XP_005272629.1; XM_005272572.4. [O60828-4]
 RefSeq; XP_011542186.1; XM_011543884.2. [O60828-1]
 RefSeq; XP_016884696.1; XM_017029207.1. [O60828-2]
 UniGene; Hs.534384; -.
 PDB; 4BWQ; X-ray; 2.10 A; B/D/F/H=223-265.
 PDB; 4BWS; X-ray; 2.50 A; B/E=229-265.
 PDB; 4CDO; X-ray; 2.50 A; A/C=223-265.
 PDBsum; 4BWQ; -.
 PDBsum; 4BWS; -.
 PDBsum; 4CDO; -.
 ProteinModelPortal; O60828; -.
 SMR; O60828; -.
 BioGrid; 115393; 52.
 IntAct; O60828; 24.
 MINT; O60828; -.
 STRING; 9606.ENSP00000218224; -.
 iPTMnet; O60828; -.
 PhosphoSitePlus; O60828; -.
 BioMuta; PQBP1; -.
 EPD; O60828; -.
 MaxQB; O60828; -.
 PaxDb; O60828; -.
 PeptideAtlas; O60828; -.
 PRIDE; O60828; -.
 ProteomicsDB; 49611; -.
 ProteomicsDB; 49612; -. [O60828-10]
 ProteomicsDB; 49613; -. [O60828-2]
 ProteomicsDB; 49614; -. [O60828-3]
 ProteomicsDB; 49615; -. [O60828-4]
 ProteomicsDB; 49616; -. [O60828-5]
 ProteomicsDB; 49617; -. [O60828-6]
 ProteomicsDB; 49618; -. [O60828-7]
 ProteomicsDB; 49619; -. [O60828-8]
 ProteomicsDB; 49620; -. [O60828-9]
 TopDownProteomics; O60828-1; -. [O60828-1]
 TopDownProteomics; O60828-2; -. [O60828-2]
 DNASU; 10084; -.
 Ensembl; ENST00000218224; ENSP00000218224; ENSG00000102103. [O60828-1]
 Ensembl; ENST00000247140; ENSP00000247140; ENSG00000102103. [O60828-4]
 Ensembl; ENST00000376563; ENSP00000365747; ENSG00000102103. [O60828-1]
 Ensembl; ENST00000376566; ENSP00000365750; ENSG00000102103. [O60828-4]
 Ensembl; ENST00000396763; ENSP00000379985; ENSG00000102103. [O60828-1]
 Ensembl; ENST00000447146; ENSP00000391759; ENSG00000102103. [O60828-1]
 GeneID; 10084; -.
 KEGG; hsa:10084; -.
 UCSC; uc004dle.4; human. [O60828-1]
 CTD; 10084; -.
 DisGeNET; 10084; -.
 EuPathDB; HostDB:ENSG00000102103.15; -.
 GeneCards; PQBP1; -.
 HGNC; HGNC:9330; PQBP1.
 HPA; HPA001880; -.
 MalaCards; PQBP1; -.
 MIM; 300463; gene.
 MIM; 309500; phenotype.
 neXtProt; NX_O60828; -.
 OpenTargets; ENSG00000102103; -.
 Orphanet; 93946; Hamel cerebro-palato-cardiac syndrome.
 Orphanet; 93947; X-linked intellectual disability, Golabi-Ito-Hall type.
 Orphanet; 93945; X-linked intellectual disability, Porteous type.
 Orphanet; 93950; X-linked intellectual disability, Sutherland-Haan type.
 PharmGKB; PA33693; -.
 eggNOG; KOG3427; Eukaryota.
 eggNOG; ENOG4111MHA; LUCA.
 GeneTree; ENSGT00390000001905; -.
 HOVERGEN; HBG053064; -.
 InParanoid; O60828; -.
 KO; K12865; -.
 OMA; SHEKSDR; -.
 OrthoDB; EOG091G0H7P; -.
 PhylomeDB; O60828; -.
 TreeFam; TF320689; -.
 Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
 SignaLink; O60828; -.
 ChiTaRS; PQBP1; human.
 GeneWiki; PQBP1; -.
 GenomeRNAi; 10084; -.
 PMAP-CutDB; O60828; -.
 PRO; PR:O60828; -.
 Proteomes; UP000005640; Chromosome X.
 Bgee; ENSG00000102103; -.
 ExpressionAtlas; O60828; baseline and differential.
 Genevisible; O60828; HS.
 GO; GO:0010494; C:cytoplasmic stress granule; IEA:Ensembl.
 GO; GO:0005829; C:cytosol; IDA:HPA.
 GO; GO:0071598; C:neuronal ribonucleoprotein granule; IEA:Ensembl.
 GO; GO:0016607; C:nuclear speck; IDA:HPA.
 GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO; GO:0005634; C:nucleus; TAS:ProtInc.
 GO; GO:0003677; F:DNA binding; TAS:ProtInc.
 GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
 GO; GO:0043021; F:ribonucleoprotein complex binding; IDA:MGI.
 GO; GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
 GO; GO:0002218; P:activation of innate immune response; IDA:UniProtKB.
 GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IMP:UniProtKB.
 GO; GO:0071360; P:cellular response to exogenous dsRNA; IDA:UniProtKB.
 GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
 GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
 GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
 GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
 GO; GO:0002230; P:positive regulation of defense response to virus by host; IDA:UniProtKB.
 GO; GO:0032481; P:positive regulation of type I interferon production; IDA:UniProtKB.
 GO; GO:0048814; P:regulation of dendrite morphogenesis; IEA:Ensembl.
 GO; GO:0043484; P:regulation of RNA splicing; IMP:MGI.
 GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:ProtInc.
 GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
 CDD; cd00201; WW; 1.
 InterPro; IPR001202; WW_dom.
 InterPro; IPR036020; WW_dom_sf.
 SMART; SM00456; WW; 1.
 SUPFAM; SSF51045; SSF51045; 1.
 PROSITE; PS50020; WW_DOMAIN_2; 1.
 1: Evidence at protein level;
 3D-structure; Alternative splicing; Complete proteome;
 Direct protein sequencing; Immunity; Innate immunity;
 Mental retardation; mRNA processing; mRNA splicing; Nucleus;
 Phosphoprotein; Polymorphism; Reference proteome; Repeat;
 Transcription; Transcription regulation.
 INIT_MET      1      1       Removed. {ECO:0000269|Ref.8}.
 CHAIN         2    265       Polyglutamine-binding protein 1.
                              /FTId=PRO_0000076089.
 DOMAIN       46     80       WW. {ECO:0000255|PROSITE-
                              ProRule:PRU00224}.
 REPEAT      104    110       1-1.
 REPEAT      111    117       1-2.
 REPEAT      118    124       1-3.
 REPEAT      125    131       1-4.
 REPEAT      132    138       1-5.
 REPEAT      139    140       2-1.
 REPEAT      141    142       2-2.
 REPEAT      143    144       2-3.
 REPEAT      150    151       3-1.
 REPEAT      152    153       3-2.
 REPEAT      154    155       3-3.
 REPEAT      156    157       3-4.
 REPEAT      158    159       3-5.
 REPEAT      160    161       3-6.
 REPEAT      162    163       3-7.
 REGION       94    265       Intrinsically disordered.
                              {ECO:0000269|PubMed:19303059}.
 REGION      104    138       5 X 7 AA approximate tandem repeats of D-
                              R-[SG]-H-D-K-S.
 REGION      139    144       3 X 2 AA tandem repeats of [DE]-R.
 REGION      150    163       7 X 2 AA tandem repeats of [DE]-R.
 REGION      245    255       Important for interaction with TXNL4A.
 COMPBIAS    140    181       Arg-rich.
 MOD_RES      94     94       Phosphoserine.
                              {ECO:0000244|PubMed:20068231}.
 MOD_RES     247    247       Phosphoserine.
                              {ECO:0000244|PubMed:18669648}.
 VAR_SEQ      55     73       VFDPSCGLPYYWNADTDLV -> RAPLLLECRHRPCILALP
                              T (in isoform 8). {ECO:0000303|Ref.4}.
                              /FTId=VSP_015896.
 VAR_SEQ      60     60       C -> W (in isoform 10).
                              {ECO:0000303|Ref.4}.
                              /FTId=VSP_015897.
 VAR_SEQ      61    265       Missing (in isoform 10).
                              {ECO:0000303|Ref.4}.
                              /FTId=VSP_015898.
 VAR_SEQ      61     67       GLPYYWN -> PGWSAMV (in isoform 9).
                              {ECO:0000303|Ref.4}.
                              /FTId=VSP_015899.
 VAR_SEQ      68    265       Missing (in isoform 9).
                              {ECO:0000303|Ref.4}.
                              /FTId=VSP_015901.
 VAR_SEQ      68    167       Missing (in isoform 5).
                              {ECO:0000303|Ref.4}.
                              /FTId=VSP_015900.
 VAR_SEQ      74    265       Missing (in isoform 8).
                              {ECO:0000303|Ref.4}.
                              /FTId=VSP_015902.
 VAR_SEQ      98    192       Missing (in isoform 4).
                              {ECO:0000303|PubMed:11163963,
                              ECO:0000303|Ref.4}.
                              /FTId=VSP_015903.
 VAR_SEQ      99    128       AEEKLDRSHDKSDRGHDKSDRSHEKLDRGH -> LCPQMLK
                              KSWTGAMTSRTGAMTSRTAAMRN (in isoform 7).
                              {ECO:0000303|PubMed:11163963}.
                              /FTId=VSP_015904.
 VAR_SEQ     129    265       Missing (in isoform 7).
                              {ECO:0000303|PubMed:11163963}.
                              /FTId=VSP_015905.
 VAR_SEQ     149    149       V -> Q (in isoform 6).
                              {ECO:0000303|Ref.4}.
                              /FTId=VSP_015906.
 VAR_SEQ     150    265       Missing (in isoform 6).
                              {ECO:0000303|Ref.4}.
                              /FTId=VSP_015907.
 VAR_SEQ     193    224       AVSRKDEELDPMDPSSYSDAPRGTWSTGLPKR -> GKLGR
                              MGLGETNKVQGALREEAFPQKDAWTWG (in isoform
                              3). {ECO:0000303|PubMed:11163963,
                              ECO:0000303|Ref.4}.
                              /FTId=VSP_015908.
 VAR_SEQ     193    193       Missing (in isoform 2).
                              {ECO:0000303|Ref.4}.
                              /FTId=VSP_015909.
 VAR_SEQ     225    265       Missing (in isoform 3).
                              {ECO:0000303|PubMed:11163963,
                              ECO:0000303|Ref.4}.
                              /FTId=VSP_015910.
 VARIANT      65     65       Y -> C (in RENS1; impairs interaction
                              with WBP11, CGAS, SF3B1 and ATN1;
                              dbSNP:rs121917899).
                              {ECO:0000269|PubMed:16740914,
                              ECO:0000269|PubMed:20410308,
                              ECO:0000269|PubMed:23512658,
                              ECO:0000269|PubMed:26046437}.
                              /FTId=VAR_071063.
 VARIANT     224    224       R -> W (in a colorectal cancer sample;
                              somatic mutation).
                              {ECO:0000269|PubMed:16959974}.
                              /FTId=VAR_036357.
 VARIANT     244    244       P -> L (probable disease-associated
                              mutation found in a patient with autism;
                              dbSNP:rs878853145).
                              {ECO:0000269|PubMed:26637798}.
                              /FTId=VAR_078695.
 MUTAGEN      52     52       W->A: Enhances transcriptional
                              activation. Reduces transcriptional
                              activation; when associated with A-75.
                              Markedly reduced transcriptional
                              activation; when associated with A-64; A-
                              65 and A-66. Abolishes transcriptional
                              activation; when associated with A-64; A-
                              65; A-66 and A-75.
                              {ECO:0000269|PubMed:10198427}.
 MUTAGEN      64     64       Y->A: No effect on transcriptional
                              activation; when associated with A-65 and
                              A-66. Markedly reduced transcriptional
                              activation; when associated with A-52; A-
                              65 and A-66. Abolishes transcriptional
                              activation; when associated with A-52; A-
                              65; A-66 and A-75.
                              {ECO:0000269|PubMed:10198427}.
 MUTAGEN      65     65       Y->A: No effect on transcriptional
                              activation; when associated with A-64 and
                              A-66. Markedly reduced transcriptional
                              activation; when associated with A-52; A-
                              64 and A-66. Abolishes transcriptional
                              activation; when associated with A-52; A-
                              64; A-66 and A-75.
                              {ECO:0000269|PubMed:10198427}.
 MUTAGEN      66     66       W->A: No effect on transcriptional
                              activation; when associated with A-64 and
                              A-65. Markedly reduced transcriptional
                              activation; when associated with A-52; A-
                              64 and A-65. Abolishes transcriptional
                              activation; when associated with A-52; A-
                              64; A-65 and A-75.
                              {ECO:0000269|PubMed:10198427}.
 MUTAGEN      75     75       W->A: No effect on transcriptional
                              activation. Reduces transcriptional
                              activation; when associated with A-52.
                              Abolishes transcriptional activation;
                              when associated with A-52; A-64; A-65 and
                              A-66. {ECO:0000269|PubMed:10198427}.
 MUTAGEN      78     78       P->G: No effect on transcriptional
                              activation.
                              {ECO:0000269|PubMed:10198427}.
 MUTAGEN     245    245       Y->D: Abolishes interaction with TXNL4A.
                              {ECO:0000269|PubMed:24781215}.
 MUTAGEN     248    248       P->D: Abolishes interaction with TXNL4A.
                              {ECO:0000269|PubMed:24781215}.
 MUTAGEN     251    251       V->D: Abolishes interaction with TXNL4A.
                              {ECO:0000269|PubMed:24781215}.
 MUTAGEN     252    252       L->D: Abolishes interaction with TXNL4A.
                              {ECO:0000269|PubMed:24781215}.
 MUTAGEN     253    253       R->D: Strongly reduces affinity for
                              TXNL4A. {ECO:0000269|PubMed:24781215}.
 MUTAGEN     255    255       N->D: Strongly reduces affinity for
                              TXNL4A. {ECO:0000269|PubMed:24781215}.
 CONFLICT      8      8       Q -> L (in Ref. 4; CAJ00539).
                              {ECO:0000305}.
 CONFLICT     57     57       D -> N (in Ref. 4; CAJ00548).
                              {ECO:0000305}.
 CONFLICT    107    113       Missing (in Ref. 4; CAJ00538/CAJ00539/
                              CAJ00540/CAJ00541). {ECO:0000305}.
 CONFLICT    107    107       H -> Q (in Ref. 4; CAJ00549).
                              {ECO:0000305}.
 CONFLICT    147    147       D -> G (in Ref. 4; CAJ00549).
                              {ECO:0000305}.
 CONFLICT    198    198       D -> G (in Ref. 4; CAJ00549).
                              {ECO:0000305}.
 CONFLICT    236    236       A -> V (in Ref. 4; CAJ00548).
                              {ECO:0000305}.
 HELIX       248    258       {ECO:0000244|PDB:4BWQ}.
 SEQUENCE   265 AA;  30472 MW;  98C3BEF18CFF0297 CRC64;
 MPLPVALQTR LAKRGILKHL EPEPEEEIIA EDYDDDPVDY EATRLEGLPP SWYKVFDPSC
 GLPYYWNADT DLVSWLSPHD PNSVVTKSAK KLRSSNADAE EKLDRSHDKS DRGHDKSDRS
 HEKLDRGHDK SDRGHDKSDR DRERGYDKVD RERERDRERD RDRGYDKADR EEGKERRHHR
 REELAPYPKS KKAVSRKDEE LDPMDPSSYS DAPRGTWSTG LPKRNEAKTG ADTTAAGPLF
 QQRPYPSPGA VLRANAEASR TKQQD

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