ID PQBP1_HUMAN Reviewed; 265 AA. AC O60828; C9JQA1; Q4VY25; Q4VY26; Q4VY27; Q4VY29; Q4VY30; Q4VY34; Q4VY35; AC Q4VY36; Q4VY37; Q4VY38; Q9GZP2; Q9GZU4; Q9GZZ4; DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 27-NOV-2024, entry version 204. DE RecName: Full=Polyglutamine-binding protein 1 {ECO:0000303|PubMed:10332029, ECO:0000303|PubMed:11163963}; DE Short=PQBP-1 {ECO:0000303|PubMed:10332029, ECO:0000303|PubMed:11163963}; DE AltName: Full=38 kDa nuclear protein containing a WW domain {ECO:0000303|PubMed:10198427}; DE Short=Npw38 {ECO:0000303|PubMed:10198427}; DE AltName: Full=Polyglutamine tract-binding protein 1 {ECO:0000303|PubMed:10332029}; GN Name=PQBP1 {ECO:0000303|PubMed:10332029, ECO:0000303|PubMed:11163963, GN ECO:0000312|HGNC:HGNC:9330}; Synonyms=NPW38 {ECO:0000303|PubMed:10198427}; GN ORFNames=JM26; 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, INTERACTION WITH POU3F2; RP HTT AND AR, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC TISSUE=Brain; RX PubMed=10332029; DOI=10.1093/hmg/8.6.977; RA Waragai M., Lammers C.-H., Takeuchi S., Imafuku I., Udagawa Y., RA Kanazawa I., Kawabata M., Mouradian M.M., Okazawa H.; RT "PQBP-1, a novel polyglutamine tract binding protein, inhibits RT transcription activation by Brn-2 and affects cell survival."; RL Hum. Mol. Genet. 8:977-987(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, RP TISSUE SPECIFICITY, AND MUTAGENESIS OF TRP-52; TYR-64; TYR-65; TRP-66; RP TRP-75 AND PRO-78. RC TISSUE=Gastric adenocarcinoma; RX PubMed=10198427; DOI=10.1093/nar/27.9.1957; RA Komuro A., Saeki M., Kato S.; RT "Npw38, a novel nuclear protein possessing a WW domain capable of RT activating basal transcription."; RL Nucleic Acids Res. 27:1957-1965(1999). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 3; 4 AND 7). RX PubMed=11163963; DOI=10.1016/s0378-1119(00)00437-6; RA Iwamoto K., Huang Y.-T., Ueda S.; RT "Genomic organization and alternative transcripts of the human PQBP-1 RT gene."; RL Gene 259:69-73(2000). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 8; 9 AND 10). RC TISSUE=Adrenal gland, Kidney, Small intestine, and Thymus; RA Eades T.L., Huckle E.L., Ross M.T.; RT "Detailed sampling of cloned cDNA samples identifies additional PQBP1 RT transcript variants."; RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Strom T.M., Nyakatura G., Hellebrand H., Drescher B., Rosenthal A., RA Meindl A.; RT "Transcription map in Xp11.23."; RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung; 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 [8] RP PROTEIN SEQUENCE OF 2-10 AND 229-243, CLEAVAGE OF INITIATOR METHIONINE, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Ovarian carcinoma; RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.; RL Submitted (DEC-2008) to UniProtKB. RN [9] RP INTERACTION WITH POU3F2. RX PubMed=9875212; DOI=10.1006/bbrc.1998.9725; RA Imafuku I., Waragai M., Takeuchi S., Kanazawa I., Kawabata M., RA Mouradian M.M., Okazawa H.; RT "Polar amino acid-rich sequences bind to polyglutamine tracts."; RL Biochem. Biophys. Res. Commun. 253:16-20(1998). RN [10] RP INTERACTION WITH TXNL4A. RX PubMed=10873650; DOI=10.1006/bbrc.2000.2992; RA Waragai M., Junn E., Kajikawa M., Takeuchi S., Kanazawa I., Shibata M., RA Mouradian M.M., Okazawa H.; RT "PQBP-1/Npw38, a nuclear protein binding to the polyglutamine tract, RT interacts with U5-15kD/dim1p via the carboxyl-terminal domain."; RL Biochem. Biophys. Res. Commun. 273:592-595(2000). RN [11] RP FUNCTION, INTERACTION WITH ATXN1 AND RNA POLYMERASE II LARGE SUBUNIT, AND RP SUBCELLULAR LOCATION. RX PubMed=12062018; DOI=10.1016/s0896-6273(02)00697-9; RA Okazawa H., Rich T., Chang A., Lin X., Waragai M., Kajikawa M., Enokido Y., RA Komuro A., Kato S., Shibata M., Hatanaka H., Mouradian M.M., Sudol M., RA Kanazawa I.; RT "Interaction between mutant ataxin-1 and PQBP-1 affects transcription and RT cell death."; RL Neuron 34:701-713(2002). RN [12] RP INVOLVEMENT IN RENS1. RX PubMed=14634649; DOI=10.1038/ng1264; RA Kalscheuer V.M., Freude K., Musante L., Jensen L.R., Yntema H.G., Gecz J., RA Sefiani A., Hoffmann K., Moser B., Haas S., Gurok U., Haesler S., RA Aranda B., Nshedjan A., Tzschach A., Hartmann N., Roloff T.C., Shoichet S., RA Hagens O., Tao J., Van Bokhoven H., Turner G., Chelly J., Moraine C., RA Fryns J.-P., Nuber U., Hoeltzenbein M., Scharff C., Scherthan H., RA Lenzner S., Hamel B.C.J., Schweiger S., Ropers H.-H.; RT "Mutations in the polyglutamine binding protein 1 gene cause X-linked RT mental retardation."; RL Nat. Genet. 35:313-315(2003). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, 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 [14] RP DOMAIN, CIRCULAR DICHROISM, NMR, AND INTERACTION WITH TXNL4A. RX PubMed=19303059; DOI=10.1016/j.bbapap.2009.03.001; RA Takahashi M., Mizuguchi M., Shinoda H., Aizawa T., Demura M., Okazawa H., RA Kawano K.; RT "Polyglutamine tract binding protein-1 is an intrinsically unstructured RT protein."; RL Biochim. Biophys. Acta 1794:936-943(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, 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 [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [17] RP INVOLVEMENT IN RENS1. RX PubMed=21315190; DOI=10.1016/j.ejmg.2011.01.010; RA Rejeb I., Ben Jemaa L., Abaied L., Kraoua L., Saillour Y., Maazoul F., RA Chelly J., Chaabouni H.; RT "A novel frame shift mutation in the PQBP1 gene identified in a Tunisian RT family with X-linked mental retardation."; RL Eur. J. Med. Genet. 54:241-246(2011). RN [18] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CAPRIN1; DDX1; SFPQ RP AND KHSRP. RX PubMed=21933836; DOI=10.1093/hmg/ddr430; RA Kunde S.A., Musante L., Grimme A., Fischer U., Mueller E., Wanker E.E., RA Kalscheuer V.M.; RT "The X-chromosome-linked intellectual disability protein PQBP1 is a RT component of neuronal RNA granules and regulates the appearance of stress RT granules."; RL Hum. Mol. Genet. 20:4916-4931(2011). RN [19] RP IDENTIFICATION BY MASS 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 FUNCTION, INTERACTION WITH SF3B1 AND WBP11, SUBUNIT, SUBCELLULAR LOCATION, RP AND CHARACTERIZATION OF VARIANT RENS1 CYS-65. RX PubMed=23512658; DOI=10.1101/gad.212308.112; RA Wang Q., Moore M.J., Adelmant G., Marto J.A., Silver P.A.; RT "PQBP1, a factor linked to intellectual disability, affects alternative RT splicing associated with neurite outgrowth."; RL Genes Dev. 27:615-626(2013). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [22] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [23] RP FUNCTION, INTERACTION WITH CGAS, AND CHARACTERIZATION OF VARIANT RENS1 RP CYS-65. RX PubMed=26046437; DOI=10.1016/j.cell.2015.04.050; RA Yoh S.M., Schneider M., Seifried J., Soonthornvacharin S., Akleh R.E., RA Olivieri K.C., De Jesus P.D., Ruan C., de Castro E., Ruiz P.A., RA Germanaud D., des Portes V., Garcia-Sastre A., Koenig R., Chanda S.K.; RT "PQBP1 is a proximal sensor of the cGAS-dependent innate response to HIV- RT 1."; RL Cell 161:1293-1305(2015). RN [24] RP INTERACTION WITH TXNL4A AND WBP11. RX PubMed=27314904; DOI=10.1002/1873-3468.12256; RA Mizuguchi M., Obita T., Kajiyama A., Kozakai Y., Nakai T., Nabeshima Y., RA Okazawa H.; RT "Allosteric modulation of the binding affinity between PQBP1 and the RT spliceosomal protein U5-15kD."; RL FEBS Lett. 590:2221-2231(2016). RN [25] RP REVIEW. RX PubMed=28627366; DOI=10.1016/j.neuint.2017.06.005; RA Okazawa H.; RT "PQBP1, an intrinsically disordered/denatured protein at the crossroad of RT intellectual disability and neurodegenerative diseases."; RL Neurochem. Int. 119:17-25(2018). RN [26] RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 223-265 IN COMPLEXES WITH TXNL4A RP AND CD2BP2, INTERACTION WITH TXNL4A AND CD2BP2, DOMAIN, AND MUTAGENESIS OF RP TYR-245; PRO-248; VAL-251; LEU-252; ARG-253 AND ASN-255. RX PubMed=24781215; DOI=10.1038/ncomms4822; RA Mizuguchi M., Obita T., Serita T., Kojima R., Nabeshima Y., Okazawa H.; RT "Mutations in the PQBP1 gene prevent its interaction with the spliceosomal RT protein U5-15 kD."; RL Nat. Commun. 5:3822-3822(2014). RN [27] RP VARIANT RENS1 CYS-65. RX PubMed=16740914; DOI=10.1136/jmg.2005.037556; RA Lubs H., Abidi F.E., Echeverri R., Holloway L., Meindl A., Stevenson R.E., RA Schwartz C.E.; RT "Golabi-Ito-Hall syndrome results from a missense mutation in the WW domain RT of the PQBP1 gene."; RL J. Med. Genet. 43:E30-E30(2006). RN [28] RP VARIANT [LARGE SCALE ANALYSIS] TRP-224. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [29] RP CHARACTERIZATION OF VARIANT RENS1 CYS-65, INTERACTION WITH WBP11 AND ATN1, RP DOMAIN, AND FUNCTION. RX PubMed=20410308; DOI=10.1074/jbc.m109.084525; RA Tapia V.E., Nicolaescu E., McDonald C.B., Musi V., Oka T., Inayoshi Y., RA Satteson A.C., Mazack V., Humbert J., Gaffney C.J., Beullens M., RA Schwartz C.E., Landgraf C., Volkmer R., Pastore A., Farooq A., Bollen M., RA Sudol M.; RT "Y65C missense mutation in the WW domain of the Golabi-Ito-Hall syndrome RT protein PQBP1 affects its binding activity and deregulates pre-mRNA RT splicing."; RL J. Biol. Chem. 285:19391-19401(2010). RN [30] RP VARIANT LEU-244. RX PubMed=26637798; DOI=10.1016/j.neuron.2015.11.009; RA D'Gama A.M., Pochareddy S., Li M., Jamuar S.S., Reiff R.E., Lam A.T., RA Sestan N., Walsh C.A.; RT "Targeted DNA Sequencing from Autism Spectrum Disorder Brains Implicates RT Multiple Genetic Mechanisms."; RL Neuron 88:910-917(2015). CC -!- FUNCTION: Intrinsically disordered protein that acts as a scaffold, and CC which is involved in different processes, such as pre-mRNA splicing, CC transcription regulation, innate immunity and neuron development CC (PubMed:10198427, PubMed:10332029, PubMed:12062018, PubMed:20410308, CC PubMed:23512658). Interacts with splicing-related factors via the CC intrinsically disordered region and regulates alternative splicing of CC target pre-mRNA species (PubMed:10332029, PubMed:12062018, CC PubMed:20410308, PubMed:23512658). May suppress the ability of POU3F2 CC to transactivate the DRD1 gene in a POU3F2 dependent manner. Can CC activate transcription directly or via association with the CC transcription machinery (PubMed:10198427). May be involved in ATXN1 CC mutant-induced cell death (PubMed:12062018). The interaction with ATXN1 CC mutant reduces levels of phosphorylated RNA polymerase II large subunit CC (PubMed:12062018). Involved in the assembly of cytoplasmic stress CC granule, possibly by participating in the transport of neuronal RNA CC granules (PubMed:21933836). Also acts as an innate immune sensor of CC infection by retroviruses, such as HIV, by detecting the presence of CC reverse-transcribed DNA in the cytosol (PubMed:26046437). Directly CC binds retroviral reverse-transcribed DNA in the cytosol and interacts CC with CGAS, leading to activate the cGAS-STING signaling pathway, CC triggering type-I interferon production (PubMed:26046437). CC {ECO:0000269|PubMed:10198427, ECO:0000269|PubMed:10332029, CC ECO:0000269|PubMed:12062018, ECO:0000269|PubMed:20410308, CC ECO:0000269|PubMed:21933836, ECO:0000269|PubMed:23512658, CC ECO:0000269|PubMed:26046437}. CC -!- SUBUNIT: Interacts with POU3F2/Brn-2, ATXN1, TXNL4A, HTT and AR CC (PubMed:10332029, PubMed:10873650, PubMed:19303059, PubMed:24781215). CC Interaction with ATXN1 correlates positively with the length of the CC polyglutamine tract (PubMed:12062018). Interacts with RNA polymerase II CC large subunit in a phosphorylation-dependent manner (PubMed:12062018). CC Forms a ternary complex with ATXN1 mutant and phosphorylated RNA CC polymerase II (PubMed:12062018). Interacts (via C-terminus) with TXNL4A CC and CD2BP2 (PubMed:10873650, PubMed:19303059, PubMed:24781215). CC Interacts (via WW domain) with ATN1 and SF3B1, and may interact with CC additional splice factors (PubMed:20410308, PubMed:23512658). Interacts CC (via WW domain) with WBP11; Leading to reduce interaction between PQBP1 CC and TXNL4A (PubMed:20410308, PubMed:23512658, PubMed:27314904). CC Interacts with CAPRIN1 (PubMed:21933836). Interacts with DDX1 CC (PubMed:21933836). Interacts with SFPQ (PubMed:21933836). Interacts CC with KHSRP (PubMed:21933836). {ECO:0000269|PubMed:10332029, CC ECO:0000269|PubMed:10873650, ECO:0000269|PubMed:12062018, CC ECO:0000269|PubMed:19303059, ECO:0000269|PubMed:20410308, CC ECO:0000269|PubMed:21933836, ECO:0000269|PubMed:23512658, CC ECO:0000269|PubMed:24781215, ECO:0000269|PubMed:27314904, CC ECO:0000269|PubMed:9875212}. CC -!- INTERACTION: CC O60828; P54253: ATXN1; NbExp=3; IntAct=EBI-713867, EBI-930964; CC O60828; Q08379: GOLGA2; NbExp=6; IntAct=EBI-713867, EBI-618309; CC O60828; P42858: HTT; NbExp=3; IntAct=EBI-713867, EBI-466029; CC O60828; Q9BRK4: LZTS2; NbExp=6; IntAct=EBI-713867, EBI-741037; CC O60828; Q15691: MAPRE1; NbExp=6; IntAct=EBI-713867, EBI-1004115; CC O60828; Q9Y2W2: WBP11; NbExp=13; IntAct=EBI-713867, EBI-714455; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10198427, CC ECO:0000269|PubMed:10332029, ECO:0000269|PubMed:12062018, CC ECO:0000269|PubMed:23512658}. Nucleus speckle CC {ECO:0000250|UniProtKB:Q91VJ5}. Cytoplasmic granule CC {ECO:0000269|PubMed:21933836}. Note=Colocalizes with SRSF2 in nuclear CC speckles (By similarity). Colocalized with POU3F2 (PubMed:10332029). CC Colocalized with ATXN1 in nuclear inclusion bodies (PubMed:12062018). CC Localizes to cytoplasmic stress granules (PubMed:21933836). CC {ECO:0000250|UniProtKB:Q91VJ5, ECO:0000269|PubMed:10332029, CC ECO:0000269|PubMed:12062018, ECO:0000269|PubMed:21933836}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=10; CC Name=1; Synonyms=PQBP-1; CC IsoId=O60828-1; Sequence=Displayed; CC Name=2; CC IsoId=O60828-2; Sequence=VSP_015909; CC Name=3; Synonyms=PQBP-1b/c; CC IsoId=O60828-3; Sequence=VSP_015908, VSP_015910; CC Name=4; Synonyms=PQBP-1d; CC IsoId=O60828-4; Sequence=VSP_015903; CC Name=5; CC IsoId=O60828-5; Sequence=VSP_015900; CC Name=6; CC IsoId=O60828-6; Sequence=VSP_015906, VSP_015907; CC Name=7; CC IsoId=O60828-7; Sequence=VSP_015904, VSP_015905; CC Name=8; Synonyms=PQBP-1a; CC IsoId=O60828-8; Sequence=VSP_015896, VSP_015902; CC Name=9; CC IsoId=O60828-9; Sequence=VSP_015899, VSP_015901; CC Name=10; CC IsoId=O60828-10; Sequence=VSP_015897, VSP_015898; CC -!- TISSUE SPECIFICITY: Widely expressed with high level in heart, skeletal CC muscle, pancreas, spleen, thymus, prostate, ovary, small intestine and CC peripheral blood leukocytes. {ECO:0000269|PubMed:10198427, CC ECO:0000269|PubMed:10332029}. CC -!- DOMAIN: The WW domain may play a role as a transcriptional activator CC directly or via association with the transcription machinery. The WW CC domain mediates interaction with WBP11, ATN1, SF3B1 and the C-terminal CC domain of the RNA polymerase II large subunit. CC {ECO:0000269|PubMed:20410308, ECO:0000269|PubMed:24781215}. CC -!- DOMAIN: Except for the WW domain, the protein is intrinsically CC disordered. {ECO:0000269|PubMed:19303059, ECO:0000269|PubMed:24781215}. CC -!- DISEASE: Renpenning syndrome 1 (RENS1) [MIM:309500]: An X-linked CC syndrome characterized by intellectual disability, microcephaly, short CC stature, and small testes. The craniofacies tends to be narrow and tall CC with upslanting palpebral fissures, abnormal nasal configuration, CC cupped ears, and short philtrum. The nose may appear long or bulbous, CC with overhanging columella. Less consistent manifestations include CC ocular colobomas, cardiac malformations, cleft palate, and anal CC anomalies. {ECO:0000269|PubMed:14634649, ECO:0000269|PubMed:16740914, CC ECO:0000269|PubMed:20410308, ECO:0000269|PubMed:21315190, CC ECO:0000269|PubMed:23512658, ECO:0000269|PubMed:26046437}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ242829; CAB44309.1; -; mRNA. DR EMBL; AB016533; BAA76400.1; -; mRNA. DR EMBL; AB041832; BAB16702.1; -; Genomic_DNA. DR EMBL; AB041832; BAB16703.1; -; Genomic_DNA. DR EMBL; AB041832; BAB16704.1; -; Genomic_DNA. DR EMBL; AB041832; BAB16705.1; -; Genomic_DNA. DR EMBL; AB041833; BAB16706.1; -; mRNA. DR EMBL; AB041834; BAB16707.1; -; mRNA. DR EMBL; AB041835; BAB16708.1; -; mRNA. DR EMBL; AB041836; BAB16709.1; -; mRNA. DR EMBL; AJ973593; CAJ00537.1; -; mRNA. DR EMBL; AJ973594; CAJ00538.1; -; mRNA. DR EMBL; AJ973595; CAJ00539.1; -; mRNA. DR EMBL; AJ973596; CAJ00540.1; -; mRNA. DR EMBL; AJ973597; CAJ00541.1; -; mRNA. DR EMBL; AJ973598; CAJ00542.1; -; mRNA. DR EMBL; AJ973599; CAJ00543.1; -; mRNA. DR EMBL; AJ973600; CAJ00544.1; -; mRNA. DR EMBL; AJ973601; CAJ00545.1; -; mRNA. DR EMBL; AJ973602; CAJ00546.1; -; mRNA. DR EMBL; AJ973603; CAJ00547.1; -; mRNA. DR EMBL; AJ973605; CAJ00548.1; -; mRNA. DR EMBL; AJ973606; CAJ00549.1; -; mRNA. DR EMBL; AJ973607; CAJ00550.1; -; mRNA. DR EMBL; AJ005893; CAA06750.1; -; mRNA. DR EMBL; AC233300; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC012358; AAH12358.1; -; mRNA. DR CCDS; CCDS14309.1; -. [O60828-1] DR CCDS; CCDS55412.1; -. [O60828-4] DR RefSeq; NP_001027553.1; NM_001032381.1. [O60828-1] DR RefSeq; NP_001027554.1; NM_001032382.1. [O60828-1] DR RefSeq; NP_001027555.1; NM_001032383.1. [O60828-1] DR RefSeq; NP_001027556.1; NM_001032384.1. [O60828-1] DR RefSeq; NP_001161461.1; NM_001167989.1. [O60828-2] DR RefSeq; NP_001161462.1; NM_001167990.1. DR RefSeq; NP_001161464.1; NM_001167992.1. [O60828-5] DR RefSeq; NP_005701.1; NM_005710.2. [O60828-1] DR RefSeq; NP_652766.1; NM_144495.2. [O60828-4] DR RefSeq; XP_005272628.1; XM_005272571.3. [O60828-2] DR RefSeq; XP_005272629.1; XM_005272572.4. [O60828-4] DR RefSeq; XP_011542186.1; XM_011543884.2. [O60828-1] DR RefSeq; XP_016884696.1; XM_017029207.1. [O60828-2] DR PDB; 4BWQ; X-ray; 2.10 A; B/D/F/H=223-265. DR PDB; 4BWS; X-ray; 2.50 A; B/E=229-265. DR PDB; 4CDO; X-ray; 2.50 A; A/C=223-265. DR PDBsum; 4BWQ; -. DR PDBsum; 4BWS; -. DR PDBsum; 4CDO; -. DR AlphaFoldDB; O60828; -. DR SASBDB; O60828; -. DR SMR; O60828; -. DR BioGRID; 115393; 98. DR IntAct; O60828; 45. DR MINT; O60828; -. DR STRING; 9606.ENSP00000498362; -. DR GlyGen; O60828; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; O60828; -. DR PhosphoSitePlus; O60828; -. DR SwissPalm; O60828; -. DR BioMuta; PQBP1; -. DR jPOST; O60828; -. DR MassIVE; O60828; -. DR PaxDb; 9606-ENSP00000218224; -. DR PeptideAtlas; O60828; -. DR ProteomicsDB; 11217; -. DR ProteomicsDB; 49611; -. [O60828-1] DR ProteomicsDB; 49612; -. [O60828-10] DR ProteomicsDB; 49613; -. [O60828-2] DR ProteomicsDB; 49614; -. [O60828-3] DR ProteomicsDB; 49615; -. [O60828-4] DR ProteomicsDB; 49616; -. [O60828-5] DR ProteomicsDB; 49617; -. [O60828-6] DR ProteomicsDB; 49618; -. [O60828-7] DR ProteomicsDB; 49619; -. [O60828-8] DR ProteomicsDB; 49620; -. [O60828-9] DR Pumba; O60828; -. DR TopDownProteomics; O60828-1; -. [O60828-1] DR TopDownProteomics; O60828-2; -. [O60828-2] DR Antibodypedia; 454; 162 antibodies from 25 providers. DR DNASU; 10084; -. DR Ensembl; ENST00000218224.9; ENSP00000218224.4; ENSG00000102103.18. [O60828-1] DR Ensembl; ENST00000247140.8; ENSP00000247140.4; ENSG00000102103.18. [O60828-4] DR Ensembl; ENST00000376563.6; ENSP00000365747.1; ENSG00000102103.18. [O60828-1] DR Ensembl; ENST00000376566.8; ENSP00000365750.4; ENSG00000102103.18. [O60828-4] DR Ensembl; ENST00000396763.6; ENSP00000379985.1; ENSG00000102103.18. [O60828-1] DR Ensembl; ENST00000443648.6; ENSP00000414861.2; ENSG00000102103.18. [O60828-1] DR Ensembl; ENST00000447146.7; ENSP00000391759.2; ENSG00000102103.18. [O60828-1] DR Ensembl; ENST00000465859.2; ENSP00000508445.1; ENSG00000102103.18. [O60828-7] DR Ensembl; ENST00000470062.5; ENSP00000509874.1; ENSG00000102103.18. [O60828-6] DR Ensembl; ENST00000472742.6; ENSP00000509191.1; ENSG00000102103.18. [O60828-6] DR Ensembl; ENST00000651767.1; ENSP00000498362.1; ENSG00000102103.18. [O60828-1] DR Ensembl; ENST00000692023.1; ENSP00000509927.1; ENSG00000102103.18. [O60828-9] DR Ensembl; ENST00000710032.1; ENSP00000518005.1; ENSG00000292208.1. [O60828-1] DR Ensembl; ENST00000710033.1; ENSP00000518006.1; ENSG00000292208.1. [O60828-4] DR Ensembl; ENST00000710035.1; ENSP00000518007.1; ENSG00000292208.1. [O60828-1] DR Ensembl; ENST00000710037.1; ENSP00000518008.1; ENSG00000292208.1. [O60828-9] DR Ensembl; ENST00000710038.1; ENSP00000518009.1; ENSG00000292208.1. [O60828-1] DR Ensembl; ENST00000710039.1; ENSP00000518010.1; ENSG00000292208.1. [O60828-4] DR Ensembl; ENST00000710041.1; ENSP00000518011.1; ENSG00000292208.1. [O60828-6] DR Ensembl; ENST00000710042.1; ENSP00000518012.1; ENSG00000292208.1. [O60828-1] DR Ensembl; ENST00000710043.1; ENSP00000518013.1; ENSG00000292208.1. [O60828-6] DR Ensembl; ENST00000710044.1; ENSP00000518014.1; ENSG00000292208.1. [O60828-1] DR Ensembl; ENST00000710046.1; ENSP00000518015.1; ENSG00000292208.1. [O60828-1] DR Ensembl; ENST00000710049.1; ENSP00000518017.1; ENSG00000292208.1. [O60828-7] DR GeneID; 10084; -. DR KEGG; hsa:10084; -. DR MANE-Select; ENST00000447146.7; ENSP00000391759.2; NM_001032382.2; NP_001027554.1. DR UCSC; uc004dle.4; human. [O60828-1] DR UCSC; uc064zca.1; human. DR AGR; HGNC:9330; -. DR CTD; 10084; -. DR DisGeNET; 10084; -. DR GeneCards; PQBP1; -. DR HGNC; HGNC:9330; PQBP1. DR HPA; ENSG00000102103; Low tissue specificity. DR MalaCards; PQBP1; -. DR MIM; 300463; gene. DR MIM; 309500; phenotype. DR neXtProt; NX_O60828; -. DR OpenTargets; ENSG00000102103; -. DR Orphanet; 93946; Hamel cerebro-palato-cardiac syndrome. DR Orphanet; 93947; X-linked intellectual disability, Golabi-Ito-Hall type. DR Orphanet; 93945; X-linked intellectual disability, Porteous type. DR Orphanet; 93950; X-linked intellectual disability, Sutherland-Haan type. DR PharmGKB; PA33693; -. DR VEuPathDB; HostDB:ENSG00000102103; -. DR eggNOG; KOG3427; Eukaryota. DR GeneTree; ENSGT00950000183102; -. DR HOGENOM; CLU_043596_1_0_1; -. DR InParanoid; O60828; -. DR OMA; YNIYHEC; -. DR OrthoDB; 5403339at2759; -. DR PhylomeDB; O60828; -. DR TreeFam; TF320689; -. DR PathwayCommons; O60828; -. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR SignaLink; O60828; -. DR BioGRID-ORCS; 10084; 81 hits in 792 CRISPR screens. DR ChiTaRS; PQBP1; human. DR EvolutionaryTrace; O60828; -. DR GeneWiki; PQBP1; -. DR GenomeRNAi; 10084; -. DR Pharos; O60828; Tbio. DR PRO; PR:O60828; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; O60828; protein. DR Bgee; ENSG00000102103; Expressed in left ovary and 209 other cell types or tissues. DR ExpressionAtlas; O60828; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:Ensembl. DR GO; GO:0071598; C:neuronal ribonucleoprotein granule; IEA:Ensembl. DR GO; GO:0016604; C:nuclear body; IBA:GO_Central. DR GO; GO:0016607; C:nuclear speck; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; TAS:ProtInc. DR GO; GO:0003677; F:DNA binding; TAS:ProtInc. DR GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB. DR GO; GO:0043021; F:ribonucleoprotein complex binding; IDA:MGI. DR GO; GO:0003713; F:transcription coactivator activity; TAS:ProtInc. DR GO; GO:0002218; P:activation of innate immune response; IDA:UniProtKB. DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IMP:UniProtKB. DR GO; GO:0071360; P:cellular response to exogenous dsRNA; IDA:UniProtKB. DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB. DR GO; GO:0002230; P:positive regulation of defense response to virus by host; IDA:UniProtKB. DR GO; GO:0032481; P:positive regulation of type I interferon production; IDA:UniProtKB. DR GO; GO:0048814; P:regulation of dendrite morphogenesis; IEA:Ensembl. DR GO; GO:0006355; P:regulation of DNA-templated transcription; TAS:ProtInc. DR GO; GO:0043484; P:regulation of RNA splicing; IMP:MGI. DR DisProt; DP01308; -. DR FunFam; 3.40.30.10:FF:000140; polyglutamine-binding protein 1 isoform X1; 1. DR Gene3D; 2.20.70.10; -; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. DR IDEAL; IID00187; -. DR InterPro; IPR001202; WW_dom. DR InterPro; IPR036020; WW_dom_sf. DR PANTHER; PTHR28145; 12 KDA HEAT SHOCK PROTEIN; 1. DR PANTHER; PTHR28145:SF1; 12 KDA HEAT SHOCK PROTEIN; 1. DR SMART; SM00456; WW; 1. DR SUPFAM; SSF51045; WW domain; 1. DR PROSITE; PS50020; WW_DOMAIN_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Direct protein sequencing; Immunity; KW Innate immunity; Intellectual disability; mRNA processing; mRNA splicing; KW Nucleus; Phosphoprotein; Proteomics identification; Reference proteome; KW Repeat; Transcription; Transcription regulation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.8" FT CHAIN 2..265 FT /note="Polyglutamine-binding protein 1" FT /id="PRO_0000076089" FT DOMAIN 46..80 FT /note="WW" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224" FT REPEAT 104..110 FT /note="1-1" FT REPEAT 111..117 FT /note="1-2" FT REPEAT 118..124 FT /note="1-3" FT REPEAT 125..131 FT /note="1-4" FT REPEAT 132..138 FT /note="1-5" FT REPEAT 139..140 FT /note="2-1" FT REPEAT 141..142 FT /note="2-2" FT REPEAT 143..144 FT /note="2-3" FT REPEAT 150..151 FT /note="3-1" FT REPEAT 152..153 FT /note="3-2" FT REPEAT 154..155 FT /note="3-3" FT REPEAT 156..157 FT /note="3-4" FT REPEAT 158..159 FT /note="3-5" FT REPEAT 160..161 FT /note="3-6" FT REPEAT 162..163 FT /note="3-7" FT REGION 94..265 FT /note="Disordered" FT /evidence="ECO:0000269|PubMed:19303059" FT REGION 104..138 FT /note="5 X 7 AA approximate tandem repeats of D-R-[SG]-H-D- FT K-S" FT REGION 139..144 FT /note="3 X 2 AA tandem repeats of [DE]-R" FT REGION 150..163 FT /note="7 X 2 AA tandem repeats of [DE]-R" FT REGION 245..255 FT /note="Important for interaction with TXNL4A" FT COMPBIAS 77..92 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 93..204 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 94 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 247 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT VAR_SEQ 55..73 FT /note="VFDPSCGLPYYWNADTDLV -> RAPLLLECRHRPCILALPT (in FT isoform 8)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_015896" FT VAR_SEQ 60 FT /note="C -> W (in isoform 10)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_015897" FT VAR_SEQ 61..265 FT /note="Missing (in isoform 10)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_015898" FT VAR_SEQ 61..67 FT /note="GLPYYWN -> PGWSAMV (in isoform 9)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_015899" FT VAR_SEQ 68..265 FT /note="Missing (in isoform 9)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_015901" FT VAR_SEQ 68..167 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_015900" FT VAR_SEQ 74..265 FT /note="Missing (in isoform 8)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_015902" FT VAR_SEQ 98..192 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:11163963, ECO:0000303|Ref.4" FT /id="VSP_015903" FT VAR_SEQ 99..128 FT /note="AEEKLDRSHDKSDRGHDKSDRSHEKLDRGH -> LCPQMLKKSWTGAMTSRT FT GAMTSRTAAMRN (in isoform 7)" FT /evidence="ECO:0000303|PubMed:11163963" FT /id="VSP_015904" FT VAR_SEQ 129..265 FT /note="Missing (in isoform 7)" FT /evidence="ECO:0000303|PubMed:11163963" FT /id="VSP_015905" FT VAR_SEQ 149 FT /note="V -> Q (in isoform 6)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_015906" FT VAR_SEQ 150..265 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_015907" FT VAR_SEQ 193..224 FT /note="AVSRKDEELDPMDPSSYSDAPRGTWSTGLPKR -> GKLGRMGLGETNKVQG FT ALREEAFPQKDAWTWG (in isoform 3)" FT /evidence="ECO:0000303|PubMed:11163963, ECO:0000303|Ref.4" FT /id="VSP_015908" FT VAR_SEQ 193 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_015909" FT VAR_SEQ 225..265 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:11163963, ECO:0000303|Ref.4" FT /id="VSP_015910" FT VARIANT 65 FT /note="Y -> C (in RENS1; impairs interaction with WBP11, FT CGAS, SF3B1 and ATN1; dbSNP:rs121917899)" FT /evidence="ECO:0000269|PubMed:16740914, FT ECO:0000269|PubMed:20410308, ECO:0000269|PubMed:23512658, FT ECO:0000269|PubMed:26046437" FT /id="VAR_071063" FT VARIANT 224 FT /note="R -> W (in a colorectal cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036357" FT VARIANT 244 FT /note="P -> L (found in a patient with autism; uncertain FT significance; dbSNP:rs878853145)" FT /evidence="ECO:0000269|PubMed:26637798" FT /id="VAR_078695" FT MUTAGEN 52 FT /note="W->A: Enhances transcriptional activation. Reduces FT transcriptional activation; when associated with A-75. FT Markedly reduced transcriptional activation; when FT associated with A-64; A-65 and A-66. Abolishes FT transcriptional activation; when associated with A-64; A- FT 65; A-66 and A-75." FT /evidence="ECO:0000269|PubMed:10198427" FT MUTAGEN 64 FT /note="Y->A: No effect on transcriptional activation; when FT associated with A-65 and A-66. Markedly reduced FT transcriptional activation; when associated with A-52; A-65 FT and A-66. Abolishes transcriptional activation; when FT associated with A-52; A-65; A-66 and A-75." FT /evidence="ECO:0000269|PubMed:10198427" FT MUTAGEN 65 FT /note="Y->A: No effect on transcriptional activation; when FT associated with A-64 and A-66. Markedly reduced FT transcriptional activation; when associated with A-52; A-64 FT and A-66. Abolishes transcriptional activation; when FT associated with A-52; A-64; A-66 and A-75." FT /evidence="ECO:0000269|PubMed:10198427" FT MUTAGEN 66 FT /note="W->A: No effect on transcriptional activation; when FT associated with A-64 and A-65. Markedly reduced FT transcriptional activation; when associated with A-52; A-64 FT and A-65. Abolishes transcriptional activation; when FT associated with A-52; A-64; A-65 and A-75." FT /evidence="ECO:0000269|PubMed:10198427" FT MUTAGEN 75 FT /note="W->A: No effect on transcriptional activation. FT Reduces transcriptional activation; when associated with A- FT 52. Abolishes transcriptional activation; when associated FT with A-52; A-64; A-65 and A-66." FT /evidence="ECO:0000269|PubMed:10198427" FT MUTAGEN 78 FT /note="P->G: No effect on transcriptional activation." FT /evidence="ECO:0000269|PubMed:10198427" FT MUTAGEN 245 FT /note="Y->D: Abolishes interaction with TXNL4A." FT /evidence="ECO:0000269|PubMed:24781215" FT MUTAGEN 248 FT /note="P->D: Abolishes interaction with TXNL4A." FT /evidence="ECO:0000269|PubMed:24781215" FT MUTAGEN 251 FT /note="V->D: Abolishes interaction with TXNL4A." FT /evidence="ECO:0000269|PubMed:24781215" FT MUTAGEN 252 FT /note="L->D: Abolishes interaction with TXNL4A." FT /evidence="ECO:0000269|PubMed:24781215" FT MUTAGEN 253 FT /note="R->D: Strongly reduces affinity for TXNL4A." FT /evidence="ECO:0000269|PubMed:24781215" FT MUTAGEN 255 FT /note="N->D: Strongly reduces affinity for TXNL4A." FT /evidence="ECO:0000269|PubMed:24781215" FT CONFLICT 8 FT /note="Q -> L (in Ref. 4; CAJ00539)" FT /evidence="ECO:0000305" FT CONFLICT 57 FT /note="D -> N (in Ref. 4; CAJ00548)" FT /evidence="ECO:0000305" FT CONFLICT 107..113 FT /note="Missing (in Ref. 4; CAJ00538/CAJ00539/CAJ00540/ FT CAJ00541)" FT /evidence="ECO:0000305" FT CONFLICT 107 FT /note="H -> Q (in Ref. 4; CAJ00549)" FT /evidence="ECO:0000305" FT CONFLICT 147 FT /note="D -> G (in Ref. 4; CAJ00549)" FT /evidence="ECO:0000305" FT CONFLICT 198 FT /note="D -> G (in Ref. 4; CAJ00549)" FT /evidence="ECO:0000305" FT CONFLICT 236 FT /note="A -> V (in Ref. 4; CAJ00548)" FT /evidence="ECO:0000305" FT HELIX 248..258 FT /evidence="ECO:0007829|PDB:4BWQ" SQ 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 //