PQBP1_HUMAN
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 03-AUG-2022, entry version 191.
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:23512658, PubMed:20410308). 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:23512658, PubMed:20410308). Interacts
CC (via WW domain) with WBP11; Leading to reduce interaction between PQBP1
CC and TXNL4A (PubMed:23512658, PubMed:20410308, 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=11; 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; 77.
DR IntAct; O60828; 30.
DR MINT; O60828; -.
DR STRING; 9606.ENSP00000218224; -.
DR GlyGen; O60828; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O60828; -.
DR PhosphoSitePlus; O60828; -.
DR SwissPalm; O60828; -.
DR BioMuta; PQBP1; -.
DR EPD; O60828; -.
DR jPOST; O60828; -.
DR MassIVE; O60828; -.
DR MaxQB; O60828; -.
DR PaxDb; O60828; -.
DR PeptideAtlas; O60828; -.
DR PRIDE; 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 TopDownProteomics; O60828-1; -. [O60828-1]
DR TopDownProteomics; O60828-2; -. [O60828-2]
DR Antibodypedia; 454; 170 antibodies from 26 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 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 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; GCPNKYN; -.
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; 78 hits in 716 CRISPR screens.
DR ChiTaRS; PQBP1; human.
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 207 other tissues.
DR ExpressionAtlas; O60828; baseline and differential.
DR Genevisible; O60828; HS.
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:0043484; P:regulation of RNA splicing; IMP:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:ProtInc.
DR CDD; cd00201; WW; 1.
DR DisProt; DP01308; -.
DR IDEAL; IID00187; -.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF51045; SSF51045; 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; Reference proteome; Repeat; Transcription;
KW 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 (probable disease-associated variant found in
FT a patient with autism; 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
