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Polyglutamine-binding protein 1 (PQBP-1) (38 kDa nuclear protein containing a WW domain) (Npw38) (Polyglutamine tract-binding protein 1)

 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.
10-OCT-2018, entry version 166.
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.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
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; 25.
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; -.
HOGENOM; HOG000231359; -.
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; Expressed in 231 organ(s), highest expression level in ectocervix.
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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