PQBP1_MOUSE
ID PQBP1_MOUSE Reviewed; 263 AA.
AC Q91VJ5; Q80WW2; Q9ER43; Q9QYY2;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Polyglutamine-binding protein 1;
DE Short=PQBP-1;
DE AltName: Full=38 kDa nuclear protein containing a WW domain;
DE Short=Npw38;
DE AltName: Full=Polyglutamine tract-binding protein 1;
GN Name=Pqbp1; Synonyms=Npw38;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF
RP 24-263.
RA Okazawa H.;
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary tumor;
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 [4]
RP TISSUE SPECIFICITY.
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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).
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 (By
CC similarity). Interacts with splicing-related factors via the
CC intrinsically disordered region and regulates alternative splicing of
CC target pre-mRNA species (PubMed:23512658). May suppress the ability of
CC POU3F2 to transactivate the DRD1 gene in a POU3F2 dependent manner (By
CC similarity). Can activate transcription directly or via association
CC with the transcription machinery (By similarity). May be involved in
CC ATXN1 mutant-induced cell death (By similarity). The interaction with
CC ATXN1 mutant reduces levels of phosphorylated RNA polymerase II large
CC subunit (By similarity). Involved in the assembly of cytoplasmic stress
CC granule, possibly by participating in the transport of neuronal RNA
CC granules (By similarity). Also acts as an innate immune sensor of
CC infection by retroviruses, by detecting the presence of reverse-
CC transcribed DNA in the cytosol (By similarity). Directly binds
CC retroviral reverse-transcribed DNA in the cytosol and interacts with
CC CGAS, leading to activate the cGAS-STING signaling pathway, triggering
CC type-I interferon production (By similarity).
CC {ECO:0000250|UniProtKB:O60828, ECO:0000269|PubMed:23512658}.
CC -!- SUBUNIT: Interacts with POU3F2/Brn-2, ATXN1, TXNL4A, HTT and AR.
CC Interaction with ATXN1 correlates positively with the length of the
CC polyglutamine tract. Interacts with RNA polymerase II large subunit in
CC a phosphorylation-dependent manner. Forms a ternary complex with ATXN1
CC mutant and phosphorylated RNA polymerase II. Interacts (via C-terminus)
CC with TXNL4A and CD2BP2. Interacts (via WW domain) with ATN1 and SF3B1,
CC and may interact with additional splice factors. Interacts (via WW
CC domain) with WBP11; Leading to reduce interaction between PQBP1 and
CC TXNL4A. Interacts with CAPRIN1. Interacts with DDX1. Interacts with
CC SFPQ. Interacts with KHSRP. {ECO:0000250|UniProtKB:O60828}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23512658}. Nucleus
CC speckle {ECO:0000269|PubMed:23512658}. Cytoplasmic granule
CC {ECO:0000250|UniProtKB:O60828}. Note=Colocalizes with SRSF2 in nuclear
CC speckles (PubMed:23512658). Colocalized with POU3F2. Colocalized with
CC ATXN1 in nuclear inclusion bodies. Localizes to cytoplasmic stress
CC granules (By similarity). {ECO:0000250|UniProtKB:O60828,
CC ECO:0000269|PubMed:23512658}.
CC -!- TISSUE SPECIFICITY: Detected in brain cortex and hippocampus neurons
CC (at protein level). Expressed in brain with high level in cerebellar
CC cortex, hippocampus and olfactory bulb. {ECO:0000269|PubMed:10332029,
CC ECO:0000269|PubMed:23512658}.
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:0000250|UniProtKB:O60828}.
CC -!- DOMAIN: Except for the WW domain, the protein is intrinsically
CC disordered. {ECO:0000250|UniProtKB:O60828}.
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DR EMBL; AJ250406; CAB59205.1; -; mRNA.
DR EMBL; AJ296289; CAC15062.1; -; Genomic_DNA.
DR EMBL; AK077652; BAC36928.1; -; mRNA.
DR EMBL; BC009657; AAH09657.1; -; mRNA.
DR EMBL; BC051673; AAH51673.1; -; mRNA.
DR CCDS; CCDS29977.1; -.
DR RefSeq; NP_001239457.1; NM_001252528.1.
DR RefSeq; NP_001239458.1; NM_001252529.1.
DR RefSeq; NP_062351.2; NM_019478.4.
DR RefSeq; XP_006527717.1; XM_006527654.1.
DR AlphaFoldDB; Q91VJ5; -.
DR SMR; Q91VJ5; -.
DR BioGRID; 207696; 30.
DR IntAct; Q91VJ5; 25.
DR STRING; 10090.ENSMUSP00000111319; -.
DR iPTMnet; Q91VJ5; -.
DR PhosphoSitePlus; Q91VJ5; -.
DR EPD; Q91VJ5; -.
DR jPOST; Q91VJ5; -.
DR MaxQB; Q91VJ5; -.
DR PaxDb; Q91VJ5; -.
DR PRIDE; Q91VJ5; -.
DR ProteomicsDB; 291732; -.
DR Antibodypedia; 454; 170 antibodies from 26 providers.
DR DNASU; 54633; -.
DR Ensembl; ENSMUST00000033497; ENSMUSP00000033497; ENSMUSG00000031157.
DR Ensembl; ENSMUST00000115654; ENSMUSP00000111318; ENSMUSG00000031157.
DR Ensembl; ENSMUST00000115655; ENSMUSP00000111319; ENSMUSG00000031157.
DR GeneID; 54633; -.
DR KEGG; mmu:54633; -.
DR UCSC; uc009snd.2; mouse.
DR CTD; 10084; -.
DR MGI; MGI:1859638; Pqbp1.
DR VEuPathDB; HostDB:ENSMUSG00000031157; -.
DR eggNOG; KOG3427; Eukaryota.
DR GeneTree; ENSGT00950000183102; -.
DR HOGENOM; CLU_043596_1_0_1; -.
DR InParanoid; Q91VJ5; -.
DR OMA; GCPNKYN; -.
DR OrthoDB; 1547704at2759; -.
DR PhylomeDB; Q91VJ5; -.
DR TreeFam; TF320689; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 54633; 4 hits in 74 CRISPR screens.
DR PRO; PR:Q91VJ5; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q91VJ5; protein.
DR Bgee; ENSMUSG00000031157; Expressed in saccule of membranous labyrinth and 273 other tissues.
DR ExpressionAtlas; Q91VJ5; baseline and differential.
DR Genevisible; Q91VJ5; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0097546; C:ciliary base; ISO:MGI.
DR GO; GO:0005929; C:cilium; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:MGI.
DR GO; GO:0071598; C:neuronal ribonucleoprotein granule; IDA:MGI.
DR GO; GO:0016604; C:nuclear body; IBA:GO_Central.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; ISO:MGI.
DR GO; GO:0002218; P:activation of innate immune response; ISS:UniProtKB.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IMP:UniProtKB.
DR GO; GO:0071360; P:cellular response to exogenous dsRNA; ISS:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0031175; P:neuron projection development; IMP:UniProtKB.
DR GO; GO:0002230; P:positive regulation of defense response to virus by host; ISS:UniProtKB.
DR GO; GO:1902857; P:positive regulation of non-motile cilium assembly; ISO:MGI.
DR GO; GO:0032481; P:positive regulation of type I interferon production; ISS:UniProtKB.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; IMP:MGI.
DR GO; GO:0043484; P:regulation of RNA splicing; ISO:MGI.
DR CDD; cd00201; WW; 1.
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 Immunity; Innate immunity; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..263
FT /note="Polyglutamine-binding protein 1"
FT /id="PRO_0000076090"
FT DOMAIN 46..80
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT REPEAT 104..110
FT /note="1-1; approximate"
FT REPEAT 111..117
FT /note="1-2"
FT REPEAT 118..124
FT /note="1-3; approximate"
FT REPEAT 125..131
FT /note="1-4; approximate"
FT REPEAT 132..138
FT /note="1-5; approximate"
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 REGION 94..263
FT /note="Disordered"
FT /evidence="ECO:0000250|UniProtKB:O60828"
FT REGION 104..138
FT /note="5 X 7 AA approximate tandem repeats of D-R-[NS]-H-E-
FT K-S"
FT REGION 139..144
FT /note="3 X 2 AA tandem repeats of [DE]-R"
FT REGION 150..161
FT /note="6 X 2 AA tandem repeats of [DE]-R"
FT REGION 243..253
FT /note="Important for interaction with TXNL4A"
FT /evidence="ECO:0000250|UniProtKB:O60828"
FT COMPBIAS 93..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60828"
FT CONFLICT 15
FT /note="G -> S (in Ref. 3; AAH51673)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="H -> L (in Ref. 1; CAB59205/CAC15062)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="A -> V (in Ref. 1; CAB59205/CAC15062)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 263 AA; 30597 MW; F62304963D34D22B CRC64;
MPLPVALQTR LAKRGILKHL EPEPEEEIIA EDYDDDPVDY EATRIEGLPP SWYKVFDPSC
GLPYYWNVET DLVSWLSPHD PNFVVTKSAK KVRNNNADAE DKSDRNLEKV DRNHEKSDRS
HEKPDRSHEK ADRNHEKNDR ERERNYDKVD RERDRDRERE RAFDKADREE GKDRRHHRRE
ELAPYPKNKK ATSRKDEELD PMDPSSYSDA PRGTWSTGLP KRNEAKTGAD TTAAGPLFQQ
RPYPSPGAVL RANAEASRTK QQD
