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Q91VJ5

- PQBP1_MOUSE

UniProt

Q91VJ5 - PQBP1_MOUSE

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Protein

Polyglutamine-binding protein 1

Gene

Pqbp1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Probably functions as scaffold protein that is part of numerous complexes and thereby plays a role in pre-mRNA splicing, transcription regulation and neuron development. 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. May be involved in ATXN1 mutant-induced cell death. The interaction with ATXN1 mutant reduces levels of phosphorylated RNA polymerase II large subunit (By similarity). Required for normal alternative splicing of target pre-mRNA species (PubMed:23512658).By similarity1 Publication

GO - Molecular functioni

  1. ribonucleoprotein complex binding Source: Ensembl

GO - Biological processi

  1. alternative mRNA splicing, via spliceosome Source: UniProtKB
  2. neuron projection development Source: UniProtKB
  3. regulation of dendrite morphogenesis Source: MGI
  4. regulation of RNA splicing Source: Ensembl
  5. regulation of transcription, DNA-templated Source: UniProtKB-KW
  6. stress granule assembly Source: MGI
  7. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing, Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Polyglutamine-binding protein 1
Short name:
PQBP-1
Alternative name(s):
38 kDa nuclear protein containing a WW domain
Short name:
Npw38
Polyglutamine tract-binding protein 1
Gene namesi
Name:Pqbp1
Synonyms:Npw38
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome X

Organism-specific databases

MGIiMGI:1859638. Pqbp1.

Subcellular locationi

Nucleus 1 Publication. Nucleus speckle 1 Publication
Note: Colocalized with ATXN1 in nuclear inclusion bodies. Colocalized with POU3F2 (By similarity). Colocalizes with SRSF2 in nuclear speckles.By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytoplasmic stress granule Source: MGI
  3. neuronal ribonucleoprotein granule Source: MGI
  4. nuclear speck Source: UniProtKB
  5. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 263262Polyglutamine-binding protein 1PRO_0000076090Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei245 – 2451PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ91VJ5.
PaxDbiQ91VJ5.
PRIDEiQ91VJ5.

PTM databases

PhosphoSiteiQ91VJ5.

Expressioni

Tissue specificityi

Detected in brain cortex and hippocampus neurons (at protein level). Expressed in brain with high level in cerebellar cortex, hippocampus and olfactory bulb.2 Publications

Gene expression databases

BgeeiQ91VJ5.
CleanExiMM_PQBP1.
ExpressionAtlasiQ91VJ5. baseline and differential.
GenevestigatoriQ91VJ5.

Interactioni

Subunit structurei

Interacts with POU3F2/Brn-2, ATXN1, TXNL4A, HTT and AR. Interaction with ATXN1 correlates positively with the length of the polyglutamine tract. Interacts with RNA polymerase II large subunit in a phosphorylation-dependent manner. Forms a ternary complex with ATXN1 mutant and phosphorylated RNA polymerase II. Interacts (via C-terminus) with TXNL4A and CD2BP2. Interacts (via WW domain) with ATN1, WBP11 and SF3B1, and may interact with additional splice factors (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ91VJ5.
SMRiQ91VJ5. Positions 236-261.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 8035WWPROSITE-ProRule annotationAdd
BLAST
Repeati104 – 11071-1; approximate
Repeati111 – 11771-2
Repeati118 – 12471-3; approximate
Repeati125 – 13171-4; approximate
Repeati132 – 13871-5; approximate
Repeati139 – 14022-1
Repeati141 – 14222-2
Repeati143 – 14422-3
Repeati150 – 15123-1
Repeati152 – 15323-2
Repeati154 – 15523-3
Repeati156 – 15723-4
Repeati158 – 15923-5
Repeati160 – 16123-6

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni94 – 263170Intrinsically disorderedBy similarityAdd
BLAST
Regioni104 – 138355 X 7 AA approximate tandem repeats of D-R-[NS]-H-E-K-SAdd
BLAST
Regioni139 – 14463 X 2 AA tandem repeats of [DE]-R
Regioni150 – 161126 X 2 AA tandem repeats of [DE]-RAdd
BLAST
Regioni243 – 25311Important for interaction with TXNL4ABy similarityAdd
BLAST

Domaini

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 (By similarity).By similarity
Except for the WW domain, the protein is intrinsically disordered.By similarity

Sequence similaritiesi

Contains 1 WW domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG265480.
GeneTreeiENSGT00390000001905.
HOGENOMiHOG000231359.
HOVERGENiHBG053064.
InParanoidiQ91VJ5.
KOiK12865.
OMAiSHEKSDR.
OrthoDBiEOG7GJ6F7.
PhylomeDBiQ91VJ5.
TreeFamiTF320689.

Family and domain databases

InterProiIPR001202. WW_dom.
[Graphical view]
PfamiPF00397. WW. 1 hit.
[Graphical view]
SMARTiSM00456. WW. 1 hit.
[Graphical view]
SUPFAMiSSF51045. SSF51045. 1 hit.
PROSITEiPS50020. WW_DOMAIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q91VJ5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPLPVALQTR LAKRGILKHL EPEPEEEIIA EDYDDDPVDY EATRIEGLPP
60 70 80 90 100
SWYKVFDPSC GLPYYWNVET DLVSWLSPHD PNFVVTKSAK KVRNNNADAE
110 120 130 140 150
DKSDRNLEKV DRNHEKSDRS HEKPDRSHEK ADRNHEKNDR ERERNYDKVD
160 170 180 190 200
RERDRDRERE RAFDKADREE GKDRRHHRRE ELAPYPKNKK ATSRKDEELD
210 220 230 240 250
PMDPSSYSDA PRGTWSTGLP KRNEAKTGAD TTAAGPLFQQ RPYPSPGAVL
260
RANAEASRTK QQD
Length:263
Mass (Da):30,597
Last modified:December 1, 2001 - v1
Checksum:iF62304963D34D22B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151G → S in AAH51673. (PubMed:15489334)Curated
Sequence conflicti177 – 1771H → L in CAB59205. 1 PublicationCurated
Sequence conflicti177 – 1771H → L in CAC15062. 1 PublicationCurated
Sequence conflicti183 – 1831A → V in CAB59205. 1 PublicationCurated
Sequence conflicti183 – 1831A → V in CAC15062. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ250406 mRNA. Translation: CAB59205.1.
AJ296289 Genomic DNA. Translation: CAC15062.1.
AK077652 mRNA. Translation: BAC36928.1.
BC009657 mRNA. Translation: AAH09657.1.
BC051673 mRNA. Translation: AAH51673.1.
CCDSiCCDS29977.1.
RefSeqiNP_001239457.1. NM_001252528.1.
NP_001239458.1. NM_001252529.1.
NP_062351.2. NM_019478.4.
XP_006527717.1. XM_006527654.1.
UniGeneiMm.14616.

Genome annotation databases

EnsembliENSMUST00000033497; ENSMUSP00000033497; ENSMUSG00000031157.
ENSMUST00000115654; ENSMUSP00000111318; ENSMUSG00000031157.
ENSMUST00000115655; ENSMUSP00000111319; ENSMUSG00000031157.
GeneIDi54633.
KEGGimmu:54633.
UCSCiuc009snd.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ250406 mRNA. Translation: CAB59205.1 .
AJ296289 Genomic DNA. Translation: CAC15062.1 .
AK077652 mRNA. Translation: BAC36928.1 .
BC009657 mRNA. Translation: AAH09657.1 .
BC051673 mRNA. Translation: AAH51673.1 .
CCDSi CCDS29977.1.
RefSeqi NP_001239457.1. NM_001252528.1.
NP_001239458.1. NM_001252529.1.
NP_062351.2. NM_019478.4.
XP_006527717.1. XM_006527654.1.
UniGenei Mm.14616.

3D structure databases

ProteinModelPortali Q91VJ5.
SMRi Q91VJ5. Positions 236-261.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q91VJ5.

Proteomic databases

MaxQBi Q91VJ5.
PaxDbi Q91VJ5.
PRIDEi Q91VJ5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000033497 ; ENSMUSP00000033497 ; ENSMUSG00000031157 .
ENSMUST00000115654 ; ENSMUSP00000111318 ; ENSMUSG00000031157 .
ENSMUST00000115655 ; ENSMUSP00000111319 ; ENSMUSG00000031157 .
GeneIDi 54633.
KEGGi mmu:54633.
UCSCi uc009snd.2. mouse.

Organism-specific databases

CTDi 10084.
MGIi MGI:1859638. Pqbp1.

Phylogenomic databases

eggNOGi NOG265480.
GeneTreei ENSGT00390000001905.
HOGENOMi HOG000231359.
HOVERGENi HBG053064.
InParanoidi Q91VJ5.
KOi K12865.
OMAi SHEKSDR.
OrthoDBi EOG7GJ6F7.
PhylomeDBi Q91VJ5.
TreeFami TF320689.

Miscellaneous databases

NextBioi 311456.
PROi Q91VJ5.
SOURCEi Search...

Gene expression databases

Bgeei Q91VJ5.
CleanExi MM_PQBP1.
ExpressionAtlasi Q91VJ5. baseline and differential.
Genevestigatori Q91VJ5.

Family and domain databases

InterProi IPR001202. WW_dom.
[Graphical view ]
Pfami PF00397. WW. 1 hit.
[Graphical view ]
SMARTi SM00456. WW. 1 hit.
[Graphical view ]
SUPFAMi SSF51045. SSF51045. 1 hit.
PROSITEi PS50020. WW_DOMAIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Okazawa H.
    Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-263.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and FVB/N.
    Tissue: Mammary tumor.
  4. "PQBP-1, a novel polyglutamine tract binding protein, inhibits transcription activation by Brn-2 and affects cell survival."
    Waragai M., Lammers C.-H., Takeuchi S., Imafuku I., Udagawa Y., Kanazawa I., Kawabata M., Mouradian M.M., Okazawa H.
    Hum. Mol. Genet. 8:977-987(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  5. "PQBP1, a factor linked to intellectual disability, affects alternative splicing associated with neurite outgrowth."
    Wang Q., Moore M.J., Adelmant G., Marto J.A., Silver P.A.
    Genes Dev. 27:615-626(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiPQBP1_MOUSE
AccessioniPrimary (citable) accession number: Q91VJ5
Secondary accession number(s): Q80WW2, Q9ER43, Q9QYY2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: December 1, 2001
Last modified: November 26, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3