| Type |
Details |
Score |
| GXD Expression |
| Probe: |
MGI:6197243 |
| Assay Type: |
Immunohistochemistry |
| Annotation Date: |
2018-09-10 |
| Strength: |
Present |
| Sex: |
Not Specified |
| Emaps: |
EMAPS:1689622 |
| Pattern: |
Regionally restricted |
| Stage: |
TS22 |
| Assay Id: |
MGI:6197255 |
| Age: |
embryonic day 14.5 |
| Image: |
2J |
| Note: |
Expression was detected in the mdDA (mesodiencephalic dopaminergic) domain. Co-expression with Pspc1 was noted. |
| Specimen Label: |
2J |
| Detected: |
true |
| Specimen Num: |
10 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
This entry represents the RNA recognition motif 1 (RRM1) of paraspeckle component 1 (PSP1). PSP1 (also known as PSPC1) is a novel nucleolar factor that accumulates within a new nucleoplasmic compartment, termed paraspeckles, and diffusely distributes in the nucleoplasm []. PSP1 belongs to the DBHS (Drosophila behavior human splicing) family. It is ubiquitously expressed and highly conserved in vertebrates. Its cellular function remains unknown currently; however, PSPC1 forms a novel heterodimer with the nuclear protein p54nrb, also known as non-POU domain-containing octamer-binding protein (NonO), which localizes to paraspeckles in an RNA-dependent manner []. PSPC1 contains two conserved RNA recognition motifs (RRMs) at the N terminus.DBHS (Drosophila behavior human splicing) family are characterised by a core domain arrangement consisting of tandem RNA recognition motifs (RRMs), a ~100 amino acid coiled-coil domain, and a conserved intervening sequence referred to as a NONA/ParaSpeckle (NOPS) domain. Its members include p54nrb (also known as NONO), PTB-associated splicing factor/splicing factor proline-glutamine rich (PSF or SFPQ) and PSPC1 (paraspeckle protein component 1). They are found in the nucleoplasm and can be triggered by binding to local high concentrations of various nucleic acids to form microscopically visible nuclear bodies, paraspeckles or large complexes such as DNA repair foci. They may also function cytoplasmically and on the cell surface in defined cell types. All three DBHS proteins are conserved throughout vertebrate species, while flies, worms, and yeast express a single DBHS protein [, ]. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
This entry represents the RNA recognition motif 2 (RRM2) of paraspeckle component 1 (PSP1).PSP1 (also known as PSPC1) is a novel nucleolar factor that accumulates within a new nucleoplasmic compartment, termed paraspeckles, and diffusely distributes in the nucleoplasm []. PSP1 belongs to the DBHS (Drosophila behavior human splicing) family. It is ubiquitously expressed and highly conserved in vertebrates. Its cellular function remains unknown currently; however, PSPC1 forms a novel heterodimer with the nuclear protein p54nrb, also known as non-POU domain-containing octamer-binding protein (NonO), which localizes to paraspeckles in an RNA-dependent manner []. PSPC1 contains two conserved RNA recognition motifs (RRMs) at the N terminus.DBHS (Drosophila behavior human splicing) family are characterised by a core domain arrangement consisting of tandem RNA recognition motifs (RRMs), a ~100 amino acid coiled-coil domain, and a conserved intervening sequence referredto as a NONA/ParaSpeckle (NOPS) domain. Its members include p54nrb (also known as NONO), PTB-associated splicing factor/splicing factor proline-glutamine rich (PSF or SFPQ) and PSPC1 (paraspeckle protein component 1). They are found in the nucleoplasm and can be triggered by binding to local high concentrations of various nucleic acids to form microscopically visible nuclear bodies, paraspeckles or large complexes such as DNA repair foci. They may also function cytoplasmically and on the cell surface in defined cell types. All three DBHS proteins are conserved throughout vertebrate species, while flies, worms, and yeast express a single DBHS protein [, ]. |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Fox AH |
| Year: |
2002 |
| Journal: |
Curr Biol |
| Title: |
Paraspeckles: a novel nuclear domain. |
| Volume: |
12 |
| Issue: |
1 |
| Pages: |
13-25 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Fox AH |
| Year: |
2005 |
| Journal: |
Mol Biol Cell |
| Title: |
P54nrb forms a heterodimer with PSP1 that localizes to paraspeckles in an RNA-dependent manner. |
| Volume: |
16 |
| Issue: |
11 |
| Pages: |
5304-15 |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
261
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
This domain is found in the DBHS (Drosophila behavior human splicing) family members. It is C-terminal to the RNA recognition motifs (RRMs).DBHS (Drosophila behavior human splicing) family are characterised by a core domain arrangement consisting of tandem RNA recognition motifs (RRMs), a conserved intervening sequence referred to as a NONA/ParaSpeckle (NOPS) domain, and a ~100 amino acid coiled-coil domain. Its members include p54nrb (also known as NONO), PTB-associated splicing factor/splicing factor proline-glutamine rich (PSF or SFPQ) and PSPC1 (paraspeckle protein component 1). They are found in the nucleoplasm and can be triggered by binding to local high concentrations of various nucleic acids to form microscopically visible nuclear bodies, paraspeckles or large complexes such as DNA repair foci. They may also function cytoplasmically and on the cell surface in defined cell types. All three DBHS proteins are conserved throughout vertebrate species, while flies, worms, and yeast express a single DBHS protein [, ]. |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Yarosh CA |
| Year: |
2015 |
| Journal: |
Wiley Interdiscip Rev RNA |
| Title: |
PSF: nuclear busy-body or nuclear facilitator? |
| Volume: |
6 |
| Issue: |
4 |
| Pages: |
351-67 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Knott GJ |
| Year: |
2016 |
| Journal: |
Nucleic Acids Res |
| Title: |
The DBHS proteins SFPQ, NONO and PSPC1: a multipurpose molecular scaffold. |
| Volume: |
44 |
| Issue: |
9 |
| Pages: |
3989-4004 |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
523
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Bladen CL |
| Year: |
2005 |
| Journal: |
J Biol Chem |
| Title: |
Identification of the polypyrimidine tract binding protein-associated splicing factor.p54(nrb) complex as a candidate DNA double-strand break rejoining factor. |
| Volume: |
280 |
| Issue: |
7 |
| Pages: |
5205-10 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Lu JY |
| Year: |
2015 |
| Journal: |
Mol Cell Biol |
| Title: |
p54nrb/NONO regulates cyclic AMP-dependent glucocorticoid production by modulating phosphodiesterase mRNA splicing and degradation. |
| Volume: |
35 |
| Issue: |
7 |
| Pages: |
1223-37 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Passon DM |
| Year: |
2012 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
Structure of the heterodimer of human NONO and paraspeckle protein component 1 and analysis of its role in subnuclear body formation. |
| Volume: |
109 |
| Issue: |
13 |
| Pages: |
4846-50 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
This entry represents the RNA recognition motif 1 (RRM1) of p54nrb. p54nrb (also known as NONO) belongs to the DBHS (Drosophila behavior human splicing) family. p54nrb is a multifunctional protein involved in numerous nuclear processes including transcription, splicing, and RNA export []. p54nrb binds both, single- and double-stranded RNA and DNA []. It forms a heterodimer with paraspeckle component 1 (PSPC1 or PSP1), localizing to paraspeckles in an RNA-dependent manner as well as with polypyrimidine tract-binding protein-associated-splicing factor (PSF) []. p54nrb contains two conserved RNA recognition motifs (RRMs) at the N terminus [, ].DBHS (Drosophila behavior human splicing) family are characterised by a core domain arrangement consisting of tandem RNA recognition motifs (RRMs), a conserved intervening sequence referred to as a NONA/ParaSpeckle (NOPS) domain, and a ~100 amino acid coiled-coil domain. Its members include p54nrb (also known as NONO), PTB-associated splicing factor/splicing factor proline-glutamine rich (PSF or SFPQ) and PSPC1 (paraspeckle protein component 1). They are found in the nucleoplasm and can be triggered by binding to local high concentrations of various nucleic acids to form microscopically visible nuclear bodies, paraspeckles or large complexes such as DNA repair foci. They may also function cytoplasmically and on the cell surface in defined cell types. All three DBHS proteins are conserved throughout vertebrate species, while flies, worms, and yeast express a single DBHS protein [, ]. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
This entry represents the RNA recognition motif 2 (RRM2) of p54nrb.p54nrb (also known as NONO) belongs to the DBHS (Drosophila behavior human splicing) family. p54nrb is a multifunctional protein involved in numerous nuclear processes including transcription, splicing, and RNA export []. p54nrb binds both, single- and double-stranded RNA and DNA []. It forms a heterodimer with paraspeckle component 1 (PSPC1 or PSP1), localizing to paraspeckles in an RNA-dependent manner as well as with polypyrimidine tract-binding protein-associated-splicing factor (PSF) []. p54nrb contains two conserved RNA recognition motifs (RRMs) at the N terminus [, ].DBHS (Drosophila behavior human splicing) family are characterised by a core domain arrangement consisting of tandem RNA recognition motifs (RRMs), a conserved intervening sequence referred to as a NONA/ParaSpeckle (NOPS) domain, and a ~100 amino acid coiled-coil domain. Its members include p54nrb (also known as NONO), PTB-associated splicing factor/splicing factor proline-glutamine rich (PSF or SFPQ) and PSPC1 (paraspeckle protein component 1). They are found in the nucleoplasm and can be triggered by binding to local high concentrations of various nucleic acids to form microscopically visible nuclear bodies, paraspeckles or large complexes such as DNA repair foci. They may also function cytoplasmically and on the cell surface in defined cell types. All three DBHS proteins are conserved throughout vertebrate species, while flies, worms, and yeast express a single DBHS protein [, ]. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
This entry represents the RNA recognition motif 1 (RRM1) of PSF.PSF is a member of the DBHS (Drosophila behavior human splicing) family. It participates in a wide range of gene regulatory processes and cellular response pathways. It has been shown to affect the alternative splicing of CD45 and Tau and regulate the 3' polyadenylation of mRNAs. It is often localised in the paraspeckles and may be involved in the nuclear retention of mRNAs. It is involved in translation and transcription. It can bind directly to DSBs and play a role in DNA repair. PSF can also be utilized as an essential host factor for viral RNA multiplication and replication [, ]. In addition to the common DHBS core, which encompasses RRM1 and RRM2, the protein-protein interaction NOPS domain and the coiled-coil domain, PSF features additional domains, such as a RGG motif and a proline-rich region in its N terminus []. DBHS (Drosophila behavior human splicing) family are characterised by a core domain arrangement consisting of tandem RNA recognition motifs (RRMs), a conserved intervening sequence referred to as a NONA/ParaSpeckle (NOPS) domain, and a ~100 amino acid coiled-coil domain. Its members include p54nrb (also known as NONO), PTB-associated splicing factor/splicing factor proline-glutamine rich (PSF or SFPQ) and PSPC1 (paraspeckle protein component 1). They are found in the nucleoplasm and can be triggered by binding to local high concentrations of various nucleic acids to form microscopically visible nuclear bodies, paraspeckles or large complexes such as DNA repair foci. They may also function cytoplasmically and on the cell surface in defined cell types. All three DBHS proteins are conserved throughout vertebrate species, while flies, worms, and yeast express a single DBHS protein [, ]. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
This entry represents the NOPS domain and the C-terminal coiled-coil region of PSF (also known as SFPQ). The C-terminal coiled-coil region functions in mediating DBHS dimerization, while some surface-exposed basic residues within the NOPS domain may be involved in nucleic acid binding [].PSF is a member of the DBHS (Drosophila behavior human splicing) family. It participates in a wide range of gene regulatory processes and cellular response pathways. It has been shown to affect the alternative splicing of CD45 and Tau and regulate the 3' polyadenylation of mRNAs. It is often localised in the paraspeckles and may be involved in the nuclear retention of mRNAs. It is involved in translation and transcription. It can bind directly to DSBs and play a role in DNA repair. PSF can also be utilized as an essential host factor for viral RNA multiplication and replication [, ]. In addition to the common DHBS core, which encompasses RRM1 and RRM2, the protein-protein interaction NOPS domain and the coiled-coil domain, PSF features additional domains, such as a RGG motif and a proline-rich region in its N terminus []. DBHS (Drosophila behavior human splicing) family are characterised by a core domain arrangement consisting of tandem RNA recognition motifs (RRMs), a conserved intervening sequence referred to as a NONA/ParaSpeckle (NOPS) domain, and a ~100 amino acid coiled-coil domain. Its members include p54nrb (also known as NONO), PTB-associated splicing factor/splicing factor proline-glutamine rich (PSF or SFPQ) and PSPC1 (paraspeckle protein component 1). They are found in the nucleoplasm and can be triggered by binding to local high concentrations of various nucleic acids to form microscopically visible nuclear bodies, paraspeckles or large complexes such as DNA repair foci. They may also function cytoplasmically and on the cell surface in defined cell types. All three DBHS proteins are conserved throughout vertebrate species, while flies, worms, and yeast express a single DBHS protein [, ]. |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
699
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
473
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
473
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
528
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
259
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
473
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
475
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
473
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
473
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
122
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
379
|
| Fragment?: |
false |
|
•
•
•
•
•
|
