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Search results 201 to 221 out of 221 for Pwp2

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Type Details Score
Strain
Attribute String: coisogenic, mutant strain, targeted mutation
Strain
Attribute String: coisogenic, endonuclease-mediated mutation, mutant strain
Strain
Attribute String: mutant strain, coisogenic, targeted mutation
Publication
First Author: Chauvin C
Year: 2014
Journal: Oncogene
Title: Ribosomal protein S6 kinase activity controls the ribosome biogenesis transcriptional program.
Volume: 33
Issue: 4
Pages: 474-83
Publication
First Author: Dosil M
Year: 2004
Journal: J Biol Chem
Title: Functional characterization of Pwp2, a WD family protein essential for the assembly of the 90 S pre-ribosomal particle.
Volume: 279
Issue: 36
Pages: 37385-97
Publication
First Author: Griffith ME
Year: 2007
Journal: Plant Cell
Title: The TORMOZ gene encodes a nucleolar protein required for regulated division planes and embryo development in Arabidopsis.
Volume: 19
Issue: 7
Pages: 2246-63
Protein Domain
Type: Domain
Description: A large ribonuclear protein complex is required for the processing of the small-ribosomal-subunit rRNA - the small-subunit (SSU) processome [, ]. This preribosomal complex contains the U3 snoRNA and at least 40 proteins, which have the following properties: They are nucleolar.They are able to coimmunoprecipitate with the U3 snoRNA and Mpp10 (a protein specific to the SSU processome). They are required for 18S rRNA biogenesis.There appears to be a linkage between polymerase I transcription and the formation of the SSU processome; as some, but not all, of the SSU processome components are required for pre-rRNA transcription initiation. These SSU processome components have been termed t-Utps. They form a pre-complex with pre-18S rRNA in the absence of snoRNA U3 and other SSU processome components. It has been proposed that the t-Utp complex proteins are both rDNA and rRNA binding proteins that are involved in the initiation of pre18S rRNA transcription. Initially binding to rDNA then associating with the 5' end of the nascent pre18S rRNA. The t-Utpcomplex forms the nucleus around which the rest of the SSU processome components, including snoRNA U3, assemble []. From electron microscopy the SSU processome may correspond to the terminal knobs visualized at the 5' ends of nascent 18S rRNA. Utp13 is a nucleolar protein and component of the small subunit (SSU) processome containing the U3 snoRNA that is involved in processing of pre-18S rRNA []. Upt13 is also a component of the Pwp2 complex that forms part of a stable particle subunit independent of the U3 small nucleolar ribonucleoprotein that is essential for the initial assembly steps of the 90S pre-ribosome []. Components of the Pwp2 complex are:Utp1 (Pwp2), Utp6, Utp12 (Dip2), Utp13, Utp18, and Utp21. The relationship between the Pwp2 complex and the t-Utps complex []that also associates with the 5' end of nascent pre-18S rRNA is unclear. This is the C-terminal helical domain of yeast Utp13 and its orthologue from human, Transducin beta-like protein 3, whose function is not clear. This domain is also found in protein TORMOZ EMBRYO DEFECTIVE from plants, which is an essential protein involved in the regulation of cell division planes during embryogenesis and defines cell patterning [].
Protein Domain
Type: Domain
Description: A large ribonuclear protein complex is required for the processing of the small-ribosomal-subunit rRNA - the small-subunit (SSU) processome [, ]. This preribosomal complex contains the U3 snoRNA and at least 40 proteins, which have the following properties: They are nucleolar.They are able to coimmunoprecipitate with the U3 snoRNA and Mpp10 (a protein specific to the SSU processome). They are required for 18S rRNA biogenesis.There appears to be a linkage between polymerase I transcription and the formation of the SSU processome; as some, but not all, of the SSU processome components are required for pre-rRNA transcription initiation. These SSU processome components have been termed t-Utps. They form a pre-complex with pre-18S rRNA in the absence of snoRNA U3 and other SSU processome components. It has been proposed that the t-Utp complex proteins are both rDNA and rRNA binding proteins that are involved in the initiation of pre18S rRNA transcription. Initially binding to rDNA then associating with the 5' end of the nascent pre18S rRNA. The t-Utpcomplex forms the nucleus around which the rest of the SSU processome components, including snoRNA U3, assemble []. From electron microscopy the SSU processome may correspond to the terminal knobs visualized at the 5' ends of nascent 18S rRNA. This domain is found at the C terminus of proteins containing WD40 repeats. These proteins are part of the U3 ribonucleoprotein. In yeast, these proteins are called Utp5, Utp1 or Pwp2, Utp12 or DIP2 . They interact with snoRNA U3 and with MPP10 []. Pwp2 is an essential Saccharomyces cerevisiae (Baker's yeast) protein involved in cell separation.
Protein
Organism: Mus musculus/domesticus
Length: 299  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 470  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 801  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 786  
Fragment?: false
Publication
First Author: Bernstein KA
Year: 2004
Journal: Eukaryot Cell
Title: The small-subunit processome is a ribosome assembly intermediate.
Volume: 3
Issue: 6
Pages: 1619-26
Publication
First Author: Gallagher JE
Year: 2004
Journal: Genes Dev
Title: RNA polymerase I transcription and pre-rRNA processing are linked by specific SSU processome components.
Volume: 18
Issue: 20
Pages: 2506-17
Protein
Organism: Mus musculus/domesticus
Length: 677  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 592  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 942  
Fragment?: false
Publication
First Author: Park J
Year: 2013
Journal: Mol Cell
Title: SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways.
Volume: 50
Issue: 6
Pages: 919-30
Publication
First Author: Villén J
Year: 2007
Journal: Proc Natl Acad Sci U S A
Title: Large-scale phosphorylation analysis of mouse liver.
Volume: 104
Issue: 5
Pages: 1488-93
Publication
First Author: Gerhard DS
Year: 2004
Journal: Genome Res
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Volume: 14
Issue: 10B
Pages: 2121-7
Publication
First Author: Huttlin EL
Year: 2010
Journal: Cell
Title: A tissue-specific atlas of mouse protein phosphorylation and expression.
Volume: 143
Issue: 7
Pages: 1174-89