Search results for RPRD1A

Showing 12 results out of 12

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Species

Types

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Protein (1 results from a total of 1)

Identifier: R-HSA-6814899
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: RPRD1A: Q96P16

Interactor (2 results from a total of 2)

Identifier: Q96P16-3
Species: Homo sapiens
Primary external reference: UniProt: Q96P16-3
Identifier: Q96P16-1
Species: Homo sapiens
Primary external reference: UniProt: Q96P16-1

Set (1 results from a total of 1)

Identifier: R-HSA-6814864
Species: Homo sapiens
Compartment: nucleoplasm

Complex (5 results from a total of 5)

Identifier: R-HSA-6814908
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-6814528
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-6814539
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-6810229
Species: Homo sapiens
Compartment: nucleoplasm

Reaction (3 results from a total of 3)

Identifier: R-HSA-6810235
Species: Homo sapiens
Compartment: nucleoplasm
The protein phosphatase RPAP2 binds RNA polymerase II phosphorylated at serine-7 of the C-terminal domain (CTD) (Egloff et al. 2012). RPRD1A and RPRD1B bind RNA polymerase II with RPAP2 and appear to act as scaffolds for the complex (Ni et al. 2011, Ni et al. 2014).
Identifier: R-HSA-6814559
Species: Homo sapiens
Compartment: nucleoplasm
A 7-methylguanosine triphosphate group is added to the 5' end of the pre-snRNA during transcription elongation (Mattaj 1986). The capping enzyme and cap methyltransferase involved in mRNA capping may also be responsible for this reaction. In the case of mRNA capping, the capping enzyme is targeted to the pre-mRNA by interaction with the phosphorylated C-terminal domain (CTD) of RNA polymerase II (McCracken et al. 1997). During elongation, the phosphorylation pattern of the CTD also changes: serine-5 is dephosphorylated by RPAP2 (Egloff et al. 2012) interacting with RPRD1A and RPRD1B (Ni et al. 2011, Ni et al. 2014) and serine-2 is phosphoryated by P-TEFb. Serine-7 is also phosphorylated, possibly, however the responsible kinase is not certain. The order of the capping and phosphorylation events is unknown.
Identifier: R-HSA-6814549
Species: Homo sapiens
Compartment: nucleoplasm
In an unknown order of events, RNA polymerase II initiates transcription and the Integrator complex (Baillat et al. 2005) and Little Elongation Complex (LEC, Hu et al. 2013) are recruited to phosphorylated RNA polymerase II (Egloff et al. 2010). The Integrator complex interacts with RPAP2, which binds phosphoserine-7 of the C-terminal domain (CTD) of RNA polymerase II and is required for recruitment of Integrator (Egloff et al. 2007, Egloff et al. 2012). RPAP2 interacts with the putative scaffold proteins RPRD1A and RPRD1B at the CTD (Ni et al. 2011, Ni et al. 2014) and DSIF is required for recruitment of Integrator (Skaar et al. 2015). The Integrator complex does not seem to play a significant role in subsequent elongation of the pre-snRNA transcript but is critical for processing of the 3' end of the pre-snRNA.
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