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Search results 201 to 227 out of 227 for Rnps1

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0.018s
Type Details Score
Protein
Organism: Mus musculus/domesticus
Length: 305  
Fragment?: false
Protein Domain
Type: Homologous_superfamily
Description: This superfamily includes several eukaryotic Sin3 associated polypeptide p18 (SAP18) sequences. SAP18 is known to be a component of the Sin3-containing complex which is responsible for the repression of transcription via the modification of histone polypeptides []. SAP18 (UBL domain) is one of the three three ASAP subunits (along with Acinus (β-hairpin motif) and RNPS1 (RRM domain)) that play a role in programmed cell death, transcriptional regulation, pre-mRNA splicing and mRNA quality control [, ]. The ASAP complex interacts with the exon-junction complex (EJC), a messenger ribonucleoprotein complex involved in post-transcriptional regulation [].The high degree of evolutionary conservation and the fortuitous crystal contacts at the α-β groove suggest that this surface of SAP18 is a hot spot for interactions. Possible binding partners targeting this surface of SAP18 are transcription factors (such as Bicoid and Kruppel) and/or Sin3a-HDAC subunits.
Publication
First Author: Yang D
Year: 1999
Journal: Cancer Res
Title: Identification of a gene coding for a protein possessing shared tumor epitopes capable of inducing HLA-A24-restricted cytotoxic T lymphocytes in cancer patients.
Volume: 59
Issue: 16
Pages: 4056-63
Publication
First Author: Stanĕk D
Year: 2003
Journal: J Cell Biol
Title: Targeting of U4/U6 small nuclear RNP assembly factor SART3/p110 to Cajal bodies.
Volume: 160
Issue: 4
Pages: 505-16
Publication
First Author: Murachelli AG
Year: 2012
Journal: Nat Struct Mol Biol
Title: The structure of the ASAP core complex reveals the existence of a Pinin-containing PSAP complex.
Volume: 19
Issue: 4
Pages: 378-86
Publication
First Author: Liu Y
Year: 2002
Journal: J Biol Chem
Title: HIV-1 Tat protein-mediated transactivation of the HIV-1 long terminal repeat promoter is potentiated by a novel nuclear Tat-interacting protein of 110 kDa, Tip110.
Volume: 277
Issue: 26
Pages: 23854-63
Publication
First Author: Medenbach J
Year: 2004
Journal: Mol Cell Biol
Title: Human U4/U6 snRNP recycling factor p110: mutational analysis reveals the function of the tetratricopeptide repeat domain in recycling.
Volume: 24
Issue: 17
Pages: 7392-401
Protein
Organism: Mus musculus/domesticus
Length: 111  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 107  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 92  
Fragment?: false
Publication
First Author: Schwerk C
Year: 2003
Journal: Mol Cell Biol
Title: ASAP, a novel protein complex involved in RNA processing and apoptosis.
Volume: 23
Issue: 8
Pages: 2981-90
Protein Domain
Type: Domain
Description: This entry represents the RNA recognition motif 1 (RRM1) of SART3 (also known as Tip110), which is an RNA-binding protein expressed in the nucleus of the majority of proliferating cells, including normal cells and malignant cells, but not in normal tissues except for the testes and fetal liver []. It is involved in the regulation of mRNA splicing probably via its complex formation with RNPS1 (an RNA-binding protein with a serine-rich domain), a pre-mRNA-splicing factor []. SART3 has also been identified as a nuclear Tat-interacting protein that regulates Tat transactivation activity through direct interaction and functions as an important cellular factor for HIV-1 gene expression and viral replication []. In addition, SART3 is required for U6 snRNP targeting to Cajal bodies []. It binds specifically and directly to the U6 snRNA, interacts transiently with the U6 and U4/U6 snRNPs, and promotes the reassembly of U4/U6 snRNPs after splicing in vitro [].SART3 contains an N-terminal HAT (half-a-tetratricopeptide repeat)-rich domain, a nuclearlocalization signal (NLS) domain, and two C-terminal RNA recognition motifs (RRMs).
Protein Domain
Type: Domain
Description: This entry represents the RNA recognition motif 2 (RRM2) of SART3 (also known as Tip110), which is an RNA-binding protein expressed in the nucleus of the majority of proliferating cells, including normal cells and malignant cells, but not in normal tissues except for the testes and fetal liver []. It is involved in the regulation of mRNA splicing probably via its complex formation with RNPS1 (an RNA-binding protein with a serine-rich domain), a pre-mRNA-splicing factor []. SART3 has also been identified as a nuclear Tat-interacting protein that regulates Tat transactivation activity through direct interaction and functions as an important cellular factor for HIV-1 gene expression and viral replication []. In addition, SART3 is required for U6 snRNP targeting to Cajal bodies []. It binds specifically and directly to the U6 snRNA, interacts transiently with the U6 and U4/U6 snRNPs, and promotes the reassembly of U4/U6 snRNPs after splicing in vitro [].SART3 contains a HAT (N-terminal half-a-tetratricopeptide repeat)-rich domain, a nuclearlocalization signal (NLS) domain, and two C-terminal RNA recognition motifs (RRMs).
Protein
Organism: Mus musculus/domesticus
Length: 153  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 153  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 172  
Fragment?: false
Publication
First Author: Zhang Y
Year: 1997
Journal: Cell
Title: Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex.
Volume: 89
Issue: 3
Pages: 357-64
Protein
Organism: Mus musculus/domesticus
Length: 552  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 634  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 580  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 581  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 378  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 962  
Fragment?: false
Publication
First Author: Sahara S
Year: 1999
Journal: Nature
Title: Acinus is a caspase-3-activated protein required for apoptotic chromatin condensation.
Volume: 401
Issue: 6749
Pages: 168-73
Protein
Organism: Mus musculus/domesticus
Length: 1338  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1272  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1266  
Fragment?: true