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Search results 101 to 110 out of 110 for Ctdp1

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0.016s
Type Details Score
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
Publication      
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
Publication
First Author: Cui P
Year: 2016
Journal: Plant Cell
Title: The RNA Polymerase II C-Terminal Domain Phosphatase-Like Protein FIERY2/CPL1 Interacts with eIF4AIII and Is Essential for Nonsense-Mediated mRNA Decay in Arabidopsis.
Volume: 28
Issue: 3
Pages: 770-85
Publication
First Author: Fukudome A
Year: 2014
Journal: Plant J
Title: Arabidopsis CPL4 is an essential C-terminal domain phosphatase that suppresses xenobiotic stress responses.
Volume: 80
Issue: 1
Pages: 27-39
Publication
First Author: Kops O
Year: 2002
Journal: FEBS Lett
Title: Pin1 modulates the dephosphorylation of the RNA polymerase II C-terminal domain by yeast Fcp1.
Volume: 513
Issue: 2-3
Pages: 305-11
Protein Domain
Type: Family
Description: This entry represents Fcp1 and its homologues, including CTDP1 from humans and CPL1/2/3/4/5 from Arabidopsis. They are carboxy-terminal domain (CTD) phosphatases. CPL1 has been shown to interact with two NMD (nonsense-mediated decay) factors, eIF4AIII and UPF3, and is involved in the dephosphorylation of eIF4AIII []. CPL4 functions as a pol II CTD phosphatase and has been shown to dephosphorylate both Ser2- and Ser5-PO(4) of CTD in vitro []. Budding yeast Fcp1 has been shown to dephosphorylate RNA polymerase (RNAP) II subunit, and this interaction is modulated by the Pin1 protein [].
Protein
Organism: Mus musculus/domesticus
Length: 960  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 960  
Fragment?: false