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Search results 101 to 109 out of 109 for Pin4

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0.019s
Type Details Score
Publication      
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
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: Pike BL
Year: 2004
Journal: Mol Cell Biol
Title: Mdt1, a novel Rad53 FHA1 domain-interacting protein, modulates DNA damage tolerance and G(2)/M cell cycle progression in Saccharomyces cerevisiae.
Volume: 24
Issue: 7
Pages: 2779-88
Publication
First Author: Traven A
Year: 2010
Journal: Yeast
Title: Dual functions of Mdt1 in genome maintenance and cell integrity pathways in Saccharomyces cerevisiae.
Volume: 27
Issue: 1
Pages: 41-52
Protein Domain
Type: Domain
Description: This entry represents the RNA recognition motif (RRM) in Pin4, a novel phosphothreonine (pThr)-containing protein that specifically interacts with the pThr-binding site of the Rad53 FHA1 domain. Pin4 is involved in normal G2/M cell cycle progression in the absence of DNA damage and functions as a novel target of checkpoint-dependent cell cycle arrest pathways [, ]. It contains an N-terminal RRM, a nuclear localization signal, a coiled coil, and a total of 15 SQ/TQ motifs.In S. pombe, Cip1 (Csx1-interacting protein 1) and Cip2 (Csx1-interacting protein 2) are novel cytoplasmic RRM-containing proteins that counteract Csx1 function during oxidative stress. They are not essential for viability in S. pombe []. Both cip1 and cip2 contain one RRM. Like Pin4, Cip2 also possesses an R3H motif that may function in sequence-specific binding to single-stranded nucleic acids.
Publication
First Author: Martín V
Year: 2006
Journal: Mol Biol Cell
Title: Cip1 and Cip2 are novel RNA-recognition-motif proteins that counteract Csx1 function during oxidative stress.
Volume: 17
Issue: 3
Pages: 1176-83