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Search results 1 to 100 out of 104 for Pop1

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0.039s
Type Details Score
Gene
Type: gene
Organism: human
Gene
Type: gene
Organism: chimpanzee
Gene
Type: gene
Organism: dog, domestic
Gene
Type: gene
Organism: cattle
Gene
Type: gene
Organism: chicken
Gene
Type: gene
Organism: zebrafish
Gene
Type: gene
Organism: macaque, rhesus
Gene
Type: gene
Organism: frog, western clawed
Gene
Type: gene
Organism: rat
Protein Domain
Type: Family
Description: Pop1 is a component of ribonuclease P, a ribonucleoprotein enzyme that cleaves precursor tRNA transcripts to give mature 5' ends. It is also a component of RNase MRP [, , ].
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Publication
First Author: Lygerou Z
Year: 1994
Journal: Genes Dev
Title: The POP1 gene encodes a protein component common to the RNase MRP and RNase P ribonucleoproteins.
Volume: 8
Issue: 12
Pages: 1423-33
Protein
Organism: Mus musculus/domesticus
Length: 241  
Fragment?: true
Publication  
First Author: de Almeida L
Year: 2022
Journal: Front Immunol
Title: POP1 inhibits MSU-induced inflammasome activation and ameliorates gout.
Volume: 13
Pages: 912069
Protein
Organism: Mus musculus/domesticus
Length: 1015  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1045  
Fragment?: false
Publication
First Author: Wu J
Year: 2018
Journal: Cell
Title: Cryo-EM Structure of the Human Ribonuclease P Holoenzyme.
Volume: 175
Issue: 5
Pages: 1393-1404.e11
Publication
First Author: de Almeida L
Year: 2015
Journal: Immunity
Title: The PYRIN Domain-only Protein POP1 Inhibits Inflammasome Assembly and Ameliorates Inflammatory Disease.
Volume: 43
Issue: 2
Pages: 264-76
Publication
First Author: Chamberlain JR
Year: 1998
Journal: Genes Dev
Title: Purification and characterization of the nuclear RNase P holoenzyme complex reveals extensive subunit overlap with RNase MRP.
Volume: 12
Issue: 11
Pages: 1678-90
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus caroli
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus pahari
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus spretus
Publication  
First Author: Xiao S
Year: 2002
Journal: Annu Rev Biochem
Title: Eukaryotic ribonuclease P: a plurality of ribonucleoprotein enzymes.
Volume: 71
Pages: 165-89
Publication
First Author: Hansen J
Year: 2003
Journal: Proc Natl Acad Sci U S A
Title: A large-scale, gene-driven mutagenesis approach for the functional analysis of the mouse genome.
Volume: 100
Issue: 17
Pages: 9918-22
Publication      
First Author: MGI and IMPC
Year: 2018
Journal: Database Release
Title: MGI Load of Endonuclease-Mediated Alleles (CRISPR) from the International Mouse Phenotyping Consortium (IMPC)
Publication
First Author: Stryke D
Year: 2003
Journal: Nucleic Acids Res
Title: BayGenomics: a resource of insertional mutations in mouse embryonic stem cells.
Volume: 31
Issue: 1
Pages: 278-81
Publication      
First Author: Wellcome Trust Sanger Institute
Year: 2009
Journal: MGI Direct Data Submission
Title: Alleles produced for the KOMP project by the Wellcome Trust Sanger Institute
Publication
First Author: Hansen GM
Year: 2008
Journal: Genome Res
Title: Large-scale gene trapping in C57BL/6N mouse embryonic stem cells.
Volume: 18
Issue: 10
Pages: 1670-9
Publication      
First Author: Mouse Genome Informatics and the International Mouse Phenotyping Consortium (IMPC)
Year: 2014
Journal: Database Release
Title: Obtaining and Loading Phenotype Annotations from the International Mouse Phenotyping Consortium (IMPC) Database
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Chromosome assignment of mouse genes using the Mouse Genome Sequencing Consortium (MGSC) assembly and the ENSEMBL Database
Publication
First Author: Kawai J
Year: 2001
Journal: Nature
Title: Functional annotation of a full-length mouse cDNA collection.
Volume: 409
Issue: 6821
Pages: 685-90
Publication
First Author: Zambrowicz BP
Year: 2003
Journal: Proc Natl Acad Sci U S A
Title: Wnk1 kinase deficiency lowers blood pressure in mice: a gene-trap screen to identify potential targets for therapeutic intervention.
Volume: 100
Issue: 24
Pages: 14109-14
Publication      
First Author: Mouse Genome Informatics (MGI) and National Center for Biotechnology Information (NCBI)
Year: 2008
Journal: Database Download
Title: Mouse Gene Trap Data Load from dbGSS
Publication
First Author: Skarnes WC
Year: 2011
Journal: Nature
Title: A conditional knockout resource for the genome-wide study of mouse gene function.
Volume: 474
Issue: 7351
Pages: 337-42
Publication      
First Author: The Jackson Laboratory Mouse Radiation Hybrid Database
Year: 2004
Journal: Database Release
Title: Mouse T31 Radiation Hybrid Data Load
Publication
First Author: Okazaki Y
Year: 2002
Journal: Nature
Title: Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs.
Volume: 420
Issue: 6915
Pages: 563-73
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Title: Human to Mouse ISO GO annotation transfer
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2).
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
Publication      
First Author: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
Publication
First Author: Gaudet P
Year: 2011
Journal: Brief Bioinform
Title: Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium.
Volume: 12
Issue: 5
Pages: 449-62
Publication      
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
Publication      
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
Publication      
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
Publication      
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
Publication      
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
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: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
Publication
First Author: Andrée B
Year: 2002
Journal: Mol Cell Biol
Title: Mouse Pop1 is required for muscle regeneration in adult skeletal muscle.
Volume: 22
Issue: 5
Pages: 1504-12
Gene
Type: gene
Organism: frog, African clawed
Protein
Organism: Mus musculus/domesticus
Length: 358  
Fragment?: false
DO Term
Publication
First Author: Kominami K
Year: 1997
Journal: Genes Dev
Title: Fission yeast WD-repeat protein pop1 regulates genome ploidy through ubiquitin-proteasome-mediated degradation of the CDK inhibitor Rum1 and the S-phase initiator Cdc18.
Volume: 11
Issue: 12
Pages: 1548-60
Publication
First Author: Lygerou Z
Year: 1996
Journal: EMBO J
Title: hPop1: an autoantigenic protein subunit shared by the human RNase P and RNase MRP ribonucleoproteins.
Volume: 15
Issue: 21
Pages: 5936-48
Protein Domain
Type: Domain
Description: Ribonucleases P/MRP protein subunit POP1 is a subunit common to both ribonuclease P, a ribonucleoprotein complex that generates mature tRNA molecules by cleaving their 5'-ends [, ], and MRP ribonuclease complex, which cleaves pre-rRNA sequences []. This domain is found towards the C-terminal of POP1 [, ].
Publication
First Author: Lan P
Year: 2020
Journal: Science
Title: Structural insight into precursor ribosomal RNA processing by ribonuclease MRP.
Volume: 369
Issue: 6504
Pages: 656-663
Protein Domain
Type: Domain
Description: This entry represents a conserved region approximately 150 residues long located towards the N terminus of the POP1 subunit that is common to both the RNase MRP and RNase P ribonucleoproteins () [, , ]. These RNA-containing enzymes generate mature tRNA molecules by cleaving their 5' ends. This is a short N-terminal domain consisting of a small helical core and a long α-helix [], which is enriched with positively charged residues involved in pre-tRNA substrate recognition [].
Protein
Organism: Mus musculus/domesticus
Length: 150  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 51  
Fragment?: true
Publication
First Author: Jarrous N
Year: 2001
Journal: RNA
Title: Function and subnuclear distribution of Rpp21, a protein subunit of the human ribonucleoprotein ribonuclease P.
Volume: 7
Issue: 8
Pages: 1153-64
Publication
First Author: Cai T
Year: 1999
Journal: Mol Cell Biol
Title: Mutagenesis of SNM1, which encodes a protein component of the yeast RNase MRP, reveals a role for this ribonucleoprotein endoribonuclease in plasmid segregation.
Volume: 19
Issue: 11
Pages: 7857-69
Publication
First Author: Houser-Scott F
Year: 2002
Journal: Proc Natl Acad Sci U S A
Title: Interactions among the protein and RNA subunits of Saccharomyces cerevisiae nuclear RNase P.
Volume: 99
Issue: 5
Pages: 2684-9
Protein Domain
Type: Family
Description: This entry contains ribonuclease P (Rnp) proteins from eukaryotes and archaea. Rnp is a ubiquitous ribozyme that catalyzes a Mg2 -dependent hydrolysis to remove the 5'-leader sequence of precursor tRNA (pre-tRNA) [, ]. Archaeal and eukaryotic RNase P consist of a single RNA and archaeal RNase P has four or five proteins, while eukaryotic RNase P consists of 9 or 10 proteins. Eukaryotic and archaeal RNase P RNAs cooperatively function with protein subunits in catalysis []. Human RNase P is composed of a singular protein Pop1 and three subcomplexes, the Rpp20-Rpp25 heterodimer, Pop5-Rpp14-(Rpp30)2-Rpp40 heteropentamer, and Rpp21-Rpp29-Rpp38 heterotrimer. Although both Pop5 and Rpp14 have similar protein structure, they share a very limited sequence similarity. Moreover, the C-terminal fragments after the conserved beta sheets in Pop5 and Rpp14 exhibit distinct structural features that mediate interactions with Pop1 and Rpp40, respectively [].In the hyperthermophilic archaeon Pyrococcus horikoshii OT3, RNase P is composed of the RNase P RNA (pRNA) and five proteins (PhoPop5, PhoRpp38, PhoRpp21, PhoRpp29, and PhoRpp30) [, ].This entry includes Rpp21 from animals, Snm1/Rpr2 from yeasts and RNP4 from archaea [, ]. Snm1 is a subunit of RNase MRP (mitochondrial RNA processing), a ribonucleoprotein endoribonuclease that has roles in both mitochondrial DNA replication and nuclear 5.8S rRNA processing. Snm1 is an RNA binding protein that binds the MRP RNA specifically []. This subunit possibly binds the precursor tRNA [].
Protein Domain
Type: Family
Description: This entry contains ribonuclease P (Rnp) proteins from eukaryotes and archaea. Rnp is a ubiquitous ribozyme that catalyzes a Mg2 -dependent hydrolysis to remove the 5'-leader sequence of precursor tRNA (pre-tRNA) [, ]. Archaeal and eukaryotic RNase P consist of a single RNA and archaeal RNase P has four or five proteins, while eukaryotic RNase P consists of 9 or 10 proteins. Eukaryotic and archaeal RNase P RNAs cooperatively function with protein subunits in catalysis []. Human RNase P is composed of a singular protein Pop1 and three subcomplexes, the Rpp20-Rpp25 heterodimer, Pop5-Rpp14-(Rpp30)2-Rpp40 heteropentamer, and Rpp21-Rpp29-Rpp38 heterotrimer. Although both Pop5 and Rpp14 have similar protein structure, they share a very limited sequence similarity. Moreover, the C-terminal fragments after the conserved beta sheets in Pop5 and Rpp14 exhibit distinct structural features that mediate interactions with Pop1 and Rpp40, respectively [].In the hyperthermophilic archaeon Pyrococcus horikoshii OT3, RNase P is composed of the RNase P RNA (pRNA) and five proteins (PhoPop5, PhoRpp38, PhoRpp21, PhoRpp29, and PhoRpp30) [, ].Proteins in this entry include Rnp2 (also known as Pop5) from archaea and Pop5/Rpp14 from humans [].
Publication
First Author: Andrée B
Year: 2000
Journal: Dev Biol
Title: Isolation and characterization of the novel popeye gene family expressed in skeletal muscle and heart.
Volume: 223
Issue: 2
Pages: 371-82
Protein
Organism: Mus musculus/domesticus
Length: 122  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 363  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 340  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 84  
Fragment?: true
Publication  
First Author: Lan P
Year: 2018
Journal: Science
Title: Structural insight into precursor tRNA processing by yeast ribonuclease P.
Volume: 362
Issue: 6415
Publication
First Author: Guerrier-Takada C
Year: 2002
Journal: RNA
Title: Purification and characterization of Rpp25, an RNA-binding protein subunit of human ribonuclease P.
Volume: 8
Issue: 3
Pages: 290-5
Protein Domain
Type: Family
Description: Ribonuclease P (Rnp) is a ubiquitous ribozyme that catalyzes a Mg2 -dependent hydrolysis to remove the 5'-leader sequence of precursor tRNA (pre-tRNA) in all three domains of life []. In bacteria, the catalytic RNA (typically ~120kDa) is aided by a small protein cofactor (~14kDa) []. Archaeal and eukaryote RNase P consist of a single RNA and archaeal RNase P has four or five proteins, while eukaryotic RNase P consists of 9 or 10 proteins. Eukaryotic and archaeal RNase P RNAs cooperatively function with protein subunits in catalysis [].This entry represents Rpp25 from animals []. Human RNase P is composed of a singular protein Pop1 and three subcomplexes, the Rpp20-Rpp25 heterodimer, Pop5-Rpp14-(Rpp30)2-Rpp40 heteropentamer, and Rpp21-Rpp29-Rpp38 heterotrimer [].
Protein Domain
Type: Family
Description: Ribonuclease P (Rnp) is a ubiquitous ribozyme that catalyzes a Mg2 -dependent hydrolysis to remove the 5'-leader sequence of precursor tRNA (pre-tRNA) in all three domains of life []. In bacteria, the catalytic RNA (typically ~120kDa) is aided by a small protein cofactor (~14kDa) []. Archaeal and eukaryote RNase P consist of a single RNA and archaeal RNase P has four or five proteins, while eukaryotic RNase P consists of 9 or 10 proteins. Eukaryotic and archaeal RNase P RNAs cooperatively function with protein subunits in catalysis [].This entry represents Rpp40 from eukaryotes. Human RNase P is composed of a singular protein Pop1 and three subcomplexes, the Rpp20-Rpp25 heterodimer, Pop5-Rpp14-(Rpp30)2-Rpp40 heteropentamer, and Rpp21-Rpp29-Rpp38 heterotrimer [].
Publication
First Author: Goldfarb KC
Year: 2017
Journal: Genes Dev
Title: Targeted CRISPR disruption reveals a role for RNase MRP RNA in human preribosomal RNA processing.
Volume: 31
Issue: 1
Pages: 59-71
Protein Domain
Type: Homologous_superfamily
Description: This superfamily contains ribonuclease P (Rnp) proteins from eukaryotes and archaea. Rnp is a ubiquitous ribozyme that catalyzes a Mg2+-dependent hydrolysis to remove the 5'-leader sequence of precursor tRNA (pre-tRNA) []. Archaeal and eukaryote RNase P consist of a single RNA and archaeal RNase P has four or five proteins, while eukaryotic RNase P consists of 9 or 10 proteins. Eukaryotic and archaeal RNase P RNAs cooperatively function with protein subunits in catalysis []. Eukaryotic nuclear RNase P shares most of its protein components with another essential RNP enzyme, nucleolar RNase MRP []. RNase MRP (mitochondrial RNA processing) is an rRNA processing enzyme that cleaves a specific site within precursor rRNA to generate the mature 5'-end of 5.8S rRNA []. Despite its name, the vast majority of RNase MRP is localized in the nucleolus []. RNase MRP has been shown to cleave primers for mitochondrial DNA replication and CLB2 mRNA. In yeast, RNase MRP possesses one putatively catalytic RNA and at least 9 protein subunits (Pop1, Pop3-Pop8, Rpp1, Snm1 and Rmp1) [].Human RNase P is composed of a singular protein Pop1 and three subcomplexes, the Rpp20-Rpp25 heterodimer, Pop5-Rpp14-(Rpp30)2-Rpp40 heteropentamer, and Rpp21-Rpp29-Rpp38 heterotrimer [].In the hyperthermophilic archaeon Pyrococcus horikoshii OT3, RNase P is composed of the RNase P RNA (pRNA) and five proteins (PhoPop5, PhoRpp38, PhoRpp21, PhoRpp29, and PhoRpp30) [, ].Proteins in this entry include Rnp2 (also known as Pop5) from archaea and Pop5/Rpp14 from humans. In eukaryotes Pop5 is a subunit of both the Rnp and MRP complexes. Although both Pop5 and Rpp14 have similar protein structure, they share a very limited sequence similarity. Moreover, the C-terminal fragments after the conserved beta sheets in Pop5 and Rpp14 exhibit distinct structural features that mediate interactions with Pop1 and Rpp40, respectively [].The structure of Rnp2 (ribonuclease P protein component 2) has a ferrodoxin-like fold composed of an α-β sandwich with antiparallel β-sheet and contains an extra C-terminal helix.
Publication
First Author: Terada A
Year: 2006
Journal: J Biochem
Title: Characterization of the archaeal ribonuclease P proteins from Pyrococcus horikoshii OT3.
Volume: 140
Issue: 2
Pages: 293-8
Publication
First Author: Kimura M
Year: 2017
Journal: Biosci Biotechnol Biochem
Title: Structural basis for activation of an archaeal ribonuclease P RNA by protein cofactors.
Volume: 81
Issue: 9
Pages: 1670-1680
Protein
Organism: Mus musculus/domesticus
Length: 169  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 199  
Fragment?: false
Publication
First Author: Bussey H
Year: 1995
Journal: Proc Natl Acad Sci U S A
Title: The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.
Volume: 92
Issue: 9
Pages: 3809-13
Publication
First Author: Jarrous N
Year: 1999
Journal: RNA
Title: Rpp14 and Rpp29, two protein subunits of human ribonuclease P.
Volume: 5
Issue: 2
Pages: 153-7
Publication
First Author: Gopalan V
Year: 2018
Journal: RNA
Title: Chance and necessity in the evolution of RNase P.
Volume: 24
Issue: 1
Pages: 1-5