|  Help  |  About  |  Contact Us

Search our database by keyword

Examples

  • Search this entire website. Enter identifiers, names or keywords for genes, diseases, strains, ontology terms, etc. (e.g. Pax6, Parkinson, ataxia)
  • Use OR to search for either of two terms (e.g. OR mus) or quotation marks to search for phrases (e.g. "dna binding").
  • Boolean search syntax is supported: e.g. Balb* for partial matches or mus AND NOT embryo to exclude a term

Search results 201 to 300 out of 336 for Prmt5

<< First    < Previous  |  Next >    Last >>
0.017s

Categories

Hits by Pathway

Hits by Category

Hits by Strain

Type Details Score
Gene
417404 | COPRS
Type: gene
Organism: chicken
•
•
•
•
•
Gene
713293 | COPRS
Type: gene
Organism: macaque, rhesus
•
•
•
•
•
Gene
100490247 | coprs
Type: gene
Organism: frog, western clawed
•
•
•
•
•
Gene
106992574 | LOC106992574
Type: gene
Organism: macaque, rhesus
•
•
•
•
•
Gene
107973638 | LOC107973638
Type: gene
Organism: chimpanzee
•
•
•
•
•
Gene
108711638 | coprs.L
Type: gene
Organism: frog, African clawed
•
•
•
•
•
HT Experiment
E-GEOD-60875 | PRMT5 protects genomic integrity during global DNA demethylation in primordial germ cells and preimplantation embryos
Series Id: GSE60875
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: ArrayExpress
•
•
•
•
•
Publication
23671120 | J:197425
First Author: Tsai WW
Year: 2013
Journal: Proc Natl Acad Sci U S A
Title: PRMT5 modulates the metabolic response to fasting signals.
Volume: 110
Issue: 22
Pages: 8870-5
•
•
•
•
•
Publication
23904475 | J:200681
First Author: Wei H
Year: 2013
Journal: Proc Natl Acad Sci U S A
Title: PRMT5 dimethylates R30 of the p65 subunit to activate NF-κB.
Volume: 110
Issue: 33
Pages: 13516-21
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 656
Description: Omega-N-methylarginine; by PRMT5
Type: modified residue
End: 656
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 563
Description: Symmetric dimethylarginine; by PRMT5
Type: modified residue
End: 563
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 19
Description: Symmetric dimethylarginine; by PRMT5
Type: modified residue
End: 19
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 98
Description: Symmetric dimethylarginine; by PRMT5
Type: modified residue
End: 98
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 102
Description: Symmetric dimethylarginine; by PRMT5
Type: modified residue
End: 102
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 190
Description: Symmetric dimethylarginine; by PRMT5
Type: modified residue
End: 190
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 927
Description: Symmetric dimethylarginine; by PRMT5
Type: modified residue
End: 927
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 49
Description: Omega-N-methylarginine; by PRMT5
Type: modified residue
End: 49
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 371
Description: Omega-N-methylarginine; by PRMT5
Type: modified residue
End: 371
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 57
Description: Symmetric dimethylarginine; by PRMT5
Type: modified residue
End: 57
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 163
Description: Symmetric dimethylarginine; by PRMT5
Type: modified residue
End: 163
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 549
Description: Symmetric dimethylarginine; by PRMT5
Type: modified residue
End: 549
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 192
Description: Symmetric dimethylarginine; by PRMT5
Type: modified residue
End: 192
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 19
Description: Symmetric dimethylarginine; by PRMT5
Type: modified residue
End: 19
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 100
Description: Symmetric dimethylarginine; by PRMT5
Type: modified residue
End: 100
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 104
Description: Symmetric dimethylarginine; by PRMT5
Type: modified residue
End: 104
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 192
Description: Symmetric dimethylarginine; by PRMT5
Type: modified residue
End: 192
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 104
Description: Symmetric dimethylarginine; by PRMT5
Type: modified residue
End: 104
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 100
Description: Symmetric dimethylarginine; by PRMT5
Type: modified residue
End: 100
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 19
Description: Symmetric dimethylarginine; by PRMT5
Type: modified residue
End: 19
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 19
Description: Symmetric dimethylarginine; by PRMT5
Type: modified residue
End: 19
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 192
Description: Symmetric dimethylarginine; by PRMT5
Type: modified residue
End: 192
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 100
Description: Symmetric dimethylarginine; by PRMT5
Type: modified residue
End: 100
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 104
Description: Symmetric dimethylarginine; by PRMT5
Type: modified residue
End: 104
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 192
Description: Symmetric dimethylarginine; by PRMT5
Type: modified residue
End: 192
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 104
Description: Symmetric dimethylarginine; by PRMT5
Type: modified residue
End: 104
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 100
Description: Symmetric dimethylarginine; by PRMT5
Type: modified residue
End: 100
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 19
Description: Symmetric dimethylarginine; by PRMT5
Type: modified residue
End: 19
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 192
Description: Symmetric dimethylarginine; by PRMT5
Type: modified residue
End: 192
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 100
Description: Symmetric dimethylarginine; by PRMT5
Type: modified residue
End: 100
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 104
Description: Symmetric dimethylarginine; by PRMT5
Type: modified residue
End: 104
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 19
Description: Symmetric dimethylarginine; by PRMT5
Type: modified residue
End: 19
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 98
Description: Symmetric dimethylarginine; by PRMT5
Type: modified residue
End: 98
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 102
Description: Symmetric dimethylarginine; by PRMT5
Type: modified residue
End: 102
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 190
Description: Symmetric dimethylarginine; by PRMT5
Type: modified residue
End: 190
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 19
Description: Symmetric dimethylarginine; by PRMT5
Type: modified residue
End: 19
•
•
•
•
•
HT Experiment
GSE107854 | PRMT5 regulates the homologous recombination DNA repair pathway by controlling the alternative splicing of key epigenetic factors
 
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: GEO
•
•
•
•
•
Publication
36609611 | J:332521
First Author: Hing ZA
Year: 2023
Journal: Nat Commun
Title: Dysregulation of PRMT5 in chronic lymphocytic leukemia promotes progression with high risk of Richter's transformation.
Volume: 14
Issue: 1
Pages: 97
•
•
•
•
•
Publication
19181385 | J:146863
First Author: Igarashi H
Year: 2009
Journal: Mol Immunol
Title: GANP suppresses the arginine methyltransferase PRMT5 regulating IL-4-mediated STAT6-signaling to IgE production in B cells.
Volume: 46
Issue: 6
Pages: 1031-41
•
•
•
•
•
Publication
24453002 | J:208148
First Author: Yan F
Year: 2014
Journal: Cancer Res
Title: Genetic validation of the protein arginine methyltransferase PRMT5 as a candidate therapeutic target in glioblastoma.
Volume: 74
Issue: 6
Pages: 1752-65
•
•
•
•
•
Publication
16087681 | J:156230
First Author: Azzouz TN
Year: 2005
Journal: J Biol Chem
Title: Toward an assembly line for U7 snRNPs: interactions of U7-specific Lsm proteins with PRMT5 and SMN complexes.
Volume: 280
Issue: 41
Pages: 34435-40
•
•
•
•
•
Publication
39424627 | J:357570
First Author: Feng M
Year: 2024
Journal: Cell Death Dis
Title: The interaction between UBR7 and PRMT5 drives PDAC resistance to gemcitabine by regulating glycolysis and immune microenvironment.
Volume: 15
Issue: 10
Pages: 758
•
•
•
•
•
Publication
33097661 | J:297531
First Author: Wei X
Year: 2020
Journal: Proc Natl Acad Sci U S A
Title: Targeted CRISPR screening identifies PRMT5 as synthetic lethality combinatorial target with gemcitabine in pancreatic cancer cells.
Volume: 117
Issue: 45
Pages: 28068-28079
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 1810
Description: Symmetric dimethylarginine; alternate; by PRMT5
Type: modified residue
End: 1810
•
•
•
•
•
Allele
Prmt5<em1Smoc> | MGI:7291832
Name: protein arginine N-methyltransferase 5; endonuclease-mediated mutation 1, Shanghai Model Organisms Center
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
•
•
•
•
•
Publication
33376131 | -
 
First Author: Chakrapani B
Year: 2021
Journal: Life Sci Alliance
Title: The uncharacterized protein FAM47E interacts with PRMT5 and regulates its functions.
Volume: 4
Issue: 3
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 4
Description: Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate
Type: modified residue
End: 4
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 1
Description: Coordinator of PRMT5 and differentiation stimulator
Type: chain
End: 173
•
•
•
•
•
UniProt Feature
UniProt Feature
Begin: 291
Description: Asymmetric dimethylarginine; by PRMT1 and PRMT5
Type: modified residue
End: 291
•
•
•
•
•
Strain
MGI:6771082 | C57BL/6JSmoc-Prmt5<em1Smoc>/Smoc
Attribute String: coisogenic, endonuclease-mediated mutation, mutant strain
•
•
•
•
•
Interaction Experiment
Dacwag CS (2007)
Description: The protein arginine methyltransferase Prmt5 is required for myogenesis because it facilitates ATP-dependent chromatin remodeling.
•
•
•
•
•
Interaction Experiment
Ancelin K (2006)
Description: Blimp1 associates with Prmt5 and directs histone arginine methylation in mouse germ cells.
•
•
•
•
•
Interaction Experiment
Calabretta S (2018)
Description: Loss of PRMT5 Promotes PDGFR Degradation during Oligodendrocyte Differentiation and Myelination.
•
•
•
•
•
Interaction Experiment
Kanamaluru D (2011)
Description: Arginine methylation by PRMT5 at a naturally occurring mutation site is critical for liver metabolic regulation by small heterodimer partner.
•
•
•
•
•
Publication
15485929 | -
First Author: Pal S
Year: 2004
Journal: Mol Cell Biol
Title: Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes.
Volume: 24
Issue: 21
Pages: 9630-45
•
•
•
•
•
Publication
11747828 | -
First Author: Meister G
Year: 2001
Journal: Curr Biol
Title: Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln.
Volume: 11
Issue: 24
Pages: 1990-4
•
•
•
•
•
Protein
E9PYM1
Organism: Mus musculus/domesticus
Length: 199  
Fragment?: false
•
•
•
•
•
Protein
Q0VG34
Organism: Mus musculus/domesticus
Length: 394  
Fragment?: false
•
•
•
•
•
Protein
Q3UN37
Organism: Mus musculus/domesticus
Length: 101  
Fragment?: false
•
•
•
•
•
Protein
B1AW18
Organism: Mus musculus/domesticus
Length: 415  
Fragment?: false
•
•
•
•
•
Protein
Q9D5A6
Organism: Mus musculus/domesticus
Length: 230  
Fragment?: false
•
•
•
•
•
Protein
D3YWC7
Organism: Mus musculus/domesticus
Length: 402  
Fragment?: false
•
•
•
•
•
Protein
H3BJN1
Organism: Mus musculus/domesticus
Length: 159  
Fragment?: true
•
•
•
•
•
Protein
H3BKF1
Organism: Mus musculus/domesticus
Length: 121  
Fragment?: false
•
•
•
•
•
Protein
E9Q0Z5
Organism: Mus musculus/domesticus
Length: 260  
Fragment?: false
•
•
•
•
•
Protein
Q9D5P7
Organism: Mus musculus/domesticus
Length: 415  
Fragment?: false
•
•
•
•
•
Protein
B2RVF4
Organism: Mus musculus/domesticus
Length: 101  
Fragment?: false
•
•
•
•
•
Protein
Q14BE7
Organism: Mus musculus/domesticus
Length: 430  
Fragment?: false
•
•
•
•
•
Protein Domain
IPR032743 | FAM47
Type: Family
Description: The function of this family of proteins from metazoa is not known. Human FAM47E localizes the arginine methyltransferase PRMT5 to chromatin and, thus, promotes histone methylation [].
•
•
•
•
•
Publication
30652083 | J:295127
First Author: Paul C
Year: 2019
Journal: FEBS Open Bio
Title: Coprs inactivation leads to a derepression of LINE1 transposons in spermatocytes.
Volume: 9
Issue: 1
Pages: 159-168
•
•
•
•
•
Protein Domain
IPR035247 | PRMT5_TIM
Type: Domain
Description: This entry represents the N-terminal TIM barrel domain of PRMT5.Proteins containing this domain includes Skb1 from S. pombe [], Hsl7 from S. cerevisiae []and their homologues PRMT5 from animals [, , ]and plants []. Skb1 is a mediator of hyperosmotic stress response in Schizosaccharomyces pombe []. Plant PMRT15 is involved in the post-transcriptional regulation of the circadian clock []. Human PRMT5 is a component of multiple protein complexes and contributes to essential cellular processes, such as RNA transport and splicing, cell cycle regulation, tumour growth, and chromatin remodelling, leading to either gene silencing or activation [].
•
•
•
•
•
Protein Domain
IPR035248 | PRMT5_C
Type: Domain
Description: This entry represents the C-terminal oligomerisation domain of PRMT5.Proteins containing this domain includes Skb1 from S. pombe [], Hsl7 from S. cerevisiae []and their homologues PRMT5 from animals [, , ]and plants []. Skb1 is a mediator of hyperosmotic stress response in Schizosaccharomyces pombe []. Plant PMRT15 is involved in the post-transcriptional regulation of the circadian clock []. Human PRMT5 is a component of multiple protein complexes and contributes to essential cellular processes, such as RNA transport and splicing, cell cycle regulation, tumour growth, and chromatin remodelling, leading to either gene silencing or activation [].
•
•
•
•
•
Publication
25681392 | J:221154
First Author: Paul C
Year: 2015
Journal: Biol Open
Title: The Wnt-target gene Dlk-1 is regulated by the Prmt5-associated factor Copr5 during adipogenic conversion.
Volume: 4
Issue: 3
Pages: 312-6
•
•
•
•
•
HT Experiment
GSE94791 | TDRD6 mediates early steps of spliceosome maturation in primary spermatocytes
 
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: GEO
•
•
•
•
•
Publication
19011621 | J:314389
First Author: Jansson M
Year: 2008
Journal: Nat Cell Biol
Title: Arginine methylation regulates the p53 response.
Volume: 10
Issue: 12
Pages: 1431-9
•
•
•
•
•
Protein Coding Gene
MGI:1913673 | Coprs
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGP_CAROLIEiJ_G0030850 | -
Type: protein_coding_gene
Organism: Mus caroli
•
•
•
•
•
Protein Coding Gene
MGP_129S1SvImJ_G0033389 | -
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGP_AJ_G0033370 | -
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGP_AKRJ_G0033300 | -
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGP_BALBcJ_G0033370 | -
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGP_C3HHeJ_G0033083 | -
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGI_C57BL6J_1913673 | -
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGP_C57BL6NJ_G0033882 | -
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGP_CASTEiJ_G0032405 | -
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGP_CBAJ_G0033056 | -
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGP_DBA2J_G0033210 | -
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGP_FVBNJ_G0033158 | -
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGP_LPJ_G0033303 | -
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGP_NODShiLtJ_G0033195 | -
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGP_NZOHlLtJ_G0033899 | -
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•




MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

Copyright © 2017 by The Jackson Laboratory. All Rights Reserved

© 2002 - 2017 Department of Genetics, University of Cambridge, Downing Street,
Cambridge CB2 3EH, United Kingdom