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Search results 101 to 161 out of 161 for Prmt7

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Type Details Score
Publication
- | J:262123
     
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
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Publication
- | J:144086
     
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
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Publication
- | J:155721
     
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
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Publication
- | J:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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Publication
- | J:53168
     
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
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Publication
- | J:91388
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
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Publication
- | J:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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Publication
- | J:90438
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
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Publication
- | J:144087
     
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
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Protein
Q922X9
Organism: Mus musculus/domesticus
Length: 692  
Fragment?: false
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HT Experiment
E-GEOD-75993 | Transcriptome sequencing of skeletal muscle for PRMT7 knockout mouse
Series Id: GSE75993
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: ArrayExpress
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UniProt Feature
UniProt Feature
Begin: 614
Description: Symmetric dimethylarginine; by PRMT7
Type: modified residue
End: 614
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Publication
15494416 | -
First Author: Lee JH
Year: 2005
Journal: J Biol Chem
Title: PRMT7, a new protein arginine methyltransferase that synthesizes symmetric dimethylarginine.
Volume: 280
Issue: 5
Pages: 3656-64
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Publication
19110445 | -
First Author: Wang H
Year: 2009
Journal: J Am Soc Mass Spectrom
Title: Accurate localization and relative quantification of arginine methylation using nanoflow liquid chromatography coupled to electron transfer dissociation and orbitrap mass spectrometry.
Volume: 20
Issue: 3
Pages: 507-19
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Protein Domain
IPR014644 | MeTrfase_PRMT7
Type: Family
Description: This entry represents protein arginine N-methyltransferase PRMT7 [].PRMT7 can catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. It mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. It also mediates the symmetric dimethylation of histone H4 'Arg-3' to form H4R3me2s. It plays a role in gene imprinting by being recruited by CTCFL at the H19 imprinted control region (ICR) and methylating histone H4 to form H4R3me2s, possibly leading to recruit DNA methyltransferases at these sites. It may also play a role in embryonic stem cell (ESC) pluripotency [, , , ].
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Publication
32409666 | J:295344
First Author: Szewczyk MM
Year: 2020
Journal: Nat Commun
Title: Pharmacological inhibition of PRMT7 links arginine monomethylation to the cellular stress response.
Volume: 11
Issue: 1
Pages: 2396
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Interaction Experiment
Jelinic P (2006)
Description: The testis-specific factor CTCFL cooperates with the protein methyltransferase PRMT7 in H19 imprinting control region methylation.
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Publication
17709427 | -
First Author: Gonsalvez GB
Year: 2007
Journal: J Cell Biol
Title: Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins.
Volume: 178
Issue: 5
Pages: 733-40
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Publication
17010682 | -
First Author: Pahlich S
Year: 2006
Journal: Biochim Biophys Acta
Title: Protein arginine methylation: Cellular functions and methods of analysis.
Volume: 1764
Issue: 12
Pages: 1890-903
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Publication
19300908 | -
First Author: Wolf SS
Year: 2009
Journal: Cell Mol Life Sci
Title: The protein arginine methyltransferase family: an update about function, new perspectives and the physiological role in humans.
Volume: 66
Issue: 13
Pages: 2109-21
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Publication
15866169 | -
First Author: Bedford MT
Year: 2005
Journal: Mol Cell
Title: Arginine methylation an emerging regulator of protein function.
Volume: 18
Issue: 3
Pages: 263-72
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Publication
18057026 | -
First Author: Bedford MT
Year: 2007
Journal: J Cell Sci
Title: Arginine methylation at a glance.
Volume: 120
Issue: Pt 24
Pages: 4243-6
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Protein Domain
IPR025799 | Arg_MeTrfase
Type: Family
Description: Protein arginine methyltransferases (PRMTs) are enzymes that transfer methyl groups to the arginine residues of histones and other proteins. Arginine methylation is an important posttranslational modification process that plays functional roles in transcriptional control, splicing, DNA repair, and signaling [, , ]. PRMTs use S-adenosylmethionine(SAM or AdoMet)-dependent methylation to modify the guanidino nitrogens of the arginine side chain by adding one or two methyl groups []. According to their methylation status, the PRMT enzymes are classified into different group types. While the type-I PRMT enzymes catalyse the formation of monomethylarginine (MMA) and asymmetric dimethylarginine (aDMA), the type-II PRMT enzymes form MMA and symmetric dimethylarginine (sDMA). The enzymes PRMT1, PRMT3, PRMT4, PRMT6 and PRMT8 belong to the type-I and PRMT5, PRMT7 and PRMT9 to type-II.
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Publication
15699352 | J:96632
First Author: Zheng Z
Year: 2005
Journal: Proc Natl Acad Sci U S A
Title: A Mendelian locus on chromosome 16 determines susceptibility to doxorubicin nephropathy in the mouse.
Volume: 102
Issue: 7
Pages: 2502-7
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Protein
Q6PAK3
Organism: Mus musculus/domesticus
Length: 394  
Fragment?: false
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Protein
Q9JIF0
Organism: Mus musculus/domesticus
Length: 371  
Fragment?: false
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Protein
Q6NZB1
Organism: Mus musculus/domesticus
Length: 378  
Fragment?: false
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Protein
Q80WV6
Organism: Mus musculus/domesticus
Length: 354  
Fragment?: false
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Protein
A0A171KXD3
Organism: Mus musculus/domesticus
Length: 318  
Fragment?: false
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Protein
A0A140LI33
Organism: Mus musculus/domesticus
Length: 164  
Fragment?: true
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Protein
Q8C2D7
Organism: Mus musculus/domesticus
Length: 343  
Fragment?: false
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Protein
Q3UIG8
Organism: Mus musculus/domesticus
Length: 353  
Fragment?: false
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Protein
D3Z1D0
Organism: Mus musculus/domesticus
Length: 113  
Fragment?: true
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Protein
Q80WB1
Organism: Mus musculus/domesticus
Length: 350  
Fragment?: true
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Protein
A0A140LJF4
Organism: Mus musculus/domesticus
Length: 193  
Fragment?: true
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Protein
A0A140LHF7
Organism: Mus musculus/domesticus
Length: 208  
Fragment?: false
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Protein
A0A140LIF7
Organism: Mus musculus/domesticus
Length: 113  
Fragment?: true
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Protein
A0A140LHS4
Organism: Mus musculus/domesticus
Length: 217  
Fragment?: true
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Protein
Q9CX58
Organism: Mus musculus/domesticus
Length: 254  
Fragment?: false
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Protein
F6RXJ8
Organism: Mus musculus/domesticus
Length: 298  
Fragment?: true
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Protein
D6RFA7
Organism: Mus musculus/domesticus
Length: 162  
Fragment?: false
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Protein
A0A140LJ68
Organism: Mus musculus/domesticus
Length: 122  
Fragment?: false
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Protein
D3Z1C9
Organism: Mus musculus/domesticus
Length: 217  
Fragment?: false
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Protein
Q3TPF5
Organism: Mus musculus/domesticus
Length: 345  
Fragment?: false
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Protein
A0A140LJ70
Organism: Mus musculus/domesticus
Length: 254  
Fragment?: false
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Protein
Q9WVG6
Organism: Mus musculus/domesticus
Length: 608  
Fragment?: false
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Protein
D3YUP1
Organism: Mus musculus/domesticus
Length: 651  
Fragment?: false
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Protein
F6QQQ6
Organism: Mus musculus/domesticus
Length: 203  
Fragment?: true
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Protein
Q922H1
Organism: Mus musculus/domesticus
Length: 528  
Fragment?: false
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Protein
Q8CIG8
Organism: Mus musculus/domesticus
Length: 637  
Fragment?: false
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Protein
Q3U3W5
Organism: Mus musculus/domesticus
Length: 846  
Fragment?: false
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Protein
F8WIU7
Organism: Mus musculus/domesticus
Length: 846  
Fragment?: false
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Protein
Q8C1M0
Organism: Mus musculus/domesticus
Length: 418  
Fragment?: false
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Protein
A0A0R4J049
Organism: Mus musculus/domesticus
Length: 637  
Fragment?: false
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Protein
A0A1B0GT44
Organism: Mus musculus/domesticus
Length: 305  
Fragment?: false
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Protein
Q9R144
Organism: Mus musculus/domesticus
Length: 448  
Fragment?: false
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Protein
Q3UKX1
Organism: Mus musculus/domesticus
Length: 445  
Fragment?: false
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Protein
Q3UID4
Organism: Mus musculus/domesticus
Length: 475  
Fragment?: false
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Protein
Q3USQ4
Organism: Mus musculus/domesticus
Length: 231  
Fragment?: false
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Protein
M0QW88
Organism: Mus musculus/domesticus
Length: 254  
Fragment?: false
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Publication
15489334 | -
First Author: Gerhard DS
Year: 2004
Journal: Genome Res
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Volume: 14
Issue: 10B
Pages: 2121-7
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