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Search results 101 to 110 out of 110 for Pelp1

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0.017s
Type Details Score
Publication
First Author: Huo L
Year: 2012
Journal: Cell Cycle
Title: The Rix1 (Ipi1p-2p-3p) complex is a critical determinant of DNA replication licensing independent of their roles in ribosome biogenesis.
Volume: 11
Issue: 7
Pages: 1325-39
Protein Domain
Type: Family
Description: SENP5 peptidase (sentrin-specific peptidase 5, MEROPS identifier C48.008) is a deSUMOylating peptidase localized predominantly to the nucleolus. SENP5 releases the tag proteins SUMO-2 and -3 from conjugates, preferentially acting as an isopeptidase rather than an endopeptidase []. Simultaneous depletion of SENP3 and SENP5 results in enhanced SUMOylation of proteins such as RPL37A and GNL2, which are involved in the processing of pre-rRNA [], PELP1 and LAS1L, which are involved in the release of mature ribosomal particles [], and Nop58, which is a component of small nucleolar ribonucleoprotein (snoRNP) and SUMOlyation is required for binding of Nop58 to snoRNA to maintain nucleolar retention []. SENP5 depletion also affects mitotic progression, and cells arrest at the G2/M transition []. SENP5 is also involved in mitochondrial fusion and fission, because SUMOylated dynamin-1-like protein (Drp1), which is a mitochondrial fission factor, is a target for SENP5 []. DeSUMOylation of Drp1 is a contributory factor to cardiomyopathy []. During the G2/M transition stage of mitosis, SENP5 transiently locates to the mitochondrion []. SENP5 is also required for neutrophil differentiation, and the SNP5 gene is repressed in clinical acute myeloid leukemia [].
Publication
First Author: Fanis P
Year: 2012
Journal: Mol Cell Proteomics
Title: Five friends of methylated chromatin target of protein-arginine-methyltransferase[prmt]-1 (chtop), a complex linking arginine methylation to desumoylation.
Volume: 11
Issue: 11
Pages: 1263-73
Publication
First Author: Haindl M
Year: 2008
Journal: EMBO Rep
Title: The nucleolar SUMO-specific protease SENP3 reverses SUMO modification of nucleophosmin and is required for rRNA processing.
Volume: 9
Issue: 3
Pages: 273-9
Protein
Organism: Mus musculus/domesticus
Length: 928  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 338  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 749  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 607  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 210  
Fragment?: true
Publication
First Author: Dou Y
Year: 2005
Journal: Cell
Title: Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.
Volume: 121
Issue: 6
Pages: 873-85