Subcellular localization of the human proto-oncogene protein DEK (Q28186821)

1

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K Burger

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M Baack

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F O Fackelmayer

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C Gruss

Journal of Biological Chemistry

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language of work or name

English

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publication date

13 July 2001

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published in

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volume

276

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issue

28

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page(s)

26317-23

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cites work

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Recruitment of chromatin remodeling machines

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The translocation (6;9), associated with a specific subtype of acute myeloid leukemia, results in the fusion of two genes, dek and can, and the expression of a chimeric, leukemia-specific dek-can mRNA

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Autoantibodies to DEK oncoprotein in a patient with systemic lupus erythematosus and sarcoidosis

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DEK, an autoantigen involved in a chromosomal translocation in acute myelogenous leukemia, binds to the HIV-2 enhancer

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The acute myeloid leukemia-associated protein, DEK, forms a splicing-dependent interaction with exon-product complexes

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The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions

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Human minichromosome maintenance proteins and human origin recognition complex 2 protein on chromatin

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids

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Chromatin association of human origin recognition complex, cdc6, and minichromosome maintenance proteins during the cell cycle: assembly of prereplication complexes in late mitosis

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The human origin recognition complex protein 1 dissociates from chromatin during S phase in HeLa cells

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Dynamic binding of histone H1 to chromatin in living cells

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Maturation of newly replicated chromatin of simian virus 40 and its host cell

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Components of the human SWI/SNF complex are enriched in active chromatin and are associated with the nuclear matrix.

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Subnuclear localization of WT1 in splicing or transcription factor domains is regulated by alternative splicing

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WT1 interacts with the splicing factor U2AF65 in an isoform-dependent manner and can be incorporated into spliceosomes

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Oncoprotein TLS interacts with serine-arginine proteins involved in RNA splicing

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The transcription factor Spi-1/PU.1 binds RNA and interferes with the RNA-binding protein p54nrb

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The transcription factor Spi-1/PU.1 interacts with the potential splicing factor TLS

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The novel SAR-binding domain of scaffold attachment factor A (SAF-A) is a target in apoptotic nuclear breakdown.

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SAF-Box, a conserved protein domain that specifically recognizes scaffold attachment region DNA.

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Apoptotic cleavage of scaffold attachment factor A (SAF-A) by caspase-3 occurs at a noncanonical cleavage site

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High mobility of proteins in the mammalian cell nucleus

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Rapid exchange of histone H1.1 on chromatin in living human cells

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release_r4dytvxes5dlpmojfxk25ooc7e

21 January 2018

Identifiers

DOI

10.1074/JBC.M100162200

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Fatcat ID

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/r4dytvxes5dlpmojfxk25ooc7e