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proteins. Page last changed on 19 Dec 2016.
Deoxynucleotidyltransferase, terminal, interacting protein 1
TdIF1
DNTTIP1 binds DNA and enhances the activity of terminal deoxynucleotidyltransferase (TDT, or DNTT; MIM 187410), a DNA polymerase that catalyzes the polymerization of DNA in the absence of a DNA template (Yamashita et al., 2001 [PubMed 11473582]).[supplied by OMIM, Mar 2008] (from
NCBI)
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Top mentioned proteins:
TdT, POLYMERASE, CAN, p65, Histone
Papers on
TdIF1
Definition of the transcription factor TdIF1 consensus-binding sequence through genomewide mapping of its binding sites.
New
Tokyo, Japan. In Genes Cells, Mar 2015
TdIF1 was originally identified as a protein that directly binds to terminal deoxynucleotidyltransferase, TdT.
TdIF1 recognizes a specific DNA sequence through its Helix-Turn-Helix and AT-hook motifs to regulate gene transcription.
Noda, Japan. In Plos One, 2012
TdIF1 was originally identified as a protein that directly binds to DNA polymerase TdT.
Chemoproteomics profiling of HDAC inhibitors reveals selective targeting of HDAC complexes.
Impact
GeneRIF
Heidelberg, Germany. In Nat Biotechnol, 2011
During cell division, DNTTIP1 is part of the mitotic deacetylase complex MIDAC, which also contains C14ORF43/MIDEAS and HDAC1/HDAC2.
TdT interacting factor 1 enhances TdT ubiquitylation through recruitment of BPOZ-2 into nucleus from cytoplasm.
Noda, Japan. In Genes Cells, 2009
We isolated human cDNA clone encoding Bood POZ containing gene type 2 (BPOZ-2) as a gene with a product that binds to TdT interacting factor 1 (TdIF1) using a yeast two-hybrid system.
Identification of functional domains in TdIF1 and its inhibitory mechanism for TdT activity.
GeneRIF
Noda, Japan. In Genes Cells, 2007
The TdT binding, DNA binding and dimerization regions, and nuclear localization signal (NLS) in TdIF1, were identified.
Direct binding of TReP-132 with TdT results in reduction of TdT activity.
Noda, Japan. In Genes Cells, 2006
TdT directly binds to TdIF1, TdIF2, PCNA and the Ku70/86 heterodimer.
Terminal deoxynucleotidyltransferase directly interacts with a novel nuclear protein that is homologous to p65.
Noda, Japan. In Genes Cells, 2001
This protein was designated as TdT interacting factor 1 (TdIF1).
