TRANSFAC-Logo

TRANSFAC FACTOR TABLE, Release 2017.2 - public - 2017-06-30, (C) QIAGEN


AC T19630 XX ID T19630 XX DT 06.12.1999 (created); ili. DT 07.11.2014 (updated); asv. CO Copyright (C), QIAGEN. XX FA Ku autoantigen XX OS human, Homo sapiens OC eukaryota; animalia; metazoa; chordata; vertebrata; tetrapoda; mammalia; eutheria; primates XX SF subunit of DNA-PK [2]; SF by itself a heterodimer composed of a p70 and a p86 subunit [1]; SF ribosylated by PARP [2]; XX CP SK-BR3 [1]. XX FF subunit of DNA-dependent protein kinase and by itself a heterodimer [1]; FF known to bind to free ends of DNA [1]; FF may also bind to DNA in sequence-dependent manner [1]; FF concluded to recognize the primary sequence of base unpairing regions [1]; FF binds also to the IgH enhancer at elevated concentrations [1]; FF ADP-ribosylation circumvents binding to base unpairing regions [1]; FF physical interaction with PARP in vivo is independent of the presence of DNA and critical for synergistic binding to S/MARs [1]; FF involved in chromosome condensation [2]; XX IN T14055 PARP; human, Homo sapiens. XX BS R33749. BS R33750. BS R33765. BS R33773. BS R33774. BS R64781. BS R64769. BS R35856. XX DR TRANSPATH: MO000056113. DR SMARTDB: SB000054. XX RN [1]; RE0013868. RX PUBMED: 10400681. RA Galande S., Kohwi-Shigematsu T. RT Poly(ADP-ribose) polymerase and Ku autoantigen form a complex and synergistically bind to matrix attachment sequences RL J. Biol. Chem. 274:20521-20528 (1999). RN [2]; RE0014969. RX PUBMED: 10813395. RA Galande S., Kohwi-Shigematsu T. RT Caught in the act: binding of Ku and PARP to MARs reveals novel aspects of their functional interaction RL Crit. Rev. Eukaryot. Gene Expr. 10:63-72 (2000). XX //