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

AC T04878 XX ID T04878 XX DT 20.11.2001 (created); mas. DT 01.02.2013 (updated); yre. CO Copyright (C), QIAGEN. XX FA Ref-1 XX SY APE; APE-1; APE1; apendonuclease 1; apex; apex nuclease; APEX1; APX; DNA-(apurinic or apyrimidinic site) lyase; HAP1; human AP endonuclease 1; redox factor 1; Ref 1; REF-1; REF-1 protein; REF1. XX OS human, Homo sapiens OC eukaryota; animalia; metazoa; chordata; vertebrata; tetrapoda; mammalia; eutheria; primates XX GE G001018 APEX1; HGNC: APEX1. XX HO Rrp1 (drosophila). XX SF redox and repair activity of Ref-1 are located on distinct domains [3]; SF although Cys65 of Ref-1 reported to be the redox catalytic site, it is not required for redox regulation of AP-1 DNA-binding [5]; SF conflict in protein sequence between EMBL entry #X59764 and SWISSPROT entry #P27695: pos. 1 (Start-Methionine) lacks in SWISSPROT entry; SF has two catalytic activities: Redox regulation (Reduction) and DNA-repair (A/P endonuclease) [3] [4] [1]; SF increase in extracellular calcium concentration causes increase of mRNA and protein levels [2]; XX CP ubiquitous [1]. XX FF Ref-1 exerts A/P (apurinic/apyrimidinic) endonuclease activity that catalyzes the initial step in AP site repair in DNA repair; FF furthermore Ref-1 exhibits redox activity [3]; FF potential transcription factor (transcriptional repressor) [2]; FF shows obviously sequence-specific DNA-binding activity [2]; FF can also function as auxiliary protein that potentiates the action of other transcription factors like AP-1 (c-Fos/c-Jun-heterodimer), Jun-Jun homodimer, NF-kappa B, Myb, and members of the ATF/CREB family by regulation of its redox state [1]; FF can also function as DNA-repair protein by its A/P (apurinic/apyrimidinic) endonuclease activity that catalyzes the initial step in AP site repair in human cells [3] [4]; XX IN T00123 c-Fos; human, Homo sapiens. IN T00132 c-Jun; rat, Rattus norvegicus. IN T00133 c-Jun; human, Homo sapiens. IN T01610 HIF-1alpha; human, Homo sapiens. IN T24826 HNRPL-isoform1; human, Homo sapiens. IN T23091 p300; Mammalia. IN T00671 p53; human, Homo sapiens. IN T08171 PSF; human, Homo sapiens. XX BS R39132. BS R34758. BS R11432. BS R25134. XX DR TRANSPATH: MO000021414. DR UniProtKB: P27695; XX RN [1]; RE0004709. RX PUBMED: 1380454. RA Xanthoudakis S., Curran T. RT Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme RL EMBO J. 11:3323-3335 (1992). RN [2]; RE0016991. RX PUBMED: 7961715. RA Okazaki T., Chung U., Nishishita T., Ebisu S., Usuda S., Mishiro S., Xanthoudakis S., Igarashi T., Ogata E. RT A redox factor protein, ref1, is involved in negative gene regulation by extracellular calcium RL J. Biol. Chem. 269:27855-27862 (1994). RN [3]; RE0017153. RX PUBMED: 7506414. RA Xanthoudakis S., Miao G. G., Curran T. RT The redox and DNA-repair activities of Ref-1 are encoded by nonoverlapping domains RL Proc. Natl. Acad. Sci. USA 91:23-27 (1994). RN [4]; RE0017154. RX PUBMED: 1719477. RA Robson C. N., Hickson I. D. RT Isolation of cDNA clones encoding a human apurinic/apyrimidinic endonuclease that corrects DNA repair and mutagenesis defects in E. coli xth (exonuclease III) mutants RL Nucleic Acids Res. 19:5519-5523 (1991). RN [5]; RE0025351. RX PUBMED: 12773568. RA Ordway J. M., Eberhart D., Curran T. RT Cysteine 64 of Ref-1 is not essential for redox regulation of AP-1 DNA binding. RL Mol. Cell. Biol. 23:4257-4266 (2003). RN [6]; RE0048117. RX PUBMED: 11092888. RA Parker A., Gu Y., Mahoney W., Lee S. H., Singh K. K., Lu A. L. RT Human homolog of the MutY repair protein (hMYH) physically interacts with proteins involved in long patch DNA base excision repair. RL J. Biol. Chem. 276:5547-5555 (2001). RN [7]; RE0048209. RX PUBMED: 15479784. RA Akbari M., Otterlei M., Pena-Diaz J., Aas P. A., Kavli B., Liabakk N. B., Hagen L., Imai K., Durandy A., Slupphaug G., Krokan H. E. RT Repair of U/G and U/A in DNA by UNG2-associated repair complexes takes place predominantly by short-patch repair both in proliferating and growth-arrested cells. RL Nucleic Acids Res. 32:5486-5498 (2004). RN [8]; RE0048234. RX PUBMED: 11601988. RA Dianova I. I., Bohr V. A., Dianov G. L. RT Interaction of human AP endonuclease 1 with flap endonuclease 1 and proliferating cell nuclear antigen involved in long-patch base excision repair. RL Biochemistry 40:12639-12644 (2001). RN [9]; RE0048237. RX PUBMED: 15713479. RA Xia L., Zheng L., Lee H. W., Bates S. E., Federico L., Shen B., O'Connor T. R. RT Human 3-methyladenine-DNA glycosylase: effect of sequence context on excision, association with PCNA, and stimulation by AP endonuclease. RL J. Mol. Biol. 346:1259-1274 (2005). RN [10]; RE0055920. RX PUBMED: 18208837. RA Zaky A., Busso C., Izumi T., Chattopadhyay R., Bassiouny A., Mitra S., Bhakat K. K. RT Regulation of the human AP-endonuclease (APE1/Ref-1) expression by the tumor suppressor p53 in response to DNA damage. RL Nucleic Acids Res. 36:1555-1566 (2008). RN [11]; RE0071307. RX PUBMED: 12036993. RA Krysan K., Lou M. F. RT Regulation of human thioltransferase (hTTase) gene by AP-1 transcription factor under oxidative stress. RL Invest. Ophthalmol. Vis. Sci. 43:1876-1883 (2002). XX //