Mouse Anti-TERF2 Recombinant Antibody (CBYJT-2536) (CBMAB-T1693-YJ)

telomeric repeat binding factor 2

TERF2 is a telomere specific protein, TERF2, which is a component of the telomere nucleoprotein complex. TERF2 is present at telomeres in metaphase of the cell cycle, is a second negative regulator of telomere length and plays a key role in the protective activity of telomeres. While having similar telomere binding activity and domain organization, TERF2 differs from TERF1 in that its N terminus is basic rather than acidic.

Telomeric Repeat Binding Factor 2; TTAGGG Repeat-Binding Factor 2; Telomeric DNA-Binding Protein; TRBF2; TRF2; Telomeric Repeat Binding Protein 2; Telomeric Repeat-Binding Factor 2

Epigenetics and nuclear signaling,Cancer

Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and plays a central role in telomere maintenance and protection against end-to-end fusion of chromosomes (PubMed:15608617, PubMed:16166375, PubMed:20655466, PubMed:28216226, PubMed:9326950, PubMed:9326951, PubMed:9476899).
In addition to its telomeric DNA-binding role, required to recruit a number of factors and enzymes required for telomere protection, including the shelterin complex, TERF2IP/RAP1 and DCLRE1B/Apollo (PubMed:16166375, PubMed:20655466).
Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection (PubMed:16166375).
Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways (PubMed:16166375).
Together with DCLRE1B/Apollo, plays a key role in telomeric loop (T loop) formation by generating 3' single-stranded overhang at the leading end telomeres: T loops have been proposed to protect chromosome ends from degradation and repair (PubMed:20655466).
Required both to recruit DCLRE1B/Apollo to telomeres and activate the exonuclease activity of DCLRE1B/Apollo (PubMed:20655466, PubMed:28216226).
Preferentially binds to positive supercoiled DNA (PubMed:15608617, PubMed:20655466).
Together with DCLRE1B/Apollo, required to control the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology (PubMed:20655466).
Recruits TERF2IP/RAP1 to telomeres, thereby participating in to repressing homology-directed repair (HDR), which can affect telomere length (By similarity).

Axonal transport of messenger ribonucleoprotein complex
Cellular senescence
In utero embryonic development
Negative regulation of beta-galactosidase activity
Negative regulation of cellular senescence
Negative regulation of exonuclease activity
Negative regulation of gene expression
Negative regulation of t-circle formation
Negative regulation of telomere capping
Negative regulation of telomere maintenance
Negative regulation of telomere maintenance via recombination
Negative regulation of telomere maintenance via semi-conservative replication
Negative regulation of telomere maintenance via telomerase
Negative regulation of telomere maintenance via telomere lengthening
Negative regulation of telomere single strand break repair
Negative regulation of telomeric D-loop disassembly
Positive regulation of gene expression
Positive regulation of nitric-oxide synthase activity
Positive regulation of telomere maintenance
Protection from non-homologous end joining at telomere
Protein localization to chromosome, telomeric region
Regulation of telomere maintenance
Regulation of telomere maintenance via telomerase
RNA-templated DNA biosynthetic process
Telomere capping
Telomere maintenance
Telomeric D-loop disassembly
Telomeric loop formation

Nucleus PROSITE-ProRule annotation
Chromosome, telomere
Note: Colocalizes with telomeric DNA in interphase cells and is located at chromosome ends during metaphase.

Phosphorylated upon DNA damage, most probably by ATM. Phosphorylated TERF2 is not bound to telomeric DNA, and rapidly localizes to damage sites.
Methylated by PRMT1 at multiple arginines within the N-terminal Arg-rich region. Methylation may control association with telomeres.