TERF1

This gene encodes a telomere specific protein which is a component of the telomere nucleoprotein complex. This protein is present at telomeres throughout the cell cycle and functions as an inhibitor of telomerase, acting in cis to limit the elongation of individual chromosome ends. The protein structure contains a C-terminal Myb motif, a dimerization domain near its N-terminus and an acidic N-terminus. Two transcripts of this gene are alternatively spliced products. [provided by RefSeq, Jul 2008]

TERF1

Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and negatively regulates telomere length. Involved in the regulation of the mitotic spindle. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. 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.

Biological Process cell divisionSource:UniProtKB-KW
Biological Process meiotic telomere clusteringSource:Ensembl
Biological Process negative regulation of DNA replicationSource:BHF-UCL1 Publication
Biological Process negative regulation of establishment of protein localization to telomereSource:BHF-UCL1 Publication
Biological Process negative regulation of establishment of protein-containing complex localization to telomereSource:BHF-UCL1 Publication
Biological Process negative regulation of establishment of RNA localization to telomereSource:BHF-UCL1 Publication
Biological Process negative regulation of exonuclease activitySource:BHF-UCL1 Publication
Biological Process negative regulation of telomerase activitySource:BHF-UCL1 Publication
Biological Process negative regulation of telomere maintenance via semi-conservative replicationSource:BHF-UCL1 Publication
Biological Process negative regulation of telomere maintenance via telomeraseSource:BHF-UCL1 Publication
Biological Process negative regulation of telomere maintenance via telomere lengtheningSource:BHF-UCL1 Publication
Biological Process negative regulation of telomeric D-loop disassemblySource:BHF-UCL1 Publication
Biological Process positive regulation of shelterin complex assemblySource:BHF-UCL1 Publication
Biological Process positive regulation of telomere maintenanceSource:ComplexPortal1 Publication
Biological Process response to xenobiotic stimulusSource:Ensembl
Biological Process t-circle formationSource:BHF-UCL1 Publication
Biological Process telomere cappingSource:ComplexPortal1 Publication
Biological Process telomere maintenanceSource:BHF-UCL1 Publication
Biological Process telomere maintenance via telomeraseSource:BHF-UCL1 Publication
Biological Process telomeric D-loop disassemblySource:BHF-UCL1 Publication

Nucleus
Cytoplasm, cytoskeleton, spindle
Chromosome, telomere
Colocalizes with telomeric DNA in interphase and prophase cells. Telomeric localization decreases in metaphase, anaphase and telophase. Associates with the mitotic spindle.

Phosphorylated preferentially on Ser-219 in an ATM-dependent manner in response to ionizing DNA damage.
ADP-ribosylation by TNKS1 or TNKS2 diminishes its ability to bind to telomeric DNA.
Ubiquitinated by RLIM/RNF12, leading to its degradation by the proteasome. Ubiquitinated by a SCF (SKP1-CUL1-F-box protein) ubiquitin-protein ligase complex, leading to its degradation by the proteasome.