An overlap between a network cluster obtained by Potts algorithm  and the best matching GO groups from the biological function GOA combined from MedScan annotation and public annotation. The cluster contains nine proteins involved in DNA repair and telomere capping: ATM – ataxia telangiectasia mutated homolog (human) (mapped); PRKDC – catalytic polypeptide of DNA activated protein kinase; NBS1 – nibrin; CHEK2 – protein kinase Chk2; XRCC5 – X-ray repair complementing defective repair in Chinese hamster cells 5; H2AFX – dolichyl-phosphate (UDP-N-acetylglucosamine) N-acetylglucosaminephosphotransferase 1 (GlcNAc-1-P transferase); G22P1 – thyroid autoantigen; NFBD1 – mediator of DNA damage checkpoint 1; TREX1 – three prime repair exonuclease 1. The ataxia-telangiectasia mutated (ATM) kinase signals the presence of DNA double-strand breaks in mammalian cells by phosphorylating proteins that initiate cell-cycle arrest, apoptosis, and DNA repair. The Mre11-Rad50-Nbs1 (MRN) complex acts as a double-strand break sensor for ATM and recruits ATM to broken DNA molecules . Activated ATM phosphorylates its downstream cellular targets H2AFX and Chk2 as well as proteins directly involved in DNA repair: XRCC5, TREX1 and NFBD1. G22P1 and PRKDC are subunits of DNA activated protein kinase that can be induced by DNA damage to promote DNA end joining . It also can attenuate CHK2 control of the damage checkpoint . A – The portion of GO classification overlapping with network cluster. The GO classification tree depiction is the same as in Figure 5A. B – The network cluster overlapping with GO classification from Figure A. Highlighted proteins belong to the best overlapping GO group from molecular function classification – telomere capping (GO:0016233). The proteins selected by the blue line belong to the second best overlapping GO group from combined biological processes classification – double-strand break repair (GO:0006302). Gray links indicate DirectRegulation relation, violet links indicate Binding relation, and green arrows represent ProtModification relations.