Search Results
Overview
| Uniprot ID | O60934 |
|---|---|
| Protein Name | Nibrin |
| Gene Name | NBN |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 288 | LIPDCQKKWIQSIMD |
| 388 | PKEIKVSKMEQKFRM |
| 435 | NYQLSPTKLPSINKS |
| 441 | TKLPSINKSKDRASQ |
| 479 | NQEMSSCKSARIETS |
| 533 | TDLKSIVKNSASKSH |
| 582 | EIDVKVQKQEEDVNV |
| 622 | SQENEIGKKRELKED |
| 623 | QENEIGKKRELKEDS |
Function
Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis (PubMed:10888888, PubMed:15616588, PubMed:18411307, PubMed:18583988, PubMed:18678890, PubMed:19759395, PubMed:23115235, PubMed:28216226, PubMed:28867292, PubMed:9705271). The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an error-free mechanism which primarily occurs during S and G2 phases (PubMed:19759395, PubMed:28867292, PubMed:9705271). The complex (1) mediates the end resection of damaged DNA, which generates proper single-stranded DNA, a key initial steps in HR, and is (2) required for the recruitment of other repair factors and efficient activation of ATM and ATR upon DNA damage (PubMed:19759395, PubMed:9705271). The MRN complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11, to initiate end resection, which is required for single-strand invasion and recombination (PubMed:19759395, PubMed:28867292, PubMed:9705271). Within the MRN complex, NBN acts as a protein-protein adapter, which specifically recognizes and binds phosphorylated proteins, promoting their recruitment to DNA damage sites (PubMed:12419185, PubMed:15616588, PubMed:18411307, PubMed:18582474, PubMed:18583988, PubMed:18678890, PubMed:19759395, PubMed:19804756, PubMed:23762398, PubMed:24534091, PubMed:27814491, PubMed:27889449, PubMed:33836577). Recruits MRE11 and RAD50 components of the MRN complex to DSBs in response to DNA damage (PubMed:12419185, PubMed:18411307, PubMed:18583988, PubMed:18678890, PubMed:24534091, PubMed:26438602). Promotes the recruitment of PI3/PI4-kinase family members ATM, ATR, and probably DNA-PKcs to the DNA damage sites, activating their functions (PubMed:15064416, PubMed:15616588, PubMed:15790808, PubMed:16622404, PubMed:22464731, PubMed:30952868, PubMed:35076389). Mediates the recruitment of phosphorylated RBBP8/CtIP to DSBs, leading to cooperation between the MRN complex and RBBP8/CtIP to initiate end resection (PubMed:19759395, PubMed:27814491, PubMed:27889449, PubMed:33836577). RBBP8/CtIP specifically promotes the endonuclease activity of the MRN complex to clear DNA ends containing protein adducts (PubMed:27814491, PubMed:27889449, PubMed:30787182, PubMed:33836577). The MRN complex is also required for the processing of R-loops (PubMed:31537797). NBN also functions in telomere length maintenance via its interaction with TERF2: interaction with TERF2 during G1 phase preventing recruitment of DCLRE1B/Apollo to telomeres (PubMed:10888888, PubMed:28216226). NBN also promotes DNA repair choice at dysfunctional telomeres: NBN phosphorylation by CDK2 promotes non-homologous end joining repair at telomeres, while unphosphorylated NBN promotes microhomology-mediated end-joining (MMEJ) repair (PubMed:28216226). Enhances AKT1 phosphorylation possibly by association with the mTORC2 complex (PubMed:23762398)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Biological Process | GO:0051321 | meiotic cell cycle |
| Cellular Component | GO:0098687 | chromosomal region |
| Cellular Component | GO:0000781 | chromosome, telomeric region |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0030870 | Mre11 complex |
| Cellular Component | GO:0042405 | nuclear inclusion body |
| Cellular Component | GO:0005730 | nucleolus |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0016605 | PML body |
| Cellular Component | GO:0005657 | replication fork |
| Cellular Component | GO:0035861 | site of double-strand break |
| Molecular Function | GO:0140463 | chromatin-protein adaptor activity |
| Molecular Function | GO:0003684 | damaged DNA binding |
| Molecular Function | GO:0140297 | DNA-binding transcription factor binding |
| Molecular Function | GO:0042393 | histone binding |
| Molecular Function | GO:0140031 | phosphorylation-dependent protein binding |
| Molecular Function | GO:0043539 | protein serine/threonine kinase activator activity |
| Biological Process | GO:0001832 | blastocyst growth |
| Biological Process | GO:0000077 | DNA damage checkpoint signaling |
| Biological Process | GO:0030330 | DNA damage response, signal transduction by p53 class mediator |
| Biological Process | GO:0000729 | DNA double-strand break processing |
| Biological Process | GO:0110025 | DNA strand resection involved in replication fork processing |
| Biological Process | GO:0006302 | double-strand break repair |
| Biological Process | GO:0097681 | double-strand break repair via alternative nonhomologous end joining |
| Biological Process | GO:0000724 | double-strand break repair via homologous recombination |
| Biological Process | GO:0035825 | homologous recombination |
| Biological Process | GO:0045190 | isotype switching |
| Biological Process | GO:0007095 | mitotic G2 DNA damage checkpoint signaling |
| Biological Process | GO:0044818 | mitotic G2/M transition checkpoint |
| Biological Process | GO:1904354 | negative regulation of telomere capping |
| Biological Process | GO:2000781 | positive regulation of double-strand break repair |
| Biological Process | GO:1905168 | positive regulation of double-strand break repair via homologous recombination |
| Biological Process | GO:0032206 | positive regulation of telomere maintenance |
| Biological Process | GO:0031848 | protection from non-homologous end joining at telomere |
| Biological Process | GO:0070534 | protein K63-linked ubiquitination |
| Biological Process | GO:1990166 | protein localization to site of double-strand break |
| Biological Process | GO:0062176 | R-loop processing |
| Biological Process | GO:0051726 | regulation of cell cycle |
| Biological Process | GO:0030174 | regulation of DNA-templated DNA replication initiation |
| Biological Process | GO:0090656 | t-circle formation |
| Biological Process | GO:0000723 | telomere maintenance |
| Biological Process | GO:0043247 | telomere maintenance in response to DNA damage |
| Biological Process | GO:0090737 | telomere maintenance via telomere trimming |
| Biological Process | GO:0031860 | telomeric 3' overhang formation |
Reference
[1] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.
[2] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.
[3] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.
[4] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.