Nbn
entrez
27354
canonical
uniprot
Q9R207
canonical
ensembl
ENSMUSG00000028224
resolver
ensp
ENSMUSP00000029879
resolver
enst
ENSMUST00000029879
resolver
genesymbol
Nbn
resolver
genesymbol_syn
Nbs1
resolver
uniprot
O88981
resolver
uniprot
Q3UY57
resolver
uniprot
Q811I6
resolver
uniprot
Q8CCY0
resolver
uniprot
Q9R1X1
resolver
uniprot_entry
NBN_MOUSE
resolver
uniprot_sec
O88981
resolver
uniprot_sec
Q3UY57
resolver
uniprot_sec
Q811I6
resolver
uniprot_sec
Q8CCY0
resolver
uniprot_sec
Q9R1X1
resolver
amino_acid_sequence
MWKLLPAAGAAPGEPYRLLAGVEYVVGRKNCGILIENDQSISRNHAVLTVNFPVTSLSQTDEIPTLTIKDNSKYGTFVNEEKMQTGLSCTLKTGDRVTFGVFESKFRVEYEPLVVCSSCLDVSGKTVLNQAILQLGGLTANNWTEECTHLVMSAVKVTIKTICALICGRPIIKPEYFSEFLKAVESKKQPPDIESFYPPIDEPAIGSKSVDLSGRHERKQIFKGKTFVFLNAKQHKKLSSAVAFGGGEARLMAEDDEEEQSFFSAPGTCVVDVGITNTQLIISHSQKKWIHLIMDTLQRNGLRPIPEAEIGLAVIFMTTENYCNPQGQPCTELKTTTPGPSLSQVLSANGKIIPSAPVNMTTYVADTESEPADTCMPLSERPEEVKIPGLEQSSRKLSQETFNIKEAPKPSSKANNVASDTLVRGKTPSYQLSPMKFPVANKNKDWTSQQQQNSIKNYFQPCTRKRERDEDNPELSSCKSSRMELSCSLLEQTQPAGPSLWKSKEHQSQNATLDREADTSSVGGMDIELNRKSPDRKPLPTETLRPRKRKDVDLATEEEVLEELLRSTKPELAVQVKVEKQEADDTIRKKPRMDAERNRPLNGGSEPESNSALQEDEREKKDELQTESWSTKHEIANSDGLQDSSEELPRKLLLTEFRSLVVSNHNSTSRNLCVNECGPLKNFKKFKKATFPGAGKLPHIIGGSDLVGHHARKNTELEEWLKQEMEVQKQQAKEESLADDLFRYNPNVKRR
uniprot
proteins
function
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:17291760, PubMed:22464731, PubMed:28216226). 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 (By similarity). 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 (By similarity). 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 (By similarity). 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 (By similarity). Recruits MRE11 and RAD50 components of the MRN complex to DSBs in response to DNA damage (By similarity). Promotes the recruitment of PI3/PI4-kinase family members ATM, ATR, and probably DNA-PKcs to the DNA damage sites, activating their functions (PubMed:22464731). Mediates the recruitment of phosphorylated RBBP8/CtIP to DSBs, leading to cooperation between the MRN complex and RBBP8/CtIP to initiate end resection (By similarity). RBBP8/CtIP specifically promotes the endonuclease activity of the MRN complex to clear DNA ends containing protein adducts (By similarity). The MRN complex is also required for the processing of R-loops (By similarity). 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: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 (By similarity). {ECO:0000250|UniProtKB:O60934, ECO:0000269|PubMed:17291760, ECO:0000269|PubMed:22464731, ECO:0000269|PubMed:28216226}.
uniprot
proteins
mass_dalton
83795
uniprot
proteins
mutagenesis
MUTAGEN 433; /note="S->A: Does not affect interaction with TERF2."; /evidence="ECO:0000269|PubMed:28216226"; MUTAGEN 433; /note="S->D: Mimics phosphorylation; impaired interaction with TERF2."; /evidence="ECO:0000269|PubMed:28216226
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated at Lys-436 via 'Lys-6'-linked ubiquitin chains by RNF8, promoting NBN recruitment to DNA double-strand breaks (DSBs) (By similarity). Ubiquitinated at Lys-684 and Lys-688 via 'Lys-63'-linked ubiquitin chains by PELI1: ubiquitination takes place following PELI1 phosphorylation and promotes ATM activation and DNA repair (By similarity). Ubiquitinated at Lys-733 via 'Lys-63'-linked ubiquitin chains by the SCF(SKP2) complex: ubiquitination takes place following SKP2 phosphorylation and promotes ATM activation and DNA repair (PubMed:22464731). {ECO:0000250|UniProtKB:O60934, ECO:0000269|PubMed:22464731}.; PTM: Phosphorylated by ATM in response of ionizing radiation, and such phosphorylation is responsible intra-S phase checkpoint control and telomere maintenance (By similarity). Phosphorylated at Ser-433 by CDK2 in S/G2 phases abolishes interaction with TERF2, enabling DCLRE1B/Apollo recruitment to telomeres (PubMed:28216226). Phosphorylation at Ser-433 in response to dysfunctional telomeres promotes non-homologous end joining repair at telomeres, while dephosphorylation by PPP1CA promotes microhomology-mediated end-joining (MMEJ) repair (PubMed:28216226). {ECO:0000250|UniProtKB:O60934, ECO:0000269|PubMed:28216226}.
uniprot
proteins
protein_family
Nibrin family
uniprot
proteins
pubmed
10640816
uniprot
proteins
pubmed
10915761
uniprot
proteins
pubmed
11231126
uniprot
proteins
pubmed
12470659
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17291760
uniprot
proteins
pubmed
17376776
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22464731
uniprot
proteins
pubmed
28216226
uniprot
proteins
pubmed
30017584
uniprot
proteins
sequence_length
751
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O60934}. Chromosome {ECO:0000250|UniProtKB:O60934}. Nucleus, PML body {ECO:0000250|UniProtKB:O60934}. Chromosome, telomere {ECO:0000269|PubMed:28216226}. Note=Localizes to discrete nuclear foci after treatment with genotoxic agents. Localizes to DNA double-strand breaks (DSBs); recruited to DNA damage sites via association with phosphorylated proteins, such as phosphorylated H2AX, phosphorylated MDC1 and phosphorylated RAD17. Acetylation of 'Lys-5' of histone H2AX (H2AXK5ac) promotes NBN/NBS1 assembly at the sites of DNA damage. {ECO:0000250|UniProtKB:O60934}.
uniprot
proteins