Q9DE07 · NBN_CHICK
- ProteinNibrin
- GeneNBN
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids753 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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:12422221).
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 (By similarity).
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).
The MRN complex and rbbp8/CtIP are also required for chromosome alignment during metaphase (By similarity).
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 (By similarity).
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).
The MRN complex and rbbp8/CtIP are also required for chromosome alignment during metaphase (By similarity).
GO annotations
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNibrin
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Galloanserae > Galliformes > Phasianidae > Phasianinae > Gallus
Accessions
- Primary accessionQ9DE07
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes to DNA double-strand breaks (DSBs); recruited to DNA damage sites via association with phosphorylated proteins, such as phosphorylated H2AX.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000231047 | 1-753 | Nibrin | |||
Sequence: MWKLVPAAGPGEPFRLLVGTEYVVGRKNCAFLIQDDQSISRSHAVLTVSRPETTHSQSVSVPVLTIKDTSKYGTFVNGSKLSGASRSLQSGDRVNFGVFESKFRVEYESLVVCSSCLDVAQKTALNEAIQQLGGLVVNEWTKECTHLIMESVKVTVKTICALICGRPIVKPEFFSELMKAVQSRQQLPTPESFYPSVDEPAIGIDNMDLSGHPERKKIFSGKTFVFLTAKQHKKLGPAVILGGGEAKLMAEERKETSLLVSPEVCVVDVGVTNSQILGSESMRNWTDSILAVLESNNLRAIPEAEIGLAVIFMSTEIYCNPQRQPDNKAVTASTASKVRPVSSQSSTVDETIMPTAAADYSTLNVADTEIEEQTCMEIERTTSQTTRREKVAFQQAAVRENPSTSGTVNAGMLISRVNRTSGFGQKNHPHSPSKILEVDKPRECTPRQQSNSITNYFHVARKRERAEEGEETSLSKQAKLEKKPLPVSECTESSASSAWNSEKEQHGKGNNIQLGRESGELASDKTDIKITFSENPAPKKRKELDDVSEDVETLEMVFESRDLDWEEQTANGDQEAQSNKRKKRCLETKGSRTEEGNTKQREENEMLRKEEVGSVLTLEDKSKIKEESSVSIRNKLINHNKLEDDSSRLPSKLLLTEFRSLVVSCPRSNSPTMRNTKCRGQNNFKTFRKVPYPGAGQLPYIIGGSDLVAHQARKNSELEEWLREELEEQNRRAREESLADDLFRYDPNVKRRR | ||||||
Modified residue | 274 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 343 | Phosphoserine; by ATM | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
Interaction
Subunit
Component of the MRN complex composed of two heterodimers RAD50 and mre11 associated with a single NBN.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 22-81 | FHA | ||||
Sequence: YVVGRKNCAFLIQDDQSISRSHAVLTVSRPETTHSQSVSVPVLTIKDTSKYGTFVNGSKL | ||||||
Domain | 101-191 | BRCT 1 | ||||
Sequence: SKFRVEYESLVVCSSCLDVAQKTALNEAIQQLGGLVVNEWTKECTHLIMESVKVTVKTICALICGRPIVKPEFFSELMKAVQSRQQLPTPE | ||||||
Domain | 221-311 | BRCT 2 | ||||
Sequence: GKTFVFLTAKQHKKLGPAVILGGGEAKLMAEERKETSLLVSPEVCVVDVGVTNSQILGSESMRNWTDSILAVLESNNLRAIPEAEIGLAVI | ||||||
Region | 442-606 | Disordered | ||||
Sequence: RECTPRQQSNSITNYFHVARKRERAEEGEETSLSKQAKLEKKPLPVSECTESSASSAWNSEKEQHGKGNNIQLGRESGELASDKTDIKITFSENPAPKKRKELDDVSEDVETLEMVFESRDLDWEEQTANGDQEAQSNKRKKRCLETKGSRTEEGNTKQREENEM | ||||||
Compositional bias | 458-486 | Basic and acidic residues | ||||
Sequence: HVARKRERAEEGEETSLSKQAKLEKKPLP | ||||||
Motif | 461-467 | Nuclear localization signal | ||||
Sequence: RKRERAE | ||||||
Compositional bias | 489-512 | Polar residues | ||||
Sequence: ECTESSASSAWNSEKEQHGKGNNI | ||||||
Compositional bias | 534-568 | Basic and acidic residues | ||||
Sequence: ENPAPKKRKELDDVSEDVETLEMVFESRDLDWEEQ | ||||||
Compositional bias | 576-606 | Basic and acidic residues | ||||
Sequence: AQSNKRKKRCLETKGSRTEEGNTKQREENEM | ||||||
Motif | 739-748 | FxF/Y motif | ||||
Sequence: ADDLFRYDPN |
Domain
The FHA and BRCT domains specifically recognize and bind phosphorylated proteins.
The C-terminal domain contains a MRE11-binding site, and this interaction is required for the nuclear localization of the MRN complex.
The FxF/Y motif (also named EEXXXDDL motif) is required for the interaction with ATM and its recruitment to sites of DNA damage and promote the phosphorylation of ATM substrates, leading to the events of DNA damage response.
Sequence similarities
Belongs to the Nibrin family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length753
- Mass (Da)83,987
- Last updated2001-03-01 v1
- Checksum410BBE74123D9B06
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 458-486 | Basic and acidic residues | ||||
Sequence: HVARKRERAEEGEETSLSKQAKLEKKPLP | ||||||
Compositional bias | 489-512 | Polar residues | ||||
Sequence: ECTESSASSAWNSEKEQHGKGNNI | ||||||
Compositional bias | 534-568 | Basic and acidic residues | ||||
Sequence: ENPAPKKRKELDDVSEDVETLEMVFESRDLDWEEQ | ||||||
Compositional bias | 576-606 | Basic and acidic residues | ||||
Sequence: AQSNKRKKRCLETKGSRTEEGNTKQREENEM |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF230342 EMBL· GenBank· DDBJ | AAG47947.1 EMBL· GenBank· DDBJ | mRNA |