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IID00759
UniprotO60934
ProteinNibrin
GeneNBN
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
754
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 423-438 Hetero dimer : IID00837Complex
 Evidence X-RAY 5wqd H Reference
       Region 5wqd H 423-424 disorder
       Region 5wqd H 425-436 order
       Region 5wqd H 437-438 disorder
 Evidence X-RAY 5wqd I Reference
       Region 5wqd I 423-423 disorder
       Region 5wqd I 424-436 order
       Region 5wqd I 437-438 disorder
 Evidence X-RAY 5wqd J Reference
       Region 5wqd J 423-426 disorder
       Region 5wqd J 427-436 order
       Region 5wqd J 437-438 disorder
 Evidence X-RAY 5wqd K Reference
       Region 5wqd K 423-426 disorder
       Region 5wqd K 427-436 order
       Region 5wqd K 437-438 disorder
 Evidence X-RAY 5wqd L Reference
       Region 5wqd L 423-426 disorder
       Region 5wqd L 427-436 order
       Region 5wqd L 437-438 disorder
 Evidence X-RAY 5wqd M Reference
       Region 5wqd M 423-428 disorder
       Region 5wqd M 429-435 order
       Region 5wqd M 436-438 disorder
 Evidence X-RAY 5wqd N Reference
       Region 5wqd N 423-426 disorder
       Region 5wqd N 427-435 order
       Region 5wqd N 436-438 disorder
SeqProS predicted 424-436 This region is predicted to be disordered by NeProc and AlphaFold (pLDDT < 68.5). Hetero dimer : IID00837Complex
       Region 5wqd H 425-436 order
       Region 5wqd I 424-436 order
       Region 5wqd J 427-436 order
       Region 5wqd K 427-436 order
       Region 5wqd L 427-436 order
       Region 5wqd M 429-435 order
       Region 5wqd N 427-435 order
Seqphosphorylation
    615-615 Phosphoserine
    518-518 Phosphoserine
    673-673 Phosphoserine
    509-509 Phosphoserine
    402-402 Phosphothreonine
    432-432 Phosphoserine
    397-397 Phosphoserine
    343-343 Phosphoserine; by ATM
    347-347 Phosphoserine
    337-337 Phosphothreonine
    278-278 Phosphoserine; by ATM
 
Prediction
NeProc
Disorder 334-704,714-717,728-754
Order 1-53,60-327,332-333,705-713,718-727
ProS 360-366,373-377,426-430,454-461,596-605,611-627,637-667,673-704,714-717,736-750
AlphaFold
Disorder 9-12,54-61,204-209,275-281,328-649,651-652,655-655,664-692,694-716,749-754
Order 1-8,13-53,62-203,210-274,282-327,650-650,653-654,656-663,693-693,717-748
Pfam Hmmer
PF00498 24-100 2.1e-13
PF00533 105-181 0.00019
PF08599 682-746 2.4e-50
SEG 410-419
Function
Function in SwissProt
Component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. The complex is involved in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity, cell cycle checkpoint control and meiosis. The complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11. RAD50 may be required to bind DNA ends and hold them in close proximity. NBN modulate the DNA damage signal sensing by recruiting PI3/PI4-kinase family members ATM, ATR, and probably DNA-PKcs to the DNA damage sites and activating their functions. It can also recruit MRE11 and RAD50 to the proximity of DSBs by an interaction with the histone H2AX. NBN also functions in telomere length maintenance by generating the 3' overhang which serves as a primer for telomerase dependent telomere elongation. NBN is a major player in the control of intra-S-phase checkpoint and there is some evidence that NBN is involved in G1 and G2 checkpoints. The roles of NBS1/MRN encompass DNA damage sensor, signal transducer, and effector, which enable cells to maintain DNA integrity and genomic stability. Forms a complex with RBBP8 to link DNA double-strand break sensing to resection. Enhances AKT1 phosphorylation possibly by association with the mTORC2 complex.
Biological Process
See also
Diagram with PDB data
H2AX/MDC1Crystal structure of the MDC1 brct repeat in complex with the histone tail of gamma-H2AX