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Protein

Nibrin

Gene

Nbn

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processCell cycle, DNA damage, DNA repair, Meiosis

Enzyme and pathway databases

ReactomeiR-MMU-2559586 DNA Damage/Telomere Stress Induced Senescence
R-MMU-5685938 HDR through Single Strand Annealing (SSA)
R-MMU-5685939 HDR through MMEJ (alt-NHEJ)
R-MMU-5685942 HDR through Homologous Recombination (HRR)
R-MMU-5693548 Sensing of DNA Double Strand Breaks
R-MMU-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-MMU-5693568 Resolution of D-loop Structures through Holliday Junction Intermediates
R-MMU-5693571 Nonhomologous End-Joining (NHEJ)
R-MMU-5693579 Homologous DNA Pairing and Strand Exchange
R-MMU-5693607 Processing of DNA double-strand break ends
R-MMU-5693616 Presynaptic phase of homologous DNA pairing and strand exchange
R-MMU-6804756 Regulation of TP53 Activity through Phosphorylation
R-MMU-69473 G2/M DNA damage checkpoint

Names & Taxonomyi

Protein namesi
Recommended name:
Nibrin
Alternative name(s):
Cell cycle regulatory protein p95
Nijmegen breakage syndrome protein 1 homolog
Gene namesi
Name:Nbn
Synonyms:Nbs1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1351625 Nbn

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Nucleus, Telomere

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002310441 – 751NibrinAdd BLAST751

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei337PhosphothreonineBy similarity1
Modified residuei343Phosphoserine; by ATM1 Publication1
Modified residuei347PhosphoserineBy similarity1
Modified residuei398PhosphoserineCombined sources1
Modified residuei433PhosphoserineBy similarity1
Modified residuei508PhosphoserineBy similarity1
Cross-linki569Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki580Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

Post-translational modificationi

Phosphorylated by ATM in response of ionizing radiation, and such phosphorylation is responsible intra-S phase checkpoint control and telomere maintenance.By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9R207
MaxQBiQ9R207
PaxDbiQ9R207
PeptideAtlasiQ9R207
PRIDEiQ9R207

PTM databases

iPTMnetiQ9R207
PhosphoSitePlusiQ9R207
SwissPalmiQ9R207

Expressioni

Tissue specificityi

High expression in the liver, heart and testis. Low expression in all other tissues analyzed. In the cerebellum the postmitotic Purkinje cells are marked specifically.1 Publication

Developmental stagei

A low level of expression is observed in all tissues. Highly specific expression was observed in organs with physiologic DNA double strand breakage (DSB), such as testis, thymus and spleen. Enhanced expression is also found at sites of high proliferative activity. These are the subventricular layer of the telencephalon and the diencephalon, the liver, lung, kidney and gut, as well as striated and smooth muscle cells in various organs.1 Publication

Gene expression databases

BgeeiENSMUSG00000028224 Expressed in 285 organ(s), highest expression level in ear
CleanExiMM_NBN
ExpressionAtlasiQ9R207 baseline and differential
GenevisibleiQ9R207 MM

Interactioni

Subunit structurei

Component of the MRN complex composed of two heterodimers RAD50/MRE11 associated with a single NBN (By similarity). As part of the MRN complex, interacts with MCM9; the interaction recruits the complex to DNA repair sites (By similarity). Component of the BASC complex, at least composed of BRCA1, MSH2, MSH6, MLH1, ATM, BLM, RAD50, MRE11 and NBN (By similarity). Interacts with histone H2AFX this requires phosphorylation of H2AFX on 'Ser-139' (By similarity). Interacts with HJURP, INTS3, KPNA2 and TERF2 (By similarity). Interacts with RBBP8; the interaction links the role of the MRN complex in DNA double-strand break sensing to resection (By similarity). Interacts with SP100; recruits NBN to PML bodies (PubMed:12470659). Interacts with ATF2 (By similarity). Interacts with MTOR, MAPKAP1 isoform 2 and RICTOR; indicative for an association with the mTORC2 complex (By similarity). Interacts with MRNIP (By similarity).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Mre11Q612162EBI-2014862,EBI-2014813

GO - Molecular functioni

Protein-protein interaction databases

BioGridi205163, 8 interactors
DIPiDIP-46804N
IntActiQ9R207, 2 interactors
STRINGi10090.ENSMUSP00000029879

Structurei

3D structure databases

ProteinModelPortaliQ9R207
SMRiQ9R207
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini24 – 83FHAPROSITE-ProRule annotationAdd BLAST60
Domaini105 – 181BRCTAdd BLAST77

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni111 – 328Mediates interaction with SP1001 PublicationAdd BLAST218
Regioni221 – 403Interaction with MTOR, MAPKAP1 and RICTORBy similarityAdd BLAST183

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi461 – 467Nuclear localization signalBy similarity7
Motifi734 – 741EEXXXDDL motif8

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi449 – 452Poly-Gln4

Domaini

The FHA and BRCT domains are likely to have a crucial role for both binding to histone H2AFX and for relocalization of MRE11/RAD50 complex to the vicinity of DNA damage.By similarity
The C-terminal domain contains a MRE11-binding site, and this interaction is required for the nuclear localization of the MRN complex.By similarity
The EEXXXDDL motif at the C-terminus 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.By similarity

Phylogenomic databases

eggNOGiENOG410IK5M Eukaryota
ENOG410Y1R8 LUCA
GeneTreeiENSGT00390000000521
HOGENOMiHOG000231654
HOVERGENiHBG053070
InParanoidiQ9R207
KOiK10867
OMAiLWSTKEE
OrthoDBiEOG091G0BJ4
PhylomeDBiQ9R207
TreeFamiTF101103

Family and domain databases

CDDicd00027 BRCT, 1 hit
cd00060 FHA, 1 hit
Gene3Di3.40.50.10190, 1 hit
InterProiView protein in InterPro
IPR001357 BRCT_dom
IPR036420 BRCT_dom_sf
IPR013908 DNA-repair_Nbs1_C
IPR000253 FHA_dom
IPR032429 Nibrin_BRCT2
IPR016592 Nibrin_met
IPR008984 SMAD_FHA_dom_sf
PfamiView protein in Pfam
PF00498 FHA, 1 hit
PF08599 Nbs1_C, 1 hit
PF16508 NIBRIN_BRCT_II, 1 hit
PIRSFiPIRSF011869 Nibrin_animal, 1 hit
SMARTiView protein in SMART
SM00240 FHA, 1 hit
SM01348 Nbs1_C, 1 hit
SUPFAMiSSF49879 SSF49879, 1 hit
SSF52113 SSF52113, 1 hit
PROSITEiView protein in PROSITE
PS50006 FHA_DOMAIN, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q9R207-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MWKLLPAAGA APGEPYRLLA GVEYVVGRKN CGILIENDQS ISRNHAVLTV
60 70 80 90 100
NFPVTSLSQT DEIPTLTIKD NSKYGTFVNE EKMQTGLSCT LKTGDRVTFG
110 120 130 140 150
VFESKFRVEY EPLVVCSSCL DVSGKTVLNQ AILQLGGLTA NNWTEECTHL
160 170 180 190 200
VMSAVKVTIK TICALICGRP IIKPEYFSEF LKAVESKKQP PDIESFYPPI
210 220 230 240 250
DEPAIGSKSV DLSGRHERKQ IFKGKTFVFL NAKQHKKLSS AVAFGGGEAR
260 270 280 290 300
LMAEDDEEEQ SFFSAPGTCV VDVGITNTQL IISHSQKKWI HLIMDTLQRN
310 320 330 340 350
GLRPIPEAEI GLAVIFMTTE NYCNPQGQPC TELKTTTPGP SLSQVLSANG
360 370 380 390 400
KIIPSAPVNM TTYVADTESE PADTCMPLSE RPEEVKIPGL EQSSRKLSQE
410 420 430 440 450
TFNIKEAPKP SSKANNVASD TLVRGKTPSY QLSPMKFPVA NKNKDWTSQQ
460 470 480 490 500
QQNSIKNYFQ PCTRKRERDE DNPELSSCKS SRMELSCSLL EQTQPAGPSL
510 520 530 540 550
WKSKEHQSQN ATLDREADTS SVGGMDIELN RKSPDRKPLP TETLRPRKRK
560 570 580 590 600
DVDLATEEEV LEELLRSTKP ELAVQVKVEK QEADDTIRKK PRMDAERNRP
610 620 630 640 650
LNGGSEPESN SALQEDEREK KDELQTESWS TKHEIANSDG LQDSSEELPR
660 670 680 690 700
KLLLTEFRSL VVSNHNSTSR NLCVNECGPL KNFKKFKKAT FPGAGKLPHI
710 720 730 740 750
IGGSDLVGHH ARKNTELEEW LKQEMEVQKQ QAKEESLADD LFRYNPNVKR

R
Length:751
Mass (Da):83,795
Last modified:May 1, 2000 - v1
Checksum:iC9F597CC08227B2C
GO

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A2AMG5A2AMG5_MOUSE
Nibrin
Nbn
548Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti9G → S in AAH44773 (PubMed:15489334).Curated1
Sequence conflicti11 – 12AP → SL in AAC62113 (Ref. 3) Curated2
Sequence conflicti325P → Q in BAE22356 (PubMed:16141072).Curated1
Sequence conflicti366D → E in BAA76298 (Ref. 2) Curated1
Sequence conflicti455I → F in BAA76298 (Ref. 2) Curated1
Sequence conflicti513L → Q in AAH44773 (PubMed:15489334).Curated1
Sequence conflicti664N → K in AAH44773 (PubMed:15489334).Curated1
Sequence conflicti676E → D in AAH44773 (PubMed:15489334).Curated1
Sequence conflicti679P → S in AAH44773 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF076687 mRNA Translation: AAD20943.1
AB016988 mRNA Translation: BAA76298.1
AF092840 mRNA Translation: AAC62113.1
BC044773 mRNA Translation: AAH44773.1
BC055061 mRNA Translation: AAH55061.1
AK134960 mRNA Translation: BAE22356.1
AK031933 mRNA Translation: BAC27610.1
CCDSiCCDS17986.1
RefSeqiNP_038780.3, NM_013752.3
UniGeneiMm.20866

Genome annotation databases

EnsembliENSMUST00000029879; ENSMUSP00000029879; ENSMUSG00000028224
GeneIDi27354
KEGGimmu:27354
UCSCiuc008sbn.1 mouse

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF076687 mRNA Translation: AAD20943.1
AB016988 mRNA Translation: BAA76298.1
AF092840 mRNA Translation: AAC62113.1
BC044773 mRNA Translation: AAH44773.1
BC055061 mRNA Translation: AAH55061.1
AK134960 mRNA Translation: BAE22356.1
AK031933 mRNA Translation: BAC27610.1
CCDSiCCDS17986.1
RefSeqiNP_038780.3, NM_013752.3
UniGeneiMm.20866

3D structure databases

ProteinModelPortaliQ9R207
SMRiQ9R207
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi205163, 8 interactors
DIPiDIP-46804N
IntActiQ9R207, 2 interactors
STRINGi10090.ENSMUSP00000029879

PTM databases

iPTMnetiQ9R207
PhosphoSitePlusiQ9R207
SwissPalmiQ9R207

Proteomic databases

EPDiQ9R207
MaxQBiQ9R207
PaxDbiQ9R207
PeptideAtlasiQ9R207
PRIDEiQ9R207

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029879; ENSMUSP00000029879; ENSMUSG00000028224
GeneIDi27354
KEGGimmu:27354
UCSCiuc008sbn.1 mouse

Organism-specific databases

CTDi4683
MGIiMGI:1351625 Nbn

Phylogenomic databases

eggNOGiENOG410IK5M Eukaryota
ENOG410Y1R8 LUCA
GeneTreeiENSGT00390000000521
HOGENOMiHOG000231654
HOVERGENiHBG053070
InParanoidiQ9R207
KOiK10867
OMAiLWSTKEE
OrthoDBiEOG091G0BJ4
PhylomeDBiQ9R207
TreeFamiTF101103

Enzyme and pathway databases

ReactomeiR-MMU-2559586 DNA Damage/Telomere Stress Induced Senescence
R-MMU-5685938 HDR through Single Strand Annealing (SSA)
R-MMU-5685939 HDR through MMEJ (alt-NHEJ)
R-MMU-5685942 HDR through Homologous Recombination (HRR)
R-MMU-5693548 Sensing of DNA Double Strand Breaks
R-MMU-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-MMU-5693568 Resolution of D-loop Structures through Holliday Junction Intermediates
R-MMU-5693571 Nonhomologous End-Joining (NHEJ)
R-MMU-5693579 Homologous DNA Pairing and Strand Exchange
R-MMU-5693607 Processing of DNA double-strand break ends
R-MMU-5693616 Presynaptic phase of homologous DNA pairing and strand exchange
R-MMU-6804756 Regulation of TP53 Activity through Phosphorylation
R-MMU-69473 G2/M DNA damage checkpoint

Miscellaneous databases

PROiPR:Q9R207
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000028224 Expressed in 285 organ(s), highest expression level in ear
CleanExiMM_NBN
ExpressionAtlasiQ9R207 baseline and differential
GenevisibleiQ9R207 MM

Family and domain databases

CDDicd00027 BRCT, 1 hit
cd00060 FHA, 1 hit
Gene3Di3.40.50.10190, 1 hit
InterProiView protein in InterPro
IPR001357 BRCT_dom
IPR036420 BRCT_dom_sf
IPR013908 DNA-repair_Nbs1_C
IPR000253 FHA_dom
IPR032429 Nibrin_BRCT2
IPR016592 Nibrin_met
IPR008984 SMAD_FHA_dom_sf
PfamiView protein in Pfam
PF00498 FHA, 1 hit
PF08599 Nbs1_C, 1 hit
PF16508 NIBRIN_BRCT_II, 1 hit
PIRSFiPIRSF011869 Nibrin_animal, 1 hit
SMARTiView protein in SMART
SM00240 FHA, 1 hit
SM01348 Nbs1_C, 1 hit
SUPFAMiSSF49879 SSF49879, 1 hit
SSF52113 SSF52113, 1 hit
PROSITEiView protein in PROSITE
PS50006 FHA_DOMAIN, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiNBN_MOUSE
AccessioniPrimary (citable) accession number: Q9R207
Secondary accession number(s): O88981
, Q3UY57, Q811I6, Q8CCY0, Q9R1X1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: May 1, 2000
Last modified: November 7, 2018
This is version 143 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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