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Protein

Nibrin

Gene

NBN

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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 MRE11A. 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.5 Publications

GO - Molecular functioni

  • damaged DNA binding Source: GO_Central
  • protein N-terminus binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB

GO - Biological processi

  • blastocyst growth Source: Ensembl
  • cell cycle arrest Source: UniProtKB
  • cell proliferation Source: Ensembl
  • DNA damage checkpoint Source: MGI
  • DNA damage response, signal transduction by p53 class mediator Source: UniProtKB
  • DNA double-strand break processing Source: Reactome
  • DNA duplex unwinding Source: BHF-UCL
  • DNA replication Source: Reactome
  • DNA synthesis involved in DNA repair Source: Reactome
  • double-strand break repair Source: UniProtKB
  • double-strand break repair via homologous recombination Source: GO_Central
  • double-strand break repair via nonhomologous end joining Source: Reactome
  • intrinsic apoptotic signaling pathway Source: Ensembl
  • isotype switching Source: Ensembl
  • meiotic cell cycle Source: UniProtKB-KW
  • mitotic cell cycle checkpoint Source: UniProtKB
  • mitotic G2 DNA damage checkpoint Source: UniProtKB
  • negative regulation of telomere capping Source: BHF-UCL
  • neuromuscular process controlling balance Source: Ensembl
  • positive regulation of kinase activity Source: BHF-UCL
  • positive regulation of protein autophosphorylation Source: BHF-UCL
  • positive regulation of telomere maintenance Source: BHF-UCL
  • regulation of DNA-dependent DNA replication initiation Source: UniProtKB
  • regulation of signal transduction by p53 class mediator Source: Reactome
  • strand displacement Source: Reactome
  • telomere maintenance Source: UniProtKB
  • telomeric 3' overhang formation Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Cell cycle, DNA damage, DNA repair, Meiosis

Enzyme and pathway databases

ReactomeiR-HSA-2559586. DNA Damage/Telomere Stress Induced Senescence.
R-HSA-5685938. HDR through Single Strand Annealing (SSA).
R-HSA-5685939. HDR through MMEJ (alt-NHEJ).
R-HSA-5685942. HDR through Homologous Recombination (HRR).
R-HSA-5693548. Sensing of DNA Double Strand Breaks.
R-HSA-5693554. Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
R-HSA-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-HSA-5693568. Resolution of D-loop Structures through Holliday Junction Intermediates.
R-HSA-5693571. Nonhomologous End-Joining (NHEJ).
R-HSA-5693579. Homologous DNA Pairing and Strand Exchange.
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-69473. G2/M DNA damage checkpoint.
R-HSA-912446. Meiotic recombination.
SIGNORiO60934.

Names & Taxonomyi

Protein namesi
Recommended name:
Nibrin
Alternative name(s):
Cell cycle regulatory protein p95
Nijmegen breakage syndrome protein 1
Gene namesi
Name:NBN
Synonyms:NBS, NBS1, P95
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:7652. NBN.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • Mre11 complex Source: UniProtKB
  • nuclear chromosome, telomeric region Source: BHF-UCL
  • nuclear inclusion body Source: UniProtKB
  • nucleolus Source: BHF-UCL
  • nucleoplasm Source: Reactome
  • nucleus Source: BHF-UCL
  • PML body Source: UniProtKB
  • replication fork Source: Ensembl
  • site of double-strand break Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus, Telomere

Pathology & Biotechi

Involvement in diseasei

Nijmegen breakage syndrome (NBS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by chromosomal instability, radiation sensitivity, microcephaly, growth retardation, immunodeficiency and predisposition to cancer, particularly to lymphoid malignancies.
See also OMIM:251260
Breast cancer (BC)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA common malignancy originating from breast epithelial tissue. Breast neoplasms can be distinguished by their histologic pattern. Invasive ductal carcinoma is by far the most common type. Breast cancer is etiologically and genetically heterogeneous. Important genetic factors have been indicated by familial occurrence and bilateral involvement. Mutations at more than one locus can be involved in different families or even in the same case.
See also OMIM:114480
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti150 – 1501L → F in BC. 1 Publication
Corresponds to variant rs773119929 [ dbSNP | Ensembl ].
VAR_025795
Aplastic anemia (AA)1 Publication
Disease susceptibility may be associated with variations affecting the gene represented in this entry.
Disease descriptionA form of anemia in which the bone marrow fails to produce adequate numbers of peripheral blood elements. It is characterized by peripheral pancytopenia and marrow hypoplasia.
See also OMIM:609135

Defects in NBN might play a role in the pathogenesis of childhood acute lymphoblastic leukemia (ALL).

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi28 – 281R → A: Disrupts nuclear foci formation and block phosphorylation in response to ionizing radiation. 1 Publication
Mutagenesisi45 – 451H → A: Disrupts nuclear foci formation and block phosphorylation in response to ionizing radiation. 1 Publication
Mutagenesisi136 – 1372GG → EE: Disrupts nuclear foci formation and block phosphorylation in response to ionizing radiation. 1 Publication
Mutagenesisi176 – 1761Y → A: Disrupts nuclear foci formation and block phosphorylation in response to ionizing radiation. 1 Publication
Mutagenesisi343 – 3431S → A: Abrogates ATM-dependent phosphorylation. 1 Publication
Mutagenesisi397 – 3971S → A: Abrogates ATM-dependent phosphorylation. No loss of interaction with KPNA2. 2 Publications
Mutagenesisi465 – 4662KR → AA: Blocks the association with KPNA2, and reduces nuclear foci formation in response to ionizing radiation. 1 Publication
Mutagenesisi583 – 5831Q → K: No loss of interaction with KPNA2. 1 Publication
Mutagenesisi615 – 6151S → A: Abrogates ATM-dependent phosphorylation. 1 Publication
Mutagenesisi736 – 7372EE → AA: Decreases ATM binding. 1 Publication
Mutagenesisi741 – 7422DD → AA: Decreases ATM binding. 1 Publication
Mutagenesisi745 – 7462RY → AA: Decreases ATM binding. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MalaCardsiNBN.
MIMi114480. phenotype.
251260. phenotype.
609135. phenotype.
Orphaneti1331. Familial prostate cancer.
145. Hereditary breast and ovarian cancer syndrome.
647. Nijmegen breakage syndrome.
PharmGKBiPA31457.

Polymorphism and mutation databases

BioMutaiNBN.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 754754NibrinPRO_0000231043Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei278 – 2781Phosphoserine; by ATM1 Publication
Modified residuei337 – 3371PhosphothreonineCombined sources
Modified residuei343 – 3431Phosphoserine; by ATMCombined sources2 Publications
Modified residuei347 – 3471PhosphoserineCombined sources
Modified residuei397 – 3971PhosphoserineCombined sources1 Publication
Modified residuei402 – 4021PhosphothreonineCombined sources
Modified residuei432 – 4321PhosphoserineCombined sources
Modified residuei509 – 5091PhosphoserineCombined sources
Modified residuei518 – 5181PhosphoserineCombined sources
Modified residuei615 – 6151Phosphoserine1 Publication
Modified residuei673 – 6731PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated by ATM in response of ionizing radiation, and such phosphorylation is responsible intra-S phase checkpoint control and telomere maintenance.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO60934.
MaxQBiO60934.
PaxDbiO60934.
PeptideAtlasiO60934.
PRIDEiO60934.

PTM databases

iPTMnetiO60934.
PhosphoSiteiO60934.

Expressioni

Tissue specificityi

Ubiquitous. Expressed at high levels in testis.

Inductioni

Up-regulated by ionizing radiation (IR).1 Publication

Gene expression databases

BgeeiENSG00000104320.
CleanExiHS_NBN.
ExpressionAtlasiO60934. baseline and differential.
GenevisibleiO60934. HS.

Organism-specific databases

HPAiCAB003836.
HPA001429.

Interactioni

Subunit structurei

Component of the MRN complex composed of two heterodimers RAD50/MRE11A associated with a single NBN. Component of the BASC complex, at least composed of BRCA1, MSH2, MSH6, MLH1, ATM, BLM, RAD50 and MRE11A. Interacts with histone H2AFX this requires phosphorylation of H2AFX on 'Ser-139'. Interacts with HJURP, INTS3, KPNA2 and TERF2. Interacts with RBBP8; the interaction links the role of the MRN complex in DNA double-strand break sensing to resection. Interacts with SP100; recruits NBN to PML bodies. Interacts with ATF2. Interacts with MTOR, MAPKAP1 isoform 2 and RICTOR; indicative for an association with the mTORC2 complex. Interacts with herpes simplex virus 1 protein UL12.13 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EP300Q094725EBI-494844,EBI-447295
FANCD2Q9BXW96EBI-494844,EBI-359343
H2AFXP1610414EBI-494844,EBI-494830
MDC1Q1467626EBI-494844,EBI-495644
MRE11AP499593EBI-494844,EBI-396513
RAD17O759435EBI-494844,EBI-968231
SIRT1Q96EB65EBI-494844,EBI-1802965
VRK1Q9998613EBI-494844,EBI-1769146

GO - Molecular functioni

  • protein N-terminus binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi110763. 80 interactions.
DIPiDIP-33605N.
IntActiO60934. 28 interactions.
MINTiMINT-203482.
STRINGi9606.ENSP00000265433.

Structurei

3D structure databases

ProteinModelPortaliO60934.
SMRiO60934. Positions 8-109, 217-326.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 8360FHAPROSITE-ProRule annotationAdd
BLAST
Domaini105 – 18177BRCTAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni111 – 328218Mediates interaction with SP100By similarityAdd
BLAST
Regioni221 – 402182Interaction with MTOR, MAPKAP1 and RICTORAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi461 – 4677Nuclear localization signal
Motifi736 – 7438EEXXXDDL motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi448 – 4514Poly-Gln

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.1 Publication
The C-terminal domain contains a MRE11-binding site, and this interaction is required for the nuclear localization of the MRN complex.1 Publication
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.1 Publication

Sequence similaritiesi

Contains 1 BRCT domain.Curated
Contains 1 FHA domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IK5M. Eukaryota.
ENOG410Y1R8. LUCA.
GeneTreeiENSGT00390000000521.
HOVERGENiHBG053070.
InParanoidiO60934.
KOiK10867.
OMAiGKLPHII.
OrthoDBiEOG091G0BJ4.
PhylomeDBiO60934.
TreeFamiTF101103.

Family and domain databases

Gene3Di2.60.200.20. 1 hit.
3.40.50.10190. 1 hit.
InterProiIPR001357. BRCT_dom.
IPR013908. DNA-repair_Nbs1_C.
IPR000253. FHA_dom.
IPR032429. Nibrin_BRCT2.
IPR016592. Nibrin_met.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PfamiPF00498. FHA. 1 hit.
PF08599. Nbs1_C. 1 hit.
PF16508. NIBRIN_BRCT_II. 1 hit.
[Graphical view]
PIRSFiPIRSF011869. Nibrin_animal. 1 hit.
SMARTiSM00240. FHA. 1 hit.
SM01348. Nbs1_C. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEiPS50006. FHA_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O60934-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWKLLPAAGP AGGEPYRLLT GVEYVVGRKN CAILIENDQS ISRNHAVLTA
60 70 80 90 100
NFSVTNLSQT DEIPVLTLKD NSKYGTFVNE EKMQNGFSRT LKSGDGITFG
110 120 130 140 150
VFGSKFRIEY EPLVACSSCL DVSGKTALNQ AILQLGGFTV NNWTEECTHL
160 170 180 190 200
VMVSVKVTIK TICALICGRP IVKPEYFTEF LKAVESKKQP PQIESFYPPL
210 220 230 240 250
DEPSIGSKNV DLSGRQERKQ IFKGKTFIFL NAKQHKKLSS AVVFGGGEAR
260 270 280 290 300
LITEENEEEH NFFLAPGTCV VDTGITNSQT LIPDCQKKWI QSIMDMLQRQ
310 320 330 340 350
GLRPIPEAEI GLAVIFMTTK NYCDPQGHPS TGLKTTTPGP SLSQGVSVDE
360 370 380 390 400
KLMPSAPVNT TTYVADTESE QADTWDLSER PKEIKVSKME QKFRMLSQDA
410 420 430 440 450
PTVKESCKTS SNNNSMVSNT LAKMRIPNYQ LSPTKLPSIN KSKDRASQQQ
460 470 480 490 500
QTNSIRNYFQ PSTKKRERDE ENQEMSSCKS ARIETSCSLL EQTQPATPSL
510 520 530 540 550
WKNKEQHLSE NEPVDTNSDN NLFTDTDLKS IVKNSASKSH AAEKLRSNKK
560 570 580 590 600
REMDDVAIED EVLEQLFKDT KPELEIDVKV QKQEEDVNVR KRPRMDIETN
610 620 630 640 650
DTFSDEAVPE SSKISQENEI GKKRELKEDS LWSAKEISNN DKLQDDSEML
660 670 680 690 700
PKKLLLTEFR SLVIKNSTSR NPSGINDDYG QLKNFKKFKK VTYPGAGKLP
710 720 730 740 750
HIIGGSDLIA HHARKNTELE EWLRQEMEVQ NQHAKEESLA DDLFRYNPYL

KRRR
Length:754
Mass (Da):84,959
Last modified:August 1, 1998 - v1
Checksum:iCD602F09BA73DAB6
GO

Sequence cautioni

The sequence AAI08651 differs from that shown.Contaminating sequence. Potential poly-A sequence starting in position 550.Curated
The sequence CAH56160 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti247 – 2471G → R in BAD96976 (Ref. 6) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti93 – 931S → L in some childhood acute lymphoblastic leukemia patients; uncertain pathological significance; rare variant. 1 Publication
Corresponds to variant rs12721593 [ dbSNP | Ensembl ].
VAR_025792
Natural varianti95 – 951D → N in some childhood acute lymphoblastic leukemia patients; uncertain pathological significance; rare variant. 1 Publication
Corresponds to variant rs61753720 [ dbSNP | Ensembl ].
VAR_025793
Natural varianti105 – 1051K → N.1 Publication
Corresponds to variant rs13312858 [ dbSNP | Ensembl ].
VAR_025794
Natural varianti142 – 1421N → S.
Corresponds to variant rs769414 [ dbSNP | Ensembl ].
VAR_051226
Natural varianti150 – 1501L → F in BC. 1 Publication
Corresponds to variant rs773119929 [ dbSNP | Ensembl ].
VAR_025795
Natural varianti171 – 1711I → V in some childhood acute lymphoblastic leukemia patients; uncertain pathological significance; rare variant; associated with aplastic anemia at homozygosity. 2 Publications
Corresponds to variant rs61754966 [ dbSNP | Ensembl ].
VAR_025796
Natural varianti185 – 1851E → Q.6 Publications
Corresponds to variant rs1805794 [ dbSNP | Ensembl ].
VAR_025797
Natural varianti210 – 2101V → F.1 Publication
Corresponds to variant rs61754796 [ dbSNP | Ensembl ].
VAR_025798
Natural varianti215 – 2151R → W.1 Publication
Corresponds to variant rs34767364 [ dbSNP | Ensembl ].
VAR_025799
Natural varianti216 – 2161Q → K.1 Publication
Corresponds to variant rs769416 [ dbSNP | Ensembl ].
VAR_025800
Natural varianti266 – 2661P → L.1 Publication
Corresponds to variant rs769420 [ dbSNP | Ensembl ].
VAR_025801
Natural varianti408 – 4081K → E.
Corresponds to variant rs34120922 [ dbSNP | Ensembl ].
VAR_051227
Natural varianti497 – 4971T → A.1 Publication
Corresponds to variant rs3026268 [ dbSNP | Ensembl ].
VAR_025802
Natural varianti574 – 5741L → I.1 Publication
Corresponds to variant rs142334798 [ dbSNP | Ensembl ].
VAR_025803
Natural varianti679 – 6791Y → H Found in a renal cell carcinoma sample; somatic mutation. 1 Publication
VAR_064738

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF051334 mRNA. Translation: AAC39732.1.
AF058696 mRNA. Translation: AAC39752.1.
AB013139 Genomic DNA. Translation: BAA28616.1.
AF069291 Genomic DNA. Translation: AAC62232.1.
AK312410 mRNA. Translation: BAG35323.1.
AK223256 mRNA. Translation: BAD96976.1.
AY566246 Genomic DNA. Translation: AAS59158.1.
CH471060 Genomic DNA. Translation: EAW91660.1.
BC108650 mRNA. Translation: AAI08651.1. Sequence problems.
BC136802 mRNA. Translation: AAI36803.1.
BC136803 mRNA. Translation: AAI36804.1.
BX640816 mRNA. Translation: CAH56160.1. Different initiation.
CCDSiCCDS6249.1.
PIRiT00393.
RefSeqiNP_001019859.1. NM_001024688.2.
NP_002476.2. NM_002485.4.
XP_011515347.1. XM_011517045.1.
UniGeneiHs.492208.

Genome annotation databases

EnsembliENST00000265433; ENSP00000265433; ENSG00000104320.
GeneIDi4683.
KEGGihsa:4683.
UCSCiuc003yej.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF051334 mRNA. Translation: AAC39732.1.
AF058696 mRNA. Translation: AAC39752.1.
AB013139 Genomic DNA. Translation: BAA28616.1.
AF069291 Genomic DNA. Translation: AAC62232.1.
AK312410 mRNA. Translation: BAG35323.1.
AK223256 mRNA. Translation: BAD96976.1.
AY566246 Genomic DNA. Translation: AAS59158.1.
CH471060 Genomic DNA. Translation: EAW91660.1.
BC108650 mRNA. Translation: AAI08651.1. Sequence problems.
BC136802 mRNA. Translation: AAI36803.1.
BC136803 mRNA. Translation: AAI36804.1.
BX640816 mRNA. Translation: CAH56160.1. Different initiation.
CCDSiCCDS6249.1.
PIRiT00393.
RefSeqiNP_001019859.1. NM_001024688.2.
NP_002476.2. NM_002485.4.
XP_011515347.1. XM_011517045.1.
UniGeneiHs.492208.

3D structure databases

ProteinModelPortaliO60934.
SMRiO60934. Positions 8-109, 217-326.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110763. 80 interactions.
DIPiDIP-33605N.
IntActiO60934. 28 interactions.
MINTiMINT-203482.
STRINGi9606.ENSP00000265433.

PTM databases

iPTMnetiO60934.
PhosphoSiteiO60934.

Polymorphism and mutation databases

BioMutaiNBN.

Proteomic databases

EPDiO60934.
MaxQBiO60934.
PaxDbiO60934.
PeptideAtlasiO60934.
PRIDEiO60934.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265433; ENSP00000265433; ENSG00000104320.
GeneIDi4683.
KEGGihsa:4683.
UCSCiuc003yej.2. human.

Organism-specific databases

CTDi4683.
GeneCardsiNBN.
GeneReviewsiNBN.
HGNCiHGNC:7652. NBN.
HPAiCAB003836.
HPA001429.
MalaCardsiNBN.
MIMi114480. phenotype.
251260. phenotype.
602667. gene.
609135. phenotype.
neXtProtiNX_O60934.
Orphaneti1331. Familial prostate cancer.
145. Hereditary breast and ovarian cancer syndrome.
647. Nijmegen breakage syndrome.
PharmGKBiPA31457.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IK5M. Eukaryota.
ENOG410Y1R8. LUCA.
GeneTreeiENSGT00390000000521.
HOVERGENiHBG053070.
InParanoidiO60934.
KOiK10867.
OMAiGKLPHII.
OrthoDBiEOG091G0BJ4.
PhylomeDBiO60934.
TreeFamiTF101103.

Enzyme and pathway databases

ReactomeiR-HSA-2559586. DNA Damage/Telomere Stress Induced Senescence.
R-HSA-5685938. HDR through Single Strand Annealing (SSA).
R-HSA-5685939. HDR through MMEJ (alt-NHEJ).
R-HSA-5685942. HDR through Homologous Recombination (HRR).
R-HSA-5693548. Sensing of DNA Double Strand Breaks.
R-HSA-5693554. Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
R-HSA-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-HSA-5693568. Resolution of D-loop Structures through Holliday Junction Intermediates.
R-HSA-5693571. Nonhomologous End-Joining (NHEJ).
R-HSA-5693579. Homologous DNA Pairing and Strand Exchange.
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-69473. G2/M DNA damage checkpoint.
R-HSA-912446. Meiotic recombination.
SIGNORiO60934.

Miscellaneous databases

GeneWikiiNibrin.
GenomeRNAii4683.
PROiO60934.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000104320.
CleanExiHS_NBN.
ExpressionAtlasiO60934. baseline and differential.
GenevisibleiO60934. HS.

Family and domain databases

Gene3Di2.60.200.20. 1 hit.
3.40.50.10190. 1 hit.
InterProiIPR001357. BRCT_dom.
IPR013908. DNA-repair_Nbs1_C.
IPR000253. FHA_dom.
IPR032429. Nibrin_BRCT2.
IPR016592. Nibrin_met.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PfamiPF00498. FHA. 1 hit.
PF08599. Nbs1_C. 1 hit.
PF16508. NIBRIN_BRCT_II. 1 hit.
[Graphical view]
PIRSFiPIRSF011869. Nibrin_animal. 1 hit.
SMARTiSM00240. FHA. 1 hit.
SM01348. Nbs1_C. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEiPS50006. FHA_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNBN_HUMAN
AccessioniPrimary (citable) accession number: O60934
Secondary accession number(s): B2R626
, B2RNC5, O60672, Q32NF7, Q53FM6, Q63HR6, Q7LDM2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: August 1, 1998
Last modified: September 7, 2016
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

In case of infection by adenovirus E4, the MRN complex is inactivated and degraded by viral oncoproteins, thereby preventing concatenation of viral genomes in infected cells.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.