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Protein

Nibrin

Gene

NBN

Organism
Homo sapiens (Human)
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.5 Publications

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.

GO - Molecular functioni

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

GO - Biological processi

Keywordsi

Biological processCell 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

EuPathDBiHostDB:ENSG00000104320.13
HGNCiHGNC:7652 NBN
MIMi602667 gene
neXtProtiNX_O60934

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

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)DescriptionActionsGraphical viewLength
Natural variantiVAR_025795150L → F in BC. 1 PublicationCorresponds to variant dbSNP:rs773119929Ensembl.1
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).1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi28R → A: Disrupts nuclear foci formation and block phosphorylation in response to ionizing radiation. 1 Publication1
Mutagenesisi45H → A: Disrupts nuclear foci formation and block phosphorylation in response to ionizing radiation. 1 Publication1
Mutagenesisi136 – 137GG → EE: Disrupts nuclear foci formation and block phosphorylation in response to ionizing radiation. 1 Publication2
Mutagenesisi176Y → A: Disrupts nuclear foci formation and block phosphorylation in response to ionizing radiation. 1 Publication1
Mutagenesisi343S → A: Abrogates ATM-dependent phosphorylation. 1 Publication1
Mutagenesisi397S → A: Abrogates ATM-dependent phosphorylation. No loss of interaction with KPNA2. 2 Publications1
Mutagenesisi465 – 466KR → AA: Blocks the association with KPNA2, and reduces nuclear foci formation in response to ionizing radiation. 1 Publication2
Mutagenesisi583Q → K: No loss of interaction with KPNA2. 1 Publication1
Mutagenesisi615S → A: Abrogates ATM-dependent phosphorylation. 1 Publication1
Mutagenesisi736 – 737EE → AA: Decreases ATM binding. 1 Publication2
Mutagenesisi741 – 742DD → AA: Decreases ATM binding. 1 Publication2
Mutagenesisi745 – 746RY → AA: Decreases ATM binding. 1 Publication2

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi4683
GeneReviewsiNBN
MalaCardsiNBN
MIMi114480 phenotype
251260 phenotype
609135 phenotype
OpenTargetsiENSG00000104320
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)DescriptionActionsGraphical viewLength
ChainiPRO_00002310431 – 754NibrinAdd BLAST754

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei278Phosphoserine; by ATM1 Publication1
Modified residuei337PhosphothreonineCombined sources1
Modified residuei343Phosphoserine; by ATMCombined sources2 Publications1
Modified residuei347PhosphoserineCombined sources1
Modified residuei397PhosphoserineCombined sources1 Publication1
Modified residuei402PhosphothreonineCombined sources1
Modified residuei432PhosphoserineCombined sources1
Modified residuei509PhosphoserineCombined sources1
Modified residuei518PhosphoserineCombined sources1
Cross-linki529Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki571Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki582Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei615Phosphoserine1 Publication1
Modified residuei673PhosphoserineCombined sources1

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

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO60934
MaxQBiO60934
PaxDbiO60934
PeptideAtlasiO60934
PRIDEiO60934
ProteomicsDBi49678

PTM databases

iPTMnetiO60934
PhosphoSitePlusiO60934

Expressioni

Tissue specificityi

Ubiquitous. Expressed at high levels in testis.

Inductioni

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

Gene expression databases

BgeeiENSG00000104320 Expressed in 244 organ(s), highest expression level in endometrium epithelium
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/MRE11 associated with a single NBN (PubMed:26215093, PubMed:9590181, PubMed:9705271, PubMed:11238951). As part of the MRN complex, interacts with MCM9; the interaction recruits the complex to DNA repair sites (PubMed:26215093). Component of the BASC complex, at least composed of BRCA1, MSH2, MSH6, MLH1, ATM, BLM, RAD50, MRE11 and NBN (PubMed:10783165). Interacts with histone H2AFX this requires phosphorylation of H2AFX on 'Ser-139' (PubMed:12419185). Interacts with HJURP (PubMed:17823411). Interacts with INTS3 (PubMed:19683501). Interacts with KPNA2 (PubMed:16188882). Interacts with TERF2 (PubMed:10888888). Interacts with RBBP8; the interaction links the role of the MRN complex in DNA double-strand break sensing to resection (PubMed:19759395). Interacts with SP100; recruits NBN to PML bodies (PubMed:12470659). Interacts with ATF2 (PubMed:15916964). Interacts with MTOR, MAPKAP1 isoform 2 and RICTOR; indicative for an association with the mTORC2 complex (PubMed:23762398). Interacts with MRNIP (PubMed:27568553).15 Publications
(Microbial infection) Interacts with herpes simplex virus 1 protein UL12.1 Publication

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi110763, 94 interactors
CORUMiO60934
DIPiDIP-33605N
ELMiO60934
IntActiO60934, 39 interactors
MINTiO60934
STRINGi9606.ENSP00000265433

Structurei

Secondary structure

1754
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliO60934
SMRiO60934
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 SP100By similarityAdd BLAST218
Regioni221 – 402Interaction with MTOR, MAPKAP1 and RICTOR1 PublicationAdd BLAST182

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi461 – 467Nuclear localization signal7
Motifi736 – 743EEXXXDDL motif8

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi448 – 451Poly-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.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

Phylogenomic databases

eggNOGiENOG410IK5M Eukaryota
ENOG410Y1R8 LUCA
GeneTreeiENSGT00390000000521
HOVERGENiHBG053070
InParanoidiO60934
KOiK10867
OMAiLWSTKEE
OrthoDBiEOG091G0BJ4
PhylomeDBiO60934
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 6 potential isoforms that are computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There are 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0C4DG07A0A0C4DG07_HUMAN
Nibrin
NBN hCG_33061
672Annotation score:
E5RGU1E5RGU1_HUMAN
Nibrin
NBN
159Annotation score:
E5RGR7E5RGR7_HUMAN
Nibrin
NBN
164Annotation score:
E5RGN7E5RGN7_HUMAN
Nibrin
NBN
92Annotation score:
E2QRP0E2QRP0_HUMAN
Nibrin
NBN
58Annotation score:
A0A087X1V5A0A087X1V5_HUMAN
Nibrin
NBN
124Annotation score:

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)DescriptionActionsGraphical viewLength
Sequence conflicti247G → R in BAD96976 (Ref. 6) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02579293S → L in some childhood acute lymphoblastic leukemia patients; uncertain pathological significance; rare variant. 1 PublicationCorresponds to variant dbSNP:rs12721593EnsemblClinVar.1
Natural variantiVAR_02579395D → N in some childhood acute lymphoblastic leukemia patients; uncertain pathological significance; rare variant. 1 PublicationCorresponds to variant dbSNP:rs61753720EnsemblClinVar.1
Natural variantiVAR_025794105K → N1 PublicationCorresponds to variant dbSNP:rs13312858Ensembl.1
Natural variantiVAR_051226142N → S. Corresponds to variant dbSNP:rs769414EnsemblClinVar.1
Natural variantiVAR_025795150L → F in BC. 1 PublicationCorresponds to variant dbSNP:rs773119929Ensembl.1
Natural variantiVAR_025796171I → V in some childhood acute lymphoblastic leukemia patients; uncertain pathological significance; rare variant; associated with aplastic anemia at homozygosity. 2 PublicationsCorresponds to variant dbSNP:rs61754966EnsemblClinVar.1
Natural variantiVAR_025797185E → Q6 PublicationsCorresponds to variant dbSNP:rs1805794EnsemblClinVar.1
Natural variantiVAR_025798210V → F1 PublicationCorresponds to variant dbSNP:rs61754796EnsemblClinVar.1
Natural variantiVAR_025799215R → W1 PublicationCorresponds to variant dbSNP:rs34767364EnsemblClinVar.1
Natural variantiVAR_025800216Q → K1 PublicationCorresponds to variant dbSNP:rs769416Ensembl.1
Natural variantiVAR_025801266P → L1 PublicationCorresponds to variant dbSNP:rs769420EnsemblClinVar.1
Natural variantiVAR_051227408K → E. Corresponds to variant dbSNP:rs34120922EnsemblClinVar.1
Natural variantiVAR_025802497T → A1 PublicationCorresponds to variant dbSNP:rs3026268EnsemblClinVar.1
Natural variantiVAR_025803574L → I1 PublicationCorresponds to variant dbSNP:rs142334798EnsemblClinVar.1
Natural variantiVAR_064738679Y → H Found in a renal cell carcinoma sample; somatic mutation. 1 Publication1

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

Similar proteinsi

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

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5WQDX-ray3.00H/I/J/K/L/M/N423-438[»]
ProteinModelPortaliO60934
SMRiO60934
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110763, 94 interactors
CORUMiO60934
DIPiDIP-33605N
ELMiO60934
IntActiO60934, 39 interactors
MINTiO60934
STRINGi9606.ENSP00000265433

PTM databases

iPTMnetiO60934
PhosphoSitePlusiO60934

Polymorphism and mutation databases

BioMutaiNBN

Proteomic databases

EPDiO60934
MaxQBiO60934
PaxDbiO60934
PeptideAtlasiO60934
PRIDEiO60934
ProteomicsDBi49678

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi4683
DisGeNETi4683
EuPathDBiHostDB:ENSG00000104320.13
GeneCardsiNBN
GeneReviewsiNBN
HGNCiHGNC:7652 NBN
HPAiCAB003836
HPA001429
MalaCardsiNBN
MIMi114480 phenotype
251260 phenotype
602667 gene
609135 phenotype
neXtProtiNX_O60934
OpenTargetsiENSG00000104320
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
OMAiLWSTKEE
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
PROiPR:O60934
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000104320 Expressed in 244 organ(s), highest expression level in endometrium epithelium
CleanExiHS_NBN
ExpressionAtlasiO60934 baseline and differential
GenevisibleiO60934 HS

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_HUMAN
AccessioniPrimary (citable) accession number: O60934
Secondary accession number(s): B2R626
, B2RNC5, O60672, Q32NF7, Q53FM6, Q63HR6, Q7LDM2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: August 1, 1998
Last modified: November 7, 2018
This is version 170 of the entry and version 1 of the sequence. See 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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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