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Q9R207

- NBN_MOUSE

UniProt

Q9R207 - NBN_MOUSE

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Protein
Nibrin
Gene
Nbn, Nbs1
Organism
Mus musculus (Mouse)
Status
Reviewed - 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 By similarity.

GO - Molecular functioni

  1. ATP-dependent DNA helicase activity Source: Ensembl
  2. damaged DNA binding Source: MGI
  3. protein N-terminus binding Source: UniProtKB
  4. transcription factor binding Source: UniProtKB

GO - Biological processi

  1. DNA damage checkpoint Source: MGI
  2. blastocyst growth Source: UniProtKB
  3. cell proliferation Source: MGI
  4. double-strand break repair Source: UniProtKB
  5. in utero embryonic development Source: UniProtKB
  6. intrinsic apoptotic signaling pathway Source: MGI
  7. isotype switching Source: UniProtKB
  8. meiotic nuclear division Source: UniProtKB-KW
  9. mitotic G2 DNA damage checkpoint Source: UniProtKB
  10. mitotic cell cycle checkpoint Source: UniProtKB
  11. neuromuscular process controlling balance Source: MGI
  12. positive regulation of kinase activity Source: Ensembl
  13. positive regulation of protein autophosphorylation Source: Ensembl
  14. regulation of fibroblast proliferation Source: UniProtKB
  15. telomere maintenance Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, DNA damage, DNA repair, Meiosis

Enzyme and pathway databases

ReactomeiREACT_188819. DNA Damage/Telomere Stress Induced Senescence.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:1351625. Nbn.

Subcellular locationi

Nucleus. NucleusPML body By similarity. Chromosometelomere By similarity
Note: Localizes to discrete nuclear foci after treatment with genotoxic agents By similarity.

GO - Cellular componenti

  1. Mre11 complex Source: UniProtKB
  2. PML body Source: UniProtKB-SubCell
  3. nuclear chromosome, telomeric region Source: Ensembl
  4. nuclear inclusion body Source: UniProtKB
  5. nucleolus Source: Ensembl
  6. nucleus Source: MGI
  7. replication fork Source: MGI
  8. site of double-strand break Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus, Telomere

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 751751Nibrin
PRO_0000231044Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei343 – 3431Phosphoserine; by ATM1 Publication
Modified residuei398 – 3981Phosphoserine By similarity
Modified residuei433 – 4331Phosphoserine 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.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9R207.
PRIDEiQ9R207.

PTM databases

PhosphoSiteiQ9R207.

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

ArrayExpressiQ9R207.
BgeeiQ9R207.
CleanExiMM_NBN.
GenevestigatoriQ9R207.

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.1 Publication

Protein-protein interaction databases

BioGridi205163. 7 interactions.
DIPiDIP-46804N.
IntActiQ9R207. 1 interaction.
MINTiMINT-4084511.

Structurei

3D structure databases

ProteinModelPortaliQ9R207.
SMRiQ9R207. Positions 217-326.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 8360FHA
Add
BLAST
Domaini105 – 18177BRCT
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni111 – 328218Mediates interaction with SP100
Add
BLAST
Regioni221 – 403183Interaction with MTOR, MAPKAP1 and RICTOR By similarity
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi461 – 4677Nuclear localization signal By similarity
Motifi734 – 7418EEXXXDDL motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi449 – 4524Poly-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 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.

Sequence similaritiesi

Contains 1 BRCT domain.
Contains 1 FHA domain.

Phylogenomic databases

eggNOGiNOG84999.
GeneTreeiENSGT00390000000521.
HOGENOMiHOG000231654.
HOVERGENiHBG053070.
InParanoidiQ9R207.
KOiK10867.
OMAiKLPHIIG.
OrthoDBiEOG7B5WV7.
PhylomeDBiQ9R207.
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.
IPR016592. Nibrin_met.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PfamiPF00498. FHA. 1 hit.
PF08599. Nbs1_C. 1 hit.
[Graphical view]
PIRSFiPIRSF011869. Nibrin_animal. 1 hit.
SMARTiSM00292. BRCT. 1 hit.
SM00240. FHA. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEiPS50006. FHA_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9R207-1 [UniParc]FASTAAdd to Basket

« Hide

MWKLLPAAGA APGEPYRLLA GVEYVVGRKN CGILIENDQS ISRNHAVLTV    50
NFPVTSLSQT DEIPTLTIKD NSKYGTFVNE EKMQTGLSCT LKTGDRVTFG 100
VFESKFRVEY EPLVVCSSCL DVSGKTVLNQ AILQLGGLTA NNWTEECTHL 150
VMSAVKVTIK TICALICGRP IIKPEYFSEF LKAVESKKQP PDIESFYPPI 200
DEPAIGSKSV DLSGRHERKQ IFKGKTFVFL NAKQHKKLSS AVAFGGGEAR 250
LMAEDDEEEQ SFFSAPGTCV VDVGITNTQL IISHSQKKWI HLIMDTLQRN 300
GLRPIPEAEI GLAVIFMTTE NYCNPQGQPC TELKTTTPGP SLSQVLSANG 350
KIIPSAPVNM TTYVADTESE PADTCMPLSE RPEEVKIPGL EQSSRKLSQE 400
TFNIKEAPKP SSKANNVASD TLVRGKTPSY QLSPMKFPVA NKNKDWTSQQ 450
QQNSIKNYFQ PCTRKRERDE DNPELSSCKS SRMELSCSLL EQTQPAGPSL 500
WKSKEHQSQN ATLDREADTS SVGGMDIELN RKSPDRKPLP TETLRPRKRK 550
DVDLATEEEV LEELLRSTKP ELAVQVKVEK QEADDTIRKK PRMDAERNRP 600
LNGGSEPESN SALQEDEREK KDELQTESWS TKHEIANSDG LQDSSEELPR 650
KLLLTEFRSL VVSNHNSTSR NLCVNECGPL KNFKKFKKAT FPGAGKLPHI 700
IGGSDLVGHH ARKNTELEEW LKQEMEVQKQ QAKEESLADD LFRYNPNVKR 750
R 751
Length:751
Mass (Da):83,795
Last modified:May 1, 2000 - v1
Checksum:iC9F597CC08227B2C
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91G → S in AAH44773. 1 Publication
Sequence conflicti11 – 122AP → SL in AAC62113. 1 Publication
Sequence conflicti325 – 3251P → Q in BAE22356. 1 Publication
Sequence conflicti366 – 3661D → E in BAA76298. 1 Publication
Sequence conflicti455 – 4551I → F in BAA76298. 1 Publication
Sequence conflicti513 – 5131L → Q in AAH44773. 1 Publication
Sequence conflicti664 – 6641N → K in AAH44773. 1 Publication
Sequence conflicti676 – 6761E → D in AAH44773. 1 Publication
Sequence conflicti679 – 6791P → S in AAH44773. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS17986.1.
RefSeqi NP_038780.3. NM_013752.3.
UniGenei Mm.20866.

3D structure databases

ProteinModelPortali Q9R207.
SMRi Q9R207. Positions 217-326.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 205163. 7 interactions.
DIPi DIP-46804N.
IntActi Q9R207. 1 interaction.
MINTi MINT-4084511.

PTM databases

PhosphoSitei Q9R207.

Proteomic databases

PaxDbi Q9R207.
PRIDEi Q9R207.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000029879 ; ENSMUSP00000029879 ; ENSMUSG00000028224 .
GeneIDi 27354.
KEGGi mmu:27354.
UCSCi uc008sbn.1. mouse.

Organism-specific databases

CTDi 4683.
MGIi MGI:1351625. Nbn.

Phylogenomic databases

eggNOGi NOG84999.
GeneTreei ENSGT00390000000521.
HOGENOMi HOG000231654.
HOVERGENi HBG053070.
InParanoidi Q9R207.
KOi K10867.
OMAi KLPHIIG.
OrthoDBi EOG7B5WV7.
PhylomeDBi Q9R207.
TreeFami TF101103.

Enzyme and pathway databases

Reactomei REACT_188819. DNA Damage/Telomere Stress Induced Senescence.

Miscellaneous databases

NextBioi 305208.
PROi Q9R207.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9R207.
Bgeei Q9R207.
CleanExi MM_NBN.
Genevestigatori Q9R207.

Family and domain databases

Gene3Di 2.60.200.20. 1 hit.
3.40.50.10190. 1 hit.
InterProi IPR001357. BRCT_dom.
IPR013908. DNA-repair_Nbs1_C.
IPR000253. FHA_dom.
IPR016592. Nibrin_met.
IPR008984. SMAD_FHA_domain.
[Graphical view ]
Pfami PF00498. FHA. 1 hit.
PF08599. Nbs1_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF011869. Nibrin_animal. 1 hit.
SMARTi SM00292. BRCT. 1 hit.
SM00240. FHA. 1 hit.
[Graphical view ]
SUPFAMi SSF49879. SSF49879. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEi PS50006. FHA_DOMAIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification, characterization, and mapping of a mouse homolog of the gene mutated in Nijmegen breakage syndrome."
    Vissinga C.S., Yeo T.C., Woessner J., Massa H.F., Wilson R.K., Trask B.J., Concannon P.
    Cytogenet. Cell Genet. 87:80-84(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Structure of the mouse Nijmegen breakage syndrome (Nibrin/Nbs1) protein."
    Saito T.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain and Testis.
  3. "Isolation of 50 cDNAs differentially expressed in embryonic forebrain as compared to mid and hindbrain: a strategy to identify candidate genes involved in human neurodevelopmental diseases."
    Mas C., Bourgeois F., Simonneau M.
    Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain stem.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech II and FVB/N.
    Tissue: Colon and Mammary gland.
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-613.
    Strain: C57BL/6J.
    Tissue: Medulla oblongata.
  6. "Expression pattern of the Nijmegen breakage syndrome gene, Nbs1, during murine development."
    Wilda M., Demuth I., Concannon P., Sperling K., Hameister H.
    Hum. Mol. Genet. 9:1739-1744(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  7. "Recruitment of NBS1 into PML oncogenic domains via interaction with SP100 protein."
    Naka K., Ikeda K., Motoyama N.
    Biochem. Biophys. Res. Commun. 299:863-871(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SP100.
  8. "Mice lacking protein phosphatase 5 are defective in ataxia telangiectasia mutated (ATM)-mediated cell cycle arrest."
    Yong W., Bao S., Chen H., Li D., Sanchez E.R., Shou W.
    J. Biol. Chem. 282:14690-14694(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-343.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiNBN_MOUSE
AccessioniPrimary (citable) accession number: Q9R207
Secondary accession number(s): O88981
, Q3UY57, Q811I6, Q8CCY0, Q9R1X1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: May 1, 2000
Last modified: September 3, 2014
This is version 107 of the entry and version 1 of the sequence. [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
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi