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Q9JIL9

- NBN_RAT

UniProt

Q9JIL9 - NBN_RAT

Protein

Nibrin

Gene

Nbn

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 2 (04 Apr 2006)
      Previous versions | rss
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    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.By similarity

    GO - Molecular functioni

    1. protein N-terminus binding Source: UniProtKB
    2. transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. blastocyst growth Source: UniProtKB
    2. double-strand break repair Source: UniProtKB
    3. in utero embryonic development Source: UniProtKB
    4. isotype switching Source: UniProtKB
    5. mitotic cell cycle checkpoint Source: UniProtKB
    6. mitotic G2 DNA damage checkpoint Source: UniProtKB
    7. negative regulation of neuron differentiation Source: RGD
    8. positive regulation of cell proliferation Source: RGD
    9. reciprocal meiotic recombination Source: RGD
    10. regulation of fibroblast proliferation Source: UniProtKB
    11. response to drug Source: RGD
    12. telomere maintenance Source: UniProtKB

    Keywords - Biological processi

    Cell cycle, DNA damage, DNA repair, Meiosis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nibrin
    Alternative name(s):
    Nijmegen breakage syndrome protein 1 homolog
    Gene namesi
    Name:Nbn
    Synonyms:Nbs1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi621420. Nbn.

    Subcellular locationi

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

    GO - Cellular componenti

    1. chromosome, telomeric region Source: UniProtKB-SubCell
    2. Mre11 complex Source: UniProtKB
    3. nuclear inclusion body Source: UniProtKB
    4. PML body Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chromosome, Nucleus, Telomere

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 750750NibrinPRO_0000231046Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei343 – 3431Phosphoserine; by ATMBy similarity
    Modified residuei433 – 4331PhosphoserineBy 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

    Phosphoprotein

    Proteomic databases

    PRIDEiQ9JIL9.

    Expressioni

    Tissue specificityi

    Present at approximately equal levels in the heart at fetal day 17, at relatively constant levels at postnatal days 10, 17 and 21 and at slightly lower levels in the adult heart. Barely detectable in the brain. Not detected in kidney, very low levels in liver and skeletal muscle and moderate levels in heart, lung and brain (at protein level).1 Publication

    Gene expression databases

    GenevestigatoriQ9JIL9.

    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 and RICTOR; indicative for an association with the mTORC2 complex By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ9JIL9.
    SMRiQ9JIL9. Positions 217-327.
    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 – 403183Interaction with MTOR, MAPKAP1 and RICTORBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi461 – 4677Nuclear localization signalBy similarity
    Motifi733 – 7408EEXXXDDL motif

    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.Curated
    Contains 1 FHA domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG84999.
    HOGENOMiHOG000231654.
    HOVERGENiHBG053070.
    InParanoidiQ9JIL9.
    KOiK10867.
    PhylomeDBiQ9JIL9.

    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.

    Q9JIL9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWKLLPAASA APGEPCRLLA GVEYIVGRKN CAILIENDQS ISRNHAVLRV    50
    NFPVTSLSQT DEIPTLTIKD NSKYGTFINE EKMQNGLSST LKTGDRVTFG 100
    VFESKFRVEY EPLVVCSSCL DVSGKTVLNQ AILQLGGLTA NSWTEECTHL 150
    AMSSVKVTIK TICALICGRP IVKPEYFSEF LKAVESKTQP PEIESFYPPI 200
    DEPAIGNKSV DLSGRRERKQ IFKGKTFVFL NAKQHKKLGS AVVFGGGEAR 250
    LMAEGGEEEQ SFFSAPGTCV VDVGITNTQL IITDSQRKWI HLIMDILQRH 300
    GLRPIPEAEI GLAVIFMTTE SYCNPQGQPC TEVKTTTPGP SLSQGLSANG 350
    KVIPSAPMNM TTYVADTESE PADTCMSLSE RPEEVKIFGL DQNSRKLLQG 400
    TCNIKETSNQ SSNSNNAASN TLVRGKAPNY QLSPMKCPAA SKNKDWSSQQ 450
    QLNSIKNYFQ PCSRKRERDE ENPEQSSCKS SRVELSCSLL EQTQPAGPSL 500
    WKSKDHESQS ETLDRASNAS SVGGIDIKPN GKSPDSKSFS TEDLRARKRK 550
    EVDLSTEEEV LEELLRSTKP ELAVQVKVEK QEADVSIRKK PRMDAERNQH 600
    LNGGPVPESN SALQEDETGK KDELQIEAWS TKREVSNTDE LQDSSEELPR 650
    KLLLTEFRSL VVHNNSSRNL CVLNGRGELK NFKKFKKATC PGAGKLPHII 700
    GGSDLIGHHA RKNTELEEWL KHEMEVQKQQ AKEDSLADDL FRYNPNVKRR 750
    Length:750
    Mass (Da):83,150
    Last modified:April 4, 2006 - v2
    Checksum:i43A93B5497102A4A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti67 – 671T → I in AAF91228. (PubMed:10908350)Curated
    Sequence conflicti84 – 841Q → L in AAH85700. (PubMed:15489334)Curated
    Sequence conflicti277 – 2771N → H in AAH85700. (PubMed:15489334)Curated
    Sequence conflicti301 – 3011G → D in AAF91228. (PubMed:10908350)Curated
    Sequence conflicti497 – 4971G → E in AAF91228. (PubMed:10908350)Curated
    Sequence conflicti514 – 5141D → G in AAF91228. (PubMed:10908350)Curated
    Sequence conflicti619 – 6191G → E in AAF91228. (PubMed:10908350)Curated
    Sequence conflicti642 – 6421Q → P in AAH85700. (PubMed:15489334)Curated
    Sequence conflicti672 – 6721V → P in AAF91228. (PubMed:10908350)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF218575 mRNA. Translation: AAF91228.1.
    BC085700 mRNA. Translation: AAH85700.1.
    RefSeqiNP_620228.1. NM_138873.2.
    UniGeneiRn.25214.

    Genome annotation databases

    GeneIDi85482.
    KEGGirno:85482.
    UCSCiRGD:621420. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF218575 mRNA. Translation: AAF91228.1 .
    BC085700 mRNA. Translation: AAH85700.1 .
    RefSeqi NP_620228.1. NM_138873.2.
    UniGenei Rn.25214.

    3D structure databases

    ProteinModelPortali Q9JIL9.
    SMRi Q9JIL9. Positions 217-327.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q9JIL9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 85482.
    KEGGi rno:85482.
    UCSCi RGD:621420. rat.

    Organism-specific databases

    CTDi 4683.
    RGDi 621420. Nbn.

    Phylogenomic databases

    eggNOGi NOG84999.
    HOGENOMi HOG000231654.
    HOVERGENi HBG053070.
    InParanoidi Q9JIL9.
    KOi K10867.
    PhylomeDBi Q9JIL9.

    Miscellaneous databases

    NextBioi 617562.
    PROi Q9JIL9.

    Gene expression databases

    Genevestigatori Q9JIL9.

    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

    1. "The MRE11-NBS1-RAD50 pathway is perturbed in SV40 large T antigen-immortalized AT-1, AT-2 and HL-1 cardiomyocytes."
      Lanson N.A. Jr., Egeland D.B., Royals B.A., Claycomb W.C.
      Nucleic Acids Res. 28:2882-2892(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    2. "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].
      Tissue: Testis.

    Entry informationi

    Entry nameiNBN_RAT
    AccessioniPrimary (citable) accession number: Q9JIL9
    Secondary accession number(s): Q5RKL2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 4, 2006
    Last sequence update: April 4, 2006
    Last modified: October 1, 2014
    This is version 92 of the entry and version 2 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3