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Entry version 119 (08 May 2019)
Sequence version 2 (04 Apr 2006)
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Protein

Nibrin

Gene

Nbn

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processCell cycle, DNA damage, DNA repair, Meiosis

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Nibrin
Alternative name(s):
Nijmegen breakage syndrome protein 1 homolog
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Nbn
Synonyms:Nbs1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
621420 Nbn

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Nucleus, Telomere

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002310461 – 750NibrinAdd BLAST750

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei337PhosphothreonineBy similarity1
Modified residuei343Phosphoserine; by ATMBy similarity1
Modified residuei347PhosphoserineBy similarity1
Modified residuei433PhosphoserineCombined sources1
Modified residuei508PhosphoserineBy similarity1
Modified residuei517PhosphoserineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki528Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q9JIL9

PRoteomics IDEntifications database

More...
PRIDEi
Q9JIL9

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9JIL9

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q9JIL9

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of the MRN complex composed of two heterodimers RAD50/MRE11 associated with a single NBN. As part of the MRN complex, interacts with MCM9; the interaction recruits the complex to DNA repair sites.

Component of the BASC complex, at least composed of BRCA1, MSH2, MSH6, MLH1, ATM, BLM, RAD50, MRE11 and NBN.

Interacts with histone H2AFX this requires phosphorylation of H2AFX on 'Ser-139'.

Interacts with HJURP.

Interacts with INTS3.

Interacts with KPNA2.

Interacts with 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 MRNIP.

By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000012377

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q9JIL9

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini24 – 83FHAPROSITE-ProRule annotationAdd BLAST60
Domaini105 – 181BRCTAdd BLAST77

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni111 – 328Mediates interaction with SP100By similarityAdd BLAST218
Regioni221 – 403Interaction with MTOR, MAPKAP1 and RICTORBy similarityAdd BLAST183

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi461 – 467Nuclear localization signalBy similarity7
Motifi733 – 740EEXXXDDL motif8

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IK5M Eukaryota
ENOG410Y1R8 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000231654

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9JIL9

KEGG Orthology (KO)

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KOi
K10867

Database of Orthologous Groups

More...
OrthoDBi
831679at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9JIL9

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00027 BRCT, 1 hit
cd00060 FHA, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.10190, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001357 BRCT_dom
IPR036420 BRCT_dom_sf
IPR013908 DNA-repair_Nbs1_C
IPR000253 FHA_dom
IPR040227 Nibrin-rel
IPR032429 Nibrin_BRCT2
IPR016592 Nibrin_met
IPR008984 SMAD_FHA_dom_sf

The PANTHER Classification System

More...
PANTHERi
PTHR12162 PTHR12162, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00498 FHA, 1 hit
PF08599 Nbs1_C, 1 hit
PF16508 NIBRIN_BRCT_II, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF011869 Nibrin_animal, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00240 FHA, 1 hit
SM01348 Nbs1_C, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49879 SSF49879, 1 hit
SSF52113 SSF52113, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50006 FHA_DOMAIN, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

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

Q9JIL9-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MWKLLPAASA APGEPCRLLA GVEYIVGRKN CAILIENDQS ISRNHAVLRV
60 70 80 90 100
NFPVTSLSQT DEIPTLTIKD NSKYGTFINE EKMQNGLSST LKTGDRVTFG
110 120 130 140 150
VFESKFRVEY EPLVVCSSCL DVSGKTVLNQ AILQLGGLTA NSWTEECTHL
160 170 180 190 200
AMSSVKVTIK TICALICGRP IVKPEYFSEF LKAVESKTQP PEIESFYPPI
210 220 230 240 250
DEPAIGNKSV DLSGRRERKQ IFKGKTFVFL NAKQHKKLGS AVVFGGGEAR
260 270 280 290 300
LMAEGGEEEQ SFFSAPGTCV VDVGITNTQL IITDSQRKWI HLIMDILQRH
310 320 330 340 350
GLRPIPEAEI GLAVIFMTTE SYCNPQGQPC TEVKTTTPGP SLSQGLSANG
360 370 380 390 400
KVIPSAPMNM TTYVADTESE PADTCMSLSE RPEEVKIFGL DQNSRKLLQG
410 420 430 440 450
TCNIKETSNQ SSNSNNAASN TLVRGKAPNY QLSPMKCPAA SKNKDWSSQQ
460 470 480 490 500
QLNSIKNYFQ PCSRKRERDE ENPEQSSCKS SRVELSCSLL EQTQPAGPSL
510 520 530 540 550
WKSKDHESQS ETLDRASNAS SVGGIDIKPN GKSPDSKSFS TEDLRARKRK
560 570 580 590 600
EVDLSTEEEV LEELLRSTKP ELAVQVKVEK QEADVSIRKK PRMDAERNQH
610 620 630 640 650
LNGGPVPESN SALQEDETGK KDELQIEAWS TKREVSNTDE LQDSSEELPR
660 670 680 690 700
KLLLTEFRSL VVHNNSSRNL CVLNGRGELK NFKKFKKATC PGAGKLPHII
710 720 730 740 750
GGSDLIGHHA RKNTELEEWL KHEMEVQKQQ AKEDSLADDL FRYNPNVKRR
Length:750
Mass (Da):83,150
Last modified:April 4, 2006 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i43A93B5497102A4A
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3V766G3V766_RAT
Nibrin
Nbn rCG_55035
750Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti67T → I in AAF91228 (PubMed:10908350).Curated1
Sequence conflicti84Q → L in AAH85700 (PubMed:15489334).Curated1
Sequence conflicti277N → H in AAH85700 (PubMed:15489334).Curated1
Sequence conflicti301G → D in AAF91228 (PubMed:10908350).Curated1
Sequence conflicti497G → E in AAF91228 (PubMed:10908350).Curated1
Sequence conflicti514D → G in AAF91228 (PubMed:10908350).Curated1
Sequence conflicti619G → E in AAF91228 (PubMed:10908350).Curated1
Sequence conflicti642Q → P in AAH85700 (PubMed:15489334).Curated1
Sequence conflicti672V → P in AAF91228 (PubMed:10908350).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF218575 mRNA Translation: AAF91228.1
BC085700 mRNA Translation: AAH85700.1

NCBI Reference Sequences

More...
RefSeqi
NP_620228.1, NM_138873.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
85482

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:85482

UCSC genome browser

More...
UCSCi
RGD:621420 rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF218575 mRNA Translation: AAF91228.1
BC085700 mRNA Translation: AAH85700.1
RefSeqiNP_620228.1, NM_138873.2

3D structure databases

SMRiQ9JIL9
ModBaseiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000012377

PTM databases

iPTMnetiQ9JIL9
PhosphoSitePlusiQ9JIL9

Proteomic databases

PaxDbiQ9JIL9
PRIDEiQ9JIL9

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi85482
KEGGirno:85482
UCSCiRGD:621420 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4683
RGDi621420 Nbn

Phylogenomic databases

eggNOGiENOG410IK5M Eukaryota
ENOG410Y1R8 LUCA
HOGENOMiHOG000231654
InParanoidiQ9JIL9
KOiK10867
OrthoDBi831679at2759
PhylomeDBiQ9JIL9

Enzyme and pathway databases

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

Miscellaneous databases

Protein Ontology

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PROi
PR:Q9JIL9

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
IPR040227 Nibrin-rel
IPR032429 Nibrin_BRCT2
IPR016592 Nibrin_met
IPR008984 SMAD_FHA_dom_sf
PANTHERiPTHR12162 PTHR12162, 1 hit
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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiNBN_RAT
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9JIL9
Secondary accession number(s): Q5RKL2
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: April 4, 2006
Last modified: May 8, 2019
This is version 119 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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