Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9JIL9

- NBN_RAT

UniProt

Q9JIL9 - NBN_RAT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Nibrin

Gene

Nbn

Organism
Rattus norvegicus (Rat)
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).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. meiotic nuclear division Source: UniProtKB-KW
  6. mitotic cell cycle checkpoint Source: UniProtKB
  7. mitotic G2 DNA damage checkpoint Source: UniProtKB
  8. negative regulation of neuron differentiation Source: RGD
  9. negative regulation of viral entry into host cell Source: RGD
  10. positive regulation of cell proliferation Source: RGD
  11. regulation of fibroblast proliferation Source: UniProtKB
  12. response to drug Source: RGD
  13. telomere maintenance Source: UniProtKB
Complete GO annotation...

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-KW
  2. Mre11 complex Source: UniProtKB
  3. nuclear inclusion body Source: UniProtKB
Complete GO annotation...

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

        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
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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

« Hide 'large scale' publications
  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 29, 2014
This is version 93 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