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Protein

Nibrin

Gene

NBN

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: 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 (By similarity).By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, DNA damage, DNA repair, Meiosis

Enzyme and pathway databases

ReactomeiR-GGA-217106. Chk1-controlled and DNA-damage induced centrosome duplication.
R-GGA-351433. ATM mediated phosphorylation of repair proteins.
R-GGA-351442. ATM mediated response to DNA double-strand break.
R-GGA-351444. Recruitment of repair and signaling proteins to double-strand breaks.

Names & Taxonomyi

Protein namesi
Recommended name:
Nibrin
Alternative name(s):
Nijmegen breakage syndrome protein 1 homolog
Gene namesi
Name:NBN
Synonyms:NBS1
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus, Telomere

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002310471 – 753NibrinAdd BLAST753

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei274PhosphoserineBy similarity1
Modified residuei343Phosphoserine; by ATMBy similarity1

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

PaxDbiQ9DE07.

Interactioni

Subunit structurei

Component of the MRN complex composed of two heterodimers RAD50/MRE11A associated with a single NBN. Interacts with RBBP8; the interaction links the role of the MRN complex in DNA double-strand break sensing to resection (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9031.ENSGALP00000025599.

Structurei

3D structure databases

ProteinModelPortaliQ9DE07.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini22 – 81FHAPROSITE-ProRule annotationAdd BLAST60
Domaini101 – 191BRCTAdd BLAST91

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi461 – 467Nuclear localization signalBy similarity7
Motifi735 – 742EEXXXDDL motif8

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.
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

eggNOGiENOG410IK5M. Eukaryota.
ENOG410Y1R8. LUCA.
HOGENOMiHOG000231654.
HOVERGENiHBG053070.
InParanoidiQ9DE07.
KOiK10867.
PhylomeDBiQ9DE07.

Family and domain databases

CDDicd00027. BRCT. 1 hit.
Gene3Di2.60.200.20. 1 hit.
3.40.50.10190. 1 hit.
InterProiIPR001357. BRCT_dom.
IPR013908. DNA-repair_Nbs1_C.
IPR000253. FHA_dom.
IPR032429. Nibrin_BRCT2.
IPR016592. Nibrin_met.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PfamiPF00533. BRCT. 1 hit.
PF00498. FHA. 1 hit.
PF08599. Nbs1_C. 1 hit.
PF16508. NIBRIN_BRCT_II. 1 hit.
[Graphical view]
PIRSFiPIRSF011869. Nibrin_animal. 1 hit.
SMARTiSM00292. BRCT. 1 hit.
SM00240. FHA. 1 hit.
SM01348. Nbs1_C. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEiPS50006. FHA_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9DE07-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWKLVPAAGP GEPFRLLVGT EYVVGRKNCA FLIQDDQSIS RSHAVLTVSR
60 70 80 90 100
PETTHSQSVS VPVLTIKDTS KYGTFVNGSK LSGASRSLQS GDRVNFGVFE
110 120 130 140 150
SKFRVEYESL VVCSSCLDVA QKTALNEAIQ QLGGLVVNEW TKECTHLIME
160 170 180 190 200
SVKVTVKTIC ALICGRPIVK PEFFSELMKA VQSRQQLPTP ESFYPSVDEP
210 220 230 240 250
AIGIDNMDLS GHPERKKIFS GKTFVFLTAK QHKKLGPAVI LGGGEAKLMA
260 270 280 290 300
EERKETSLLV SPEVCVVDVG VTNSQILGSE SMRNWTDSIL AVLESNNLRA
310 320 330 340 350
IPEAEIGLAV IFMSTEIYCN PQRQPDNKAV TASTASKVRP VSSQSSTVDE
360 370 380 390 400
TIMPTAAADY STLNVADTEI EEQTCMEIER TTSQTTRREK VAFQQAAVRE
410 420 430 440 450
NPSTSGTVNA GMLISRVNRT SGFGQKNHPH SPSKILEVDK PRECTPRQQS
460 470 480 490 500
NSITNYFHVA RKRERAEEGE ETSLSKQAKL EKKPLPVSEC TESSASSAWN
510 520 530 540 550
SEKEQHGKGN NIQLGRESGE LASDKTDIKI TFSENPAPKK RKELDDVSED
560 570 580 590 600
VETLEMVFES RDLDWEEQTA NGDQEAQSNK RKKRCLETKG SRTEEGNTKQ
610 620 630 640 650
REENEMLRKE EVGSVLTLED KSKIKEESSV SIRNKLINHN KLEDDSSRLP
660 670 680 690 700
SKLLLTEFRS LVVSCPRSNS PTMRNTKCRG QNNFKTFRKV PYPGAGQLPY
710 720 730 740 750
IIGGSDLVAH QARKNSELEE WLREELEEQN RRAREESLAD DLFRYDPNVK

RRR
Length:753
Mass (Da):83,987
Last modified:March 1, 2001 - v1
Checksum:i410BBE74123D9B06
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF230342 mRNA. Translation: AAG47947.1.
RefSeqiNP_989668.1. NM_204337.1.
UniGeneiGga.196.

Genome annotation databases

GeneIDi374246.
KEGGigga:374246.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF230342 mRNA. Translation: AAG47947.1.
RefSeqiNP_989668.1. NM_204337.1.
UniGeneiGga.196.

3D structure databases

ProteinModelPortaliQ9DE07.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000025599.

Proteomic databases

PaxDbiQ9DE07.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi374246.
KEGGigga:374246.

Organism-specific databases

CTDi4683.

Phylogenomic databases

eggNOGiENOG410IK5M. Eukaryota.
ENOG410Y1R8. LUCA.
HOGENOMiHOG000231654.
HOVERGENiHBG053070.
InParanoidiQ9DE07.
KOiK10867.
PhylomeDBiQ9DE07.

Enzyme and pathway databases

ReactomeiR-GGA-217106. Chk1-controlled and DNA-damage induced centrosome duplication.
R-GGA-351433. ATM mediated phosphorylation of repair proteins.
R-GGA-351442. ATM mediated response to DNA double-strand break.
R-GGA-351444. Recruitment of repair and signaling proteins to double-strand breaks.

Miscellaneous databases

PROiQ9DE07.

Family and domain databases

CDDicd00027. BRCT. 1 hit.
Gene3Di2.60.200.20. 1 hit.
3.40.50.10190. 1 hit.
InterProiIPR001357. BRCT_dom.
IPR013908. DNA-repair_Nbs1_C.
IPR000253. FHA_dom.
IPR032429. Nibrin_BRCT2.
IPR016592. Nibrin_met.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PfamiPF00533. BRCT. 1 hit.
PF00498. FHA. 1 hit.
PF08599. Nbs1_C. 1 hit.
PF16508. NIBRIN_BRCT_II. 1 hit.
[Graphical view]
PIRSFiPIRSF011869. Nibrin_animal. 1 hit.
SMARTiSM00292. BRCT. 1 hit.
SM00240. FHA. 1 hit.
SM01348. Nbs1_C. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEiPS50006. FHA_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNBN_CHICK
AccessioniPrimary (citable) accession number: Q9DE07
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: March 1, 2001
Last modified: November 30, 2016
This is version 91 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.