NBN_DANRE
ID NBN_DANRE Reviewed; 818 AA.
AC Q5I2W8; B3DHD3;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Nibrin;
DE AltName: Full=Nijmegen breakage syndrome protein 1 homolog;
GN Name=nbn; Synonyms=nbs1; ORFNames=zgc:194152;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Sampath S., Tang X., Manning J.P. Sr., Xu B.;
RT "Zebrafish NBS1 complements human Nijmegen breakage syndrome phenotype.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the MRE11-RAD50-NBN (MRN complex) which plays a
CC critical role in the cellular response to DNA damage and the
CC maintenance of chromosome integrity. The complex is involved in double-
CC strand break (DSB) repair, DNA recombination, maintenance of telomere
CC integrity, cell cycle checkpoint control and meiosis. The complex
CC possesses single-strand endonuclease activity and double-strand-
CC specific 3'-5' exonuclease activity (By similarity).
CC {ECO:0000250|UniProtKB:O60934}.
CC -!- SUBUNIT: Component of the MRN complex composed of two heterodimers
CC rad50/mre11 associated with a single nbn.
CC {ECO:0000250|UniProtKB:O60934}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O60934}.
CC Chromosome, telomere {ECO:0000250|UniProtKB:O60934}.
CC -!- DOMAIN: The EEXXXDDL motif at the C-terminus is required for the
CC interaction with atm and its recruitment to sites of DNA damage and
CC promote the phosphorylation of atm substrates, leading to the events of
CC DNA damage response. {ECO:0000250|UniProtKB:O60934}.
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DR EMBL; AY858826; AAW50708.1; -; mRNA.
DR EMBL; BC162723; AAI62723.1; -; mRNA.
DR RefSeq; NP_001014819.1; NM_001014819.1.
DR AlphaFoldDB; Q5I2W8; -.
DR STRING; 7955.ENSDARP00000121705; -.
DR PaxDb; Q5I2W8; -.
DR PRIDE; Q5I2W8; -.
DR Ensembl; ENSDART00000058974; ENSDARP00000058973; ENSDARG00000040303.
DR GeneID; 544655; -.
DR KEGG; dre:544655; -.
DR CTD; 4683; -.
DR ZFIN; ZDB-GENE-041008-35; nbn.
DR eggNOG; ENOG502QQ7Y; Eukaryota.
DR GeneTree; ENSGT00390000000521; -.
DR HOGENOM; CLU_023410_0_0_1; -.
DR InParanoid; Q5I2W8; -.
DR OMA; LESPHSC; -.
DR OrthoDB; 831679at2759; -.
DR PhylomeDB; Q5I2W8; -.
DR TreeFam; TF101103; -.
DR Reactome; R-DRE-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-DRE-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-DRE-5685939; HDR through MMEJ (alt-NHEJ).
DR Reactome; R-DRE-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-DRE-5693548; Sensing of DNA Double Strand Breaks.
DR Reactome; R-DRE-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-DRE-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR Reactome; R-DRE-5693571; Nonhomologous End-Joining (NHEJ).
DR Reactome; R-DRE-5693579; Homologous DNA Pairing and Strand Exchange.
DR Reactome; R-DRE-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-DRE-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
DR Reactome; R-DRE-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-DRE-69473; G2/M DNA damage checkpoint.
DR PRO; PR:Q5I2W8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 16.
DR Bgee; ENSDARG00000040303; Expressed in early embryo and 25 other tissues.
DR ExpressionAtlas; Q5I2W8; baseline.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0030870; C:Mre11 complex; IBA:GO_Central.
DR GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR CDD; cd00060; FHA; 1.
DR Gene3D; 3.40.50.10190; -; 1.
DR Gene3D; 3.40.50.10980; -; 1.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR013908; DNA-repair_Nbs1_C.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR040227; Nibrin-rel.
DR InterPro; IPR032429; Nibrin_BRCT2.
DR InterPro; IPR043014; Nibrin_BRCT2_sf.
DR InterPro; IPR016592; Nibrin_met.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR12162; PTHR12162; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF08599; Nbs1_C; 1.
DR Pfam; PF16508; NIBRIN_BRCT_II; 1.
DR PIRSF; PIRSF011869; Nibrin_animal; 1.
DR SMART; SM00240; FHA; 1.
DR SMART; SM01348; Nbs1_C; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Chromosome; DNA damage; DNA repair; Meiosis; Nucleus;
KW Reference proteome; Telomere.
FT CHAIN 1..818
FT /note="Nibrin"
FT /id="PRO_0000231672"
FT DOMAIN 22..70
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT DOMAIN 91..168
FT /note="BRCT"
FT REGION 372..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 470..475
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:O60934"
FT MOTIF 800..807
FT /note="EEXXXDDL motif"
FT /evidence="ECO:0000250|UniProtKB:O60934"
FT COMPBIAS 372..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..567
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..676
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..710
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..812
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 167
FT /note="L -> F (in Ref. 1; AAW50708)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="D -> E (in Ref. 1; AAW50708)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="S -> G (in Ref. 1; AAW50708)"
FT /evidence="ECO:0000305"
FT CONFLICT 504
FT /note="F -> S (in Ref. 1; AAW50708)"
FT /evidence="ECO:0000305"
FT CONFLICT 660
FT /note="S -> T (in Ref. 1; AAW50708)"
FT /evidence="ECO:0000305"
FT CONFLICT 700
FT /note="Q -> R (in Ref. 1; AAW50708)"
FT /evidence="ECO:0000305"
FT CONFLICT 802
FT /note="T -> Y (in Ref. 1; AAW50708)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 818 AA; 89407 MW; DCF20D4B7A0374E3 CRC64;
MWKLQPTESG GESVILLAGQ EYVVGRKNCE ILLTNDQSIS RVHAVLTVTE QAVTLKDSSK
YGTFVNGEKL ESGSTKTLQT GYKITFGVFQ SKFSLEKECI VVCSSCVDNE GKVTLSQDIR
SVGGRLVSSW TSDCTHLVMP TVKVTIKTIC ALLCCRPIVK PAFFSALSKA VQQKLPLPKA
ERFRPQIDEP SLARDDVDLS ARPERKSLFK GKTFLFLSSK QMKRLSVAVS CGGGVSQLLD
EGALPVSLLE SSSTCVLDMI SGNSQPVISP ASKKWLDSVG QILHRKGLRF ITESEVGLAA
IHVSNQTYCN PCSSLQSESV KTNPVFASAT LSQSTAVDET ALAAPSQNIT AYVVNTEISQ
DQSRMVTSGI SAVGETPEKT NPTQKASTTN KPLSLGQEPS STRIVQETVM SSESFSVVES
EQKMKKGSVV SARGRVEGPV KQKAPSSGNT TLKHSPQKQT ALTSFFQPSS KKRPRESSAS
SVQPEPKFFK KDIKDNEDDI QQSFSVNRSH KTSSEETSLG QACGTGQNSS SKKRKEPEQD
TLLGAEEPTA ADDLEMSLEE LEFLMSDEMD EPPQTAANKK QRLESGLTSK INSEQLSNQQ
EVTESKGRKG EKNQQSSSSN IQSMQLDRAG PAVTNQDTQT QSKRSPPDLE AHSSANKGPS
KNKTPELEEV KKEEVSFVVN SRPQNGISQT SEAVLKQEMQ ASTSNSGPKN DPDLPRKLLQ
VQFMSLTVNN SSRSRPGPLQ THNPNDKNVK RFRKKNVPGF DGLPKIIGGS DLVAHNRSKH
SELEEWLRQA AEEEKLNERE ETLGDDLFRY NPRPAKKR
