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NBS1_ARATH
ID   NBS1_ARATH              Reviewed;         542 AA.
AC   Q0H8D7; A1YEB0; Q9M874;
DT   26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Nibrin homolog {ECO:0000305};
DE   AltName: Full=Nijmegen breakage syndrome 1 protein {ECO:0000303|PubMed:17182003};
DE            Short=AtNbs1 {ECO:0000303|PubMed:17182003};
GN   Name=NBS1 {ECO:0000303|PubMed:17182003};
GN   OrderedLocusNames=At3g02680 {ECO:0000312|Araport:AT3G02680};
GN   ORFNames=F16B3.31 {ECO:0000312|EMBL:AAF32475.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702 {ECO:0000312|EMBL:ABA54896.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INDUCTION BY X-RAYS.
RC   STRAIN=cv. Columbia;
RX   PubMed=17182003; DOI=10.1016/j.bbrc.2006.12.030;
RA   Akutsu N., Iijima K., Hinata T., Tauchi H.;
RT   "Characterization of the plant homolog of Nijmegen breakage syndrome 1:
RT   Involvement in DNA repair and recombination.";
RL   Biochem. Biophys. Res. Commun. 353:394-398(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, DISRUPTION PHENOTYPE,
RP   INTERACTION WITH MRE11, AND MUTAGENESIS OF 465-VAL--VAL-500.
RC   STRAIN=cv. Columbia;
RX   PubMed=17672843; DOI=10.1111/j.1365-313x.2007.03220.x;
RA   Waterworth W.M., Altun C., Armstrong S.J., Roberts N., Dean P.J., Young K.,
RA   Weil C.F., Bray C.M., West C.E.;
RT   "NBS1 is involved in DNA repair and plays a synergistic role with ATM in
RT   mediating meiotic homologous recombination in plants.";
RL   Plant J. 52:41-52(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [5]
RP   REVIEW ON DNA REPAIR.
RX   PubMed=16202663; DOI=10.1016/j.dnarep.2005.08.017;
RA   Bleuyard J.Y., Gallego M.E., White C.I.;
RT   "Recent advances in understanding of the DNA double-strand break repair
RT   machinery of plants.";
RL   DNA Repair 5:1-12(2006).
CC   -!- FUNCTION: Component of the MRE11-RAD50-NBN complex (MRN complex) which
CC       plays a critical role in the cellular response to DNA damage and the
CC       maintenance of chromosome integrity. The complex may be involved in
CC       double-strand break (DSB) repair, DNA recombination, maintenance of
CC       telomere integrity, and cell cycle checkpoint control. Functions also
CC       in the very early stages of meiosis. {ECO:0000269|PubMed:17672843}.
CC   -!- SUBUNIT: Component of the MRN complex composed of two heterodimers
CC       RAD50/MRE11 associated with a single NBN (By similarity). Interacts
CC       with MRE11. {ECO:0000250|UniProtKB:O60934,
CC       ECO:0000269|PubMed:17672843}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, PML body {ECO:0000250|UniProtKB:O60934}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q0H8D7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q0H8D7-2; Sequence=VSP_057110;
CC   -!- INDUCTION: By X-rays. {ECO:0000269|PubMed:17182003}.
CC   -!- DOMAIN: The FHA and BRCT domains are likely to have a crucial role for
CC       both binding to histone H2AFX and for relocalization of MRE11/RAD50
CC       complex to the vicinity of DNA damage. {ECO:0000250|UniProtKB:O60934}.
CC   -!- DISRUPTION PHENOTYPE: Hypersensitivity to the DNA cross-linking reagent
CC       mitomycin C. {ECO:0000269|PubMed:17672843}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF32475.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; DQ917672; ABK59968.1; -; mRNA.
DR   EMBL; DQ167217; ABA54896.1; -; mRNA.
DR   EMBL; AC021640; AAF32475.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE73847.1; -; Genomic_DNA.
DR   RefSeq; NP_186917.2; NM_111136.3. [Q0H8D7-1]
DR   AlphaFoldDB; Q0H8D7; -.
DR   STRING; 3702.AT3G02680.1; -.
DR   iPTMnet; Q0H8D7; -.
DR   PaxDb; Q0H8D7; -.
DR   PRIDE; Q0H8D7; -.
DR   ProteomicsDB; 251201; -. [Q0H8D7-1]
DR   EnsemblPlants; AT3G02680.1; AT3G02680.1; AT3G02680. [Q0H8D7-1]
DR   GeneID; 821254; -.
DR   Gramene; AT3G02680.1; AT3G02680.1; AT3G02680. [Q0H8D7-1]
DR   KEGG; ath:AT3G02680; -.
DR   Araport; AT3G02680; -.
DR   TAIR; locus:2076934; AT3G02680.
DR   eggNOG; ENOG502QQ7Y; Eukaryota.
DR   HOGENOM; CLU_036857_0_0_1; -.
DR   InParanoid; Q0H8D7; -.
DR   OMA; DEFCANS; -.
DR   OrthoDB; 831679at2759; -.
DR   PhylomeDB; Q0H8D7; -.
DR   PRO; PR:Q0H8D7; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q0H8D7; baseline and differential.
DR   Genevisible; Q0H8D7; AT.
DR   GO; GO:0030870; C:Mre11 complex; IBA:GO_Central.
DR   GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR   GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR   GO; GO:0071479; P:cellular response to ionizing radiation; IEP:UniProtKB.
DR   GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
DR   GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IBA:GO_Central.
DR   GO; GO:0006312; P:mitotic recombination; IMP:UniProtKB.
DR   GO; GO:0007131; P:reciprocal meiotic recombination; IMP:UniProtKB.
DR   CDD; cd00060; FHA; 1.
DR   Gene3D; 3.40.50.10190; -; 1.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR040227; Nibrin-rel.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   PANTHER; PTHR12162; PTHR12162; 1.
DR   Pfam; PF00498; FHA; 1.
DR   SUPFAM; SSF49879; SSF49879; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell cycle; DNA damage; DNA repair; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..542
FT                   /note="Nibrin homolog"
FT                   /id="PRO_0000430944"
FT   DOMAIN          25..90
FT                   /note="FHA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT   DOMAIN          119..195
FT                   /note="BRCT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT   REGION          409..430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          465..500
FT                   /note="Involved in MRE11-binding"
FT                   /evidence="ECO:0000269|PubMed:17672843"
FT   VAR_SEQ         334..342
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_057110"
FT   MUTAGEN         465..500
FT                   /note="Missing: Impaired MRE11-binding."
FT                   /evidence="ECO:0000269|PubMed:17672843"
SQ   SEQUENCE   542 AA;  60078 MW;  0CAD7920E4682628 CRC64;
     MVWGLFPVDP LSGEDKYYIF SKGIYKVGRK GCDIIINKDK GVSRIHAELT FDATTVSTSR
     RNKSSSDTSS FVIRVKDCSK YGTFVKTDLG TKDKVHELSN KEKILQDGDV IAFGTGSAIY
     RLSLIPLVFY LCPSSETFKV DQPVQDAVSS IGARISPTLS EECTHVLLEP RMQVNEALIN
     AILAKKTIIL TNWVMLLAEK SICSEIPGYS QYRPSVMVEE ALVDVLELNV REKCLEGFTF
     VLEPTDTYRF GCSFPSLLEV CGAETVTIED ISSMSQDSQF GEINRMICVI PKSAGDKFGR
     FKHLSLLSRV NEMDLVCAVF SGNLPSTSLI PPSVVISSSC STDETVVADS EAEEEETTSS
     VHMIDATEKA ETPEKPAAIV IEDSPVTILE ETSNLNEFKS VNLLADTESR GHMDEKNSSD
     SVTIRRDRND EAETGKSEII YTQDLIVRDL RSTRKVQSTG GEGVVDFKRF RKGNVTCGNS
     FSSLIPFAKD PYKEYDSWDV TDFMKEEKKR KQMEAIAEDL FKTEKARKRG TAGSIRGFLS
     GS
 
 
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