NBS1_SCHPO
ID NBS1_SCHPO Reviewed; 613 AA.
AC O43070; Q86ZQ0;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2003, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=DNA repair and telomere maintenance protein nbs1;
GN Name=nbs1; ORFNames=SPBC6B1.09c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12944481; DOI=10.1128/mcb.23.18.6553-6563.2003;
RA Ueno M., Nakazaki T., Akamatsu Y., Watanabe K., Tomita K., Lindsay H.D.,
RA Shinagawa H., Iwasaki H.;
RT "Molecular characterization of the Schizosaccharomyces pombe nbs1+ gene
RT involved in DNA repair and telomere maintenance.";
RL Mol. Cell. Biol. 23:6553-6563(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=12944482; DOI=10.1128/mcb.23.18.6564-6573.2003;
RA Chahwan C., Nakamura T.M., Sivakumar S., Russell P., Rhind N.;
RT "The fission yeast Rad32 (Mre11)-Rad50-Nbs1 complex is required for the S-
RT phase DNA damage checkpoint.";
RL Mol. Cell. Biol. 23:6564-6573(2003).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Required for DNA damage repair and S-phase DNA damage
CC checkpoint. Involved in telomere length maintenance and maintenance of
CC chromatin structure. {ECO:0000269|PubMed:12944481,
CC ECO:0000269|PubMed:12944482}.
CC -!- SUBUNIT: Associates with rad32. Forms a multisubunit endonuclease
CC complex, MRN, together with rad32 and rad50.
CC {ECO:0000269|PubMed:12944482}.
CC -!- INTERACTION:
CC O43070; O74986: ctp1; NbExp=6; IntAct=EBI-2125045, EBI-2463766;
CC O43070; Q09683: rad32; NbExp=6; IntAct=EBI-2125045, EBI-2124866;
CC O43070; Q14676: MDC1; Xeno; NbExp=2; IntAct=EBI-2125045, EBI-495644;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12944481}.
CC Chromosome, telomere {ECO:0000269|PubMed:12944481,
CC ECO:0000269|PubMed:12944482}.
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DR EMBL; AB099299; BAC80248.1; -; mRNA.
DR EMBL; AY269280; AAP32157.1; -; mRNA.
DR EMBL; CU329671; CAD88196.1; -; Genomic_DNA.
DR RefSeq; NP_001018823.1; NM_001022003.2.
DR PDB; 3HUE; X-ray; 2.80 A; A=1-330.
DR PDB; 3HUF; X-ray; 2.15 A; A/B/C=1-321.
DR PDB; 3I0M; X-ray; 2.60 A; A=1-324.
DR PDB; 3I0N; X-ray; 2.30 A; A/B=1-324.
DR PDB; 4FBK; X-ray; 2.38 A; A/B=474-531.
DR PDB; 4FBQ; X-ray; 2.50 A; A/B=474-531.
DR PDB; 4FBW; X-ray; 2.20 A; C/D=474-531.
DR PDBsum; 3HUE; -.
DR PDBsum; 3HUF; -.
DR PDBsum; 3I0M; -.
DR PDBsum; 3I0N; -.
DR PDBsum; 4FBK; -.
DR PDBsum; 4FBQ; -.
DR PDBsum; 4FBW; -.
DR AlphaFoldDB; O43070; -.
DR SMR; O43070; -.
DR BioGRID; 280382; 14.
DR DIP; DIP-52387N; -.
DR IntAct; O43070; 3.
DR STRING; 4896.SPBC6B1.09c.1; -.
DR iPTMnet; O43070; -.
DR MaxQB; O43070; -.
DR PaxDb; O43070; -.
DR PRIDE; O43070; -.
DR EnsemblFungi; SPBC6B1.09c.1; SPBC6B1.09c.1:pep; SPBC6B1.09c.
DR GeneID; 3361306; -.
DR KEGG; spo:SPBC6B1.09c; -.
DR PomBase; SPBC6B1.09c; nbs1.
DR VEuPathDB; FungiDB:SPBC6B1.09c; -.
DR eggNOG; ENOG502RS0G; Eukaryota.
DR HOGENOM; CLU_445609_0_0_1; -.
DR InParanoid; O43070; -.
DR OMA; ARWSTPL; -.
DR Reactome; R-SPO-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-SPO-5685939; HDR through MMEJ (alt-NHEJ).
DR Reactome; R-SPO-5693548; Sensing of DNA Double Strand Breaks.
DR Reactome; R-SPO-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-SPO-5693607; Processing of DNA double-strand break ends.
DR EvolutionaryTrace; O43070; -.
DR PRO; PR:O43070; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0140445; C:chromosome, telomeric repeat region; IDA:PomBase.
DR GO; GO:0030870; C:Mre11 complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0035861; C:site of double-strand break; IDA:PomBase.
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:0006281; P:DNA repair; IMP:UniProtKB.
DR GO; GO:0006302; P:double-strand break repair; IGI:PomBase.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:PomBase.
DR GO; GO:1990898; P:meiotic DNA double-strand break clipping; IMP:PomBase.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IMP:PomBase.
DR GO; GO:0070198; P:protein localization to chromosome, telomeric region; IMP:PomBase.
DR GO; GO:1990166; P:protein localization to site of double-strand break; IMP:PomBase.
DR GO; GO:0000723; P:telomere maintenance; IDA:UniProtKB.
DR GO; GO:0000722; P:telomere maintenance via recombination; IGI:PomBase.
DR CDD; cd00060; FHA; 1.
DR DisProt; DP02839; -.
DR Gene3D; 3.40.50.10190; -; 1.
DR IDEAL; IID50239; -.
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 SMART; SM00240; FHA; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; DNA damage; DNA repair; Nucleus; Phosphoprotein;
KW Reference proteome; Telomere.
FT CHAIN 1..613
FT /note="DNA repair and telomere maintenance protein nbs1"
FT /id="PRO_0000096751"
FT DOMAIN 23..86
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT REGION 381..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..560
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..613
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:3HUF"
FT TURN 8..13
FT /evidence="ECO:0007829|PDB:3HUF"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:3HUF"
FT STRAND 20..28
FT /evidence="ECO:0007829|PDB:3HUF"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:3HUF"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:3I0M"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:3HUF"
FT HELIX 57..62
FT /evidence="ECO:0007829|PDB:3HUF"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:3HUF"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:3HUF"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:3I0M"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:3HUF"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:3HUF"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:3HUF"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:3HUF"
FT HELIX 123..134
FT /evidence="ECO:0007829|PDB:3HUF"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:3HUF"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:3HUF"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:3HUF"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:3I0N"
FT HELIX 163..170
FT /evidence="ECO:0007829|PDB:3HUF"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:3HUF"
FT HELIX 178..184
FT /evidence="ECO:0007829|PDB:3HUF"
FT HELIX 190..193
FT /evidence="ECO:0007829|PDB:3I0N"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:3I0N"
FT HELIX 198..209
FT /evidence="ECO:0007829|PDB:3HUF"
FT HELIX 219..222
FT /evidence="ECO:0007829|PDB:3HUF"
FT TURN 223..228
FT /evidence="ECO:0007829|PDB:3HUF"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:3HUF"
FT HELIX 238..246
FT /evidence="ECO:0007829|PDB:3HUF"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:3HUF"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:3I0N"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:3HUF"
FT STRAND 269..273
FT /evidence="ECO:0007829|PDB:3HUF"
FT HELIX 275..279
FT /evidence="ECO:0007829|PDB:3I0N"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:3I0M"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:3HUF"
FT HELIX 294..302
FT /evidence="ECO:0007829|PDB:3HUF"
FT STRAND 303..306
FT /evidence="ECO:0007829|PDB:3HUF"
FT TURN 307..312
FT /evidence="ECO:0007829|PDB:3HUF"
FT HELIX 314..319
FT /evidence="ECO:0007829|PDB:3HUF"
FT HELIX 478..486
FT /evidence="ECO:0007829|PDB:4FBK"
FT STRAND 491..496
FT /evidence="ECO:0007829|PDB:4FBW"
SQ SEQUENCE 613 AA; 68807 MW; B3384CCC85F96DD1 CRC64;
MWIIEAEGDI LKGKSRILFP GTYIVGRNVS DDSSHIQVIS KSISKRHARF TILTPSEKDY
FTGGPCEFEV KDLDTKFGTK VNEKVVGQNG DSYKEKDLKI QLGKCPFTIN AYWRSMCIQF
DNPEMLSQWA SNLNLLGIPT GLRDSDATTH FVMNRQAGSS ITVGTMYAFL KKTVIIDDSY
LQYLSTVKES VIEDASLMPD ALECFKNIIK NNDQFPSSPE DCINSLEGFS CAMLNTSSES
HHLLELLGLR ISTFMSLGDI DKELISKTDF VVLNNAVYDS EKISFPEGIF CLTIEQLWKI
IIERNSRELI SKEIERLKYA TASNSTPQKI IQPQRHIQKN IVDDLFSVKK PLPCSPKSKR
VKTLENLSIM DFVQPKQMFG KEPEGYLSNQ SNNGSAQNKK SGDNSEKTKN SLKSSSKKSA
NTGSGQGKTK VEYVSYNSVD KGNSSPFKPL ELNVVGEKKA NAEVDSLPSE NVQESEDDKA
FEENRRLRNL GSVEYIRIMS SEKSNANSRH TSKYYSGRKN FKKFQKKASQ KAPLQAFLSL
SEHKKTEVFD QDDTDLEPVP RLMSKVESIP AGASSDKSGK SSISKKSSNS FKELSPKTNN
DEDDEFNDLK FHF
