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Protein

DNA repair and telomere maintenance protein nbs1

Gene

nbs1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for DNA damage repair and S-phase DNA damage checkpoint. Involved in telomere length maintenance and maintenance of chromatin structure.2 Publications

GO - Biological processi

  • DNA repair Source: UniProtKB
  • double-strand break repair Source: PomBase
  • intra-S DNA damage checkpoint Source: PomBase
  • meiotic DNA double-strand break formation Source: PomBase
  • mitotic DNA damage checkpoint Source: PomBase
  • regulation of histone phosphorylation Source: PomBase
  • telomere maintenance Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair

Names & Taxonomyi

Protein namesi
Recommended name:
DNA repair and telomere maintenance protein nbs1
Gene namesi
Name:nbs1
ORF Names:SPBC6B1.09c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC6B1.09c.
PomBaseiSPBC6B1.09c. nbs1.

Subcellular locationi

GO - Cellular componenti

  • Mre11 complex Source: PomBase
  • nuclear chromosome, telomeric region Source: PomBase
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus, Telomere

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 613613DNA repair and telomere maintenance protein nbs1PRO_0000096751Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei355 – 3551Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO43070.

PTM databases

iPTMnetiO43070.

Interactioni

Subunit structurei

Associates with rad32. Forms a multisubunit endonuclease complex, MRN, together with rad32 and rad50.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ctp1O749866EBI-2125045,EBI-2463766
MDC1Q146762EBI-2125045,EBI-495644From a different organism.

Protein-protein interaction databases

BioGridi280382. 12 interactions.
DIPiDIP-52387N.
IntActiO43070. 3 interactions.
MINTiMINT-4675065.

Structurei

Secondary structure

1
613
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 76Combined sources
Turni8 – 136Combined sources
Beta strandi16 – 183Combined sources
Beta strandi20 – 289Combined sources
Beta strandi35 – 373Combined sources
Beta strandi41 – 433Combined sources
Beta strandi48 – 525Combined sources
Helixi57 – 626Combined sources
Beta strandi68 – 725Combined sources
Beta strandi79 – 813Combined sources
Beta strandi84 – 863Combined sources
Beta strandi91 – 933Combined sources
Beta strandi95 – 1028Combined sources
Beta strandi109 – 1135Combined sources
Beta strandi118 – 1214Combined sources
Helixi123 – 13412Combined sources
Turni135 – 1373Combined sources
Beta strandi140 – 1434Combined sources
Beta strandi150 – 1523Combined sources
Beta strandi157 – 1593Combined sources
Helixi163 – 1708Combined sources
Beta strandi174 – 1763Combined sources
Helixi178 – 1847Combined sources
Helixi188 – 1936Combined sources
Helixi195 – 1973Combined sources
Helixi198 – 20912Combined sources
Helixi219 – 2224Combined sources
Turni223 – 2286Combined sources
Beta strandi230 – 2345Combined sources
Helixi238 – 2469Combined sources
Beta strandi250 – 2545Combined sources
Helixi257 – 2593Combined sources
Beta strandi264 – 2674Combined sources
Beta strandi269 – 2735Combined sources
Helixi275 – 2795Combined sources
Beta strandi283 – 2853Combined sources
Beta strandi291 – 2933Combined sources
Helixi294 – 3029Combined sources
Beta strandi303 – 3064Combined sources
Turni307 – 3126Combined sources
Helixi314 – 3196Combined sources
Beta strandi491 – 4966Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3HUEX-ray2.80A1-330[»]
3HUFX-ray2.15A/B/C1-321[»]
3I0MX-ray2.60A1-324[»]
3I0NX-ray2.30A/B1-324[»]
4FBKX-ray2.38A/B474-531[»]
4FBQX-ray2.50A/B474-531[»]
4FBWX-ray2.20C/D474-531[»]
ProteinModelPortaliO43070.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43070.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 8664FHAPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 FHA domain.PROSITE-ProRule annotation

Phylogenomic databases

InParanoidiO43070.
OrthoDBiEOG7SN8NB.

Family and domain databases

Gene3Di2.60.200.20. 1 hit.
InterProiIPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PfamiPF00498. FHA. 1 hit.
[Graphical view]
SMARTiSM00240. FHA. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
PROSITEiPS50006. FHA_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O43070-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWIIEAEGDI LKGKSRILFP GTYIVGRNVS DDSSHIQVIS KSISKRHARF
60 70 80 90 100
TILTPSEKDY FTGGPCEFEV KDLDTKFGTK VNEKVVGQNG DSYKEKDLKI
110 120 130 140 150
QLGKCPFTIN AYWRSMCIQF DNPEMLSQWA SNLNLLGIPT GLRDSDATTH
160 170 180 190 200
FVMNRQAGSS ITVGTMYAFL KKTVIIDDSY LQYLSTVKES VIEDASLMPD
210 220 230 240 250
ALECFKNIIK NNDQFPSSPE DCINSLEGFS CAMLNTSSES HHLLELLGLR
260 270 280 290 300
ISTFMSLGDI DKELISKTDF VVLNNAVYDS EKISFPEGIF CLTIEQLWKI
310 320 330 340 350
IIERNSRELI SKEIERLKYA TASNSTPQKI IQPQRHIQKN IVDDLFSVKK
360 370 380 390 400
PLPCSPKSKR VKTLENLSIM DFVQPKQMFG KEPEGYLSNQ SNNGSAQNKK
410 420 430 440 450
SGDNSEKTKN SLKSSSKKSA NTGSGQGKTK VEYVSYNSVD KGNSSPFKPL
460 470 480 490 500
ELNVVGEKKA NAEVDSLPSE NVQESEDDKA FEENRRLRNL GSVEYIRIMS
510 520 530 540 550
SEKSNANSRH TSKYYSGRKN FKKFQKKASQ KAPLQAFLSL SEHKKTEVFD
560 570 580 590 600
QDDTDLEPVP RLMSKVESIP AGASSDKSGK SSISKKSSNS FKELSPKTNN
610
DEDDEFNDLK FHF
Length:613
Mass (Da):68,807
Last modified:November 7, 2003 - v3
Checksum:iB3384CCC85F96DD1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB099299 mRNA. Translation: BAC80248.1.
AY269280 mRNA. Translation: AAP32157.1.
CU329671 Genomic DNA. Translation: CAD88196.1.
RefSeqiNP_001018823.1. NM_001022003.2.

Genome annotation databases

EnsemblFungiiSPBC6B1.09c.1; SPBC6B1.09c.1:pep; SPBC6B1.09c.
GeneIDi3361306.
KEGGispo:SPBC6B1.09c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB099299 mRNA. Translation: BAC80248.1.
AY269280 mRNA. Translation: AAP32157.1.
CU329671 Genomic DNA. Translation: CAD88196.1.
RefSeqiNP_001018823.1. NM_001022003.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3HUEX-ray2.80A1-330[»]
3HUFX-ray2.15A/B/C1-321[»]
3I0MX-ray2.60A1-324[»]
3I0NX-ray2.30A/B1-324[»]
4FBKX-ray2.38A/B474-531[»]
4FBQX-ray2.50A/B474-531[»]
4FBWX-ray2.20C/D474-531[»]
ProteinModelPortaliO43070.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi280382. 12 interactions.
DIPiDIP-52387N.
IntActiO43070. 3 interactions.
MINTiMINT-4675065.

PTM databases

iPTMnetiO43070.

Proteomic databases

MaxQBiO43070.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC6B1.09c.1; SPBC6B1.09c.1:pep; SPBC6B1.09c.
GeneIDi3361306.
KEGGispo:SPBC6B1.09c.

Organism-specific databases

EuPathDBiFungiDB:SPBC6B1.09c.
PomBaseiSPBC6B1.09c. nbs1.

Phylogenomic databases

InParanoidiO43070.
OrthoDBiEOG7SN8NB.

Miscellaneous databases

EvolutionaryTraceiO43070.
PROiO43070.

Family and domain databases

Gene3Di2.60.200.20. 1 hit.
InterProiIPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PfamiPF00498. FHA. 1 hit.
[Graphical view]
SMARTiSM00240. FHA. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
PROSITEiPS50006. FHA_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization of the Schizosaccharomyces pombe nbs1+ gene involved in DNA repair and telomere maintenance."
    Ueno M., Nakazaki T., Akamatsu Y., Watanabe K., Tomita K., Lindsay H.D., Shinagawa H., Iwasaki H.
    Mol. Cell. Biol. 23:6553-6563(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
  2. "The fission yeast Rad32 (Mre11)-Rad50-Nbs1 complex is required for the S-phase DNA damage checkpoint."
    Chahwan C., Nakamura T.M., Sivakumar S., Russell P., Rhind N.
    Mol. Cell. Biol. 23:6564-6573(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
  3. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiNBS1_SCHPO
AccessioniPrimary (citable) accession number: O43070
Secondary accession number(s): Q86ZQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: November 7, 2003
Last modified: June 8, 2016
This is version 104 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. 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.