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NSE3_SCHPO
ID   NSE3_SCHPO              Reviewed;         328 AA.
AC   Q9Y7U4;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 118.
DE   RecName: Full=Non-structural maintenance of chromosome element 3;
DE            Short=Non-SMC element 3;
GN   Name=nse3; ORFNames=SPCC645.04;
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 [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   [2]
RP   PARTIAL PROTEIN SEQUENCE, FUNCTION, INTERACTION WITH NSE1, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=15331764; DOI=10.1091/mbc.e04-05-0436;
RA   Pebernard S., McDonald W.H., Pavlova Y., Yates J.R. III, Boddy M.N.;
RT   "Nse1, Nse2, and a novel subunit of the Smc5-Smc6 complex, Nse3, play a
RT   crucial role in meiosis.";
RL   Mol. Biol. Cell 15:4866-4876(2004).
RN   [3]
RP   PARTIAL PROTEIN SEQUENCE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=16478984; DOI=10.1128/mcb.26.5.1617-1630.2006;
RA   Pebernard S., Wohlschlegel J., McDonald W.H., Yates J.R. III, Boddy M.N.;
RT   "The Nse5-Nse6 dimer mediates DNA repair roles of the Smc5-Smc6 complex.";
RL   Mol. Cell. Biol. 26:1617-1630(2006).
RN   [4]
RP   INTERACTION WITH NSE1; NSE2 AND NSE4, AND SUBCELLULAR LOCATION.
RX   PubMed=15601840; DOI=10.1128/mcb.25.1.172-184.2005;
RA   Sergeant J., Taylor E., Palecek J., Fousteri M., Andrews E.A., Sweeney S.,
RA   Shinagawa H., Watts F.Z., Lehmann A.R.;
RT   "Composition and architecture of the Schizosaccharomyces pombe Rad18 (Smc5-
RT   6) complex.";
RL   Mol. Cell. Biol. 25:172-184(2005).
RN   [5]
RP   SUMOYLATION BY NSE2.
RX   PubMed=15601841; DOI=10.1128/mcb.25.1.185-196.2005;
RA   Andrews E.A., Palecek J., Sergeant J., Taylor E., Lehmann A.R., Watts F.Z.;
RT   "Nse2, a component of the Smc5-6 complex, is a SUMO ligase required for the
RT   response to DNA damage.";
RL   Mol. Cell. Biol. 25:185-196(2005).
RN   [6]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Acts in a DNA repair pathway for removal of UV-induced DNA
CC       damage that is distinct from classical nucleotide excision repair and
CC       in repair of ionizing radiation damage. Functions in homologous
CC       recombination repair of DNA double strand breaks and in recovery of
CC       stalled replication forks. Plays a critical role in meiosis.
CC       {ECO:0000269|PubMed:15331764}.
CC   -!- SUBUNIT: Two subcomplexes smc5-smc6-nse2 and nse1-nse3-nse4 exist.
CC       These subcomplexes are then brought together via a number of
CC       interactions, forming the Smc5-Smc6 complex.
CC   -!- INTERACTION:
CC       Q9Y7U4; Q53EK2: nse1; NbExp=9; IntAct=EBI-605466, EBI-605440;
CC       Q9Y7U4; Q4PIR3: nse2; NbExp=2; IntAct=EBI-605466, EBI-605449;
CC       Q9Y7U4; Q6BDR8: nse4; NbExp=7; IntAct=EBI-605466, EBI-605484;
CC       Q9Y7U4; O13710: smc5; NbExp=5; IntAct=EBI-605466, EBI-603756;
CC       Q9Y7U4; P53692: smc6; NbExp=5; IntAct=EBI-605466, EBI-603745;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15331764,
CC       ECO:0000269|PubMed:15601840, ECO:0000269|PubMed:16823372}.
CC   -!- PTM: Sumoylated by nse2. {ECO:0000269|PubMed:15601841}.
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DR   EMBL; CU329672; CAB39900.1; -; Genomic_DNA.
DR   PIR; T41521; T41521.
DR   RefSeq; NP_588113.1; NM_001023103.2.
DR   AlphaFoldDB; Q9Y7U4; -.
DR   SMR; Q9Y7U4; -.
DR   BioGRID; 275999; 10.
DR   IntAct; Q9Y7U4; 6.
DR   STRING; 4896.SPCC645.04.1; -.
DR   PaxDb; Q9Y7U4; -.
DR   EnsemblFungi; SPCC645.04.1; SPCC645.04.1:pep; SPCC645.04.
DR   GeneID; 2539436; -.
DR   KEGG; spo:SPCC645.04; -.
DR   PomBase; SPCC645.04; nse3.
DR   VEuPathDB; FungiDB:SPCC645.04; -.
DR   eggNOG; KOG4562; Eukaryota.
DR   HOGENOM; CLU_829383_0_0_1; -.
DR   InParanoid; Q9Y7U4; -.
DR   OMA; WHVGPRG; -.
DR   PhylomeDB; Q9Y7U4; -.
DR   Reactome; R-SPO-114608; Platelet degranulation.
DR   Reactome; R-SPO-3108214; SUMOylation of DNA damage response and repair proteins.
DR   PRO; PR:Q9Y7U4; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0030915; C:Smc5-Smc6 complex; IDA:PomBase.
DR   GO; GO:0003690; F:double-stranded DNA binding; IDA:PomBase.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IGI:PomBase.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.1200; -; 1.
DR   Gene3D; 1.10.10.1210; -; 1.
DR   InterPro; IPR037445; MAGE.
DR   InterPro; IPR041898; MAGE_WH1.
DR   InterPro; IPR041899; MAGE_WH2.
DR   InterPro; IPR002190; MHD_dom.
DR   PANTHER; PTHR11736; PTHR11736; 1.
DR   Pfam; PF01454; MAGE; 1.
DR   SMART; SM01373; MAGE; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; DNA damage; DNA recombination; DNA repair;
KW   Meiosis; Nucleus; Reference proteome; Ubl conjugation.
FT   CHAIN           1..328
FT                   /note="Non-structural maintenance of chromosome element 3"
FT                   /id="PRO_0000057961"
FT   REGION          1..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..50
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   328 AA;  37276 MW;  80E2E470076B11E0 CRC64;
     MSQLSFTGKS SSKGRSRLTQ EVRPTASQII ADEEASDLDE YEEDLEGSGN EDDFGPSMSR
     SSRGRKRRKG DPLELQSQFE ERNETDAINF QLLVRNVVRY AICSQTSHNT ITRKDIVQKA
     FPEGTSRNLF QSVFEEADRQ LQLSFGFRLV AVTQSNRKKD MAVSQLRRPA TSNANSSNLH
     RYWVLRSTLP MELQKDSRLI VDSVLDTAYY GFLMTVIAFI AVSHCSVGHS ELQSFLQELL
     TEEETTPLHL DITRSLSLLV RQGYLDRVKD DTHNQFVYYI GSRAVTEISI EGLKSFVTEF
     FPDSDIDMDA LLTEYRQEYQ NQSSSSAA
 
 
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