NSE2_SCHPO
ID NSE2_SCHPO Reviewed; 250 AA.
AC Q4PIR3;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 3.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=E3 SUMO-protein ligase nse2;
DE EC=2.3.2.-;
DE AltName: Full=E3 SUMO-protein transferase nse2 {ECO:0000305};
DE AltName: Full=Non-structural maintenance of chromosomes element 2;
DE Short=Non-SMC element 2;
GN Name=nse2; Synonyms=pli2; ORFNames=SPAC16A10.06c;
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 REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP FUNCTION, INTERACTION WITH SMC5 AND SMC6, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12966087; DOI=10.1074/jbc.m308828200;
RA McDonald W.H., Pavlova Y., Yates J.R. III, Boddy M.N.;
RT "Novel essential DNA repair proteins Nse1 and Nse2 are subunits of the
RT fission yeast Smc5-Smc6 complex.";
RL J. Biol. Chem. 278:45460-45467(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY.
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 [5]
RP INTERACTION WITH NSE3 AND SMC5.
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 [6]
RP FUNCTION, INTERACTION WITH SMC5 AND SMC6, AUTOSUMOYLATION, MUTAGENESIS OF
RP CYS-195 AND HIS-197, AND REVISION OF GENE MODEL.
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 [7]
RP 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 [8]
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 as an E3 ligase mediating SUMO/Smt3 attachment to other
CC proteins. 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:12966087, ECO:0000269|PubMed:15601841}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
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 Q4PIR3; Q9Y7U4: nse3; NbExp=2; IntAct=EBI-605449, EBI-605466;
CC Q4PIR3; O13688: nse6; NbExp=2; IntAct=EBI-605449, EBI-1150368;
CC Q4PIR3; O13710: smc5; NbExp=9; IntAct=EBI-605449, EBI-603756;
CC Q4PIR3; P53692: smc6; NbExp=3; IntAct=EBI-605449, EBI-603745;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12966087,
CC ECO:0000269|PubMed:16823372}.
CC -!- PTM: Autosumoylated.
CC -!- SIMILARITY: Belongs to the NSE2 family. {ECO:0000305}.
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DR EMBL; CU329670; CAJ01913.3; -; Genomic_DNA.
DR RefSeq; XP_001713077.3; XM_001713025.3.
DR AlphaFoldDB; Q4PIR3; -.
DR SMR; Q4PIR3; -.
DR BioGRID; 278778; 14.
DR IntAct; Q4PIR3; 5.
DR STRING; 4896.SPAC16A10.06c.1; -.
DR MaxQB; Q4PIR3; -.
DR PaxDb; Q4PIR3; -.
DR PRIDE; Q4PIR3; -.
DR EnsemblFungi; SPAC16A10.06c.1; SPAC16A10.06c.1:pep; SPAC16A10.06c.
DR PomBase; SPAC16A10.06c; nse2.
DR VEuPathDB; FungiDB:SPAC16A10.06c; -.
DR eggNOG; KOG2979; Eukaryota.
DR HOGENOM; CLU_1116301_0_0_1; -.
DR InParanoid; Q4PIR3; -.
DR OMA; QDYKCPI; -.
DR Reactome; R-SPO-3108214; SUMOylation of DNA damage response and repair proteins.
DR UniPathway; UPA00886; -.
DR PRO; PR:Q4PIR3; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0030915; C:Smc5-Smc6 complex; IDA:PomBase.
DR GO; GO:0061665; F:SUMO ligase activity; IDA:PomBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:PomBase.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0016925; P:protein sumoylation; IDA:PomBase.
DR CDD; cd16651; SPL-RING_NSE2; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR026846; Nse2(Mms21).
DR InterPro; IPR004181; Znf_MIZ.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR21330; PTHR21330; 1.
DR Pfam; PF11789; zf-Nse; 1.
DR PROSITE; PS51044; ZF_SP_RING; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA recombination; DNA repair; Meiosis; Metal-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..250
FT /note="E3 SUMO-protein ligase nse2"
FT /id="PRO_0000218992"
FT ZN_FING 164..243
FT /note="SP-RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT MUTAGEN 195
FT /note="C->S: No sumoylation activity."
FT /evidence="ECO:0000269|PubMed:15601841"
FT MUTAGEN 197
FT /note="H->A: No sumoylation activity."
FT /evidence="ECO:0000269|PubMed:15601841"
SQ SEQUENCE 250 AA; 28676 MW; 8DC276BCB3A0E107 CRC64;
MSEAQLKTSL EALSQNLLPG NQNHCSFDFQ LKEIDDSIKQ VIKCALVAAE IKNNECLDML
DSGIRELLDA KQRLLLMQQS VDTLANKTSE NISDFENKSL LDIYTQIFKE LIQEYEEKSD
YGKYGTQGEY IEFKKTIWHE QNTDGSDFPS MKTFFNVMNT EEQEADEVMV YSATFDNRCP
LTLQPIVHPI LSTACNHFYE KDAILSLLNP TCVCPVVGCE ARLQRSLLKE DEILERRLRR
AQEISNLKEA
