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NSE4_YEAST
ID   NSE4_YEAST              Reviewed;         402 AA.
AC   P43124; D6VRP5;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=Non-structural maintenance of chromosome element 4;
DE            Short=Non-SMC element 4;
DE   AltName: Full=Protein QRI2;
GN   Name=NSE4; Synonyms=QRI2; OrderedLocusNames=YDL105W; ORFNames=D2354;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7725801; DOI=10.1002/yea.320101215;
RA   Simon M., Benit P., Vassal A., Dubois C., Faye G.;
RT   "Sequence of the PHO2-POL3 (CDC2) region of chromosome IV of Saccharomyces
RT   cerevisiae.";
RL   Yeast 10:1653-1656(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8896274;
RX   DOI=10.1002/(sici)1097-0061(199609)12:10b<1077::aid-yea8>3.0.co;2-z;
RA   Saiz J.E., Buitrago M.J., Garcia R., Revuelta J.L., del Rey F.;
RT   "The sequence of a 20.3 kb DNA fragment from the left arm of Saccharomyces
RT   cerevisiae chromosome IV contains the KIN28, MSS2, PHO2, POL3 and DUN1
RT   genes, and six new open reading frames.";
RL   Yeast 12:1077-1084(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH NSE3.
RX   PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA   Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA   Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA   Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT   "Assigning function to yeast proteins by integration of technologies.";
RL   Mol. Cell 12:1353-1365(2003).
RN   [6]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [7]
RP   FUNCTION, INTERACTION WITH NSE3, AND SUBCELLULAR LOCATION.
RX   PubMed=15752197; DOI=10.1111/j.1365-2958.2005.04531.x;
RA   Hu B., Liao C., Millson S.H., Mollapour M., Prodromou C., Pearl L.H.,
RA   Piper P.W., Panaretou B.;
RT   "Qri2/Nse4, a component of the essential Smc5/6 DNA repair complex.";
RL   Mol. Microbiol. 55:1735-1750(2005).
RN   [8]
RP   SUBUNIT.
RX   PubMed=15738391; DOI=10.1073/pnas.0500537102;
RA   Zhao X., Blobel G.;
RT   "A SUMO ligase is part of a nuclear multiprotein complex that affects DNA
RT   repair and chromosomal organization.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:4777-4782(2005).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
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. {ECO:0000269|PubMed:15752197}.
CC   -!- SUBUNIT: Component of the Smc5-Smc6 complex which consists of KRE29,
CC       MMS21, NSE1, NSE3, NSE4, NSE5, SMC5 and SMC6. Interacts with NSE3.
CC       {ECO:0000269|PubMed:14690591, ECO:0000269|PubMed:15738391,
CC       ECO:0000269|PubMed:15752197}.
CC   -!- INTERACTION:
CC       P43124; Q05541: NSE3; NbExp=4; IntAct=EBI-14410, EBI-36625;
CC       P43124; Q08204: SMC5; NbExp=3; IntAct=EBI-14410, EBI-34125;
CC       P43124; Q12306: SMT3; NbExp=2; IntAct=EBI-14410, EBI-17490;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:15752197}.
CC   -!- SIMILARITY: Belongs to the NSE4 family. {ECO:0000305}.
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DR   EMBL; X79380; CAA55925.1; -; Genomic_DNA.
DR   EMBL; X95644; CAA64908.1; -; Genomic_DNA.
DR   EMBL; Z74153; CAA98672.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11755.1; -; Genomic_DNA.
DR   PIR; S50739; S50739.
DR   RefSeq; NP_010178.1; NM_001180164.1.
DR   AlphaFoldDB; P43124; -.
DR   SMR; P43124; -.
DR   BioGRID; 31957; 808.
DR   ComplexPortal; CPX-1364; SMC5-SMC6 SUMO ligase complex.
DR   DIP; DIP-2839N; -.
DR   IntAct; P43124; 12.
DR   MINT; P43124; -.
DR   STRING; 4932.YDL105W; -.
DR   iPTMnet; P43124; -.
DR   MaxQB; P43124; -.
DR   PaxDb; P43124; -.
DR   PRIDE; P43124; -.
DR   EnsemblFungi; YDL105W_mRNA; YDL105W; YDL105W.
DR   GeneID; 851453; -.
DR   KEGG; sce:YDL105W; -.
DR   SGD; S000002263; NSE4.
DR   VEuPathDB; FungiDB:YDL105W; -.
DR   eggNOG; KOG2866; Eukaryota.
DR   GeneTree; ENSGT00940000165188; -.
DR   HOGENOM; CLU_041037_5_1_1; -.
DR   InParanoid; P43124; -.
DR   OMA; IFQMDMP; -.
DR   BioCyc; YEAST:G3O-29506-MON; -.
DR   Reactome; R-SCE-3108214; SUMOylation of DNA damage response and repair proteins.
DR   PRO; PR:P43124; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P43124; protein.
DR   GO; GO:0000781; C:chromosome, telomeric region; IC:ComplexPortal.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0030915; C:Smc5-Smc6 complex; IDA:SGD.
DR   GO; GO:0006281; P:DNA repair; IMP:SGD.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IC:ComplexPortal.
DR   GO; GO:0016925; P:protein sumoylation; IC:ComplexPortal.
DR   GO; GO:0032204; P:regulation of telomere maintenance; IC:ComplexPortal.
DR   InterPro; IPR027786; Nse4/EID.
DR   InterPro; IPR014854; Nse4_C.
DR   InterPro; IPR029225; Nse4_Nse3-bd.
DR   PANTHER; PTHR16140; PTHR16140; 1.
DR   Pfam; PF15412; Nse4-Nse3_bdg; 1.
DR   Pfam; PF08743; Nse4_C; 1.
PE   1: Evidence at protein level;
KW   DNA damage; DNA recombination; DNA repair; Nucleus; Reference proteome.
FT   CHAIN           1..402
FT                   /note="Non-structural maintenance of chromosome element 4"
FT                   /id="PRO_0000214100"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          166..195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..42
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        175..192
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   402 AA;  46121 MW;  503FD4614C01CD51 CRC64;
     MSSTVISRKR RNSTVTEPDS SGETRKQKKS RSDEKSSSSK DGDPQLEFKV LQGYRDLESE
     MHKGRAQVTR TGDIGVAMDN LNAVDSLFNK VIGIKNNGLF AHDARAMVSI SELAQISVRN
     LKFDDSRSMV NLENIVNSLK RYMLKEHFKL NNIAENRNDL TLAADEQSAA DQQEESDGDI
     DRTPDDNHTD KATSSFKATS MRHSYLQQFS HYNEFSQFNW FRIGALYNTI SKNAPITDHL
     MGPLSIEKKP RVLTQRRRNN DQVGEKITAE KITQHSLNST QQETTPEQVK KCFKKLSKKL
     GPEGSINLFK FIIDPNSFSR SIENLFYTSF LIKEGKLLME HDEEGLPTIK IKQSISHTDS
     RSKEIERQRR RAAHQNHIIF QMDMPTWRKL IKKYNITSPF LD
 
 
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