NET1_YEAST
ID NET1_YEAST Reviewed; 1189 AA.
AC P47035; D6VWA8;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Nucleolar protein NET1;
GN Name=NET1; Synonyms=CFI1, ESC5, SRM8; OrderedLocusNames=YJL076W;
GN ORFNames=J1038;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [2]
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 [3]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=12056824; DOI=10.1016/s0006-291x(02)00544-2;
RA Yoshida S., Toh-e A.;
RT "Budding yeast Cdc5 phosphorylates Net1 and assists Cdc14 release from the
RT nucleolus.";
RL Biochem. Biophys. Res. Commun. 294:687-691(2002).
RN [4]
RP FUNCTION, AND SUBUNIT.
RX PubMed=11511359; DOI=10.1016/s1097-2765(01)00291-x;
RA Shou W., Sakamoto K.M., Keener J., Morimoto K.W., Traverso E.E., Azzam R.,
RA Hoppe G.J., Feldman R.M.R., DeModena J., Moazed D., Charbonneau H.,
RA Nomura M., Deshaies R.J.;
RT "Net1 stimulates RNA polymerase I transcription and regulates nucleolar
RT structure independently of controlling mitotic exit.";
RL Mol. Cell 8:45-55(2001).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231; SER-497 AND THR-676, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231; SER-252; SER-830 AND
RP THR-1042, AND 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; SER-166; SER-231;
RP SER-437; SER-439; SER-447; SER-452; SER-497; THR-1042; SER-1056 AND
RP SER-1059, AND 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).
RN [10]
RP INTERACTION WITH NSI1.
RX PubMed=22362748; DOI=10.1093/nar/gks188;
RA Ha C.W., Sung M.K., Huh W.K.;
RT "Nsi1 plays a significant role in the silencing of ribosomal DNA in
RT Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 40:4892-4903(2012).
CC -!- FUNCTION: Has a role in chromosome maintenance and is involved in
CC mitotic exit. Inhibits the action of CDC14 by sequestering it in the
CC nucleolus. Also binds to RNA polymerase I and stimulates rRNA
CC synthesis. Influences RDNA chromatin by tethering SIR2 to rDNA in the
CC nucleolus. {ECO:0000269|PubMed:11511359, ECO:0000269|PubMed:12056824}.
CC -!- SUBUNIT: Component of the RENT complex which is composed of at least
CC NET1, CDC14 and SIR2 (PubMed:12056824, PubMed:11511359). Interacts with
CC NSI1 (PubMed:22362748). {ECO:0000269|PubMed:11511359,
CC ECO:0000269|PubMed:12056824, ECO:0000269|PubMed:22362748}.
CC -!- INTERACTION:
CC P47035; Q00684: CDC14; NbExp=13; IntAct=EBI-25953, EBI-4192;
CC P47035; P00572: CDC8; NbExp=2; IntAct=EBI-25953, EBI-9957;
CC P47035; P53131: PRP43; NbExp=2; IntAct=EBI-25953, EBI-505;
CC P47035; Q02208: TOF2; NbExp=6; IntAct=EBI-25953, EBI-27048;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12056824}.
CC -!- PTM: Phosphorylated by CDC5. {ECO:0000269|PubMed:12056824}.
CC -!- MISCELLANEOUS: Present with 1590 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: To yeast YKR010c. {ECO:0000305}.
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DR EMBL; Z49351; CAA89367.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08724.1; -; Genomic_DNA.
DR PIR; S56852; S56852.
DR RefSeq; NP_012459.1; NM_001181509.1.
DR AlphaFoldDB; P47035; -.
DR BioGRID; 33680; 109.
DR ComplexPortal; CPX-1669; RENT complex.
DR DIP; DIP-5153N; -.
DR IntAct; P47035; 101.
DR MINT; P47035; -.
DR STRING; 4932.YJL076W; -.
DR CarbonylDB; P47035; -.
DR iPTMnet; P47035; -.
DR MaxQB; P47035; -.
DR PaxDb; P47035; -.
DR PRIDE; P47035; -.
DR EnsemblFungi; YJL076W_mRNA; YJL076W; YJL076W.
DR GeneID; 853369; -.
DR KEGG; sce:YJL076W; -.
DR SGD; S000003612; NET1.
DR VEuPathDB; FungiDB:YJL076W; -.
DR eggNOG; ENOG502QW4V; Eukaryota.
DR GeneTree; ENSGT00940000176631; -.
DR HOGENOM; CLU_004459_0_0_1; -.
DR InParanoid; P47035; -.
DR OMA; KCEKMYP; -.
DR BioCyc; YEAST:G3O-31533-MON; -.
DR PRO; PR:P47035; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47035; protein.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0030869; C:RENT complex; IDA:SGD.
DR GO; GO:0019211; F:phosphatase activator activity; IBA:GO_Central.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IDA:SGD.
DR GO; GO:0000182; F:rDNA binding; IDA:SGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0001100; P:negative regulation of exit from mitosis; IMP:SGD.
DR GO; GO:0031030; P:negative regulation of septation initiation signaling; IBA:GO_Central.
DR GO; GO:0007000; P:nucleolus organization; IMP:SGD.
DR GO; GO:1904751; P:positive regulation of protein localization to nucleolus; IMP:SGD.
DR GO; GO:0000183; P:rDNA heterochromatin assembly; IMP:SGD.
DR InterPro; IPR018844; Dnt1-like_N.
DR InterPro; IPR043185; Dnt1/Tof2/Net1.
DR PANTHER; PTHR28196; PTHR28196; 1.
DR Pfam; PF10407; Cytokin_check_N; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1189
FT /note="Nucleolar protein NET1"
FT /id="PRO_0000096784"
FT REGION 160..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..1189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..779
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..870
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..935
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..1003
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1039
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1072
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1138..1154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 497
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 676
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 830
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 1042
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1056
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1059
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1189 AA; 128531 MW; 80EDF9A8065EB5A2 CRC64;
MYKLQVVLVP PSLQATMPIQ FGYGPTIAES SQLLPNRTNM AQSAGDASLQ YANLRSANVS
FTPSYFNQSR FRKFLLFTKP TNTLLNLSDE IIDKCEKMYP SLQEDIEILS LQDNSGCDLD
PDFLVKDVFN VNNIVRVILK NEIDLDDSAP VSLYKSVKRS KLNNGSPQSV QPQQQIPSSS
GVLRIAKKRP PTGTTTTTTI RSATNGSMRV STPLARQIYP PPSSKIVSNN SDDEDEDIGE
RSFLPPPTQP QSPPIRISSG IDAGKKIKSS IVEEDIVSRS ATVDPDKTKQ QRLLSGTPIM
STMTPNRVTL TGQRVVSEHA HKNELVFSAS ASSSSFANGG TAAVTAQDIN RKPPVTTPRI
TSGMLKIPEP RISEIEKELK EGPSSPASIL PAKAAKIPMK KPYLENGENY ESDDSSSSEN
QETPETEPHS KASLQRSQSS IADNNGSPVK NSPLGDAMPH NVHLAELPKA SNTSITKSSN
GESWGKQQEH QPPRKSSLET IVEKKSQAEP SGIVEPKRMT NFLDDNQVRE KEDTNDKLLE
KEILPTIPHN DQPILASSDK SNGTLKSLAG KVSSNNNASK EDGTIINGTI EDDGNDNDEV
DTTVRIVPQD SDSSSFPKSD LFKMIEGDDT DLPQWFKGKN SRTSGNSKNS KPYTTVLNKD
IDNSKPDPRN ILPQRTPRSA AKRAAQLLAG AKKNEVPQKS TEDSSSAAST DDESESGIET
DFSSDDDFKR KNMSVPNNGP KDISLHSLKG SVVPVKDSKI INKEVDEERN DKRDSQKKSA
VSESSVTNSK ISEQMAKSFY PNSNKKQNEA TKVETKPATQ ASSFPVVGGS PSVATKGTTS
FNEEGNRKNV KTKAKNESAQ IDRQQKETTS RVADLKSANI GGEDLNKKAE GSKEPEKASA
NIQDANDKNN SKEKEDSKSK QVSQKKLKMT DHLKEGNVQL PKPSANDKLK DLKAKFTNSK
TLVPPGIISN EKNNSSANDD DSSSSGSSTE DESSSSSSSS DEETSTSRKA RRVVVNTPRE
PVRSSSKIEA PSPSVNKKIN ATPDKIPVTQ LMDMSSPPSV KSKTTSNPSS ILHDLPRKVR
PSLSSLSDLV SRGIPDVKEK TSKSNEKSQT KAPSSSDDES SSDSDSNSSS DSVSDSSSDS
KSESDSDDSG DSSDDGKSFI SAKSASAALG KKKKPSGGFA SLIKDFKKK
