NOL10_YEAST
ID NOL10_YEAST Reviewed; 707 AA.
AC P48234; D6VUS5;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Ribosome biogenesis protein ENP2;
DE AltName: Full=Essential nuclear protein 2;
GN Name=ENP2; OrderedLocusNames=YGR145W; ORFNames=G6623;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8585325; DOI=10.1002/yea.320111410;
RA Skala J., Nawrocki A., Goffeau A.;
RT "The sequence of a 27 kb segment on the right arm of chromosome VII from
RT Saccharomyces cerevisiae reveals MOL1, NAT2, RPL30B, RSR1, CYS4, PEM1/CHO2,
RT NSR1 genes and ten new open reading frames.";
RL Yeast 11:1421-1427(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 678.
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 [4]
RP IDENTIFICATION IN THE 90S PRE-RIBOSOME, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=12150911; DOI=10.1016/s1097-2765(02)00579-8;
RA Grandi P., Rybin V., Bassler J., Petfalski E., Strauss D., Marzioch M.,
RA Schaefer T., Kuster B., Tschochner H., Tollervey D., Gavin A.-C., Hurt E.;
RT "90S pre-ribosomes include the 35S pre-rRNA, the U3 snoRNP, and 40S subunit
RT processing factors but predominantly lack 60S synthesis factors.";
RL Mol. Cell 10:105-115(2002).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
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.
RX PubMed=15590835; DOI=10.1128/ec.3.6.1619-1626.2004;
RA Bernstein K.A., Gallagher J.E.G., Mitchell B.M., Granneman S.,
RA Baserga S.J.;
RT "The small-subunit processome is a ribosome assembly intermediate.";
RL Eukaryot. Cell 3:1619-1626(2004).
RN [7]
RP ASSOCIATION WITH THE 90S PRE-RIBOSOME, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16429126; DOI=10.1038/nature04532;
RA Gavin A.-C., Aloy P., Grandi P., Krause R., Boesche M., Marzioch M.,
RA Rau C., Jensen L.J., Bastuck S., Duempelfeld B., Edelmann A.,
RA Heurtier M.-A., Hoffman V., Hoefert C., Klein K., Hudak M., Michon A.-M.,
RA Schelder M., Schirle M., Remor M., Rudi T., Hooper S., Bauer A.,
RA Bouwmeester T., Casari G., Drewes G., Neubauer G., Rick J.M., Kuster B.,
RA Bork P., Russell R.B., Superti-Furga G.;
RT "Proteome survey reveals modularity of the yeast cell machinery.";
RL Nature 440:631-636(2006).
RN [8]
RP FUNCTION.
RX PubMed=16544271; DOI=10.1002/yea.1353;
RA Wade C.H., Umbarger M.A., McAlear M.A.;
RT "The budding yeast rRNA and ribosome biosynthesis (RRB) regulon contains
RT over 200 genes.";
RL Yeast 23:293-306(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529; SER-550 AND SER-555, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529, AND IDENTIFICATION BY
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529; SER-550 AND SER-555, AND
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529; SER-550 AND SER-555, AND
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: May be involved in rRNA-processing and ribosome biosynthesis.
CC {ECO:0000269|PubMed:16544271}.
CC -!- SUBUNIT: Component of the 90S pre-ribosomes.
CC {ECO:0000269|PubMed:12150911}.
CC -!- INTERACTION:
CC P48234; Q06631: BFR2; NbExp=13; IntAct=EBI-23354, EBI-36432;
CC P48234; P20448: HCA4; NbExp=3; IntAct=EBI-23354, EBI-5612;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14690591,
CC ECO:0000269|PubMed:15590835}.
CC -!- SIMILARITY: Belongs to the WD repeat NOL10/ENP2 family. {ECO:0000305}.
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DR EMBL; X85807; CAA59803.1; -; Genomic_DNA.
DR EMBL; Z72930; CAA97158.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08236.2; -; Genomic_DNA.
DR PIR; S60436; S60436.
DR RefSeq; NP_011661.2; NM_001181274.2.
DR PDB; 5WLC; EM; 3.80 A; LV=1-707.
DR PDB; 6KE6; EM; 3.40 A; RA=1-707.
DR PDB; 6LQP; EM; 3.20 A; RA=1-707.
DR PDB; 6LQQ; EM; 4.10 A; RA=1-707.
DR PDB; 6LQR; EM; 8.60 A; RA=1-707.
DR PDB; 6LQU; EM; 3.70 A; RA=1-707.
DR PDB; 6LQV; EM; 4.80 A; RA=1-707.
DR PDB; 6ZQB; EM; 3.90 A; JC=1-707.
DR PDB; 6ZQC; EM; 3.80 A; JC=1-707.
DR PDB; 7AJT; EM; 4.60 A; JC=1-707.
DR PDB; 7D63; EM; 12.30 A; RA=1-707.
DR PDBsum; 5WLC; -.
DR PDBsum; 6KE6; -.
DR PDBsum; 6LQP; -.
DR PDBsum; 6LQQ; -.
DR PDBsum; 6LQR; -.
DR PDBsum; 6LQU; -.
DR PDBsum; 6LQV; -.
DR PDBsum; 6ZQB; -.
DR PDBsum; 6ZQC; -.
DR PDBsum; 7AJT; -.
DR PDBsum; 7D63; -.
DR AlphaFoldDB; P48234; -.
DR SMR; P48234; -.
DR BioGRID; 33393; 114.
DR DIP; DIP-5535N; -.
DR IntAct; P48234; 17.
DR MINT; P48234; -.
DR STRING; 4932.YGR145W; -.
DR iPTMnet; P48234; -.
DR MaxQB; P48234; -.
DR PaxDb; P48234; -.
DR PRIDE; P48234; -.
DR EnsemblFungi; YGR145W_mRNA; YGR145W; YGR145W.
DR GeneID; 853048; -.
DR KEGG; sce:YGR145W; -.
DR SGD; S000003377; ENP2.
DR VEuPathDB; FungiDB:YGR145W; -.
DR eggNOG; KOG2321; Eukaryota.
DR GeneTree; ENSGT00390000007900; -.
DR HOGENOM; CLU_009923_0_0_1; -.
DR InParanoid; P48234; -.
DR OMA; GEWVMST; -.
DR BioCyc; YEAST:G3O-30849-MON; -.
DR PRO; PR:P48234; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P48234; protein.
DR GO; GO:0030686; C:90S preribosome; HDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0032040; C:small-subunit processome; IMP:SGD.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:SGD.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR040382; NOL10/Enp2.
DR InterPro; IPR012580; NUC153.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR14927; PTHR14927; 1.
DR Pfam; PF08159; NUC153; 1.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ribosome biogenesis; rRNA processing; WD repeat.
FT CHAIN 1..707
FT /note="Ribosome biogenesis protein ENP2"
FT /id="PRO_0000051473"
FT REPEAT 54..94
FT /note="WD 1"
FT REPEAT 178..217
FT /note="WD 2"
FT REPEAT 226..265
FT /note="WD 3"
FT REPEAT 269..310
FT /note="WD 4"
FT REPEAT 312..351
FT /note="WD 5"
FT REGION 523..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..643
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..701
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 550
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT CONFLICT 678
FT /note="D -> E (in Ref. 1; CAA59803 and 2; CAA97158)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 707 AA; 81734 MW; 6C3DFB372C058A04 CRC64;
MVLKSTSAND VSVYQVSGTN VSRSLPDWIA KKRKRQLKND LEYQNRVELI QDFEFSEASN
KIKVSRDGQY CMATGTYKPQ IHVYDFANLS LKFDRHTDAE NVDFTILSDD WTKSVHLQND
RSIQFQNKGG LHYTTRIPKF GRSLVYNKVN CDLYVGASGN ELYRLNLEKG RFLNPFKLDT
EGVNHVSINE VNGLLAAGTE TNVVEFWDPR SRSRVSKLYL ENNIDNRPFQ VTTTSFRNDG
LTFACGTSNG YSYIYDLRTS EPSIIKDQGY GFDIKKIIWL DNVGTENKIV TCDKRIAKIW
DRLDGKAYAS MEPSVDINDI EHVPGTGMFF TANESIPMHT YYIPSLGPSP RWCSFLDSIT
EELEEKPSDT VYSNYRFITR DDVKKLNLTH LVGSRVLRAY MHGFFINTEL YDKVSLIANP
DAYKDERERE IRRRIEKERE SRIRSSGAVQ KPKIKVNKTL VDKLSQKRGD KVAGKVLTDD
RFKEMFEDEE FQVDEDDYDF KQLNPVKSIK ETEEGAAKRI RALTAAEESD EERIAMKDGR
GHYDYEDEES DEEESDDETN QKSNKEELSE KDLRKMEKQK ALIERRKKEK EQSERFMNEM
KAGTSTSTQR DESAHVTFGE QVGELLEVEN GKKSNESILR RNQRGEAELT FIPQRKSKKD
GNYKSRRHDN SSDEEGIDEN GNKKDNGRSK PRFENRRRAS KNAFRGM
