NOP58_YEAST
ID NOP58_YEAST Reviewed; 511 AA.
AC Q12499; D6W309;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Nucleolar protein 58;
DE AltName: Full=Nucleolar protein 5;
GN Name=NOP58; Synonyms=NOP5; OrderedLocusNames=YOR310C; ORFNames=O6108;
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 96604 / S288c / FY1679;
RX PubMed=8896266;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1021::aid-yea981>3.0.co;2-7;
RA Pearson B.M., Hernando Y., Payne J., Wolf S.S., Kalogeropoulos A.,
RA Schweizer M.;
RT "Sequencing of a 35.71 kb DNA segment on the right arm of yeast chromosome
RT XV reveals regions of similarity to chromosomes I and XIII.";
RL Yeast 12:1021-1031(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 200060 / W303;
RX PubMed=9632712; DOI=10.1074/jbc.273.26.16453;
RA Wu P., Brockenbrough J.S., Metcalfe A.C., Chen S., Aris J.P.;
RT "Nop5p is a small nucleolar ribonucleoprotein component required for pre-
RT 18S rRNA processing in yeast.";
RL J. Biol. Chem. 273:16453-16463(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 FUNCTION, AND INTERACTION WITH NOP1 AND SIK1.
RX PubMed=9372940; DOI=10.1128/mcb.17.12.7088;
RA Gautier T., Berges T., Tollervey D., Hurt E.;
RT "Nucleolar KKE/D repeat proteins Nop56p and Nop58p interact with Nop1p and
RT are required for ribosome biogenesis.";
RL Mol. Cell. Biol. 17:7088-7098(1997).
RN [6]
RP INTERACTION WITH TGS1.
RX PubMed=11983179; DOI=10.1016/s1097-2765(02)00484-7;
RA Mouaikel J., Verheggen C., Bertrand E., Tazi J., Bordonne R.;
RT "Hypermethylation of the cap structure of both yeast snRNAs and snoRNAs
RT requires a conserved methyltransferase that is localized to the
RT nucleolus.";
RL Mol. Cell 9:891-901(2002).
RN [7]
RP IDENTIFICATION IN SSU PROCESSOME BY MASS SPECTROMETRY.
RX PubMed=12068309; DOI=10.1038/nature00769;
RA Dragon F., Gallagher J.E.G., Compagnone-Post P.A., Mitchell B.M.,
RA Porwancher K.A., Wehner K.A., Wormsley S., Settlage R.E., Shabanowitz J.,
RA Osheim Y., Beyer A.L., Hunt D.F., Baserga S.J.;
RT "A large nucleolar U3 ribonucleoprotein required for 18S ribosomal RNA
RT biogenesis.";
RL Nature 417:967-970(2002).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY.
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 [9]
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 [10]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-281, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Required for pre-18S rRNA processing. May bind microtubules.
CC {ECO:0000269|PubMed:9372940, ECO:0000269|PubMed:9632712}.
CC -!- SUBUNIT: Interacts with SIK1/NOP56 and NOP1. Interacts with the
CC trimethylguanosine synthase TGS1. Component of the ribosomal small
CC subunit (SSU) processome composed of at least 40 protein subunits and
CC snoRNA U3. {ECO:0000269|PubMed:11983179, ECO:0000269|PubMed:12068309,
CC ECO:0000269|PubMed:9372940}.
CC -!- INTERACTION:
CC Q12499; P15646: NOP1; NbExp=4; IntAct=EBI-12126, EBI-6838;
CC Q12499; Q05022: RRP5; NbExp=4; IntAct=EBI-12126, EBI-16011;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:9632712}.
CC -!- MISCELLANEOUS: Present with 34700 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NOP5/NOP56 family. {ECO:0000305}.
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DR EMBL; AF056070; AAC39484.1; -; Genomic_DNA.
DR EMBL; X90565; CAA62165.1; -; Genomic_DNA.
DR EMBL; Z75217; CAA99630.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11075.1; -; Genomic_DNA.
DR PIR; S58322; S58322.
DR RefSeq; NP_014955.1; NM_001183730.1.
DR PDB; 5WLC; EM; 3.80 A; SB=133-511.
DR PDB; 5WYJ; EM; 8.70 A; 3E=1-511.
DR PDB; 5WYK; EM; 4.50 A; 3E=1-511.
DR PDB; 6KE6; EM; 3.40 A; 3E=1-511.
DR PDB; 6LQP; EM; 3.20 A; 3E=1-511.
DR PDB; 6LQQ; EM; 4.10 A; 3E=1-511.
DR PDB; 6LQR; EM; 8.60 A; 3E=1-511.
DR PDB; 6LQS; EM; 3.80 A; 3E=1-511.
DR PDB; 6LQT; EM; 4.90 A; 3E=1-511.
DR PDB; 6LQU; EM; 3.70 A; 3E=1-511.
DR PDB; 6LQV; EM; 4.80 A; 3E=1-511.
DR PDB; 6ND4; EM; 4.30 A; b=133-511.
DR PDB; 6ZQA; EM; 4.40 A; CE=1-511.
DR PDB; 6ZQB; EM; 3.90 A; CE=1-511.
DR PDB; 6ZQC; EM; 3.80 A; CE=1-511.
DR PDB; 6ZQD; EM; 3.80 A; CE=1-511.
DR PDB; 6ZQE; EM; 7.10 A; CE=1-511.
DR PDB; 7AJT; EM; 4.60 A; CE=1-511.
DR PDB; 7AJU; EM; 3.80 A; CE=1-511.
DR PDB; 7D4I; EM; 4.00 A; 3E=1-511.
DR PDB; 7D5S; EM; 4.60 A; 3E=1-511.
DR PDB; 7D5T; EM; 6.00 A; 3E=1-511.
DR PDB; 7D63; EM; 12.30 A; 3E=1-511.
DR PDBsum; 5WLC; -.
DR PDBsum; 5WYJ; -.
DR PDBsum; 5WYK; -.
DR PDBsum; 6KE6; -.
DR PDBsum; 6LQP; -.
DR PDBsum; 6LQQ; -.
DR PDBsum; 6LQR; -.
DR PDBsum; 6LQS; -.
DR PDBsum; 6LQT; -.
DR PDBsum; 6LQU; -.
DR PDBsum; 6LQV; -.
DR PDBsum; 6ND4; -.
DR PDBsum; 6ZQA; -.
DR PDBsum; 6ZQB; -.
DR PDBsum; 6ZQC; -.
DR PDBsum; 6ZQD; -.
DR PDBsum; 6ZQE; -.
DR PDBsum; 7AJT; -.
DR PDBsum; 7AJU; -.
DR PDBsum; 7D4I; -.
DR PDBsum; 7D5S; -.
DR PDBsum; 7D5T; -.
DR PDBsum; 7D63; -.
DR AlphaFoldDB; Q12499; -.
DR SMR; Q12499; -.
DR BioGRID; 34698; 327.
DR ComplexPortal; CPX-1604; Small ribosomal subunit processome, variant 1.
DR ComplexPortal; CPX-1607; Small ribosomal subunit processome, variant 2.
DR ComplexPortal; CPX-1608; Small ribosomal subunit processome, variant 3.
DR ComplexPortal; CPX-729; Box C/D snoRNP complex.
DR DIP; DIP-5843N; -.
DR IntAct; Q12499; 87.
DR MINT; Q12499; -.
DR STRING; 4932.YOR310C; -.
DR iPTMnet; Q12499; -.
DR MaxQB; Q12499; -.
DR PaxDb; Q12499; -.
DR PRIDE; Q12499; -.
DR EnsemblFungi; YOR310C_mRNA; YOR310C; YOR310C.
DR GeneID; 854487; -.
DR KEGG; sce:YOR310C; -.
DR SGD; S000005837; NOP58.
DR VEuPathDB; FungiDB:YOR310C; -.
DR eggNOG; KOG2572; Eukaryota.
DR GeneTree; ENSGT00940000153534; -.
DR HOGENOM; CLU_015495_5_2_1; -.
DR InParanoid; Q12499; -.
DR OMA; MGMRSNW; -.
DR BioCyc; YEAST:G3O-33793-MON; -.
DR Reactome; R-SCE-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:Q12499; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12499; protein.
DR GO; GO:0030686; C:90S preribosome; HDA:SGD.
DR GO; GO:0031428; C:box C/D RNP complex; IDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0032040; C:small-subunit processome; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0030515; F:snoRNA binding; IBA:GO_Central.
DR GO; GO:0017069; F:snRNA binding; IDA:UniProtKB.
DR GO; GO:0000494; P:box C/D RNA 3'-end processing; IDA:ComplexPortal.
DR GO; GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IC:ComplexPortal.
DR GO; GO:1902570; P:protein localization to nucleolus; IMP:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IDA:UniProtKB.
DR GO; GO:0000452; P:snoRNA guided rRNA 2'-O-methylation; IDA:ComplexPortal.
DR Gene3D; 1.10.246.90; -; 1.
DR InterPro; IPR045056; Nop56/Nop58.
DR InterPro; IPR012974; NOP5_N.
DR InterPro; IPR042239; Nop_C.
DR InterPro; IPR002687; Nop_dom.
DR InterPro; IPR036070; Nop_dom_sf.
DR InterPro; IPR012976; NOSIC.
DR PANTHER; PTHR10894; PTHR10894; 1.
DR Pfam; PF01798; Nop; 1.
DR Pfam; PF08156; NOP5NT; 1.
DR SMART; SM00931; NOSIC; 1.
DR SUPFAM; SSF89124; SSF89124; 1.
DR PROSITE; PS51358; NOP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Isopeptide bond; Nucleus; Reference proteome;
KW Ribonucleoprotein; Ribosome biogenesis; rRNA processing; Ubl conjugation.
FT CHAIN 1..511
FT /note="Nucleolar protein 58"
FT /id="PRO_0000219029"
FT DOMAIN 283..403
FT /note="Nop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00690"
FT REGION 423..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 435..511
FT /evidence="ECO:0000255"
FT COMPBIAS 448..495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..511
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 281
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
SQ SEQUENCE 511 AA; 56956 MW; 8A2889448B2A19E2 CRC64;
MAYVLTETSA GYALLKASDK KIYKSSSLIQ DLDSSDKVLK EFKIAAFSKF NSAANALEEA
NSIIEGKVSS QLEKLLEEIK KDKKSTLIVS ETKLANAINK LGLNFNVVSD AVTLDIYRAI
KEYLPELLPG MSDNDLSKMS LGLAHSIGRH KLKFSADKVD VMIIQAIALL DDLDKELNTY
AMRCKEWYGW HFPELAKIVT DSVAYARIIL TMGIRSKASE TDLSEILPEE IEERVKTAAE
VSMGTEITQT DLDNINALAE QIVEFAAYRE QLSNYLSARM KAIAPNLTQL VGELVGARLI
AHSGSLISLA KSPASTIQIL GAEKALFRAL KTKHDTPKYG LLYHASLVGQ ATGKNKGKIA
RVLAAKAAVS LRYDALAEDR DDSGDIGLES RAKVENRLSQ LEGRDLRTTP KVVREAKKVE
MTEARAYNAD ADTAKAASDS ESDSDDEEEE KKEKKEKKRK RDDDEDSKDS KKAKKEKKDK
KEKKEKKEKK EKKEKKEKKE KKSKKEKKEK K
