NOP15_YEAST
ID NOP15_YEAST Reviewed; 220 AA.
AC P53927; D6W171;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Ribosome biogenesis protein 15;
DE AltName: Full=Nucleolar protein 15 {ECO:0000303|PubMed:11583614};
GN Name=NOP15 {ECO:0000303|PubMed:11583614}; OrderedLocusNames=YNL110C;
GN ORFNames=N1954;
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=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=10953080;
RX DOI=10.1002/1097-0061(20000915)16:12<1089::aid-yea600>3.0.co;2-g;
RA Capozzo C., Sartorello F., Dal Pero F., D'Angelo M., Vezzi A.,
RA Campanaro S., Valle G.;
RT "Gene disruption and basic phenotypic analysis of nine novel yeast genes
RT from chromosome XIV.";
RL Yeast 16:1089-1097(2000).
RN [5]
RP IDENTIFICATION IN THE PRE-66S RIBOSOMAL PARTICLE, FUNCTION, INTERACTION
RP WITH NOP7, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11583614; DOI=10.1016/s1097-2765(01)00344-6;
RA Harnpicharnchai P., Jakovljevic J., Horsey E., Miles T., Roman J., Rout M.,
RA Meagher D., Imai B., Guo Y., Brame C.J., Shabanowitz J., Hunt D.F.,
RA Woolford J.L. Jr.;
RT "Composition and functional characterization of yeast 66S ribosome assembly
RT intermediates.";
RL Mol. Cell 8:505-515(2001).
RN [6]
RP FUNCTION, SUBUNIT, RNA-BINDING, AND DISRUPTION PHENOTYPE.
RX PubMed=14657029; DOI=10.1093/emboj/cdg616;
RA Oeffinger M., Tollervey D.;
RT "Yeast Nop15p is an RNA-binding protein required for pre-rRNA processing
RT and cytokinesis.";
RL EMBO J. 22:6573-6583(2003).
RN [7]
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 [8]
RP INTERACTION WITH RRP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15100437; DOI=10.1261/rna.5255804;
RA Horsey E.W., Jakovljevic J., Miles T.D., Harnpicharnchai P.,
RA Woolford J.L. Jr.;
RT "Role of the yeast Rrp1 protein in the dynamics of pre-ribosome
RT maturation.";
RL RNA 10:813-827(2004).
CC -!- FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit.
CC Required for pre-rRNA processing and cytokinesis. Associates with the
CC precursors of the 25S and 5.8S rRNAs. {ECO:0000269|PubMed:11583614,
CC ECO:0000269|PubMed:14657029}.
CC -!- SUBUNIT: Component of the pre-66S ribosomal particle. Interacts with
CC NOP7 and RRP1. {ECO:0000269|PubMed:11583614,
CC ECO:0000269|PubMed:14657029, ECO:0000269|PubMed:15100437}.
CC -!- INTERACTION:
CC P53927; P38779: CIC1; NbExp=3; IntAct=EBI-28853, EBI-24538;
CC P53927; Q03532: HAS1; NbExp=4; IntAct=EBI-28853, EBI-8170;
CC P53927; P40078: NSA2; NbExp=3; IntAct=EBI-28853, EBI-22681;
CC P53927; P53131: PRP43; NbExp=3; IntAct=EBI-28853, EBI-505;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11583614}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:10953080, ECO:0000269|PubMed:11583614}.
CC -!- DISRUPTION PHENOTYPE: Essential gene. Abrupt growth arrest prior to
CC substantial depletion of ribosomal subunits. Fails to synthesize the
CC 25S and 5.8S rRNA components of the 60S ribosomal subunit, and
CC exonucleolytic 5' processing of 5.8S rRNA is strongly inhibited.
CC Arrests at cytokinesis and fails to assemble a contractile actin ring
CC at the bud neck. {ECO:0000269|PubMed:10953080,
CC ECO:0000269|PubMed:14657029}.
CC -!- MISCELLANEOUS: Present with 4280 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z69382; CAA93397.1; -; Genomic_DNA.
DR EMBL; Z71386; CAA95989.1; -; Genomic_DNA.
DR EMBL; AY693098; AAT93117.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10437.1; -; Genomic_DNA.
DR PIR; S63051; S63051.
DR RefSeq; NP_014289.1; NM_001182948.1.
DR PDB; 3JCT; EM; 3.08 A; o=1-220.
DR PDB; 5T9P; X-ray; 2.00 A; A/B/C/D=81-191.
DR PDB; 5Z3G; EM; 3.65 A; E=1-220.
DR PDB; 6C0F; EM; 3.70 A; o=1-220.
DR PDB; 6CB1; EM; 4.60 A; o=1-220.
DR PDB; 6ELZ; EM; 3.30 A; o=1-220.
DR PDB; 6EM1; EM; 3.60 A; o=1-220.
DR PDB; 6EM3; EM; 3.20 A; o=1-220.
DR PDB; 6EM4; EM; 4.10 A; o=1-220.
DR PDB; 6EM5; EM; 4.30 A; o=1-220.
DR PDB; 6M62; EM; 3.20 A; o=1-220.
DR PDB; 6YLX; EM; 3.90 A; o=1-220.
DR PDB; 6YLY; EM; 3.80 A; o=1-220.
DR PDB; 7BTB; EM; 3.22 A; o=1-220.
DR PDB; 7OHP; EM; 3.90 A; o=1-220.
DR PDB; 7OHQ; EM; 3.10 A; o=1-220.
DR PDB; 7OHR; EM; 4.72 A; o=1-220.
DR PDB; 7OHS; EM; 4.38 A; o=1-220.
DR PDB; 7OHV; EM; 3.90 A; o=1-220.
DR PDB; 7OHW; EM; 3.50 A; o=1-220.
DR PDB; 7OHX; EM; 3.30 A; o=1-220.
DR PDBsum; 3JCT; -.
DR PDBsum; 5T9P; -.
DR PDBsum; 5Z3G; -.
DR PDBsum; 6C0F; -.
DR PDBsum; 6CB1; -.
DR PDBsum; 6ELZ; -.
DR PDBsum; 6EM1; -.
DR PDBsum; 6EM3; -.
DR PDBsum; 6EM4; -.
DR PDBsum; 6EM5; -.
DR PDBsum; 6M62; -.
DR PDBsum; 6YLX; -.
DR PDBsum; 6YLY; -.
DR PDBsum; 7BTB; -.
DR PDBsum; 7OHP; -.
DR PDBsum; 7OHQ; -.
DR PDBsum; 7OHR; -.
DR PDBsum; 7OHS; -.
DR PDBsum; 7OHV; -.
DR PDBsum; 7OHW; -.
DR PDBsum; 7OHX; -.
DR AlphaFoldDB; P53927; -.
DR SASBDB; P53927; -.
DR SMR; P53927; -.
DR BioGRID; 35715; 249.
DR DIP; DIP-4741N; -.
DR IntAct; P53927; 54.
DR MINT; P53927; -.
DR STRING; 4932.YNL110C; -.
DR iPTMnet; P53927; -.
DR MaxQB; P53927; -.
DR PaxDb; P53927; -.
DR PRIDE; P53927; -.
DR EnsemblFungi; YNL110C_mRNA; YNL110C; YNL110C.
DR GeneID; 855613; -.
DR KEGG; sce:YNL110C; -.
DR SGD; S000005054; NOP15.
DR VEuPathDB; FungiDB:YNL110C; -.
DR eggNOG; KOG4208; Eukaryota.
DR GeneTree; ENSGT00940000172371; -.
DR HOGENOM; CLU_025741_2_0_1; -.
DR InParanoid; P53927; -.
DR OMA; KVIPWKK; -.
DR BioCyc; YEAST:G3O-33134-MON; -.
DR PRO; PR:P53927; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53927; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IDA:GO_Central.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:GO_Central.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:SGD.
DR CDD; cd12552; RRM_Nop15p; 1.
DR DisProt; DP02808; -.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR034469; Nop15_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Nucleus; Reference proteome; Ribonucleoprotein;
KW Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..220
FT /note="Ribosome biogenesis protein 15"
FT /id="PRO_0000082035"
FT DOMAIN 91..169
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..55
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 89..96
FT /evidence="ECO:0007829|PDB:5T9P"
FT HELIX 104..111
FT /evidence="ECO:0007829|PDB:5T9P"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:5T9P"
FT STRAND 117..124
FT /evidence="ECO:0007829|PDB:5T9P"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:5T9P"
FT STRAND 131..141
FT /evidence="ECO:0007829|PDB:5T9P"
FT HELIX 142..152
FT /evidence="ECO:0007829|PDB:5T9P"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:5T9P"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:5T9P"
FT HELIX 181..186
FT /evidence="ECO:0007829|PDB:5T9P"
FT TURN 187..190
FT /evidence="ECO:0007829|PDB:5T9P"
FT HELIX 195..207
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 209..213
FT /evidence="ECO:0007829|PDB:6EM3"
SQ SEQUENCE 220 AA; 25447 MW; EC86E3C77C863292 CRC64;
MVKSTSKTST KETVTKQPTE EKPIQEKEEL ALETSSSSSD EEDEKDEDEI EGLAASDDEQ
SGTHKIKRLN PKKQANEKKS KDKKTLEEYS GIIYVSRLPH GFHEKELSKY FAQFGDLKEV
RLARNKKTGN SRHYGFLEFV NKEDAMIAQE SMNNYLLMGH LLQVRVLPKG AKIEKLYKYK
KRVLVEKGIT KPVKQLKDNM KQKHEERIKK LAKSGIEFKW
