NOP19_YEAST
ID NOP19_YEAST Reviewed; 196 AA.
AC P53317; D6VV31;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Nucleolar protein 19;
GN Name=NOP19; OrderedLocusNames=YGR251W;
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=9133742;
RX DOI=10.1002/(sici)1097-0061(19970330)13:4<373::aid-yea82>3.0.co;2-v;
RA Feroli F., Carignani G., Pavanello A., Guerreiro P., Azevedo D.,
RA Rodrigues-Pousada C., Melchioretto P., Panzeri L., Agostoni Carbone M.L.;
RT "Analysis of a 17.9 kb region from Saccharomyces cerevisiae chromosome VII
RT reveals the presence of eight open reading frames, including BRF1
RT (TFIIIB70) and GCN5 genes.";
RL Yeast 13:373-377(1997).
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.
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 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 [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 FUNCTION.
RX PubMed=12837249; DOI=10.1016/s0092-8674(03)00466-5;
RA Peng W.-T., Robinson M.D., Mnaimneh S., Krogan N.J., Cagney G.,
RA Morris Q.D., Davierwala A.P., Grigull J., Yang X., Zhang W., Mitsakakis N.,
RA Ryan O.W., Datta N., Jojic V., Pal C., Canadien V., Richards D.P.,
RA Beattie B., Wu L.F., Altschuler S.J., Roweis S., Frey B.J., Emili A.,
RA Greenblatt J.F., Hughes T.R.;
RT "A panoramic view of yeast noncoding RNA processing.";
RL Cell 113:919-933(2003).
RN [7]
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 [8]
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).
RN [9]
RP SUBCELLULAR LOCATION, FUNCTION, ASSOCIATION WITH THE 90S PRE-RIBOSOME, AND
RP INTERACTION WITH DHR2 AND UTP25.
RX PubMed=21941128; DOI=10.4161/rna.8.6.17699;
RA Choque E., Marcellin M., Burlet-Schiltz O., Gadal O., Dez C.;
RT "The nucleolar protein Nop19p interacts preferentially with Utp25p and
RT Dhr2p and is essential for the production of the 40S ribosomal subunit in
RT Saccharomyces cerevisiae.";
RL RNA Biol. 8:1158-1172(2011).
CC -!- FUNCTION: Ribosome biogenesis factor required for cleavage of pre-rRNA
CC at A0, A1 and A2 sites. Essential for the incorporation of UTP25 in
CC pre-ribosomes. {ECO:0000269|PubMed:12837249,
CC ECO:0000269|PubMed:21941128}.
CC -!- SUBUNIT: Associates with the 90S pre-ribosome. Interacts with RNA
CC helicase DHR2 and RNA helicase-like protein UTP25.
CC {ECO:0000269|PubMed:21941128}.
CC -!- INTERACTION:
CC P53317; P36009: DHR2; NbExp=3; IntAct=EBI-23590, EBI-5844;
CC P53317; Q12136: SAS10; NbExp=3; IntAct=EBI-23590, EBI-36084;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:21941128}.
CC -!- MISCELLANEOUS: Present with 1460 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z73036; CAA97280.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08342.1; -; Genomic_DNA.
DR PIR; S64583; S64583.
DR RefSeq; NP_011767.3; NM_001181380.3.
DR AlphaFoldDB; P53317; -.
DR BioGRID; 33502; 323.
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 DIP; DIP-5523N; -.
DR IntAct; P53317; 12.
DR MINT; P53317; -.
DR STRING; 4932.YGR251W; -.
DR iPTMnet; P53317; -.
DR MaxQB; P53317; -.
DR PaxDb; P53317; -.
DR PRIDE; P53317; -.
DR EnsemblFungi; YGR251W_mRNA; YGR251W; YGR251W.
DR GeneID; 853166; -.
DR KEGG; sce:YGR251W; -.
DR SGD; S000003483; NOP19.
DR VEuPathDB; FungiDB:YGR251W; -.
DR eggNOG; ENOG502S1GY; Eukaryota.
DR HOGENOM; CLU_094334_0_0_1; -.
DR InParanoid; P53317; -.
DR OMA; RNNMYRI; -.
DR BioCyc; YEAST:G3O-30924-MON; -.
DR PRO; PR:P53317; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53317; protein.
DR GO; GO:0030686; C:90S preribosome; IDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0032040; C:small-subunit processome; IPI: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:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR InterPro; IPR022592; Nucleolar_19.
DR Pfam; PF10863; NOP19; 1.
PE 1: Evidence at protein level;
KW Nucleus; Reference proteome; Ribonucleoprotein; Ribosome biogenesis.
FT CHAIN 1..196
FT /note="Nucleolar protein 19"
FT /id="PRO_0000202860"
FT REGION 101..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 196 AA; 22320 MW; 9D106ADCA2BF018E CRC64;
MSRAKELQEK LNLQAKLQST FSNNTAAVLD WLKESDETGI SNDTERNKQL KDHKELEDGK
KAFFKLPVLQ IGSGLHFRTQ DDASAKEDIH TIGEFIEGDK KVSSLAKKKK RSDPGLQRNN
MYRITKDDTK AMIALKRKMR KGEKEGLRKK QEHSKSSVSN SYSASDEEDE DAGTMPQKST
KKKFGLLFDK KKKARK
