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UniProtKB/Swiss-Prot entry Q01560


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NOP3_YEAST
Primary accession number Q01560
Secondary accession numbers None
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on July 1, 1993 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 86)
Name and origin of the protein
Protein name Nucleolar protein 3
Synonyms Mitochondrial targeting suppressor 1 protein
Nuclear polyadenylated RNA-binding protein 1
Gene name
Name: NOP3
Synonyms: MTS1, NAB1, NPL3
OrderedLocusNames: YDR432W
ORFNames: D9461.19
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1083/jcb.119.4.737; PubMed=1429834 [NCBI, ExPASy, EBI, Israel, Japan]
Russell I.D., Tollervey D.;
"NOP3 is an essential yeast protein which is required for pre-rRNA processing.";
J. Cell Biol. 119:737-747(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1392078 [NCBI, ExPASy, EBI, Israel, Japan]
Bossie M.A., Dehoratious C., Barcelo G., Silver P.;
"A mutant nuclear protein with similarity to RNA binding proteins interferes with nuclear import in yeast.";
Mol. Biol. Cell 3:875-893(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0378-1119(93)90193-7; PubMed=8224861 [NCBI, ExPASy, EBI, Israel, Japan]
Ellis E.M., Reid G.A.;
"The Saccharomyces cerevisiae MTS1 gene encodes a putative RNA-binding protein involved in mitochondrial protein targeting.";
Gene 132:175-183(1993).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867 [NCBI, ExPASy, EBI, Israel, Japan]
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[5]
SUBCELLULAR LOCATION, AND BINDING TO POLYADENYLATED RNA.
DOI=10.1083/jcb.127.5.1173; PubMed=7962083 [NCBI, ExPASy, EBI, Israel, Japan]
Wilson S.M., Datar K.V., Paddy M.R., Swedlow J.R., Swanson M.S.;
"Characterization of nuclear polyadenylated RNA-binding proteins in Saccharomyces cerevisiae.";
J. Cell Biol. 127:1173-1184(1994).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, AND MASS SPECTROMETRY.
DOI=10.1038/nbt0302-301; PubMed=11875433 [NCBI, ExPASy, EBI, Israel, Japan]
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M.;
"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae.";
Nat. Biotechnol. 20:301-305(2002).
[7]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M400219-MCP200; PubMed=15665377 [NCBI, ExPASy, EBI, Israel, Japan]
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, AND MASS SPECTROMETRY.
DOI=10.1021/pr060559j; PubMed=17330950 [NCBI, ExPASy, EBI, Israel, Japan]
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224 AND THR-227, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0701622104; PubMed=17563356 [NCBI, ExPASy, EBI, Israel, Japan]
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.";
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182; SER-224 AND THR-228, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X66019; CAA46817.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M86731; AAA34818.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X70951; CAA50291.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U33007; AAB64865.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JN0866; JN0866.
RefSeq NP_010720.1; -.
3D structure databases
PDB
2JVR; NMR; -; A=193-282.[ExPASy / RCSB / EBI]
2OSQ; NMR; -; A=121-194.[ExPASy / RCSB / EBI]
2OSR; NMR; -; A=194-280.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2JVR; -.
2OSQ; -.
2OSR; -.
ModBase Q01560.
Protein-protein interaction databases
DIP DIP:6464N; -.
IntAct Q01560; -.
Organism-specific databases
CYGD YDR432w; -.
SGD S000002840; NPL3.
Yeast-GFP YDR432W.
Gene expression databases
GermOnline YDR432W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from mutant phenotype from SGD).
GO:0005634; Cellular component: nucleus (inferred from direct assay from SGD).
GO:0008143; Molecular function: poly(A) binding (inferred from direct assay from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006406; Biological process: mRNA export from nucleus (inferred from genetic interaction from SGD).
GO:0007124; Biological process: pseudohyphal growth (inferred from mutant phenotype from SGD).
QuickGo view.
Family and domain databases
InterPro IPR000504; RRM_RNP1.
Graphical view of domain structure.
Pfam PF00076; RRM_1; 2.
Pfam graphical view of domain structure.
SMART SM00360; RRM; 2.
SMART graphical view of domain structure.
PROSITE PS50102; RRM; 2.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q01560.
Proteomic databases
PeptideAtlas Q01560; -.
Genome annotation databases
Ensembl YDR432W; Saccharomyces cerevisiae. [Contig view]
GeneID 852042; -.
GenomeReviews Z71256_GR; YDR432W.
KEGG sce:YDR432W; -.
NMPDR fig|4932.3.peg.1493; -.
Phylogenomic databases
HOGENOM Q01560; -.
Other
LinkHub Q01560; -.
ProtoNet Q01560.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Nucleus; Phosphoprotein; Repeat; Ribonucleoprotein; Ribosome biogenesis; RNA-binding; rRNA processing.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   414  414     Nucleolar protein 3. PRO_0000081676
DOMAIN   125   195  71     RRM 1. 
DOMAIN   200   275  76     RRM 2. 
COMPBIAS   280   398  119     Arg/Gly-rich. 
MOD_RES   182   182        Phosphoserine. 
MOD_RES   224   224        Phosphoserine. 
MOD_RES   227   227        Phosphothreonine. 
MOD_RES   228   228        Phosphothreonine. 
MOD_RES   356   356        Phosphoserine. 
Sequence information
Length: 414 AA [This is the length of the unprocessed precursor] Molecular weight: 45407 Da [This is the MW of the unprocessed precursor] CRC64: 024439E4B6578787 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSEAQETHVE QLPESVVDAP VEEQHQEPPQ APDAPQEPQV PQESAPQESA PQEPPAPQEQ 

        70         80         90        100        110        120 
NDVPPPSNAP IYEGEESHSV QDYQEAHQHH QPPEPQPYYP PPPPGEHMHG RPPMHHRQEG 

       130        140        150        160        170        180 
ELSNTRLFVR PFPLDVQESE LNEIFGPFGP MKEVKILNGF AFVEFEEAES AAKAIEEVHG 

       190        200        210        220        230        240 
KSFANQPLEV VYSKLPAKRY RITMKNLPEG CSWQDLKDLA RENSLETTFS SVNTRDFDGT 

       250        260        270        280        290        300 
GALEFPSEEI LVEALERLNN IEFRGSVITV ERDDNPPPIR RSNRGGFRGR GGFRGGFRGG 

       310        320        330        340        350        360 
FRGGFSRGGF GGPRGGFGGP RGGYGGYSRG GYGGYSRGGY GGSRGGYDSP RGGYDSPRGG 

       370        380        390        400        410 
YSRGGYGGPR NDYGPPRGSY GGSRGGYDGP RGDYGPPRDA YRTRDAPRER SPTR 

Q01560 in FASTA format

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