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Q01560 (NOP3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nucleolar protein 3
Alternative name(s):
Mitochondrial targeting suppressor 1 protein
Nuclear polyadenylated RNA-binding protein 1
Gene names
Name:NPL3
Synonyms:MTR13, MTS1, NAB1, NOP3
Ordered Locus Names:YDR432W
ORF Names:D9461.19
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length414 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for pre-rRNA processing and nuclear import as well as mitochondrial protein targeting. Binds to poly(A).

Subunit structure

Interacts with RRP6. Ref.7

Subcellular location

Nucleusnucleolus Ref.6 Ref.8.

Miscellaneous

Present with 78700 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the RRM GAR family.

Contains 2 RRM (RNA recognition motif) domains.

Ontologies

Keywords
   Biological processRibosome biogenesis
rRNA processing
   Cellular componentNucleus
   DomainRepeat
   LigandRNA-binding
   Molecular functionRibonucleoprotein
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmRNA export from nucleus

Inferred from genetic interaction PubMed 11459827. Source: SGD

mRNA splicing, via spliceosome

Inferred from mutant phenotype PubMed 19061647. Source: SGD

negative regulation of termination of RNA polymerase II transcription, poly(A)-coupled

Inferred from direct assay PubMed 15902270. Source: SGD

negative regulation of translation

Inferred from direct assay PubMed 22284680. Source: SGD

positive regulation of transcription elongation from RNA polymerase II promoter

Inferred from direct assay PubMed 18818768. Source: SGD

rRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

translational termination

Inferred from mutant phenotype PubMed 19733178. Source: SGD

   Cellular_componentcytoplasm

Inferred from mutant phenotype PubMed 8675010. Source: SGD

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 15572678Ref.6. Source: SGD

ribonucleoprotein complex

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionRNA polymerase II core binding

Inferred from physical interaction PubMed 18818768. Source: SGD

eukaryotic initiation factor 4G binding

Inferred from direct assay PubMed 22284680. Source: SGD

identical protein binding

Inferred from physical interaction PubMed 23348965. Source: IntAct

mRNA binding

Inferred from direct assay PubMed 17684230PubMed 7774613. Source: SGD

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) binding

Inferred from direct assay Ref.6. Source: SGD

protein binding

Inferred from physical interaction PubMed 10896665PubMed 16606443PubMed 21852791PubMed 22997150PubMed 23706744. Source: IntAct

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 414414Nucleolar protein 3
PRO_0000081676

Regions

Domain125 – 19571RRM 1
Domain200 – 27576RRM 2
Compositional bias280 – 398119Arg/Gly-rich

Amino acid modifications

Modified residue1821Phosphoserine Ref.11
Modified residue2241Phosphoserine Ref.10 Ref.11 Ref.12

Secondary structure

............................. 414
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q01560 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 024439E4B6578787

FASTA41445,407
        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 

« Hide

References

« Hide 'large scale' references
[1]"NOP3 is an essential yeast protein which is required for pre-rRNA processing."
Russell I.D., Tollervey D.
J. Cell Biol. 119:737-747(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"A mutant nuclear protein with similarity to RNA binding proteins interferes with nuclear import in yeast."
Bossie M.A., Dehoratious C., Barcelo G., Silver P.
Mol. Biol. Cell 3:875-893(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The Saccharomyces cerevisiae MTS1 gene encodes a putative RNA-binding protein involved in mitochondrial protein targeting."
Ellis E.M., Reid G.A.
Gene 132:175-183(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
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. expand/collapse author list , 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.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[6]"Characterization of nuclear polyadenylated RNA-binding proteins in Saccharomyces cerevisiae."
Wilson S.M., Datar K.V., Paddy M.R., Swedlow J.R., Swanson M.S.
J. Cell Biol. 127:1173-1184(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, BINDING TO POLYADENYLATED RNA.
[7]"A nuclear 3'-5' exonuclease involved in mRNA degradation interacts with Poly(A) polymerase and the hnRNA protein Npl3p."
Burkard K.T.D., Butler J.S.
Mol. Cell. Biol. 20:604-616(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RRP6.
[8]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[11]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 AND SER-224, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X66019 Genomic DNA. Translation: CAA46817.1.
M86731 Genomic DNA. Translation: AAA34818.1.
X70951 Genomic DNA. Translation: CAA50291.1.
U33007 Genomic DNA. Translation: AAB64865.1.
BK006938 Genomic DNA. Translation: DAA12270.1.
PIRJN0866.
RefSeqNP_010720.3. NM_001180740.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JVONMR-A116-201[»]
2JVRNMR-A193-282[»]
2OSQNMR-A121-194[»]
2OSRNMR-A194-280[»]
ProteinModelPortalQ01560.
SMRQ01560. Positions 121-280.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32489. 1112 interactions.
DIPDIP-6464N.
IntActQ01560. 34 interactions.
MINTMINT-600838.
STRING4932.YDR432W.

Proteomic databases

MaxQBQ01560.
PaxDbQ01560.
PeptideAtlasQ01560.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR432W; YDR432W; YDR432W.
GeneID852042.
KEGGsce:YDR432W.

Organism-specific databases

CYGDYDR432w.
SGDS000002840. NPL3.

Phylogenomic databases

eggNOGCOG0724.
GeneTreeENSGT00700000104103.
KOK14651.
OMAPEGCSWQ.
OrthoDBEOG7QVMDQ.

Enzyme and pathway databases

BioCycYEAST:G3O-29970-MONOMER.

Gene expression databases

GenevestigatorQ01560.

Family and domain databases

Gene3D3.30.70.330. 2 hits.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTSM00360. RRM. 2 hits.
[Graphical view]
PROSITEPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ01560.
NextBio970290.
PROQ01560.

Entry information

Entry nameNOP3_YEAST
AccessionPrimary (citable) accession number: Q01560
Secondary accession number(s): D6VT60
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: July 9, 2014
This is version 151 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references