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Q01560 (NOP3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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)
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.9.

Miscellaneous

Present with 78700 molecules/cell in log phase SD medium. Ref.10

Sequence similarities

Belongs to the RRM GAR family.

Contains 2 RRM (RNA recognition motif) domains.

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.14
Modified residue2241Phosphoserine Ref.11 Ref.12 Ref.13 Ref.14
Modified residue2271Phosphothreonine Ref.13
Modified residue2281Phosphothreonine Ref.14
Modified residue3561Phosphoserine Ref.8

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: 1429834] [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: 1392078] [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: 8224861] [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: 9169867] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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: 7962083] [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: 10611239] [Abstract]
Cited for: INTERACTION WITH RRP6.
[8]"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae."
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M.
Nat. Biotechnol. 20:301-305(2002) [PubMed: 11875433] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, MASS SPECTROMETRY.
Strain: 2124.
[9]"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: 14562095] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[10]"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: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[11]"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, MASS SPECTROMETRY.
Strain: YAL6B.
[12]"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: 17330950] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, MASS SPECTROMETRY.
Strain: ADR376.
[13]"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases."
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224 AND THR-227, MASS SPECTROMETRY.
[14]"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: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182; SER-224 AND THR-228, MASS SPECTROMETRY.
+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_010720.1. NM_001180740.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JVONMR-A114-201[»]
2JVRNMR-A193-282[»]
2OSQNMR-A121-194[»]
2OSRNMR-A194-280[»]
ProteinModelPortalQ01560.
SMRQ01560. Positions 121-280.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-6464N.
IntActQ01560. 31 interactions.
MINTMINT-600838.
STRINGQ01560.

Proteomic databases

PeptideAtlasQ01560.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR432W; YDR432W; YDR432W.
GeneID852042.
KEGGsce:YDR432W.
NMPDRfig|4932.3.peg.1493.

Organism-specific databases

CYGDYDR432w.
SGDS000002840. NPL3.

Phylogenomic databases

eggNOGfuNOG12461.
GeneTreeEFGT00050000000572.
OMADDNPPPI.
OrthoDBEOG4BP4N7.

Gene expression databases

ArrayExpressQ01560.
GenevestigatorQ01560.
GermOnlineYDR432W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
Gene3DG3DSA:3.30.70.330. a_b_plait_nuc_bd. 2 hits.
PfamPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTSM00360. RRM. 2 hits.
[Graphical view]
PROSITEPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio970290.

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: January 25, 2012
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families