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P15646 (FBRL_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 136. 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:
rRNA 2'-O-methyltransferase fibrillarin

EC=2.1.1.-
Alternative name(s):
Histone-glutamine methyltransferase
U3 small nucleolar RNA-associated protein NOP1
Short name=Nucleolar protein 1
Short name=U3 snoRNA-associated protein NOP1
Gene names
Name:NOP1
Synonyms:LOT3
Ordered Locus Names:YDL014W
ORF Names:D2870
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length327 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

S-adenosyl-L-methionine-dependent methyltransferase that has the ability to methylate both RNAs and proteins. Involved in pre-rRNA processing by catalyzing the site-specific 2'-hydroxyl methylation of ribose moieties in pre-ribosomal RNA (Ref.5). Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA. Involved in the biogenesis of the 18S rRNA. Also acts as a protein methyltransferase by mediating methylation of 'Gln-105' of histone H2A (H2AQ105me), a modification that impairs binding of the FACT complex and is specifically present at 35S ribosomal DNA locus (Ref.11). Ref.1 Ref.5 Ref.11

Catalytic activity

S-adenosyl-L-methionine + L-glutamine-[histone] = S-adenosyl-L-homocysteine + N(5)-methyl-L-glutamine-[histone]. Ref.11

Subunit structure

Component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles that contain SNU13, NOP1, SIK1/NOP56 and NOP58, plus a guide RNA. Interacts with snoRNA U3. Interacts with MPP10, NOP58, SIK1 and SOF1. Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3. Ref.1 Ref.6 Ref.7 Ref.8

Subcellular location

Nucleusnucleolus. Note: Fibrillar region of the nucleolus. Ref.1 Ref.2 Ref.9

Post-translational modification

Methylated by HMT1, forming asymmetric dimethylarginines (DMA) within a domain referred to as an RGG box, made up of repeated Gly-Gly dipeptides interspersed with Arg and aromatic residues. Ref.9

Sequence similarities

Belongs to the methyltransferase superfamily. Fibrillarin family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NOP58Q124994EBI-6838,EBI-12126

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 327327rRNA 2'-O-methyltransferase fibrillarin HAMAP-Rule MF_00351
PRO_0000148527

Regions

Region8 – 8376RGG-box HAMAP-Rule MF_00351
Region22 – 4221RNA-binding RGG-box By similarity
Region58 – 7518RNA-binding RGG-box By similarity
Region179 – 1802S-adenosyl-L-methionine binding By similarity
Region198 – 1992S-adenosyl-L-methionine binding By similarity
Region223 – 2242S-adenosyl-L-methionine binding By similarity
Region243 – 2464S-adenosyl-L-methionine binding By similarity
Region281 – 31333Helical Potential
Compositional bias6 – 8378DMA/Gly-rich HAMAP-Rule MF_00351

Amino acid modifications

Modified residue81Asymmetric dimethylarginine Probable
Modified residue121Asymmetric dimethylarginine Probable
Modified residue161Asymmetric dimethylarginine Probable
Modified residue221Asymmetric dimethylarginine Probable
Modified residue261Asymmetric dimethylarginine Probable
Modified residue301Asymmetric dimethylarginine Probable
Modified residue341Asymmetric dimethylarginine Probable
Modified residue401Asymmetric dimethylarginine Probable
Modified residue441Asymmetric dimethylarginine Probable
Modified residue481Asymmetric dimethylarginine Probable
Modified residue521Asymmetric dimethylarginine Probable
Modified residue581Asymmetric dimethylarginine Probable
Modified residue621Asymmetric dimethylarginine Probable
Modified residue661Asymmetric dimethylarginine Probable
Modified residue701Asymmetric dimethylarginine Probable
Modified residue731Asymmetric dimethylarginine Probable
Modified residue811Asymmetric dimethylarginine Probable

Experimental info

Mutagenesis871V → D in nop1.3; thermosensitive allele showing a decrease in histone-glutamine N-methyltransferase activity upon shift to restrictive temperature; when associated with G-103; V-175 and S-219. Ref.11
Mutagenesis1031E → G in nop1.3; thermosensitive allele showing a decrease in histone-glutamine N-methyltransferase activity upon shift to restrictive temperature; when associated with D-87; V-175 and S-219. Ref.11
Mutagenesis1751A → V in nop1.3; thermosensitive allele showing a decrease in histone-glutamine N-methyltransferase activity upon shift to restrictive temperature; when associated with D-87; G-103 and S-219. Ref.11
Mutagenesis2191P → S in nop1.3; thermosensitive allele showing a decrease in histone-glutamine N-methyltransferase activity upon shift to restrictive temperature; when associated with D-87; G-103 and V-175. Ref.11

Sequences

Sequence LengthMass (Da)Tools
P15646 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 56A8B958A7B6066E

FASTA32734,465
        10         20         30         40         50         60 
MSFRPGSRGG SRGGSRGGFG GRGGSRGGAR GGSRGGFGGR GGSRGGARGG SRGGFGGRGG 

        70         80         90        100        110        120 
SRGGARGGSR GGRGGAAGGA RGGAKVVIEP HRHAGVYIAR GKEDLLVTKN MAPGESVYGE 

       130        140        150        160        170        180 
KRISVEEPSK EDGVPPTKVE YRVWNPFRSK LAAGIMGGLD ELFIAPGKKV LYLGAASGTS 

       190        200        210        220        230        240 
VSHVSDVVGP EGVVYAVEFS HRPGRELISM AKKRPNIIPI IEDARHPQKY RMLIGMVDCV 

       250        260        270        280        290        300 
FADVAQPDQA RIIALNSHMF LKDQGGVVIS IKANCIDSTV DAETVFAREV QKLREERIKP 

       310        320 
LEQLTLEPYE RDHCIVVGRY MRSGLKK 

« Hide

References

« Hide 'large scale' references
[1]"A yeast nucleolar protein related to mammalian fibrillarin is associated with small nucleolar RNA and is essential for viability."
Schimmang T., Tollervey D., Kern H., Frank R., Hurt E.C.
EMBO J. 8:4015-4024(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 264-270 AND 298-310, FUNCTION, INTERACTION WITH SNORNAS, SUBCELLULAR LOCATION.
[2]"Isolation and sequencing of NOP1. A yeast gene encoding a nucleolar protein homologous to a human autoimmune antigen."
Henriquez R., Blobel G., Aris J.P.
J. Biol. Chem. 265:2209-2215(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 112-142; 157-181 AND 211-231, SUBCELLULAR LOCATION.
[3]"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.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"The small nucleolar RNP protein NOP1 (fibrillarin) is required for pre-rRNA processing in yeast."
Tollervey D., Lehtonen H., Carmo-Fonseca M., Hurt E.C.
EMBO J. 10:573-583(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"A U3 snoRNP protein with homology to splicing factor PRP4 and G beta domains is required for ribosomal RNA processing."
Jansen R., Tollervey D., Hurt E.C.
EMBO J. 12:2549-2558(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SOF1.
[7]"Nucleolar KKE/D repeat proteins Nop56p and Nop58p interact with Nop1p and are required for ribosome biogenesis."
Gautier T., Berges T., Tollervey D., Hurt E.
Mol. Cell. Biol. 17:7088-7098(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SIK1 AND NOP58.
[8]"A large nucleolar U3 ribonucleoprotein required for 18S ribosomal RNA biogenesis."
Dragon F., Gallagher J.E.G., Compagnone-Post P.A., Mitchell B.M., Porwancher K.A., Wehner K.A., Wormsley S., Settlage R.E., Shabanowitz J., Osheim Y., Beyer A.L., Hunt D.F., Baserga S.J.
Nature 417:967-970(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MPP10 AND SNORNA U3, IDENTIFICATION IN SSU PROCESSOME BY MASS SPECTROMETRY.
[9]"In vivo analysis of nucleolar proteins modified by the yeast arginine methyltransferase Hmt1/Rmt1p."
Xu C., Henry P.A., Setya A., Henry M.F.
RNA 9:746-759(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, METHYLATION BY HMT1.
[10]"Sites of ubiquitin attachment in Saccharomyces cerevisiae."
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated modification."
Tessarz P., Santos-Rosa H., Robson S.C., Sylvestersen K.B., Nelson C.J., Nielsen M.L., Kouzarides T.
Nature 505:564-568(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF VAL-87; GLU-103; ALA-175 AND PRO-219.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05230 Genomic DNA. Translation: AAA34816.1.
Z48432 Genomic DNA. Translation: CAA88345.1.
Z74061 Genomic DNA. Translation: CAA98571.1.
Z74062 Genomic DNA. Translation: CAA98572.1.
BK006938 Genomic DNA. Translation: DAA11835.1.
PIRS25421.
RefSeqNP_010270.1. NM_001180073.1.

3D structure databases

ProteinModelPortalP15646.
SMRP15646. Positions 87-320.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32040. 290 interactions.
DIPDIP-698N.
IntActP15646. 44 interactions.
MINTMINT-382637.
STRING4932.YDL014W.

Proteomic databases

PaxDbP15646.
PeptideAtlasP15646.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDL014W; YDL014W; YDL014W.
GeneID851548.
KEGGsce:YDL014W.

Organism-specific databases

CYGDYDL014w.
SGDS000002172. NOP1.

Phylogenomic databases

eggNOGCOG1889.
GeneTreeENSGT00550000074792.
HOGENOMHOG000106741.
KOK14563.
OMAGEAKIEY.
OrthoDBEOG7FNCK0.

Enzyme and pathway databases

BioCycYEAST:G3O-29444-MONOMER.

Gene expression databases

GenevestigatorP15646.

Family and domain databases

HAMAPMF_00351. RNA_methyltransf_FlpA.
InterProIPR000692. Fibrillarin.
IPR020813. Fibrillarin_CS.
[Graphical view]
PANTHERPTHR10335. PTHR10335. 1 hit.
PfamPF01269. Fibrillarin. 1 hit.
[Graphical view]
PIRSFPIRSF006540. Nop17p. 1 hit.
PRINTSPR00052. FIBRILLARIN.
PROSITEPS00566. FIBRILLARIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio968964.
PROP15646.

Entry information

Entry nameFBRL_YEAST
AccessionPrimary (citable) accession number: P15646
Secondary accession number(s): D6VRX5, P89890
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: April 16, 2014
This is version 136 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