P15646 (FBRL_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
rRNA 2'-O-methyltransferase fibrillarin
EC=2.1.1.-

Alternative name(s):
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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	327 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in pre-rRNA processing. Utilizes the methyl donor S-adenosyl-L-methionine to catalyze the site-specific 2'-hydroxyl methylation of ribose moieties in pre-ribosomal RNA. 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. Ref.1 Ref.5
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	Nucleus › nucleolus. Note: Fibrillar region of the nucleolus. Ref.1 Ref.2
Post-translational modification	By homology to other fibrillarins, some or all of the N-terminal domain arginines are modified to asymmetric dimethylarginine (DMA).
Sequence similarities	Belongs to the methyltransferase superfamily. Fibrillarin family.

Ontologies

Keywords
Biological process	Ribosome biogenesis rRNA processing
Cellular component	Nucleus
Ligand	RNA-binding
Molecular function	Methyltransferase Ribonucleoprotein Transferase
PTM	Methylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	box C/D snoRNA 3'-end processing Inferred from mutant phenotype PubMed 10733567PubMed 15167896. Source: SGD tRNA processing Inferred from electronic annotation. Source: InterPro
Cellular_component	90S preribosome Inferred from direct assay PubMed 12150911. Source: SGD box C/D snoRNP complex Inferred from direct assay PubMed 11081632. Source: SGD small-subunit processome Inferred from direct assay Ref.8. Source: SGD
Molecular_function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW rRNA methyltransferase activity Inferred from mutant phenotype PubMed 12215523. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NOP58	Q12499	4	EBI-6838,EBI-12126

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 327	327	rRNA 2'-O-methyltransferase fibrillarin		PRO_0000148527
Regions
	Region	22 – 42	21	RNA-binding RGG-box By similarity
	Region	58 – 75	18	RNA-binding RGG-box By similarity
	Region	179 – 180	2	S-adenosyl-L-methionine binding By similarity
	Region	198 – 199	2	S-adenosyl-L-methionine binding By similarity
	Region	223 – 224	2	S-adenosyl-L-methionine binding By similarity
	Region	281 – 313	33	Helical Potential
	Compositional bias	6 – 83	78	DMA/Gly-rich
Sites
	Binding site	150	1	S-adenosyl-L-methionine By similarity
	Binding site	243	1	S-adenosyl-L-methionine By similarity
Amino acid modifications
	Modified residue	8	1	Asymmetric dimethylarginine By similarity
	Modified residue	12	1	Asymmetric dimethylarginine By similarity
	Modified residue	16	1	Asymmetric dimethylarginine By similarity
	Modified residue	22	1	Asymmetric dimethylarginine By similarity
	Modified residue	26	1	Asymmetric dimethylarginine By similarity
	Modified residue	30	1	Asymmetric dimethylarginine By similarity
	Modified residue	34	1	Asymmetric dimethylarginine By similarity
	Modified residue	40	1	Asymmetric dimethylarginine By similarity
	Modified residue	44	1	Asymmetric dimethylarginine By similarity
	Modified residue	48	1	Asymmetric dimethylarginine By similarity
	Modified residue	52	1	Asymmetric dimethylarginine By similarity
	Modified residue	58	1	Asymmetric dimethylarginine By similarity
	Modified residue	62	1	Asymmetric dimethylarginine By similarity
	Modified residue	66	1	Asymmetric dimethylarginine By similarity
	Modified residue	69	1	Phosphoserine Ref.9
	Modified residue	70	1	Asymmetric dimethylarginine By similarity
	Modified residue	73	1	Asymmetric dimethylarginine By similarity
	Modified residue	81	1	Asymmetric dimethylarginine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P15646 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 56A8B958A7B6066E	FASTA	327	34,465
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69, MASS SPECTROMETRY.
+	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.
PIR	S25421.
RefSeq	NP_010270.1. NM_001180073.1.
3D structure databases
ProteinModelPortal	P15646.
SMR	P15646. Positions 87-320.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-698N.
IntAct	P15646. 43 interactions.
MINT	MINT-382637.
STRING	4932.YDL014W.
Proteomic databases
PaxDb	P15646.
PeptideAtlas	P15646.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YDL014W; YDL014W; YDL014W.
GeneID	851548.
KEGG	sce:YDL014W.
Organism-specific databases
CYGD	YDL014w.
SGD	S000002172. NOP1.
Phylogenomic databases
eggNOG	COG1889.
GeneTree	ENSGT00550000074792.
HOGENOM	HOG000106741.
KO	K14563.
OMA	VGMVDTI.
OrthoDB	EOG4WT0KN.
Gene expression databases
Genevestigator	P15646.
GermOnline	YDL014W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000692. Fibrillarin. IPR020813. Fibrillarin_CS. [Graphical view]
PANTHER	PTHR10335. PTHR10335. 1 hit.
Pfam	PF01269. Fibrillarin. 1 hit. [Graphical view]
PIRSF	PIRSF006540. Nop17p. 1 hit.
PRINTS	PR00052. FIBRILLARIN.
PROSITE	PS00566. FIBRILLARIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	968964.

Entry information

Entry name

FBRL_YEAST

Accession

Primary (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 3, 2013
This is version 127 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program