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P15646

- FBRL_YEAST

UniProt

P15646 - FBRL_YEAST

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Protein

rRNA 2'-O-methyltransferase fibrillarin

Gene
NOP1, LOT3, YDL014W, D2870
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 (1 Publication). 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 (1 Publication).3 Publications

Catalytic activityi

S-adenosyl-L-methionine + L-glutamine-[histone] = S-adenosyl-L-homocysteine + N(5)-methyl-L-glutamine-[histone].1 Publication

GO - Molecular functioni

  1. histone-glutamine methyltransferase activity Source: UniProtKB
  2. protein binding Source: IntAct
  3. RNA binding Source: UniProtKB-KW
  4. rRNA methyltransferase activity Source: SGD

GO - Biological processi

  1. box C/D snoRNA 3'-end processing Source: SGD
  2. histone glutamine methylation Source: SGD
  3. regulation of transcription from RNA polymerase I promoter Source: UniProtKB
  4. rRNA methylation Source: SGD
  5. rRNA processing Source: SGD
  6. snoRNA processing Source: SGD
  7. tRNA processing Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Ribonucleoprotein, Transferase

Keywords - Biological processi

Ribosome biogenesis, rRNA processing

Keywords - Ligandi

RNA-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciYEAST:G3O-29444-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:NOP1
Synonyms:LOT3
Ordered Locus Names:YDL014W
ORF Names:D2870
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDL014w.
SGDiS000002172. NOP1.

Subcellular locationi

Nucleusnucleolus
Note: Fibrillar region of the nucleolus.3 Publications

GO - Cellular componenti

  1. box C/D snoRNP complex Source: SGD
  2. nucleolus Source: SGD
  3. small-subunit processome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi87 – 871V → 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. 1 Publication
Mutagenesisi103 – 1031E → 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. 1 Publication
Mutagenesisi175 – 1751A → 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. 1 Publication
Mutagenesisi219 – 2191P → 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. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 327327rRNA 2'-O-methyltransferase fibrillarinUniRule annotationPRO_0000148527Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8 – 81Asymmetric dimethylarginine Inferred
Modified residuei12 – 121Asymmetric dimethylarginine Inferred
Modified residuei16 – 161Asymmetric dimethylarginine Inferred
Modified residuei22 – 221Asymmetric dimethylarginine Inferred
Modified residuei26 – 261Asymmetric dimethylarginine Inferred
Modified residuei30 – 301Asymmetric dimethylarginine Inferred
Modified residuei34 – 341Asymmetric dimethylarginine Inferred
Modified residuei40 – 401Asymmetric dimethylarginine Inferred
Modified residuei44 – 441Asymmetric dimethylarginine Inferred
Modified residuei48 – 481Asymmetric dimethylarginine Inferred
Modified residuei52 – 521Asymmetric dimethylarginine Inferred
Modified residuei58 – 581Asymmetric dimethylarginine Inferred
Modified residuei62 – 621Asymmetric dimethylarginine Inferred
Modified residuei66 – 661Asymmetric dimethylarginine Inferred
Modified residuei70 – 701Asymmetric dimethylarginine Inferred
Modified residuei73 – 731Asymmetric dimethylarginine Inferred
Modified residuei81 – 811Asymmetric dimethylarginine Inferred

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Methylation

Proteomic databases

MaxQBiP15646.
PaxDbiP15646.
PeptideAtlasiP15646.

Expressioni

Gene expression databases

GenevestigatoriP15646.

Interactioni

Subunit structurei

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 U3.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NOP58Q124994EBI-6838,EBI-12126

Protein-protein interaction databases

BioGridi32040. 290 interactions.
DIPiDIP-698N.
IntActiP15646. 44 interactions.
MINTiMINT-382637.
STRINGi4932.YDL014W.

Structurei

3D structure databases

ProteinModelPortaliP15646.
SMRiP15646. Positions 87-320.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni8 – 8376RGG-boxUniRule annotationAdd
BLAST
Regioni22 – 4221RNA-binding RGG-box By similarityAdd
BLAST
Regioni58 – 7518RNA-binding RGG-box By similarityAdd
BLAST
Regioni179 – 1802S-adenosyl-L-methionine binding By similarity
Regioni198 – 1992S-adenosyl-L-methionine binding By similarity
Regioni223 – 2242S-adenosyl-L-methionine binding By similarity
Regioni243 – 2464S-adenosyl-L-methionine binding By similarity
Regioni281 – 31333Helical Reviewed predictionAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi6 – 8378DMA/Gly-richUniRule annotationAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1889.
GeneTreeiENSGT00550000074792.
HOGENOMiHOG000106741.
KOiK14563.
OMAiGEKRMSV.
OrthoDBiEOG7FNCK0.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_00351. RNA_methyltransf_FlpA.
InterProiIPR000692. Fibrillarin.
IPR020813. Fibrillarin_CS.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PfamiPF01269. Fibrillarin. 1 hit.
[Graphical view]
PIRSFiPIRSF006540. Nop17p. 1 hit.
PRINTSiPR00052. FIBRILLARIN.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS00566. FIBRILLARIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P15646-1 [UniParc]FASTAAdd to Basket

« Hide

MSFRPGSRGG SRGGSRGGFG GRGGSRGGAR GGSRGGFGGR GGSRGGARGG    50
SRGGFGGRGG SRGGARGGSR GGRGGAAGGA RGGAKVVIEP HRHAGVYIAR 100
GKEDLLVTKN MAPGESVYGE KRISVEEPSK EDGVPPTKVE YRVWNPFRSK 150
LAAGIMGGLD ELFIAPGKKV LYLGAASGTS VSHVSDVVGP EGVVYAVEFS 200
HRPGRELISM AKKRPNIIPI IEDARHPQKY RMLIGMVDCV FADVAQPDQA 250
RIIALNSHMF LKDQGGVVIS IKANCIDSTV DAETVFAREV QKLREERIKP 300
LEQLTLEPYE RDHCIVVGRY MRSGLKK 327
Length:327
Mass (Da):34,465
Last modified:April 1, 1990 - v1
Checksum:i56A8B958A7B6066E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiS25421.
RefSeqiNP_010270.1. NM_001180073.1.

Genome annotation databases

EnsemblFungiiYDL014W; YDL014W; YDL014W.
GeneIDi851548.
KEGGisce:YDL014W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi S25421.
RefSeqi NP_010270.1. NM_001180073.1.

3D structure databases

ProteinModelPortali P15646.
SMRi P15646. Positions 87-320.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32040. 290 interactions.
DIPi DIP-698N.
IntActi P15646. 44 interactions.
MINTi MINT-382637.
STRINGi 4932.YDL014W.

Proteomic databases

MaxQBi P15646.
PaxDbi P15646.
PeptideAtlasi P15646.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDL014W ; YDL014W ; YDL014W .
GeneIDi 851548.
KEGGi sce:YDL014W.

Organism-specific databases

CYGDi YDL014w.
SGDi S000002172. NOP1.

Phylogenomic databases

eggNOGi COG1889.
GeneTreei ENSGT00550000074792.
HOGENOMi HOG000106741.
KOi K14563.
OMAi GEKRMSV.
OrthoDBi EOG7FNCK0.

Enzyme and pathway databases

BioCyci YEAST:G3O-29444-MONOMER.

Miscellaneous databases

NextBioi 968964.
PROi P15646.

Gene expression databases

Genevestigatori P15646.

Family and domain databases

Gene3Di 3.40.50.150. 1 hit.
HAMAPi MF_00351. RNA_methyltransf_FlpA.
InterProi IPR000692. Fibrillarin.
IPR020813. Fibrillarin_CS.
IPR029063. SAM-dependent_MTases-like.
[Graphical view ]
Pfami PF01269. Fibrillarin. 1 hit.
[Graphical view ]
PIRSFi PIRSF006540. Nop17p. 1 hit.
PRINTSi PR00052. FIBRILLARIN.
SUPFAMi SSF53335. SSF53335. 1 hit.
PROSITEi PS00566. FIBRILLARIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiFBRL_YEAST
AccessioniPrimary (citable) accession number: P15646
Secondary accession number(s): D6VRX5, P89890
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: June 11, 2014
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3

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