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Protein

rRNA 2'-O-methyltransferase fibrillarin

Gene

Fbl

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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. 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. Also acts as a protein methyltransferase by mediating methylation of 'Gln-105' of histone H2A (H2AQ104me), a modification that impairs binding of the FACT complex and is specifically present at 35S ribosomal DNA locus (By similarity).By similarity

Catalytic activityi

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

GO - Molecular functioni

  • histone-glutamine methyltransferase activity Source: UniProtKB
  • poly(A) RNA binding Source: Ensembl
  • RNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Ribonucleoprotein, Transferase

Keywords - Biological processi

rRNA processing

Keywords - Ligandi

RNA-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

ReactomeiR-RNO-6791226. Major pathway of rRNA processing in the nucleolus.

Names & Taxonomyi

Protein namesi
Recommended name:
rRNA 2'-O-methyltransferase fibrillarin (EC:2.1.1.-)
Alternative name(s):
Histone-glutamine methyltransferase
Nucleolar protein 1
Gene namesi
Name:Fbl
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi1305542. Fbl.

Subcellular locationi

  • Nucleusnucleolus 1 Publication

  • Note: Fibrillar region of the nucleolus.

GO - Cellular componenti

  • Cajal body Source: RGD
  • chromosome Source: RGD
  • dense fibrillar component Source: UniProtKB
  • extracellular exosome Source: Ensembl
  • granular component Source: Ensembl
  • intracellular ribonucleoprotein complex Source: UniProtKB-KW
  • membrane Source: Ensembl
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 327327rRNA 2'-O-methyltransferase fibrillarinPRO_0000148509Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8 – 81Asymmetric dimethylarginine1 Publication
Modified residuei15 – 151Asymmetric dimethylarginine1 Publication
Modified residuei21 – 211Asymmetric dimethylarginine1 Publication
Modified residuei24 – 241Asymmetric dimethylarginine1 Publication
Modified residuei28 – 281Asymmetric dimethylarginine1 Publication
Modified residuei31 – 311Asymmetric dimethylarginine1 Publication
Modified residuei130 – 1301PhosphoserineCombined sources

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

PaxDbiP22509.
PRIDEiP22509.

PTM databases

iPTMnetiP22509.
PhosphoSiteiP22509.

Expressioni

Gene expression databases

GenevisibleiP22509. RN.

Interactioni

Subunit structurei

Component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles that contain SNU13, FBL, NOP5 and NOP56, plus a guide RNA. It is associated with the U3, U8, U13, X and Y small nuclear RNAs. Component of several ribosomal and nucleolar protein complexes. Interacts with PRMT5 and UTP20. Interacts with DDX5 and C1QBP (By similarity). Interacts with NOL11 (By similarity). Interacts with NOLC1. Interacts with PIH1D1 (By similarity).By similarity1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000026021.

Structurei

3D structure databases

ProteinModelPortaliP22509.
SMRiP22509. Positions 93-321.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni178 – 1792S-adenosyl-L-methionine bindingBy similarity
Regioni197 – 1982S-adenosyl-L-methionine bindingBy similarity
Regioni222 – 2232S-adenosyl-L-methionine bindingBy similarity
Regioni242 – 2454S-adenosyl-L-methionine bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1596. Eukaryota.
COG1889. LUCA.
GeneTreeiENSGT00550000074792.
HOGENOMiHOG000106741.
HOVERGENiHBG002472.
InParanoidiP22509.
KOiK14563.
OMAiANEVNIM.
OrthoDBiEOG7KWSJP.
PhylomeDBiP22509.
TreeFamiTF300639.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_00351. RNA_methyltransf_FlpA.
InterProiIPR000692. Fibrillarin.
IPR020813. Fibrillarin_CS.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01269. Fibrillarin. 1 hit.
[Graphical view]
PRINTSiPR00052. FIBRILLARIN.
SMARTiSM01206. Fibrillarin. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS00566. FIBRILLARIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P22509-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPGFSPRGG GFGGRGGFGD RGGRGGGRGG RGGFGGGRGG FGGGGRGRGG
60 70 80 90 100
GGGGFRGRGG GGGRGGGFQS GGGRGRGGGR GGKRGNQSGK NVMVEPHRHE
110 120 130 140 150
GVFICRGKED ALVTKNLVPG ESVYGEKRVS ISEGDDKIEY RAWNPFRSKL
160 170 180 190 200
AAAILGGVDQ IHIKPGAKVL YLGAASGTTV SHVSDIVGPD GLVYAVEFSH
210 220 230 240 250
RSGRDLINLA KKRTNIIPVI EDARHPHKYR MLIAMVDVIF ADVAQPDQTR
260 270 280 290 300
IVALNAHTFL RNGGHFVISI KANCIDSTAS AEAVFASEVK KMQQENMKPQ
310 320
EQLTLEPYER DHAVVVGVYR PPPKAKN
Length:327
Mass (Da):34,222
Last modified:August 30, 2005 - v2
Checksum:i0E22E63175808BAE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21K → D AA sequence (PubMed:10679015).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC099198 mRNA. Translation: AAH99198.1.
PIRiA23887.
RefSeqiNP_001020814.1. NM_001025643.1.
UniGeneiRn.98803.

Genome annotation databases

EnsembliENSRNOT00000026021; ENSRNOP00000026021; ENSRNOG00000019229.
GeneIDi292747.
KEGGirno:292747.
UCSCiRGD:1305542. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC099198 mRNA. Translation: AAH99198.1.
PIRiA23887.
RefSeqiNP_001020814.1. NM_001025643.1.
UniGeneiRn.98803.

3D structure databases

ProteinModelPortaliP22509.
SMRiP22509. Positions 93-321.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000026021.

PTM databases

iPTMnetiP22509.
PhosphoSiteiP22509.

Proteomic databases

PaxDbiP22509.
PRIDEiP22509.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000026021; ENSRNOP00000026021; ENSRNOG00000019229.
GeneIDi292747.
KEGGirno:292747.
UCSCiRGD:1305542. rat.

Organism-specific databases

CTDi2091.
RGDi1305542. Fbl.

Phylogenomic databases

eggNOGiKOG1596. Eukaryota.
COG1889. LUCA.
GeneTreeiENSGT00550000074792.
HOGENOMiHOG000106741.
HOVERGENiHBG002472.
InParanoidiP22509.
KOiK14563.
OMAiANEVNIM.
OrthoDBiEOG7KWSJP.
PhylomeDBiP22509.
TreeFamiTF300639.

Enzyme and pathway databases

ReactomeiR-RNO-6791226. Major pathway of rRNA processing in the nucleolus.

Miscellaneous databases

PROiP22509.

Gene expression databases

GenevisibleiP22509. RN.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_00351. RNA_methyltransf_FlpA.
InterProiIPR000692. Fibrillarin.
IPR020813. Fibrillarin_CS.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01269. Fibrillarin. 1 hit.
[Graphical view]
PRINTSiPR00052. FIBRILLARIN.
SMARTiSM01206. Fibrillarin. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS00566. FIBRILLARIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Thymus.
  2. "Purification and partial characterization of a nucleolar scleroderma antigen (Mr = 34,000; pI, 8.5) rich in NG,NG-dimethylarginine."
    Lischwe M.A., Ochs R.L., Reddy R., Cook R.G., Yeoman L.C., Tan E.M., Reichlin M., Busch H.
    J. Biol. Chem. 260:14304-14310(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-31, SUBCELLULAR LOCATION, METHYLATION AT ARG-8; ARG-15; ARG-21; ARG-24; ARG-28 AND ARG-31.
  3. "Conserved composition of mammalian box H/ACA and box C/D small nucleolar ribonucleoprotein particles and their interaction with the common factor Nopp140."
    Yang Y., Isaac C., Wang C., Dragon F., Pogacic V., Meier U.T.
    Mol. Biol. Cell 11:567-577(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-28, INTERACTION WITH NOLC1.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFBRL_RAT
AccessioniPrimary (citable) accession number: P22509
Secondary accession number(s): Q4KLH8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 30, 2005
Last modified: June 8, 2016
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.