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Protein

rRNA 2'-O-methyltransferase fibrillarin

Gene

Fbl

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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 + N5-methyl-L-glutamine-[histone].

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionMethyltransferase, Ribonucleoprotein, RNA-binding, Transferase
Biological processrRNA processing
LigandS-adenosyl-L-methionine

Enzyme and pathway databases

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

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi1305542 Fbl

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001485091 – 327rRNA 2'-O-methyltransferase fibrillarinAdd BLAST327

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei8Asymmetric dimethylarginine1 Publication1
Modified residuei15Asymmetric dimethylarginine1 Publication1
Modified residuei21Asymmetric dimethylarginine1 Publication1
Modified residuei24Asymmetric dimethylarginine1 Publication1
Modified residuei28Asymmetric dimethylarginine1 Publication1
Modified residuei31Asymmetric dimethylarginine1 Publication1
Cross-linki90Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki108Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki115Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei122PhosphoserineBy similarity1
Modified residuei130PhosphoserineCombined sources1
Modified residuei132PhosphoserineBy similarity1
Cross-linki137Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki149Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki164Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

Post-translational modificationi

Ubiquitinated. Ubiquitination leads to proteasomal degradation. Deubiquitinated by USP36.By similarity

Keywords - PTMi

Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP22509
PRIDEiP22509

PTM databases

iPTMnetiP22509
PhosphoSitePlusiP22509

Expressioni

Gene expression databases

BgeeiENSRNOG00000019229
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 (PubMed:10679015). Interacts with PIH1D1 (By similarity). Interacts with RRP1B (By similarity).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000026021

Structurei

3D structure databases

ProteinModelPortaliP22509
SMRiP22509
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni178 – 179S-adenosyl-L-methionine bindingBy similarity2
Regioni197 – 198S-adenosyl-L-methionine bindingBy similarity2
Regioni222 – 223S-adenosyl-L-methionine bindingBy similarity2
Regioni242 – 245S-adenosyl-L-methionine bindingBy similarity4

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1596 Eukaryota
COG1889 LUCA
GeneTreeiENSGT00550000074792
HOGENOMiHOG000106741
HOVERGENiHBG002472
InParanoidiP22509
KOiK14563
OMAiQPNQAEI
OrthoDBiEOG091G0GV0
PhylomeDBiP22509
TreeFamiTF300639

Family and domain databases

HAMAPiMF_00351 RNA_methyltransf_FlpA, 1 hit
InterProiView protein in InterPro
IPR000692 Fibrillarin
IPR020813 Fibrillarin_CS
IPR029063 SAM-dependent_MTases
PfamiView protein in Pfam
PF01269 Fibrillarin, 1 hit
PIRSFiPIRSF006540 Nop17p, 1 hit
PRINTSiPR00052 FIBRILLARIN
SMARTiView protein in SMART
SM01206 Fibrillarin, 1 hit
SUPFAMiSSF53335 SSF53335, 1 hit
PROSITEiView protein in PROSITE
PS00566 FIBRILLARIN, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti2K → D AA sequence (PubMed:10679015).Curated1

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

Similar proteinsi

Entry informationi

Entry nameiFBRL_RAT
AccessioniPrimary (citable) accession number: P22509
Secondary accession number(s): Q4KLH8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 30, 2005
Last modified: April 25, 2018
This is version 123 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome