Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

rRNA 2'-O-methyltransferase fibrillarin

Gene

FBL

Organism
Homo sapiens (Human)
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 (PubMed:24352239).1 Publication

Catalytic activityi

S-adenosyl-L-methionine + L-glutamine-[histone] = S-adenosyl-L-homocysteine + N5-methyl-L-glutamine-[histone].1 Publication

GO - Molecular functioni

  • ATPase binding Source: UniProtKB
  • histone-glutamine methyltransferase activity Source: UniProtKB
  • RNA binding Source: UniProtKB
  • rRNA methyltransferase activity Source: GO_Central
  • TFIID-class transcription factor binding Source: UniProtKB

GO - Biological processi

  • box C/D snoRNA 3'-end processing Source: GO_Central
  • histone glutamine methylation Source: UniProtKB
  • osteoblast differentiation Source: UniProtKB
  • rRNA methylation Source: GO_Central
  • rRNA processing Source: Reactome
  • snoRNA localization Source: UniProtKB

Keywordsi

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

Enzyme and pathway databases

ReactomeiR-HSA-6790901 rRNA modification in the nucleus and cytosol
R-HSA-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):
34 kDa nucleolar scleroderma antigen
Histone-glutamine methyltransferase
Gene namesi
Name:FBL
Synonyms:FIB1, FLRN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

EuPathDBiHostDB:ENSG00000105202.7
HGNCiHGNC:3599 FBL
MIMi134795 gene
neXtProtiNX_P22087

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

Pathology & Biotechi

Organism-specific databases

DisGeNETi2091
OpenTargetsiENSG00000105202
PharmGKBiPA28012

Polymorphism and mutation databases

BioMutaiFBL
DMDMi14549159

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001485071 – 321rRNA 2'-O-methyltransferase fibrillarinAdd BLAST321

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei8Asymmetric dimethylarginineBy similarity1
Modified residuei15Asymmetric dimethylarginineBy similarity1
Modified residuei21Asymmetric dimethylarginineBy similarity1
Modified residuei24Asymmetric dimethylarginineBy similarity1
Modified residuei27Asymmetric dimethylarginineBy similarity1
Cross-linki84Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki102Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki109Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei116PhosphoserineCombined sources1
Modified residuei124PhosphoserineCombined sources1
Modified residuei126PhosphoserineCombined sources1
Cross-linki131Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki143Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki158Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Post-translational modificationi

Ubiquitinated. Ubiquitination leads to proteasomal degradation (PubMed:19208757). Deubiquitinated by USP36 (PubMed:19208757).1 Publication
By homology to other fibrillarins, some or all of the N-terminal domain arginines are modified to asymmetric dimethylarginine (DMA).

Keywords - PTMi

Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP22087
MaxQBiP22087
PaxDbiP22087
PeptideAtlasiP22087
PRIDEiP22087
ProteomicsDBi53959

2D gel databases

SWISS-2DPAGEiP22087

PTM databases

iPTMnetiP22087
PhosphoSitePlusiP22087
SwissPalmiP22087

Expressioni

Gene expression databases

BgeeiENSG00000105202
CleanExiHS_FBL
ExpressionAtlasiP22087 baseline and differential
GenevisibleiP22087 HS

Organism-specific databases

HPAiCAB001514
HPA049546

Interactioni

Subunit structurei

Interacts with NOLC1 (By similarity). 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. Interacts with NOL11. Interacts with PIH1D1 (PubMed:17636026). Interacts with RRP1B (PubMed:20926688).By similarity10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DDX5P178446EBI-358318,EBI-351962

GO - Molecular functioni

  • ATPase binding Source: UniProtKB
  • TFIID-class transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108399, 249 interactors
CORUMiP22087
DIPiDIP-27569N
IntActiP22087, 255 interactors
MINTiP22087
STRINGi9606.ENSP00000221801

Structurei

Secondary structure

1321
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi96 – 98Combined sources3
Beta strandi107 – 109Combined sources3
Beta strandi117 – 119Combined sources3
Beta strandi122 – 125Combined sources4
Beta strandi132 – 136Combined sources5
Turni139 – 141Combined sources3
Helixi143 – 149Combined sources7
Beta strandi162 – 166Combined sources5
Helixi172 – 181Combined sources10
Beta strandi186 – 190Combined sources5
Helixi194 – 206Combined sources13
Beta strandi210 – 213Combined sources4
Helixi220 – 226Combined sources7
Beta strandi230 – 235Combined sources6
Helixi242 – 253Combined sources12
Beta strandi254 – 265Combined sources12
Helixi266 – 269Combined sources4
Beta strandi271 – 273Combined sources3
Helixi275 – 284Combined sources10
Helixi285 – 289Combined sources5
Beta strandi291 – 298Combined sources8
Turni300 – 302Combined sources3
Beta strandi303 – 313Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IPXX-ray1.82A83-315[»]
ProteinModelPortaliP22087
SMRiP22087
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22087

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni172 – 173S-adenosyl-L-methionine bindingBy similarity2
Regioni191 – 192S-adenosyl-L-methionine binding2
Regioni216 – 217S-adenosyl-L-methionine binding2
Regioni236 – 239S-adenosyl-L-methionine binding4
Regioni274 – 306HelicalSequence analysisAdd BLAST33

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi8 – 77DMA/Gly-richAdd BLAST70

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1596 Eukaryota
COG1889 LUCA
GeneTreeiENSGT00550000074792
HOGENOMiHOG000106741
HOVERGENiHBG002472
KOiK14563
OMAiQPNQAEI
OrthoDBiEOG091G0GV0
PhylomeDBiP22087
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.

P22087-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPGFSPRGG GFGGRGGFGD RGGRGGRGGF GGGRGRGGGF RGRGRGGGGG
60 70 80 90 100
GGGGGGGGRG GGGFHSGGNR GRGRGGKRGN QSGKNVMVEP HRHEGVFICR
110 120 130 140 150
GKEDALVTKN LVPGESVYGE KRVSISEGDD KIEYRAWNPF RSKLAAAILG
160 170 180 190 200
GVDQIHIKPG AKVLYLGAAS GTTVSHVSDI VGPDGLVYAV EFSHRSGRDL
210 220 230 240 250
INLAKKRTNI IPVIEDARHP HKYRMLIAMV DVIFADVAQP DQTRIVALNA
260 270 280 290 300
HTFLRNGGHF VISIKANCID STASAEAVFA SEVKKMQQEN MKPQEQLTLE
310 320
PYERDHAVVV GVYRPPPKVK N
Length:321
Mass (Da):33,784
Last modified:June 20, 2001 - v2
Checksum:i2123F41E01EC557A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti132I → F in AAA52453 (PubMed:1846968).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59849 mRNA Translation: AAA52453.1
X56597 mRNA Translation: CAA39935.1
BT006830 mRNA Translation: AAP35476.1
BT020144 mRNA Translation: AAV38946.1
CR457069 mRNA Translation: CAG33350.1
AB451384 mRNA Translation: BAG70198.1
AC006950 Genomic DNA Translation: AAD15623.1
AC005393 Genomic DNA Translation: AAC28913.1
CH471126 Genomic DNA Translation: EAW56925.1
BC019260 mRNA Translation: AAH19260.1
CCDSiCCDS12545.1
PIRiA38712
RefSeqiNP_001427.2, NM_001436.3
UniGeneiHs.299002

Genome annotation databases

EnsembliENST00000221801; ENSP00000221801; ENSG00000105202
ENST00000625241; ENSP00000487390; ENSG00000280548
GeneIDi2091
KEGGihsa:2091
UCSCiuc002omn.4 human

Similar proteinsi

Entry informationi

Entry nameiFBRL_HUMAN
AccessioniPrimary (citable) accession number: P22087
Secondary accession number(s): B5BUE8
, O75259, Q6IAT5, Q9UPI6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: June 20, 2001
Last modified: June 20, 2018
This is version 189 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health