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Protein

rRNA 2'-O-methyltransferase fibrillarin

Gene

FBL

Organism
Homo sapiens (Human)
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 (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
  • tRNA processing Source: InterPro

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.

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

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.

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).By similarity9 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. 237 interactors.
CORUMiP22087.
DIPiDIP-27569N.
IntActiP22087. 58 interactors.
MINTiMINT-207612.
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: October 25, 2017
This is version 183 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

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families