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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 + N(5)-methyl-L-glutamine-[histone].1 Publication

GO - Molecular functioni

  • ATPase binding Source: UniProtKB
  • histone-glutamine methyltransferase activity Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: ProtInc
  • 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
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-HSA-6790901. rRNA modification in the nucleus.
R-HSA-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):
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 Componentsi: Chromosome 1, Chromosome 19

Organism-specific databases

HGNCiHGNC:3599. FBL.

Subcellular locationi

GO - Cellular componenti

  • box C/D snoRNP complex Source: BHF-UCL
  • Cajal body Source: BHF-UCL
  • dense fibrillar component Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • granular component Source: Ensembl
  • membrane Source: UniProtKB
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • small-subunit processome Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28012.

Polymorphism and mutation databases

BioMutaiFBL.
DMDMi14549159.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 321321rRNA 2'-O-methyltransferase fibrillarinPRO_0000148507Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8 – 81Asymmetric dimethylarginineBy similarity
Modified residuei15 – 151Asymmetric dimethylarginineBy similarity
Modified residuei21 – 211Asymmetric dimethylarginineBy similarity
Modified residuei24 – 241Asymmetric dimethylarginineBy similarity
Modified residuei27 – 271Asymmetric dimethylarginineBy similarity
Modified residuei116 – 1161PhosphoserineCombined sources
Modified residuei124 – 1241PhosphoserineCombined sources
Modified residuei126 – 1261PhosphoserineCombined 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

Methylation, Phosphoprotein

Proteomic databases

EPDiP22087.
MaxQBiP22087.
PaxDbiP22087.
PeptideAtlasiP22087.
PRIDEiP22087.

2D gel databases

SWISS-2DPAGEP22087.

PTM databases

iPTMnetiP22087.
PhosphoSiteiP22087.
SwissPalmiP22087.

Expressioni

Gene expression databases

BgeeiENSG00000105202.
CleanExiHS_FBL.
ExpressionAtlasiP22087. baseline and differential.
GenevisibleiP22087. HS.

Organism-specific databases

HPAiCAB001514.

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. 233 interactions.
DIPiDIP-27569N.
IntActiP22087. 43 interactions.
MINTiMINT-207612.
STRINGi9606.ENSP00000221801.

Structurei

Secondary structure

1
321
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi96 – 983Combined sources
Beta strandi107 – 1093Combined sources
Beta strandi117 – 1193Combined sources
Beta strandi122 – 1254Combined sources
Beta strandi132 – 1365Combined sources
Turni139 – 1413Combined sources
Helixi143 – 1497Combined sources
Beta strandi162 – 1665Combined sources
Helixi172 – 18110Combined sources
Beta strandi186 – 1905Combined sources
Helixi194 – 20613Combined sources
Beta strandi210 – 2134Combined sources
Helixi220 – 2267Combined sources
Beta strandi230 – 2356Combined sources
Helixi242 – 25312Combined sources
Beta strandi254 – 26512Combined sources
Helixi266 – 2694Combined sources
Beta strandi271 – 2733Combined sources
Helixi275 – 28410Combined sources
Helixi285 – 2895Combined sources
Beta strandi291 – 2988Combined sources
Turni300 – 3023Combined sources
Beta strandi303 – 31311Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IPXX-ray1.82A83-315[»]
ProteinModelPortaliP22087.
SMRiP22087. Positions 87-315.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22087.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni172 – 1732S-adenosyl-L-methionine bindingBy similarity
Regioni191 – 1922S-adenosyl-L-methionine binding
Regioni216 – 2172S-adenosyl-L-methionine binding
Regioni236 – 2394S-adenosyl-L-methionine binding
Regioni274 – 30633HelicalSequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi8 – 7770DMA/Gly-richAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1596. Eukaryota.
COG1889. LUCA.
GeneTreeiENSGT00550000074792.
HOGENOMiHOG000106741.
HOVERGENiHBG002472.
KOiK14563.
OMAiPGVYIVI.
OrthoDBiEOG091G0GV0.
PhylomeDBiP22087.
TreeFamiTF300639.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_00351. RNA_methyltransf_FlpA. 1 hit.
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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti132 – 1321I → F in AAA52453 (PubMed:1846968).Curated

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.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IPXX-ray1.82A83-315[»]
ProteinModelPortaliP22087.
SMRiP22087. Positions 87-315.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108399. 233 interactions.
DIPiDIP-27569N.
IntActiP22087. 43 interactions.
MINTiMINT-207612.
STRINGi9606.ENSP00000221801.

PTM databases

iPTMnetiP22087.
PhosphoSiteiP22087.
SwissPalmiP22087.

Polymorphism and mutation databases

BioMutaiFBL.
DMDMi14549159.

2D gel databases

SWISS-2DPAGEP22087.

Proteomic databases

EPDiP22087.
MaxQBiP22087.
PaxDbiP22087.
PeptideAtlasiP22087.
PRIDEiP22087.

Protocols and materials databases

DNASUi2091.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2091.
GeneCardsiFBL.
HGNCiHGNC:3599. FBL.
HPAiCAB001514.
MIMi134795. gene.
neXtProtiNX_P22087.
PharmGKBiPA28012.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1596. Eukaryota.
COG1889. LUCA.
GeneTreeiENSGT00550000074792.
HOGENOMiHOG000106741.
HOVERGENiHBG002472.
KOiK14563.
OMAiPGVYIVI.
OrthoDBiEOG091G0GV0.
PhylomeDBiP22087.
TreeFamiTF300639.

Enzyme and pathway databases

ReactomeiR-HSA-6790901. rRNA modification in the nucleus.
R-HSA-6791226. Major pathway of rRNA processing in the nucleolus.

Miscellaneous databases

ChiTaRSiFBL. human.
EvolutionaryTraceiP22087.
GeneWikiiFibrillarin.
GenomeRNAii2091.
PROiP22087.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000105202.
CleanExiHS_FBL.
ExpressionAtlasiP22087. baseline and differential.
GenevisibleiP22087. HS.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_00351. RNA_methyltransf_FlpA. 1 hit.
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...

Entry informationi

Entry nameiFBRL_HUMAN
AccessioniPrimary (citable) accession number: P22087
Secondary accession number(s): B5BUE8
, O75259, Q6IAT5, Q9UPI6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: June 20, 2001
Last modified: September 7, 2016
This is version 171 of the entry and version 2 of the sequence. [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

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.