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Protein

rRNA 2'-O-methyltransferase fibrillarin

Gene

Fbl

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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

  1. histone-glutamine methyltransferase activity Source: UniProtKB
  2. poly(A) RNA binding Source: MGI
  3. snoRNA binding Source: MGI

GO - Biological processi

  1. histone glutamine methylation Source: UniProtKB
  2. osteoblast differentiation Source: MGI
  3. rRNA processing Source: MGI
  4. snoRNA metabolic process Source: MGI
  5. 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

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:95486. Fbl.

Subcellular locationi

Nucleusnucleolus
Note: Fibrillar region of the nucleolus.

GO - Cellular componenti

  1. Cajal body Source: MGI
  2. extracellular vesicular exosome Source: MGI
  3. granular component Source: MGI
  4. membrane Source: MGI
  5. nucleolus Source: MGI
  6. nucleus Source: MGI
  7. ribonucleoprotein complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 327327rRNA 2'-O-methyltransferase fibrillarinPRO_0000148508Add
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 residuei28 – 281Asymmetric dimethylarginineBy similarity
Modified residuei31 – 311Asymmetric dimethylarginineBy similarity
Modified residuei130 – 1301PhosphoserineBy similarity

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

MaxQBiP35550.
PaxDbiP35550.
PRIDEiP35550.

PTM databases

PhosphoSiteiP35550.

Expressioni

Gene expression databases

BgeeiP35550.
CleanExiMM_FBL.
GenevestigatoriP35550.

Interactioni

Subunit structurei

Component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles that contain NHP2L1, 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, NOLC1 and UTP20. Interacts with DDX5 and C1QBP (By similarity). Interacts with NOL11 (By similarity).By similarity

Protein-protein interaction databases

BioGridi199604. 1 interaction.
IntActiP35550. 6 interactions.
MINTiMINT-1854224.

Structurei

3D structure databases

ProteinModelPortaliP35550.
SMRiP35550. 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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi4 – 8582DMA/Gly-richAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1889.
GeneTreeiENSGT00550000074792.
HOGENOMiHOG000106741.
HOVERGENiHBG002472.
InParanoidiP35550.
KOiK14563.
OMAiANEVNIM.
OrthoDBiEOG7KWSJP.
PhylomeDBiP35550.
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]
PIRSFiPIRSF006540. Nop17p. 1 hit.
PRINTSiPR00052. FIBRILLARIN.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS00566. FIBRILLARIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P35550-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKPGFSPRGG GFGGRGGFGD RGGRGGGRGG RGGFGGGRGG FGGGGRGRGG
60 70 80 90 100
GGGGFRGRGG GGGRGGGFQS GGNRGRGGGR 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 PPPKVKN
Length:327
Mass (Da):34,307
Last modified:August 30, 2005 - v2
Checksum:i0E22FE7C758089C3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61S → R in CAA80307. (PubMed:8218401)Curated
Sequence conflicti63 – 631G → V in CAA80307. (PubMed:8218401)Curated
Sequence conflicti113 – 1131V → F in CAA80307. (PubMed:8218401)Curated
Sequence conflicti137 – 1371K → T in CAA80307. (PubMed:8218401)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z22593 mRNA. Translation: CAA80307.1.
BC003813 mRNA. Translation: AAH03813.1.
BC092274 mRNA. Translation: AAH92274.1.
CCDSiCCDS21036.1.
PIRiS38342.
RefSeqiNP_032017.2. NM_007991.3.
XP_006543829.1. XM_006543766.1.
UniGeneiMm.4595.

Genome annotation databases

EnsembliENSMUST00000042405; ENSMUSP00000037613; ENSMUSG00000046865.
GeneIDi102643269.
14113.
KEGGimmu:102643269.
mmu:14113.
UCSCiuc009fxy.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z22593 mRNA. Translation: CAA80307.1.
BC003813 mRNA. Translation: AAH03813.1.
BC092274 mRNA. Translation: AAH92274.1.
CCDSiCCDS21036.1.
PIRiS38342.
RefSeqiNP_032017.2. NM_007991.3.
XP_006543829.1. XM_006543766.1.
UniGeneiMm.4595.

3D structure databases

ProteinModelPortaliP35550.
SMRiP35550. Positions 93-321.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199604. 1 interaction.
IntActiP35550. 6 interactions.
MINTiMINT-1854224.

PTM databases

PhosphoSiteiP35550.

Proteomic databases

MaxQBiP35550.
PaxDbiP35550.
PRIDEiP35550.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000042405; ENSMUSP00000037613; ENSMUSG00000046865.
GeneIDi102643269.
14113.
KEGGimmu:102643269.
mmu:14113.
UCSCiuc009fxy.1. mouse.

Organism-specific databases

CTDi2091.
MGIiMGI:95486. Fbl.

Phylogenomic databases

eggNOGiCOG1889.
GeneTreeiENSGT00550000074792.
HOGENOMiHOG000106741.
HOVERGENiHBG002472.
InParanoidiP35550.
KOiK14563.
OMAiANEVNIM.
OrthoDBiEOG7KWSJP.
PhylomeDBiP35550.
TreeFamiTF300639.

Miscellaneous databases

ChiTaRSiFbl. mouse.
NextBioi285166.
PROiP35550.
SOURCEiSearch...

Gene expression databases

BgeeiP35550.
CleanExiMM_FBL.
GenevestigatoriP35550.

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]
PIRSFiPIRSF006540. Nop17p. 1 hit.
PRINTSiPR00052. FIBRILLARIN.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS00566. FIBRILLARIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and sequence analysis of U3 snoRNA-associated mouse fibrillarin."
    Turley S.J., Tan E.M., Pollard K.M.
    Biochim. Biophys. Acta 1216:119-122(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Macrophage.
  2. "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].
    Strain: FVB/N.
    Tissue: Liver and Mammary tumor.

Entry informationi

Entry nameiFBRL_MOUSE
AccessioniPrimary (citable) accession number: P35550
Secondary accession number(s): Q99L58
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: August 30, 2005
Last modified: February 4, 2015
This is version 119 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, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.