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P35550 (FBRL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
rRNA 2'-O-methyltransferase fibrillarin

EC=2.1.1.-
Alternative name(s):
Histone-glutamine methyltransferase
Nucleolar protein 1
Gene names
Name:Fbl
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length327 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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. HAMAP-Rule MF_00351

Catalytic activity

S-adenosyl-L-methionine + L-glutamine-[histone] = S-adenosyl-L-homocysteine + N(5)-methyl-L-glutamine-[histone]. HAMAP-Rule MF_00351

Subunit structure

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.

Subcellular location

Nucleusnucleolus. Note: Fibrillar region of the nucleolus. HAMAP-Rule MF_00351

Post-translational modification

By homology to other fibrillarins, some or all of the N-terminal domain arginines are modified to asymmetric dimethylarginine (DMA). HAMAP-Rule MF_00351

Sequence similarities

Belongs to the methyltransferase superfamily. Fibrillarin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 327327rRNA 2'-O-methyltransferase fibrillarin HAMAP-Rule MF_00351
PRO_0000148508

Regions

Region178 – 1792S-adenosyl-L-methionine binding By similarity
Region197 – 1982S-adenosyl-L-methionine binding By similarity
Region222 – 2232S-adenosyl-L-methionine binding By similarity
Region242 – 2454S-adenosyl-L-methionine binding By similarity
Compositional bias4 – 8582DMA/Gly-rich HAMAP-Rule MF_00351

Amino acid modifications

Modified residue81Asymmetric dimethylarginine By similarity
Modified residue151Asymmetric dimethylarginine By similarity
Modified residue211Asymmetric dimethylarginine By similarity
Modified residue241Asymmetric dimethylarginine By similarity
Modified residue281Asymmetric dimethylarginine By similarity
Modified residue311Asymmetric dimethylarginine By similarity
Modified residue1301Phosphoserine By similarity

Experimental info

Sequence conflict61S → R in CAA80307. Ref.1
Sequence conflict631G → V in CAA80307. Ref.1
Sequence conflict1131V → F in CAA80307. Ref.1
Sequence conflict1371K → T in CAA80307. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P35550 [UniParc].

Last modified August 30, 2005. Version 2.
Checksum: 0E22FE7C758089C3

FASTA32734,307
        10         20         30         40         50         60 
MKPGFSPRGG GFGGRGGFGD RGGRGGGRGG RGGFGGGRGG FGGGGRGRGG GGGGFRGRGG 

        70         80         90        100        110        120 
GGGRGGGFQS GGNRGRGGGR GGKRGNQSGK NVMVEPHRHE GVFICRGKED ALVTKNLVPG 

       130        140        150        160        170        180 
ESVYGEKRVS ISEGDDKIEY RAWNPFRSKL AAAILGGVDQ IHIKPGAKVL YLGAASGTTV 

       190        200        210        220        230        240 
SHVSDIVGPD GLVYAVEFSH RSGRDLINLA KKRTNIIPVI EDARHPHKYR MLIAMVDVIF 

       250        260        270        280        290        300 
ADVAQPDQTR IVALNAHTFL RNGGHFVISI KANCIDSTAS AEAVFASEVK KMQQENMKPQ 

       310        320 
EQLTLEPYER DHAVVVGVYR PPPKVKN 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z22593 mRNA. Translation: CAA80307.1.
BC003813 mRNA. Translation: AAH03813.1.
BC092274 mRNA. Translation: AAH92274.1.
CCDSCCDS21036.1.
PIRS38342.
RefSeqNP_032017.2. NM_007991.3.
XP_006543829.1. XM_006543766.1.
UniGeneMm.4595.

3D structure databases

ProteinModelPortalP35550.
SMRP35550. Positions 93-321.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199604. 1 interaction.
IntActP35550. 6 interactions.
MINTMINT-1854224.

PTM databases

PhosphoSiteP35550.

Proteomic databases

MaxQBP35550.
PaxDbP35550.
PRIDEP35550.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000042405; ENSMUSP00000037613; ENSMUSG00000046865.
GeneID102643269.
14113.
KEGGmmu:102643269.
mmu:14113.
UCSCuc009fxy.1. mouse.

Organism-specific databases

CTD2091.
MGIMGI:95486. Fbl.

Phylogenomic databases

eggNOGCOG1889.
GeneTreeENSGT00550000074792.
HOGENOMHOG000106741.
HOVERGENHBG002472.
InParanoidP35550.
KOK14563.
OMAWNPNKSK.
OrthoDBEOG7KWSJP.
PhylomeDBP35550.
TreeFamTF300639.

Gene expression databases

BgeeP35550.
CleanExMM_FBL.
GenevestigatorP35550.

Family and domain databases

Gene3D3.40.50.150. 1 hit.
HAMAPMF_00351. RNA_methyltransf_FlpA.
InterProIPR000692. Fibrillarin.
IPR020813. Fibrillarin_CS.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PfamPF01269. Fibrillarin. 1 hit.
[Graphical view]
PIRSFPIRSF006540. Nop17p. 1 hit.
PRINTSPR00052. FIBRILLARIN.
SUPFAMSSF53335. SSF53335. 1 hit.
PROSITEPS00566. FIBRILLARIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFBL. mouse.
NextBio285166.
PROP35550.
SOURCESearch...

Entry information

Entry nameFBRL_MOUSE
AccessionPrimary (citable) accession number: P35550
Secondary accession number(s): Q99L58
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: August 30, 2005
Last modified: July 9, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot