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P22509 (FBRL_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
rRNA 2'-O-methyltransferase fibrillarin
EC=2.1.1.-
Alternative name(s):
Nucleolar protein 1
Gene names
Name:Fbl
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

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

General annotation (Comments)

Function

Involved in pre-rRNA processing. Utilizes the methyl donor S-adenosyl-L-methionine to catalyze 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 By similarity.

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 and UTP20 By similarity. Interacts with NOLC1. Ref.3

Subcellular location

Nucleus › nucleolus. Note: Fibrillar region of the nucleolus. Ref.2

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
PRO_0000148509

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

Sites

Binding site1491S-adenosyl-L-methionine By similarity
Binding site2421S-adenosyl-L-methionine By similarity

Amino acid modifications

Modified residue81Asymmetric dimethylarginine Ref.2
Modified residue151Asymmetric dimethylarginine Ref.2
Modified residue211Asymmetric dimethylarginine Ref.2
Modified residue241Asymmetric dimethylarginine Ref.2
Modified residue281Asymmetric dimethylarginine Ref.2
Modified residue311Asymmetric dimethylarginine Ref.2
Modified residue1301Phosphoserine By similarity
Modified residue2111N6-acetyllysine By similarity

Experimental info

Sequence conflict21K → D AA sequence Ref.3

Sequences

Sequence LengthMass (Da)Tools
P22509 [UniParc].

Last modified August 30, 2005. Version 2.
Checksum: 0E22E63175808BAE

FASTA32734,222
        10         20         30         40         50         60 
MKPGFSPRGG GFGGRGGFGD RGGRGGGRGG RGGFGGGRGG FGGGGRGRGG GGGGFRGRGG 

        70         80         90        100        110        120 
GGGRGGGFQS GGGRGRGGGR 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 PPPKAKN

« Hide

References

« Hide 'large scale' references
[1]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Thymus.
[2]"Purification and partial characterization of a nucleolar scleroderma antigen (Mr = 34,000; pI, 8.5) rich in NG,NG-dimethylarginine."
Lischwe M.A., Ochs R.L., Reddy R., Cook R.G., Yeoman L.C., Tan E.M., Reichlin M., Busch H.
J. Biol. Chem. 260:14304-14310(1985) [PubMed: 2414294] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-31, SUBCELLULAR LOCATION, METHYLATION AT ARG-8; ARG-15; ARG-21; ARG-24; ARG-28 AND ARG-31.
[3]"Conserved composition of mammalian box H/ACA and box C/D small nucleolar ribonucleoprotein particles and their interaction with the common factor Nopp140."
Yang Y., Isaac C., Wang C., Dragon F., Pogacic V., Meier U.T.
Mol. Biol. Cell 11:567-577(2000) [PubMed: 10679015] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-28, INTERACTION WITH NOLC1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC099198 mRNA. Translation: AAH99198.1.
IPIIPI00208091.
PIRA23887.
RefSeqNP_001020814.1. NM_001025643.1.
UniGeneRn.98803.

3D structure databases

ProteinModelPortalP22509.
SMRP22509. Positions 93-321.
ModBaseSearch...

Protein-protein interaction databases

STRINGP22509.

PTM databases

PhosphoSiteP22509.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000026021; ENSRNOP00000026021; ENSRNOG00000019229.
GeneID292747.
KEGGrno:292747.
NMPDRfig|10116.3.peg.1394.
UCSCNM_001025643. rat.

Organism-specific databases

CTD2091.
RGD1305542. Fbl.

Phylogenomic databases

eggNOGmaNOG11735.
GeneTreeENSGT00550000074792.
HOVERGENHBG002472.
InParanoidP22509.
OMAYERDHCI.
OrthoDBEOG4K3KX0.
PhylomeDBP22509.

Gene expression databases

ArrayExpressP22509.
GenevestigatorP22509.
GermOnlineENSRNOG00000019229. Rattus norvegicus.

Family and domain databases

InterProIPR000692. Fibrillarin.
IPR020813. Fibrillarin_CS.
[Graphical view]
KOK14563.
PANTHERPTHR10335. Fibrillarin. 1 hit.
PfamPF01269. Fibrillarin. 1 hit.
[Graphical view]
PIRSFPIRSF006540. Nop17p. 1 hit.
PRINTSPR00052. FIBRILLARIN.
PROSITEPS00566. FIBRILLARIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio634662.

Entry information

Entry nameFBRL_RAT
AccessionPrimary (citable) accession number: P22509
Secondary accession number(s): Q4KLH8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 30, 2005
Last modified: November 16, 2011
This is version 75 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

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