P35550 (FBRL_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 101.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: rRNA 2'-O-methyltransferase fibrillarin EC=2.1.1.- Alternative name(s): Nucleolar protein 1 | ||
| Gene names |
| ||
| Organism | Mus musculus (Mouse) [Reference proteome] | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 327 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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, NOLC1 and UTP20. Interacts with DDX5 and C1QBP By similarity. |
| Subcellular location | Nucleus › nucleolus. Note: Fibrillar region of the nucleolus. |
| Post-translational modification | By homology to other fibrillarins, some or all of the N-terminal domain arginines are modified to asymmetric dimethylarginine (DMA). |
| Sequence similarities | Belongs to the methyltransferase superfamily. Fibrillarin family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | rRNA processing |
| Cellular component | Nucleus |
| Ligand | RNA-binding |
| Molecular function | Methyltransferase Ribonucleoprotein Transferase |
| PTM | Methylation Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | rRNA processing Traceable author statement Ref.1. Source: MGI snoRNA metabolic processInferred from mutant phenotype PubMed 14612397. Source: MGI tRNA processingInferred from electronic annotation. Source: InterPro |
| Cellular_component | Cajal body Inferred from direct assay PubMed 7768196. Source: MGI granular componentInferred from direct assay PubMed 15485902. Source: MGI ribonucleoprotein complexInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | methyltransferase activity Inferred from electronic annotation. Source: UniProtKB-KW snoRNA bindingTraceable author statement Ref.1. Source: MGI |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 327 | 327 | rRNA 2'-O-methyltransferase fibrillarin | PRO_0000148508 | |||||
Regions | |||||||||
| Region | 178 – 179 | 2 | S-adenosyl-L-methionine binding By similarity | ||||||
| Region | 197 – 198 | 2 | S-adenosyl-L-methionine binding By similarity | ||||||
| Region | 222 – 223 | 2 | S-adenosyl-L-methionine binding By similarity | ||||||
| Compositional bias | 4 – 85 | 82 | DMA/Gly-rich | ||||||
Sites | |||||||||
| Binding site | 149 | 1 | S-adenosyl-L-methionine By similarity | ||||||
| Binding site | 242 | 1 | S-adenosyl-L-methionine By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 8 | 1 | Asymmetric dimethylarginine By similarity | ||||||
| Modified residue | 15 | 1 | Asymmetric dimethylarginine By similarity | ||||||
| Modified residue | 21 | 1 | Asymmetric dimethylarginine By similarity | ||||||
| Modified residue | 24 | 1 | Asymmetric dimethylarginine By similarity | ||||||
| Modified residue | 28 | 1 | Asymmetric dimethylarginine By similarity | ||||||
| Modified residue | 31 | 1 | Asymmetric dimethylarginine By similarity | ||||||
| Modified residue | 130 | 1 | Phosphoserine Ref.3 | ||||||
Experimental info | |||||||||
| Sequence conflict | 6 | 1 | S → R in CAA80307. Ref.1 | ||||||
| Sequence conflict | 63 | 1 | G → V in CAA80307. Ref.1 | ||||||
| Sequence conflict | 113 | 1 | V → F in CAA80307. Ref.1 | ||||||
| Sequence conflict | 137 | 1 | K → T in CAA80307. Ref.1 | ||||||
Sequences
| ||||||||||||||||||
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. |
| [3] | "Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, MASS SPECTROMETRY. Tissue: Melanoma. |
| + | 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. |
| IPI | IPI00119581. |
| PIR | S38342. |
| RefSeq | NP_032017.2. NM_007991.3. XP_001472922.1. XM_001472872.3. |
| UniGene | Mm.4595. |
3D structure databases | |
| ProteinModelPortal | P35550. |
| SMR | P35550. Positions 93-321. |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | P35550. |
Proteomic databases | |
| PaxDb | P35550. |
| PRIDE | P35550. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000042405; ENSMUSP00000037613; ENSMUSG00000046865. |
| GeneID | 100044829. 14113. |
| KEGG | mmu:100044829. mmu:14113. |
| UCSC | uc009fxy.1. mouse. |
Organism-specific databases | |
| CTD | 2091. |
| MGI | MGI:95486. Fbl. |
Phylogenomic databases | |
| eggNOG | COG1889. |
| GeneTree | ENSGT00550000074792. |
| HOGENOM | HOG000106741. |
| HOVERGEN | HBG002472. |
| InParanoid | P35550. |
| KO | K14563. |
| OMA | VGMVDTI. |
| OrthoDB | EOG4K3KX0. |
Gene expression databases | |
| Bgee | P35550. |
| CleanEx | MM_FBL. |
| Genevestigator | P35550. |
| GermOnline | ENSMUSG00000046865. Mus musculus. |
Family and domain databases | |
| InterPro | IPR000692. Fibrillarin. IPR020813. Fibrillarin_CS. [Graphical view] |
| PANTHER | PTHR10335. PTHR10335. 1 hit. |
| Pfam | PF01269. Fibrillarin. 1 hit. [Graphical view] |
| PIRSF | PIRSF006540. Nop17p. 1 hit. |
| PRINTS | PR00052. FIBRILLARIN. |
| PROSITE | PS00566. FIBRILLARIN. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| ChiTaRS | FBL. mouse. |
| NextBio | 285166. |
| SOURCE | Search... |
Entry information
| Entry name | FBRL_MOUSE | ||||||||
| Accession | Primary (citable) accession number: P35550 Secondary accession number(s): Q99L58 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
