Fbl
entrez
14113
canonical
uniprot
P35550
canonical
ensembl
ENSMUSG00000046865
resolver
ensp
ENSMUSP00000037613
resolver
ensp
ENSMUSP00000173885
resolver
enst
ENSMUST00000042405
resolver
genesymbol
Fbl
resolver
uniprot
Q99L58
resolver
uniprot_entry
FBRL_MOUSE
resolver
uniprot_sec
Q99L58
resolver
amino_acid_sequence
MKPGFSPRGGGFGGRGGFGDRGGRGGGRGGRGGFGGGRGGFGGGGRGRGGGGGGFRGRGGGGGRGGGFQSGGNRGRGGGRGGKRGNQSGKNVMVEPHRHEGVFICRGKEDALVTKNLVPGESVYGEKRVSISEGDDKIEYRAWNPFRSKLAAAILGGVDQIHIKPGAKVLYLGAASGTTVSHVSDIVGPDGLVYAVEFSHRSGRDLINLAKKRTNIIPVIEDARHPHKYRMLIAMVDVIFADVAQPDQTRIVALNAHTFLRNGGHFVISIKANCIDSTASAEAVFASEVKKMQQENMKPQEQLTLEPYERDHAVVVGVYRPPPKVKN
uniprot
proteins
ec_number
2.1.1.-
uniprot
proteins
function
FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that has the ability to methylate both RNAs and proteins (PubMed:32017896). Involved in pre-rRNA processing by catalyzing the site-specific 2'-hydroxyl methylation of ribose moieties in pre-ribosomal RNA (By similarity). Site specificity is provided by a guide RNA that base pairs with the substrate (By similarity). Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA (By similarity). Probably catalyzes 2'-O-methylation of U6 snRNAs in box C/D RNP complexes (PubMed:32017896). U6 snRNA 2'-O-methylation is required for mRNA splicing fidelity (PubMed:32017896). 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). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (By similarity). {ECO:0000250|UniProtKB:P15646, ECO:0000250|UniProtKB:P22087, ECO:0000269|PubMed:32017896}.
uniprot
proteins
mass_dalton
34307
uniprot
proteins
post_translational_modification
PTM: By homology to other fibrillarins, some or all of the N-terminal domain arginines are modified to asymmetric dimethylarginine (DMA). {ECO:0000250|UniProtKB:P22509}.; PTM: Ubiquitinated. Ubiquitination leads to proteasomal degradation. Deubiquitinated by USP36. {ECO:0000250|UniProtKB:P22087}.; PTM: Acetylated by CREBBP/CBP, preventing methylation of 'Gln-105' of histone H2A (H2AQ104me), without affecting rRNA methylation. Deacetylation by SIRT7 restores methylation of 'Gln-105' of histone H2A (H2AQ104me). {ECO:0000250|UniProtKB:P22087}.
uniprot
proteins
protein_family
Fibrillarin family
uniprot
proteins
protein_family
Methyltransferase superfamily
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
30283081
uniprot
proteins
pubmed
32017896
uniprot
proteins
pubmed
8218401
uniprot
proteins
sequence_length
327
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:30283081}. Nucleus, nucleoplasm {ECO:0000305|PubMed:32017896}. Note=Fibrillar region of the nucleolus. {ECO:0000250|UniProtKB:P22087}.
uniprot
proteins