FBL
entrez
2091
canonical
uniprot
P22087
canonical
ensembl
ENSG00000105202
resolver
ensembl
ENSG00000280548
resolver
ensp
ENSP00000221801
resolver
ensp
ENSP00000487390
resolver
ensp
ENSP00000572478
resolver
ensp
ENSP00000762721
resolver
enst
ENST00000221801
resolver
enst
ENST00000625241
resolver
genesymbol
FBL
resolver
genesymbol_syn
FIB1
resolver
genesymbol_syn
FLRN
resolver
hgnc
HGNC:3599
resolver
uniprot
B5BUE8
resolver
uniprot
O75259
resolver
uniprot
Q6IAT5
resolver
uniprot
Q9UPI6
resolver
uniprot_entry
FBRL_HUMAN
resolver
uniprot_sec
B5BUE8
resolver
uniprot_sec
O75259
resolver
uniprot_sec
Q6IAT5
resolver
uniprot_sec
Q9UPI6
resolver
amino_acid_sequence
MKPGFSPRGGGFGGRGGFGDRGGRGGRGGFGGGRGRGGGFRGRGRGGGGGGGGGGGGGRGGGGFHSGGNRGRGRGGKRGNQSGKNVMVEPHRHEGVFICRGKEDALVTKNLVPGESVYGEKRVSISEGDDKIEYRAWNPFRSKLAAAILGGVDQIHIKPGAKVLYLGAASGTTVSHVSDIVGPDGLVYAVEFSHRSGRDLINLAKKRTNIIPVIEDARHPHKYRMLIAMVDVIFADVAQPDQTRIVALNAHTFLRNGGHFVISIKANCIDSTASAEAVFASEVKKMQQENMKPQEQLTLEPYERDHAVVVGVYRPPPKVKN
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:24352239, PubMed:30540930, PubMed:32017898). Involved in pre-rRNA processing by catalyzing the site-specific 2'-hydroxyl methylation of ribose moieties in pre-ribosomal RNA (PubMed:30540930). 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:32017898). U6 snRNA 2'-O-methylation is required for mRNA splicing fidelity (PubMed:32017898). 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 (PubMed:24352239, PubMed:30540930). 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 (PubMed:34516797). {ECO:0000250|UniProtKB:P15646, ECO:0000269|PubMed:24352239, ECO:0000269|PubMed:30540930, ECO:0000269|PubMed:32017898, ECO:0000269|PubMed:34516797}.
uniprot
proteins
mass_dalton
33784
uniprot
proteins
mutagenesis
MUTAGEN 102; /note="K->Q: Mimics acetylation; impaired ability to methylate histone H2A; when associated with Q-121 and 205-Q-Q-206."; /evidence="ECO:0000269|PubMed:30540930"; MUTAGEN 102; /note="K->R: Decreased acetylation; restores ability to methylate histone H2A; when associated with R-121 and 205-R-R-206."; /evidence="ECO:0000269|PubMed:30540930"; MUTAGEN 121; /note="K->Q: Mimics acetylation; impaired ability to methylate histone H2A; when associated with Q-102 and 205-Q-Q-206."; /evidence="ECO:0000269|PubMed:30540930"; MUTAGEN 121; /note="K->R: Decreased acetylation; restores ability to methylate histone H2A; when associated with R-102 and 205-R-R-206."; /evidence="ECO:0000269|PubMed:30540930"; MUTAGEN 205..206; /note="KK->QQ: Mimics acetylation; impaired ability to methylate histone H2A; when associated with Q-102 and Q-121."; /evidence="ECO:0000269|PubMed:30540930"; MUTAGEN 205..206; /note="KK->RR: Decreased acetylation; restores ability to methylate histone H2A; when associated with R-102 and R-121."; /evidence="ECO:0000269|PubMed:30540930
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated. Ubiquitination leads to proteasomal degradation (PubMed:19208757). Deubiquitinated by USP36 (PubMed:19208757). {ECO:0000269|PubMed:19208757}.; 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: Acetylated by CREBBP/CBP, preventing methylation of 'Gln-105' of histone H2A (H2AQ104me), without affecting rRNA methylation (PubMed:30540930). Deacetylation by SIRT7 restores methylation of 'Gln-105' of histone H2A (H2AQ104me) (PubMed:30540930). {ECO:0000269|PubMed:30540930}.
uniprot
proteins
protein_family
Fibrillarin family
uniprot
proteins
protein_family
Methyltransferase superfamily
uniprot
proteins
pubmed
10837141
uniprot
proteins
pubmed
14583623
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1714385
uniprot
proteins
pubmed
17498821
uniprot
proteins
pubmed
17636026
uniprot
proteins
pubmed
1846968
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19054851
uniprot
proteins
pubmed
19208757
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
2026646
uniprot
proteins
pubmed
20926688
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21536856
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
22916032
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
2414294
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24352239
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
30540930
uniprot
proteins
pubmed
32017898
uniprot
proteins
pubmed
34365507
uniprot
proteins
pubmed
34516797
uniprot
proteins
pubmed
36161484
uniprot
proteins
sequence_length
321
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14583623, ECO:0000269|PubMed:19208757, ECO:0000269|PubMed:2026646, ECO:0000269|PubMed:2414294, ECO:0000269|PubMed:24352239, ECO:0000269|PubMed:34516797}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P35550}. Note=Fibrillar region of the nucleolus.
uniprot
proteins