FBLL1_MOUSE
ID FBLL1_MOUSE Reviewed; 314 AA.
AC Q80WS3;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=rRNA/tRNA 2'-O-methyltransferase fibrillarin-like protein 1;
DE EC=2.1.1.-;
DE AltName: Full=Protein-glutamine methyltransferase;
GN Name=Fbll1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-7, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that has
CC the ability to methylate both RNAs and proteins. Involved in pre-rRNA
CC processing by catalyzing the site-specific 2'-hydroxyl methylation of
CC ribose moieties in pre-ribosomal RNA. Also acts as a protein
CC methyltransferase by mediating methylation of glutamine residues (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Note=Fibrillar region of the
CC nucleolus. {ECO:0000250}.
CC -!- PTM: By homology to other fibrillarins, some or all of the N-terminal
CC domain arginines are modified to asymmetric dimethylarginine (DMA).
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Fibrillarin
CC family. {ECO:0000305}.
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DR EMBL; BC052068; AAH52068.1; -; mRNA.
DR CCDS; CCDS36128.1; -.
DR RefSeq; NP_001004147.1; NM_001004147.3.
DR AlphaFoldDB; Q80WS3; -.
DR SMR; Q80WS3; -.
DR BioGRID; 231898; 1.
DR STRING; 10090.ENSMUSP00000128889; -.
DR iPTMnet; Q80WS3; -.
DR PhosphoSitePlus; Q80WS3; -.
DR EPD; Q80WS3; -.
DR MaxQB; Q80WS3; -.
DR PaxDb; Q80WS3; -.
DR PeptideAtlas; Q80WS3; -.
DR PRIDE; Q80WS3; -.
DR ProteomicsDB; 271871; -.
DR Antibodypedia; 71194; 8 antibodies from 4 providers.
DR DNASU; 237730; -.
DR Ensembl; ENSMUST00000160726; ENSMUSP00000128889; ENSMUSG00000051062.
DR GeneID; 237730; -.
DR KEGG; mmu:237730; -.
DR UCSC; uc007ilg.1; mouse.
DR CTD; 345630; -.
DR MGI; MGI:3034689; Fbll1.
DR VEuPathDB; HostDB:ENSMUSG00000051062; -.
DR eggNOG; KOG1596; Eukaryota.
DR GeneTree; ENSGT00550000074792; -.
DR HOGENOM; CLU_059055_1_0_1; -.
DR InParanoid; Q80WS3; -.
DR OMA; KLEYRTW; -.
DR OrthoDB; 1411035at2759; -.
DR PhylomeDB; Q80WS3; -.
DR TreeFam; TF300639; -.
DR BioGRID-ORCS; 237730; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q80WS3; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q80WS3; protein.
DR Bgee; ENSMUSG00000051062; Expressed in central gray substance of midbrain and 75 other tissues.
DR Genevisible; Q80WS3; MM.
DR GO; GO:0031428; C:box C/D RNP complex; IBA:GO_Central.
DR GO; GO:0015030; C:Cajal body; IBA:GO_Central.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR GO; GO:1990259; F:histone-glutamine methyltransferase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0008649; F:rRNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0001835; P:blastocyst hatching; IMP:MGI.
DR GO; GO:0000494; P:box C/D RNA 3'-end processing; IBA:GO_Central.
DR GO; GO:1990258; P:histone glutamine methylation; IBA:GO_Central.
DR GO; GO:0031167; P:rRNA methylation; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_00351; RNA_methyltransf_FlpA; 1.
DR InterPro; IPR000692; Fibrillarin.
DR InterPro; IPR020813; Fibrillarin_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF01269; Fibrillarin; 1.
DR PIRSF; PIRSF006540; Nop17p; 1.
DR PRINTS; PR00052; FIBRILLARIN.
DR SMART; SM01206; Fibrillarin; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS00566; FIBRILLARIN; 1.
PE 1: Evidence at protein level;
KW Methylation; Methyltransferase; Nucleus; Reference proteome;
KW Ribonucleoprotein; RNA-binding; rRNA processing; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..314
FT /note="rRNA/tRNA 2'-O-methyltransferase fibrillarin-like
FT protein 1"
FT /id="PRO_0000331763"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 166..167
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 185..186
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 210..211
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 230..233
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT MOD_RES 7
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
SQ SEQUENCE 314 AA; 33339 MW; FF5E0D2A60A8BA72 CRC64;
MKPAGGRGGW GWGGGKGGSK GGDTGSGTKG GFGARTRGSS GGGRGRGRGG GGGGGGGGGD
RQRRGGPGKN KNRRKKGITV SVEPHRHEGV FIYRGAEDAL VTLNMVPGVS VYGEKRVTVM
ENGEKQEYRT WNPFRSKLAA AILGGVDQIH IKPKSKVLYL GAASGTTVSH VSDIIGPDGL
VYAVEFSHRA GRDLVNVAKK RTNIIPVLED ARHPLKYRML IGMVDVIFAD VAQPDQSRIV
ALNAHTFLRN GGHFLISIKA NCIDSTASAE AVFASEVRKL QQENLKPQEQ LTLEPYERDH
AVVVGVYRPP PKSK
