FBLL1_HUMAN
ID FBLL1_HUMAN Reviewed; 334 AA.
AC A6NHQ2; R4GMW7;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2015, sequence version 2.
DT 03-AUG-2022, entry version 103.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
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; AC020894; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS87345.1; -.
DR AlphaFoldDB; A6NHQ2; -.
DR SMR; A6NHQ2; -.
DR IntAct; A6NHQ2; 6.
DR MINT; A6NHQ2; -.
DR STRING; 9606.ENSP00000473383; -.
DR iPTMnet; A6NHQ2; -.
DR PhosphoSitePlus; A6NHQ2; -.
DR BioMuta; FBLL1; -.
DR EPD; A6NHQ2; -.
DR jPOST; A6NHQ2; -.
DR MassIVE; A6NHQ2; -.
DR PeptideAtlas; A6NHQ2; -.
DR PRIDE; A6NHQ2; -.
DR ProteomicsDB; 1216; -.
DR Antibodypedia; 71194; 8 antibodies from 4 providers.
DR Ensembl; ENST00000338333.5; ENSP00000473383.1; ENSG00000188573.8.
DR MANE-Select; ENST00000338333.5; ENSP00000473383.1; NM_001355274.2; NP_001342203.1.
DR UCSC; uc011dep.3; human.
DR GeneCards; FBLL1; -.
DR HGNC; HGNC:35458; FBLL1.
DR HPA; ENSG00000188573; Group enriched (brain, pituitary gland).
DR neXtProt; NX_A6NHQ2; -.
DR OpenTargets; ENSG00000188573; -.
DR VEuPathDB; HostDB:ENSG00000188573; -.
DR eggNOG; KOG1596; Eukaryota.
DR GeneTree; ENSGT00550000074792; -.
DR HOGENOM; CLU_059055_1_0_1; -.
DR OMA; KLEYRTW; -.
DR PhylomeDB; A6NHQ2; -.
DR PathwayCommons; A6NHQ2; -.
DR SignaLink; A6NHQ2; -.
DR Pharos; A6NHQ2; Tdark.
DR PRO; PR:A6NHQ2; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; A6NHQ2; protein.
DR Bgee; ENSG00000188573; Expressed in prefrontal cortex and 142 other tissues.
DR Genevisible; A6NHQ2; HS.
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; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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; IEA:Ensembl.
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 PRINTS; PR00052; FIBRILLARIN.
DR SMART; SM01206; Fibrillarin; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS00566; FIBRILLARIN; 1.
PE 3: Inferred from homology;
KW Methylation; Methyltransferase; Nucleus; Reference proteome;
KW Ribonucleoprotein; RNA-binding; rRNA processing; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..333
FT /note="rRNA/tRNA 2'-O-methyltransferase fibrillarin-like
FT protein 1"
FT /id="PRO_0000331762"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 184..185
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 203..204
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 228..229
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 248..251
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT MOD_RES 15
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q80WS3"
SQ SEQUENCE 334 AA; 34803 MW; 01C9A3155FAC0930 CRC64;
MKSAASSRGG GGGGRGGGGW GSWGGGRGGG GGAGKGGGGD GGGQGGKGGF GARARGFGGG
GRGRGRGGGD GKDRGGGGQR RGGVAKSKSR RRKGAMVVSV EPHRHEGVFI YRGAEDALVT
LNMVPGQSVY GERRVTVTEG GVKQEYRTWN PFRSKLAAAI LGGVDQIHIK PKSKVLYLGA
ASGTTVSHVS DIIGPDGLVY AVEFSHRAGR DLVNVAKKRT NIIPVLEDAR HPLKYRMLIG
MVDVIFADVA QPDQSRIVAL NAHTFLRNGG HFLISIKANC IDSTASAEAV FASEVRKLQQ
ENLKPQEQLT LEPYERDHAV VVGVYRPLPK SSSK
