FBRL_RAT
ID FBRL_RAT Reviewed; 327 AA.
AC P22509; Q4KLH8;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=rRNA 2'-O-methyltransferase fibrillarin;
DE EC=2.1.1.- {ECO:0000250|UniProtKB:P22087};
DE AltName: Full=Histone-glutamine methyltransferase;
DE AltName: Full=Nucleolar protein 1;
DE AltName: Full=U6 snRNA 2'-O-methyltransferase fibrillarin {ECO:0000305};
GN Name=Fbl;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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 PROTEIN SEQUENCE OF 1-31, SUBCELLULAR LOCATION, AND METHYLATION AT ARG-8;
RP ARG-15; ARG-21; ARG-24; ARG-28 AND ARG-31.
RX PubMed=2414294; DOI=10.1016/s0021-9258(17)38718-5;
RA Lischwe M.A., Ochs R.L., Reddy R., Cook R.G., Yeoman L.C., Tan E.M.,
RA Reichlin M., Busch H.;
RT "Purification and partial characterization of a nucleolar scleroderma
RT antigen (Mr = 34,000; pI, 8.5) rich in NG,NG-dimethylarginine.";
RL J. Biol. Chem. 260:14304-14310(1985).
RN [3]
RP PROTEIN SEQUENCE OF 1-28, AND INTERACTION WITH NOLC1.
RX PubMed=10679015; DOI=10.1091/mbc.11.2.567;
RA Yang Y., Isaac C., Wang C., Dragon F., Pogacic V., Meier U.T.;
RT "Conserved composition of mammalian box H/ACA and box C/D small nucleolar
RT ribonucleoprotein particles and their interaction with the common factor
RT Nopp140.";
RL Mol. Biol. Cell 11:567-577(2000).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (By similarity). Site specificity
CC is provided by a guide RNA that base pairs with the substrate (By
CC similarity). Methylation occurs at a characteristic distance from the
CC sequence involved in base pairing with the guide RNA (By similarity).
CC Probably catalyzes 2'-O-methylation of U6 snRNAs in box C/D RNP
CC complexes. U6 snRNA 2'-O-methylation is required for mRNA splicing
CC fidelity. Also acts as a protein methyltransferase by mediating
CC methylation of 'Gln-105' of histone H2A (H2AQ104me), a modification
CC that impairs binding of the FACT complex and is specifically present at
CC 35S ribosomal DNA locus (By similarity). {ECO:0000250|UniProtKB:P15646,
CC ECO:0000250|UniProtKB:P22087}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutaminyl-[histone H2A] + S-adenosyl-L-methionine = H(+) +
CC N(5)-methyl-L-glutaminyl-[histone H2A] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:50904, Rhea:RHEA-COMP:12837, Rhea:RHEA-COMP:12839,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30011, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61891;
CC Evidence={ECO:0000250|UniProtKB:P22087};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleotide in rRNA + S-adenosyl-L-methionine = a 2'-O-
CC methylribonucleotide in rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:48628, Rhea:RHEA-COMP:12164, Rhea:RHEA-COMP:12165,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:90675, ChEBI:CHEBI:90676;
CC Evidence={ECO:0000250|UniProtKB:P15646};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48629;
CC Evidence={ECO:0000250|UniProtKB:P15646};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleotide in U6 snRNA + S-adenosyl-L-methionine = a 2'-
CC O-methylribonucleotide in U6 snRNA + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:63088, Rhea:RHEA-COMP:16262, Rhea:RHEA-
CC COMP:16263, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:90675, ChEBI:CHEBI:90676;
CC Evidence={ECO:0000250|UniProtKB:P22087};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63089;
CC Evidence={ECO:0000250|UniProtKB:P22087};
CC -!- SUBUNIT: Component of box C/D small nucleolar ribonucleoprotein
CC (snoRNP) particles that contain SNU13, FBL, NOP5 and NOP56, plus a
CC guide RNA. It is associated with the U3, U8, U13, X and Y small nuclear
CC RNAs. Component of several ribosomal and nucleolar protein complexes.
CC Interacts with PRMT5 and UTP20. Interacts with DDX5 and C1QBP.
CC Interacts with NOL11. Interacts with PIH1D1. Interacts with RRP1B (By
CC similarity). Interacts with NOLC1 (PubMed:10679015).
CC {ECO:0000250|UniProtKB:P22087, ECO:0000269|PubMed:10679015}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:2414294}.
CC Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P35550}. Note=Fibrillar
CC region of the nucleolus.
CC -!- PTM: Ubiquitinated. Ubiquitination leads to proteasomal degradation.
CC Deubiquitinated by USP36. {ECO:0000250|UniProtKB:P22087}.
CC -!- PTM: By homology to other fibrillarins, some or all of the N-terminal
CC domain arginines are modified to asymmetric dimethylarginine (DMA).
CC {ECO:0000269|PubMed:2414294}.
CC -!- PTM: Acetylated by CREBBP/CBP, preventing methylation of 'Gln-105' of
CC histone H2A (H2AQ104me), without affecting rRNA methylation.
CC Deacetylation by SIRT7 restores methylation of 'Gln-105' of histone H2A
CC (H2AQ104me). {ECO:0000250|UniProtKB:P22087}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Fibrillarin
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC099198; AAH99198.1; -; mRNA.
DR PIR; A23887; A23887.
DR RefSeq; NP_001020814.1; NM_001025643.1.
DR AlphaFoldDB; P22509; -.
DR SMR; P22509; -.
DR BioGRID; 253952; 3.
DR IntAct; P22509; 3.
DR STRING; 10116.ENSRNOP00000026021; -.
DR iPTMnet; P22509; -.
DR PhosphoSitePlus; P22509; -.
DR jPOST; P22509; -.
DR PaxDb; P22509; -.
DR PRIDE; P22509; -.
DR GeneID; 292747; -.
DR KEGG; rno:292747; -.
DR UCSC; RGD:1305542; rat.
DR CTD; 2091; -.
DR RGD; 1305542; Fbl.
DR VEuPathDB; HostDB:ENSRNOG00000019229; -.
DR eggNOG; KOG1596; Eukaryota.
DR HOGENOM; CLU_059055_1_0_1; -.
DR InParanoid; P22509; -.
DR OMA; INMATHR; -.
DR OrthoDB; 1411035at2759; -.
DR PhylomeDB; P22509; -.
DR TreeFam; TF300639; -.
DR Reactome; R-RNO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:P22509; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000019229; Expressed in spleen and 19 other tissues.
DR Genevisible; P22509; RN.
DR GO; GO:0031428; C:box C/D RNP complex; IBA:GO_Central.
DR GO; GO:0015030; C:Cajal body; IDA:RGD.
DR GO; GO:0005694; C:chromosome; IDA:RGD.
DR GO; GO:0001651; C:dense fibrillar component; IDA:UniProtKB.
DR GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
DR GO; GO:0001652; C:granular component; ISO:RGD.
DR GO; GO:0005730; C:nucleolus; IDA:RGD.
DR GO; GO:0005654; C:nucleoplasm; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR GO; GO:0051117; F:ATPase binding; ISO:RGD.
DR GO; GO:1990259; F:histone-glutamine methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISO:RGD.
DR GO; GO:0008649; F:rRNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0001094; F:TFIID-class transcription factor complex binding; ISO:RGD.
DR GO; GO:0000494; P:box C/D RNA 3'-end processing; IBA:GO_Central.
DR GO; GO:1990258; P:histone glutamine methylation; ISS:UniProtKB.
DR GO; GO:0031167; P:rRNA methylation; ISS:UniProtKB.
DR GO; GO:0016074; P:sno(s)RNA metabolic process; ISO:RGD.
DR GO; GO:0048254; P:snoRNA localization; ISO:RGD.
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 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Isopeptide bond; Methylation;
KW Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; RNA-binding; rRNA processing; S-adenosyl-L-methionine;
KW Transferase; Ubl conjugation.
FT CHAIN 1..327
FT /note="rRNA 2'-O-methyltransferase fibrillarin"
FT /id="PRO_0000148509"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 178..179
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9Y9U3"
FT BINDING 197..198
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P22087"
FT BINDING 222..223
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P22087"
FT BINDING 242..245
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P22087"
FT MOD_RES 8
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:2414294"
FT MOD_RES 15
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:2414294"
FT MOD_RES 21
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:2414294"
FT MOD_RES 24
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:2414294"
FT MOD_RES 28
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:2414294"
FT MOD_RES 31
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:2414294"
FT MOD_RES 108
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P22087"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22087"
FT MOD_RES 127
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P22087"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22087"
FT MOD_RES 211
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P22087"
FT MOD_RES 212
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P22087"
FT CROSSLNK 90
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P22087"
FT CROSSLNK 108
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P22087"
FT CROSSLNK 115
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P22087"
FT CROSSLNK 137
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P22087"
FT CROSSLNK 149
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P22087"
FT CROSSLNK 164
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P22087"
FT CONFLICT 2
FT /note="K -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 327 AA; 34222 MW; 0E22E63175808BAE CRC64;
MKPGFSPRGG GFGGRGGFGD RGGRGGGRGG RGGFGGGRGG FGGGGRGRGG GGGGFRGRGG
GGGRGGGFQS GGGRGRGGGR GGKRGNQSGK NVMVEPHRHE GVFICRGKED ALVTKNLVPG
ESVYGEKRVS ISEGDDKIEY RAWNPFRSKL AAAILGGVDQ IHIKPGAKVL YLGAASGTTV
SHVSDIVGPD GLVYAVEFSH RSGRDLINLA KKRTNIIPVI EDARHPHKYR MLIAMVDVIF
ADVAQPDQTR IVALNAHTFL RNGGHFVISI KANCIDSTAS AEAVFASEVK KMQQENMKPQ
EQLTLEPYER DHAVVVGVYR PPPKAKN
