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rRNA 2'-O-methyltransferase fibrillarin (EC 2.1.1.-) (34 kDa nucleolar scleroderma antigen) (Histone-glutamine methyltransferase)

 FBRL_HUMAN              Reviewed;         321 AA.
P22087; B5BUE8; O75259; Q6IAT5; Q9UPI6;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
20-JUN-2001, sequence version 2.
10-OCT-2018, entry version 192.
RecName: Full=rRNA 2'-O-methyltransferase fibrillarin;
EC=2.1.1.-;
AltName: Full=34 kDa nucleolar scleroderma antigen;
AltName: Full=Histone-glutamine methyltransferase;
Name=FBL; Synonyms=FIB1, FLRN;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1846968; DOI=10.1073/pnas.88.3.931;
Aris J.P., Blobel G.;
"cDNA cloning and sequencing of human fibrillarin, a conserved
nucleolar protein recognized by autoimmune antisera.";
Proc. Natl. Acad. Sci. U.S.A. 88:931-935(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
TISSUE=Cervix carcinoma;
PubMed=2026646; DOI=10.1083/jcb.113.4.715;
Jansen R.P., Hurt E.C., Kern H., Lehtonen H., Carmo-Fonseca M.,
Lapeyre B., Tollervey D.;
"Evolutionary conservation of the human nucleolar protein fibrillarin
and its functional expression in yeast.";
J. Cell Biol. 113:715-729(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=19054851; DOI=10.1038/nmeth.1273;
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
Isogai T., Imai J., Watanabe S., Nomura N.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=2414294;
Lischwe M.A., Ochs R.L., Reddy R., Cook R.G., Yeoman L.C., Tan E.M.,
Reichlin M., Busch H.;
"Purification and partial characterization of a nucleolar scleroderma
antigen (Mr = 34,000; pI, 8.5) rich in NG,NG-dimethylarginine.";
J. Biol. Chem. 260:14304-14310(1985).
[10]
IDENTIFICATION IN A COMPLEX WITH SMALL NUCLEOLAR RNA U3; U8; U13; X
AND Y.
PubMed=1714385;
Baserga S.J., Yang X.D., Steitz J.A.;
"An intact Box C sequence in the U3 snRNA is required for binding of
fibrillarin, the protein common to the major family of nucleolar
snRNPs.";
EMBO J. 10:2645-2651(1991).
[11]
INTERACTION WITH DDX5.
PubMed=10837141; DOI=10.1006/excr.2000.4886;
Nicol S.M., Causevic M., Prescott A.R., Fuller-Pace F.V.;
"The nuclear DEAD box RNA helicase p68 interacts with the nucleolar
protein fibrillarin and colocalizes specifically in nascent nucleoli
during telophase.";
Exp. Cell Res. 257:272-280(2000).
[12]
INTERACTION WITH PRMT5, IDENTIFICATION IN A COMPLEX WITH NOP5 AND
NOP56, IDENTIFICATION IN A COMPLEX WITH RIBOSOMAL PROTEINS AND WITH
NUMEROUS NUCLEOLAR PROTEINS, IDENTIFICATION BY MASS SPECTROMETRY, AND
SUBCELLULAR LOCATION.
PubMed=14583623; DOI=10.1074/jbc.M305604200;
Yanagida M., Hayano T., Yamauchi Y., Shinkawa T., Natsume T.,
Isobe T., Takahashi N.;
"Human fibrillarin forms a sub-complex with splicing factor 2-
associated p32, protein arginine methyltransferases, and tubulins
alpha 3 and beta 1 that is independent of its association with
preribosomal ribonucleoprotein complexes.";
J. Biol. Chem. 279:1607-1614(2004).
[13]
INTERACTION WITH UTP20.
PubMed=17498821; DOI=10.1016/j.bbamcr.2007.04.002;
Wang Y., Liu J., Zhao H., Lue W., Zhao J., Yang L., Li N., Du X.,
Ke Y.;
"Human 1A6/DRIM, the homolog of yeast Utp20, functions in the 18S rRNA
processing.";
Biochim. Biophys. Acta 1773:863-868(2007).
[14]
INTERACTION WITH PIH1D1.
PubMed=17636026; DOI=10.1128/MCB.01097-07;
McKeegan K.S., Debieux C.M., Boulon S., Bertrand E., Watkins N.J.;
"A dynamic scaffold of pre-snoRNP factors facilitates human box C/D
snoRNP assembly.";
Mol. Cell. Biol. 27:6782-6793(2007).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]
SUBCELLULAR LOCATION, UBIQUITINATION, AND DEUBIQUITINATION BY USP36.
PubMed=19208757; DOI=10.1242/jcs.044461;
Endo A., Matsumoto M., Inada T., Yamamoto A., Nakayama K.I.,
Kitamura N., Komada M.;
"Nucleolar structure and function are regulated by the
deubiquitylating enzyme USP36.";
J. Cell Sci. 122:678-686(2009).
[17]
INTERACTION WITH RRP1B.
PubMed=20926688; DOI=10.1091/mbc.E10-04-0287;
Chamousset D., De Wever V., Moorhead G.B., Chen Y., Boisvert F.M.,
Lamond A.I., Trinkle-Mulcahy L.;
"RRP1B targets PP1 to mammalian cell nucleoli and is associated with
pre-60S ribosomal subunits.";
Mol. Biol. Cell 21:4212-4226(2010).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
INTERACTION WITH C1QBP.
PubMed=21536856; DOI=10.1074/mcp.M110.006148;
Yoshikawa H., Komatsu W., Hayano T., Miura Y., Homma K., Izumikawa K.,
Ishikawa H., Miyazawa N., Tachikawa H., Yamauchi Y., Isobe T.,
Takahashi N.;
"Splicing factor 2-associated protein p32 participates in ribosome
biogenesis by regulating the binding of Nop52 and fibrillarin to
preribosome particles.";
Mol. Cell. Proteomics 10:0-0(2011).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[22]
INTERACTION WITH NOL11.
PubMed=22916032; DOI=10.1371/journal.pgen.1002892;
Freed E.F., Prieto J.L., McCann K.L., McStay B., Baserga S.J.;
"NOL11, implicated in the pathogenesis of North American Indian
childhood cirrhosis, is required for pre-rRNA transcription and
processing.";
PLoS Genet. 8:E1002892-E1002892(2012).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-124 AND
SER-126, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[26]
FUNCTION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
PubMed=24352239; DOI=10.1038/nature12819;
Tessarz P., Santos-Rosa H., Robson S.C., Sylvestersen K.B.,
Nelson C.J., Nielsen M.L., Kouzarides T.;
"Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated
modification.";
Nature 505:564-568(2014).
[27]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-84; LYS-102; LYS-109;
LYS-131; LYS-143 AND LYS-158, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[28]
X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 83-315 IN COMPLEX WITH
S-ADENOSYL-L-HOMOCYSTEINE.
Structural genomics consortium (SGC);
"The crystal structure of human fibrillarin in complex with SAH.";
Submitted (FEB-2009) to the PDB data bank.
-!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
has the ability to methylate both RNAs and proteins. Involved in
pre-rRNA processing by catalyzing the site-specific 2'-hydroxyl
methylation of ribose moieties in pre-ribosomal RNA. Site
specificity is provided by a guide RNA that base pairs with the
substrate. Methylation occurs at a characteristic distance from
the sequence involved in base pairing with the guide RNA. 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).
{ECO:0000269|PubMed:24352239}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-glutamine-
[histone] = S-adenosyl-L-homocysteine + N(5)-methyl-L-glutamine-
[histone]. {ECO:0000269|PubMed:24352239}.
-!- SUBUNIT: Interacts with NOLC1 (By similarity). Component of box
C/D small nucleolar ribonucleoprotein (snoRNP) particles that
contain SNU13, FBL, NOP5 and NOP56, plus a guide RNA. It is
associated with the U3, U8, U13, X and Y small nuclear RNAs.
Component of several ribosomal and nucleolar protein complexes.
Interacts with PRMT5 and UTP20. Interacts with DDX5 and C1QBP.
Interacts with NOL11. Interacts with PIH1D1 (PubMed:17636026).
Interacts with RRP1B (PubMed:20926688).
{ECO:0000250|UniProtKB:P22509, ECO:0000269|PubMed:10837141,
ECO:0000269|PubMed:14583623, ECO:0000269|PubMed:1714385,
ECO:0000269|PubMed:17498821, ECO:0000269|PubMed:17636026,
ECO:0000269|PubMed:20926688, ECO:0000269|PubMed:21536856,
ECO:0000269|PubMed:22916032, ECO:0000269|PubMed:2414294,
ECO:0000269|Ref.28}.
-!- INTERACTION:
P17844:DDX5; NbExp=6; IntAct=EBI-358318, EBI-351962;
Q14684:RRP1B; NbExp=4; IntAct=EBI-358318, EBI-372051;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000269|PubMed:14583623, ECO:0000269|PubMed:19208757,
ECO:0000269|PubMed:2026646, ECO:0000269|PubMed:2414294,
ECO:0000269|PubMed:24352239}. Note=Fibrillar region of the
nucleolus.
-!- 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).
-!- SIMILARITY: Belongs to the methyltransferase superfamily.
Fibrillarin family. {ECO:0000305}.
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EMBL; M59849; AAA52453.1; -; mRNA.
EMBL; X56597; CAA39935.1; -; mRNA.
EMBL; BT006830; AAP35476.1; -; mRNA.
EMBL; BT020144; AAV38946.1; -; mRNA.
EMBL; CR457069; CAG33350.1; -; mRNA.
EMBL; AB451384; BAG70198.1; -; mRNA.
EMBL; AC006950; AAD15623.1; -; Genomic_DNA.
EMBL; AC005393; AAC28913.1; -; Genomic_DNA.
EMBL; CH471126; EAW56925.1; -; Genomic_DNA.
EMBL; BC019260; AAH19260.1; -; mRNA.
CCDS; CCDS12545.1; -.
PIR; A38712; A38712.
RefSeq; NP_001427.2; NM_001436.3.
UniGene; Hs.299002; -.
PDB; 2IPX; X-ray; 1.82 A; A=83-315.
PDBsum; 2IPX; -.
ProteinModelPortal; P22087; -.
SMR; P22087; -.
BioGrid; 108399; 249.
CORUM; P22087; -.
DIP; DIP-27569N; -.
IntAct; P22087; 263.
MINT; P22087; -.
STRING; 9606.ENSP00000221801; -.
iPTMnet; P22087; -.
PhosphoSitePlus; P22087; -.
SwissPalm; P22087; -.
BioMuta; FBL; -.
DMDM; 14549159; -.
SWISS-2DPAGE; P22087; -.
EPD; P22087; -.
MaxQB; P22087; -.
PaxDb; P22087; -.
PeptideAtlas; P22087; -.
PRIDE; P22087; -.
ProteomicsDB; 53959; -.
DNASU; 2091; -.
Ensembl; ENST00000221801; ENSP00000221801; ENSG00000105202.
Ensembl; ENST00000625241; ENSP00000487390; ENSG00000280548.
GeneID; 2091; -.
KEGG; hsa:2091; -.
UCSC; uc002omn.4; human.
CTD; 2091; -.
DisGeNET; 2091; -.
EuPathDB; HostDB:ENSG00000105202.7; -.
GeneCards; FBL; -.
HGNC; HGNC:3599; FBL.
HPA; CAB001514; -.
HPA; HPA049546; -.
MIM; 134795; gene.
neXtProt; NX_P22087; -.
OpenTargets; ENSG00000105202; -.
PharmGKB; PA28012; -.
eggNOG; KOG1596; Eukaryota.
eggNOG; COG1889; LUCA.
GeneTree; ENSGT00550000074792; -.
HOGENOM; HOG000106741; -.
HOVERGEN; HBG002472; -.
KO; K14563; -.
OMA; QPNQAEI; -.
OrthoDB; EOG091G0GV0; -.
PhylomeDB; P22087; -.
TreeFam; TF300639; -.
Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol.
Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
ChiTaRS; FBL; human.
EvolutionaryTrace; P22087; -.
GeneWiki; Fibrillarin; -.
GenomeRNAi; 2091; -.
PRO; PR:P22087; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000105202; Expressed in 233 organ(s), highest expression level in testis.
CleanEx; HS_FBL; -.
ExpressionAtlas; P22087; baseline and differential.
Genevisible; P22087; HS.
GO; GO:0031428; C:box C/D snoRNP complex; IBA:GO_Central.
GO; GO:0015030; C:Cajal body; IDA:BHF-UCL.
GO; GO:0005694; C:chromosome; IEA:Ensembl.
GO; GO:0001651; C:dense fibrillar component; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0001650; C:fibrillar center; IDA:HPA.
GO; GO:0001652; C:granular component; IEA:Ensembl.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
GO; GO:1990259; F:histone-glutamine methyltransferase activity; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0008649; F:rRNA methyltransferase activity; IBA:GO_Central.
GO; GO:0001094; F:TFIID-class transcription factor binding; IPI:UniProtKB.
GO; GO:0000494; P:box C/D snoRNA 3'-end processing; IBA:GO_Central.
GO; GO:1990258; P:histone glutamine methylation; IDA:UniProtKB.
GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB.
GO; GO:0031167; P:rRNA methylation; IBA:GO_Central.
GO; GO:0006364; P:rRNA processing; TAS:Reactome.
GO; GO:0048254; P:snoRNA localization; IMP:UniProtKB.
HAMAP; MF_00351; RNA_methyltransf_FlpA; 1.
InterPro; IPR000692; Fibrillarin.
InterPro; IPR020813; Fibrillarin_CS.
InterPro; IPR029063; SAM-dependent_MTases.
Pfam; PF01269; Fibrillarin; 1.
PIRSF; PIRSF006540; Nop17p; 1.
PRINTS; PR00052; FIBRILLARIN.
SMART; SM01206; Fibrillarin; 1.
SUPFAM; SSF53335; SSF53335; 1.
PROSITE; PS00566; FIBRILLARIN; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Isopeptide bond; Methylation;
Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
Ribonucleoprotein; RNA-binding; rRNA processing;
S-adenosyl-L-methionine; Transferase; Ubl conjugation.
CHAIN 1 321 rRNA 2'-O-methyltransferase fibrillarin.
/FTId=PRO_0000148507.
REGION 172 173 S-adenosyl-L-methionine binding.
{ECO:0000250}.
REGION 191 192 S-adenosyl-L-methionine binding.
REGION 216 217 S-adenosyl-L-methionine binding.
REGION 236 239 S-adenosyl-L-methionine binding.
REGION 274 306 Helical. {ECO:0000255}.
COMPBIAS 8 77 DMA/Gly-rich.
MOD_RES 8 8 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:P22509}.
MOD_RES 15 15 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:P22509}.
MOD_RES 21 21 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:P22509}.
MOD_RES 24 24 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:P22509}.
MOD_RES 27 27 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:P22509}.
MOD_RES 116 116 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 124 124 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 126 126 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 84 84 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 102 102 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 109 109 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 131 131 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 143 143 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 158 158 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CONFLICT 132 132 I -> F (in Ref. 1; AAA52453).
{ECO:0000305}.
STRAND 96 98 {ECO:0000244|PDB:2IPX}.
STRAND 107 109 {ECO:0000244|PDB:2IPX}.
STRAND 117 119 {ECO:0000244|PDB:2IPX}.
STRAND 122 125 {ECO:0000244|PDB:2IPX}.
STRAND 132 136 {ECO:0000244|PDB:2IPX}.
TURN 139 141 {ECO:0000244|PDB:2IPX}.
HELIX 143 149 {ECO:0000244|PDB:2IPX}.
STRAND 162 166 {ECO:0000244|PDB:2IPX}.
HELIX 172 181 {ECO:0000244|PDB:2IPX}.
STRAND 186 190 {ECO:0000244|PDB:2IPX}.
HELIX 194 206 {ECO:0000244|PDB:2IPX}.
STRAND 210 213 {ECO:0000244|PDB:2IPX}.
HELIX 220 226 {ECO:0000244|PDB:2IPX}.
STRAND 230 235 {ECO:0000244|PDB:2IPX}.
HELIX 242 253 {ECO:0000244|PDB:2IPX}.
STRAND 254 265 {ECO:0000244|PDB:2IPX}.
HELIX 266 269 {ECO:0000244|PDB:2IPX}.
STRAND 271 273 {ECO:0000244|PDB:2IPX}.
HELIX 275 284 {ECO:0000244|PDB:2IPX}.
HELIX 285 289 {ECO:0000244|PDB:2IPX}.
STRAND 291 298 {ECO:0000244|PDB:2IPX}.
TURN 300 302 {ECO:0000244|PDB:2IPX}.
STRAND 303 313 {ECO:0000244|PDB:2IPX}.
SEQUENCE 321 AA; 33784 MW; 2123F41E01EC557A CRC64;
MKPGFSPRGG GFGGRGGFGD RGGRGGRGGF GGGRGRGGGF RGRGRGGGGG GGGGGGGGRG
GGGFHSGGNR GRGRGGKRGN QSGKNVMVEP HRHEGVFICR GKEDALVTKN LVPGESVYGE
KRVSISEGDD KIEYRAWNPF RSKLAAAILG GVDQIHIKPG AKVLYLGAAS GTTVSHVSDI
VGPDGLVYAV EFSHRSGRDL INLAKKRTNI IPVIEDARHP HKYRMLIAMV DVIFADVAQP
DQTRIVALNA HTFLRNGGHF VISIKANCID STASAEAVFA SEVKKMQQEN MKPQEQLTLE
PYERDHAVVV GVYRPPPKVK N


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