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P22087 (FBRL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
rRNA 2'-O-methyltransferase fibrillarin

EC=2.1.1.-
Alternative name(s):
34 kDa nucleolar scleroderma antigen
Histone-glutamine methyltransferase
Gene names
Name:FBL
Synonyms:FIB1, FLRN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length321 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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 (Ref.21). Ref.21

Catalytic activity

S-adenosyl-L-methionine + L-glutamine-[histone] = S-adenosyl-L-homocysteine + N(5)-methyl-L-glutamine-[histone]. Ref.21

Subunit structure

Interacts with NOLC1 By similarity. Component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles that contain NHP2L1, 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. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.17 Ref.19

Subcellular location

Nucleusnucleolus. Note: Fibrillar region of the nucleolus. Ref.2 Ref.9 Ref.12 Ref.21

Post-translational modification

By homology to other fibrillarins, some or all of the N-terminal domain arginines are modified to asymmetric dimethylarginine (DMA). HAMAP-Rule MF_00351

Sequence similarities

Belongs to the methyltransferase superfamily. Fibrillarin family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DDX5P178446EBI-358318,EBI-351962

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 321321rRNA 2'-O-methyltransferase fibrillarin HAMAP-Rule MF_00351
PRO_0000148507

Regions

Region172 – 1732S-adenosyl-L-methionine binding By similarity
Region191 – 1922S-adenosyl-L-methionine binding HAMAP-Rule MF_00351
Region216 – 2172S-adenosyl-L-methionine binding HAMAP-Rule MF_00351
Region236 – 2394S-adenosyl-L-methionine binding HAMAP-Rule MF_00351
Region274 – 30633Helical Potential
Compositional bias8 – 7770DMA/Gly-rich HAMAP-Rule MF_00351

Amino acid modifications

Modified residue81Asymmetric dimethylarginine By similarity
Modified residue151Asymmetric dimethylarginine By similarity
Modified residue211Asymmetric dimethylarginine By similarity
Modified residue241Asymmetric dimethylarginine By similarity
Modified residue271Asymmetric dimethylarginine By similarity
Modified residue1241Phosphoserine Ref.15 Ref.18

Experimental info

Sequence conflict1321I → F in AAA52453. Ref.1

Secondary structure

........................................... 321
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P22087 [UniParc].

Last modified June 20, 2001. Version 2.
Checksum: 2123F41E01EC557A

FASTA32133,784
        10         20         30         40         50         60 
MKPGFSPRGG GFGGRGGFGD RGGRGGRGGF GGGRGRGGGF RGRGRGGGGG GGGGGGGGRG 

        70         80         90        100        110        120 
GGGFHSGGNR GRGRGGKRGN QSGKNVMVEP HRHEGVFICR GKEDALVTKN LVPGESVYGE 

       130        140        150        160        170        180 
KRVSISEGDD KIEYRAWNPF RSKLAAAILG GVDQIHIKPG AKVLYLGAAS GTTVSHVSDI 

       190        200        210        220        230        240 
VGPDGLVYAV EFSHRSGRDL INLAKKRTNI IPVIEDARHP HKYRMLIAMV DVIFADVAQP 

       250        260        270        280        290        300 
DQTRIVALNA HTFLRNGGHF VISIKANCID STASAEAVFA SEVKKMQQEN MKPQEQLTLE 

       310        320 
PYERDHAVVV GVYRPPPKVK N 

« Hide

References

« Hide 'large scale' references
[1]"cDNA cloning and sequencing of human fibrillarin, a conserved nucleolar protein recognized by autoimmune antisera."
Aris J.P., Blobel G.
Proc. Natl. Acad. Sci. U.S.A. 88:931-935(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Evolutionary conservation of the human nucleolar protein fibrillarin and its functional expression in yeast."
Jansen R.P., Hurt E.C., Kern H., Lehtonen H., Carmo-Fonseca M., Lapeyre B., Tollervey D.
J. Cell Biol. 113:715-729(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
Tissue: Cervix carcinoma.
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
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.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
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. expand/collapse author list , 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.
Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"The DNA sequence and biology of human chromosome 19."
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. expand/collapse author list , 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.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[9]"Purification and partial characterization of a nucleolar scleroderma antigen (Mr = 34,000; pI, 8.5) rich in NG,NG-dimethylarginine."
Lischwe M.A., Ochs R.L., Reddy R., Cook R.G., Yeoman L.C., Tan E.M., Reichlin M., Busch H.
J. Biol. Chem. 260:14304-14310(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, SUBCELLULAR LOCATION.
[10]"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."
Baserga S.J., Yang X.D., Steitz J.A.
EMBO J. 10:2645-2651(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH SMALL NUCLEOLAR RNA U3; U8; U13; X AND Y.
[11]"The nuclear DEAD box RNA helicase p68 interacts with the nucleolar protein fibrillarin and colocalizes specifically in nascent nucleoli during telophase."
Nicol S.M., Causevic M., Prescott A.R., Fuller-Pace F.V.
Exp. Cell Res. 257:272-280(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DDX5.
[12]"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."
Yanagida M., Hayano T., Yamauchi Y., Shinkawa T., Natsume T., Isobe T., Takahashi N.
J. Biol. Chem. 279:1607-1614(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: 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, SUBCELLULAR LOCATION.
[13]"Human 1A6/DRIM, the homolog of yeast Utp20, functions in the 18S rRNA processing."
Wang Y., Liu J., Zhao H., Lue W., Zhao J., Yang L., Li N., Du X., Ke Y.
Biochim. Biophys. Acta 1773:863-868(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UTP20.
[14]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Splicing factor 2-associated protein p32 participates in ribosome biogenesis by regulating the binding of Nop52 and fibrillarin to preribosome particles."
Yoshikawa H., Komatsu W., Hayano T., Miura Y., Homma K., Izumikawa K., Ishikawa H., Miyazawa N., Tachikawa H., Yamauchi Y., Isobe T., Takahashi N.
Mol. Cell. Proteomics 10:0-0(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH C1QBP.
[18]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"NOL11, implicated in the pathogenesis of North American Indian childhood cirrhosis, is required for pre-rRNA transcription and processing."
Freed E.F., Prieto J.L., McCann K.L., McStay B., Baserga S.J.
PLoS Genet. 8:E1002892-E1002892(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NOL11.
[20]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated modification."
Tessarz P., Santos-Rosa H., Robson S.C., Sylvestersen K.B., Nelson C.J., Nielsen M.L., Kouzarides T.
Nature 505:564-568(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY.
[22]"The crystal structure of human fibrillarin in complex with SAH."
Structural genomics consortium (SGC)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 83-315 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M59849 mRNA. Translation: AAA52453.1.
X56597 mRNA. Translation: CAA39935.1.
BT006830 mRNA. Translation: AAP35476.1.
BT020144 mRNA. Translation: AAV38946.1.
CR457069 mRNA. Translation: CAG33350.1.
AB451384 mRNA. Translation: BAG70198.1.
AC006950 Genomic DNA. Translation: AAD15623.1.
AC005393 Genomic DNA. Translation: AAC28913.1.
CH471126 Genomic DNA. Translation: EAW56925.1.
BC019260 mRNA. Translation: AAH19260.1.
PIRA38712.
RefSeqNP_001427.2. NM_001436.3.
UniGeneHs.299002.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2IPXX-ray1.82A83-315[»]
ProteinModelPortalP22087.
SMRP22087. Positions 87-315.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108399. 120 interactions.
DIPDIP-27569N.
IntActP22087. 29 interactions.
MINTMINT-207612.

PTM databases

PhosphoSiteP22087.

Polymorphism databases

DMDM14549159.

2D gel databases

SWISS-2DPAGEP22087.

Proteomic databases

PaxDbP22087.
PeptideAtlasP22087.
PRIDEP22087.

Protocols and materials databases

DNASU2091.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000221801; ENSP00000221801; ENSG00000105202.
GeneID2091.
KEGGhsa:2091.
UCSCuc002omm.1. human.

Organism-specific databases

CTD2091.
GeneCardsGC19M040325.
HGNCHGNC:3599. FBL.
HPACAB001514.
MIM134795. gene.
neXtProtNX_P22087.
PharmGKBPA28012.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1889.
HOGENOMHOG000106741.
HOVERGENHBG002472.
InParanoidP22087.
KOK14563.
OMAYREWNPY.
PhylomeDBP22087.
TreeFamTF300639.

Gene expression databases

ArrayExpressP22087.
BgeeP22087.
CleanExHS_FBL.
GenevestigatorP22087.

Family and domain databases

HAMAPMF_00351. RNA_methyltransf_FlpA.
InterProIPR000692. Fibrillarin.
IPR020813. Fibrillarin_CS.
[Graphical view]
PANTHERPTHR10335. PTHR10335. 1 hit.
PfamPF01269. Fibrillarin. 1 hit.
[Graphical view]
PIRSFPIRSF006540. Nop17p. 1 hit.
PRINTSPR00052. FIBRILLARIN.
PROSITEPS00566. FIBRILLARIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFBL. human.
EvolutionaryTraceP22087.
GeneWikiFibrillarin.
GenomeRNAi2091.
NextBio8479.
PROP22087.
SOURCESearch...

Entry information

Entry nameFBRL_HUMAN
AccessionPrimary (citable) accession number: P22087
Secondary accession number(s): B5BUE8 expand/collapse secondary AC list , O75259, Q6IAT5, Q9UPI6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: June 20, 2001
Last modified: April 16, 2014
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM