P22087 (FBRL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
rRNA 2'-O-methyltransferase fibrillarin
EC=2.1.1.-

Alternative name(s):
34 kDa nucleolar scleroderma antigen

Gene names

Name:	FBL
Synonyms:	FIB1, FLRN

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	321 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in pre-rRNA processing. Utilizes the methyl donor S-adenosyl-L-methionine to catalyze 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.
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. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.17
Subcellular location	Nucleus › nucleolus. Note: Fibrillar region of the nucleolus. Ref.2 Ref.9 Ref.12
Post-translational modification	By homology to other fibrillarins, some or all of the N-terminal domain arginines are modified to asymmetric dimethylarginine (DMA).
Sequence similarities	Belongs to the methyltransferase superfamily. Fibrillarin family.

Ontologies

Keywords
Biological process	rRNA processing
Cellular component	Nucleus
Ligand	RNA-binding
Molecular function	Methyltransferase Ribonucleoprotein Transferase
PTM	Methylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	rRNA processing Traceable author statement Ref.1. Source: ProtInc snoRNA metabolic process Inferred from electronic annotation. Source: Compara tRNA processing Inferred from electronic annotation. Source: InterPro
Cellular_component	Cajal body Inferred from direct assay PubMed 16687569. Source: BHF-UCL box C/D snoRNP complex Non-traceable author statement PubMed 17636026. Source: BHF-UCL granular component Inferred from electronic annotation. Source: Compara
Molecular_function	RNA binding Traceable author statement Ref.1. Source: ProtInc methyltransferase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DDX5	P17844	6	EBI-358318,EBI-351962

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 321

321

rRNA 2'-O-methyltransferase fibrillarin

PRO_0000148507

Regions

Region

172 – 173

2

S-adenosyl-L-methionine binding By similarity

Region

191 – 192

2

S-adenosyl-L-methionine binding By similarity

Region

216 – 217

2

S-adenosyl-L-methionine binding By similarity

Region

274 – 306

33

Helical Potential

Compositional bias

8 – 77

70

DMA/Gly-rich

Sites

Binding site

143

1

S-adenosyl-L-methionine By similarity

Binding site

236

1

S-adenosyl-L-methionine By similarity

Amino acid modifications

Modified residue

8

1

Asymmetric dimethylarginine By similarity

Modified residue

15

1

Asymmetric dimethylarginine By similarity

Modified residue

21

1

Asymmetric dimethylarginine By similarity

Modified residue

24

1

Asymmetric dimethylarginine By similarity

Modified residue

27

1

Asymmetric dimethylarginine By similarity

Modified residue

124

1

Phosphoserine Ref.15 Ref.18

Experimental info

Sequence conflict

132

1

I → F in AAA52453. Ref.1

Secondary structure

1

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321

Helix Strand Turn

Details...

Beta strand

96 – 98

3

Beta strand

107 – 109

3

Beta strand

117 – 119

3

Beta strand

122 – 125

4

Beta strand

132 – 136

5

Turn

139 – 141

3

Helix

143 – 149

7

Beta strand

162 – 166

5

Helix

172 – 181

10

Beta strand

186 – 190

5

Helix

194 – 206

13

Beta strand

210 – 213

4

Helix

220 – 226

7

Beta strand

230 – 235

6

Helix

242 – 253

12

Beta strand

254 – 265

12

Helix

266 – 269

4

Beta strand

271 – 273

3

Helix

275 – 284

10

Helix

285 – 289

5

Beta strand

291 – 298

8

Turn

300 – 302

3

Beta strand

303 – 313

11

Sequences

	Sequence		Length	Mass (Da)
	P22087 [UniParc]. Last modified June 20, 2001. Version 2. Checksum: 2123F41E01EC557A	FASTA	321	33,784
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
+	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.

IPI

IPI00025039.

PIR

A38712.

RefSeq

NP_001427.2. NM_001436.3.

UniGene

Hs.299002.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2IPX	X-ray	1.82	A	83-315	[»]

ProteinModelPortal

P22087.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-27569N.

IntAct

P22087. 21 interactions.

MINT

MINT-207612.

PTM databases

PhosphoSite

P22087.

Polymorphism databases

DMDM

14549159.

2D gel databases

SWISS-2DPAGE

P22087.

Proteomic databases

PaxDb

P22087.

PeptideAtlas

P22087.

PRIDE

P22087.

Protocols and materials databases

DNASU

2091.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000221801; ENSP00000221801; ENSG00000105202.

GeneID

2091.

KEGG

hsa:2091.

UCSC

uc002omm.1. human.

Organism-specific databases

CTD

2091.

GeneCards

GC19M040325.

HGNC

HGNC:3599. FBL.

HPA

CAB001514.

MIM

134795. gene.

neXtProt

NX_P22087.

PharmGKB

PA28012.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1889.

HOGENOM

HOG000106741.

HOVERGEN

HBG002472.

InParanoid

P22087.

KO

K14563.

OMA

VGMVDTI.

OrthoDB

EOG4K3KX0.

PhylomeDB

P22087.

Gene expression databases

ArrayExpress

P22087.

Bgee

P22087.

CleanEx

HS_FBL.

Genevestigator

P22087.

GermOnline

ENSG00000105202. Homo sapiens.

Family and domain databases

InterPro

IPR000692. Fibrillarin.
IPR020813. Fibrillarin_CS.
[Graphical view]

PANTHER

PTHR10335. PTHR10335. 1 hit.

Pfam

PF01269. Fibrillarin. 1 hit.
[Graphical view]

PIRSF

PIRSF006540. Nop17p. 1 hit.

PRINTS

PR00052. FIBRILLARIN.

PROSITE

PS00566. FIBRILLARIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

FBL. human.

EvolutionaryTrace

P22087.

GenomeRNAi

2091.

NextBio

8479.

SOURCE

Search...

Entry information

Entry name

FBRL_HUMAN

Accession

Primary (citable) accession number: P22087
Secondary accession number(s): B5BUE8 , O75259, Q6IAT5, Q9UPI6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	June 20, 2001
Last modified:	May 1, 2013
This is version 138 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.