Reviewed, UniProtKB/Swiss-Prot P22087 (FBRL_HUMAN)

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) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	321 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Subcellular location	Nucleus › nucleolus. Note: Fibrillar region of the nucleolus. Ref.2 Ref.7 Ref.9
Post-translational modification	By homology to other fibrillarins, some or all of the N-terminal domain arginines are modified to asymmetric dimethylarginine (DMA).
Involvement in disease	Antisera from circa 8% of humans with the autoimmune disease scleroderma recognize fibrillarin.
Sequence similarities	Belongs to the fibrillarin family.

Ontologies

Keywords
Biological process	rRNA processing
Cellular component	Nucleus
Ligand	RNA-binding
Molecular function	Methyltransferase Ribonucleoprotein Transferase
PTM	Methylation
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	rRNA processing Ref.1 Traceable author statement. Source: ProtInc
Cellular component	ribonucleoprotein complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	RNA binding Ref.1 Traceable author statement. Source: ProtInc methyltransferase activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARRB2	P32121	1	EBI-358318,EBI-714559
BAK1	Q16611	1	EBI-358318,EBI-519866
CD40	P25942	1	EBI-358318,EBI-525714
CDK2	P24941	1	EBI-358318,EBI-375096
DDX56	Q9NY93	1	EBI-358318,EBI-372376
PASK	Q96RG2	1	EBI-358318,EBI-1042651
RIOK3	O14730	1	EBI-358318,EBI-1047061
RTCD1	Q5VSU9	1	EBI-358318,EBI-1045306

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

34

1

Asymmetric dimethylarginine By similarity

Modified residue

36

1

Asymmetric dimethylarginine By similarity

Modified residue

41

1

Asymmetric dimethylarginine By similarity

Modified residue

43

1

Asymmetric dimethylarginine By similarity

Modified residue

45

1

Asymmetric dimethylarginine By similarity

Modified residue

59

1

Asymmetric dimethylarginine By similarity

Modified residue

70

1

Asymmetric dimethylarginine By similarity

Modified residue

72

1

Asymmetric dimethylarginine By similarity

Modified residue

74

1

Asymmetric dimethylarginine By similarity

Modified residue

78

1

Asymmetric dimethylarginine By similarity

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)
	P22087-1 [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: 1846968] [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: 2026646] [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]	"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: 15057824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[7]	"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: 2414294] [Abstract] Cited for: SUBUNIT, SUBCELLULAR LOCATION.
[8]	"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: 1714385] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH SMALL NUCLEOLAR RNA U3; U8; U13; X AND Y.
[9]	"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: 14583623] [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.
[10]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.
AC006950 Genomic DNA. Translation: AAD15623.1.
AC005393 Genomic DNA. Translation: AAC28913.1.
BC019260 mRNA. Translation: AAH19260.1.

IPI

IPI00025039.

PIR

A38712.

RefSeq

NP_001427.2.

UniGene

Hs.299002

3D structure databases

PDBPDBe

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

SMR

P22087. Positions 87-315.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:27569N.

IntAct

P22087. 22 interactions.

PTM databases

PhosphoSite

P22087.

2-D gel databases

SWISS-2DPAGE

P22087.

Proteomic databases

PeptideAtlas

P22087.

PRIDE

P22087.

Genome annotation databases

Ensembl

ENSG00000105202. Homo sapiens. [Contig view]

GeneID

2091.

KEGG

hsa:2091.

UCSC

uc002omn.1. human.

Organism-specific databases

GeneCards

GC19M045016.

H-InvDB

HIX0015126.
HIX0032650.

HGNC

HGNC:3599. FBL.

HPA

CAB001514.

MIM

134795. gene.

PharmGKB

PA28012.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P22087.

HOVERGEN

P22087.

OMA

P22087. FIARGKE.

Gene expression databases

ArrayExpress

P22087.

Bgee

P22087.

CleanEx

HS_FBL.

GermOnline

ENSG00000105202. Homo sapiens.

Family and domain databases

InterPro

IPR000692. Fibrillarin.
[Graphical view]

PANTHER

PTHR10335. Fibrillarin. 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 Resources

NextBio

8479.

SOURCE

Search...

Entry information

Entry name

FBRL_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	June 20, 2001
Last modified:	July 7, 2009
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)