ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P22087


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name FBRL_HUMAN
Primary accession number P22087
Secondary accession numbers O75259 Q6IAT5 Q9UPI6
Integrated into Swiss-Prot on August 1, 1991
Sequence was last modified on June 20, 2001 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 90)
Name and origin of the protein
Protein name rRNA 2'-O-methyltransferase fibrillarin
Synonyms EC 2.1.1.-
34 kDa nucleolar scleroderma antigen
Gene name
Name: FBL
Synonyms: FIB1, FLRN
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1846968 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1083/jcb.113.4.715; PubMed=2026646 [NCBI, ExPASy, EBI, Israel, Japan]
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 GENOMIC DNA].
DOI=10.1038/nature02399; PubMed=15057824 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[7]
SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=2414294 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[8]
IDENTIFICATION IN A COMPLEX WITH SMALL NUCLEOLAR RNA U3; U8; U13; X AND Y.
PubMed=1714385 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[9]
INTERACTION WITH PRMT5, IDENTIFICATION IN A COMPLEX WITH NOP5 AND NOL5A, IDENTIFICATION IN A COMPLEX WITH RIBOSOMAL PROTEINS AND WITH NUMEROUS NUCLEOLAR PROTEINS, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
DOI=10.1074/jbc.M305604200; PubMed=14583623 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M59849; AAA52453.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X56597; CAA39935.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT006830; AAP35476.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT020144; AAV38946.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR457069; CAG33350.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC006950; AAD15623.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC005393; AAC28913.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC019260; AAH19260.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A38712; A38712.
RefSeq NP_001427.2; -.
UniGene Hs.299002
3D structure databases
PDB
2IPX; X-ray; 1.82 A; A=83-315.[ExPASy / RCSB / EBI]
PDBsum 2IPX; -.
SMR P22087; 87-315.
ModBase P22087.
Protein-protein interaction databases
DIP DIP:27569N; -.
IntAct P22087; -.
PTM databases
PhosphoSite P22087; -.
2D gel databases
SWISS-2DPAGE P22087; -.
Organism-specific databases
H-InvDB HIX0015126; -.
HIX0032650; -.
HGNC HGNC:3599; FBL.
GenAtlas FBL.
HPA CAB001514; -.
MIM 134795; gene. [NCBI / EBI]
PharmGKB PA28012; -.
GeneCards P22087.
Gene expression databases
ArrayExpress P22087; -.
CleanEx HS_FBL; -.
GermOnline ENSG00000105202; Homo sapiens.
Ontologies
GO
GO:0030529; Cellular component: ribonucleoprotein complex (inferred from electronic annotation from UniProtKB-KW).
GO:0008168; Molecular function: methyltransferase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0003723; Molecular function: RNA binding (traceable author statement from ProtInc).
GO:0006364; Biological process: rRNA processing (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR000692; Fibrillarin.
Graphical view of domain structure.
PANTHER PTHR10335; Fibrillarin; 1.
Pfam PF01269; Fibrillarin; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF006540; Nop17p; 1.
PRINTS PR00052; FIBRILLARIN.
PROSITE PS00566; FIBRILLARIN; 1.
ProtoNet P22087.
Proteomic databases
PeptideAtlas P22087; -.
Genome annotation databases
Ensembl ENSG00000105202; Homo sapiens. [Contig view]
GeneID 2091; -.
KEGG hsa:2091; -.
Phylogenomic databases
HOGENOM P22087; -.
HOVERGEN P22087; -.
Other
LinkHub P22087; -.
NextBio 8479; -.
SOURCE FBL; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Methylation; Methyltransferase; Nucleus; Ribonucleoprotein; RNA-binding; rRNA processing; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   321  321     rRNA 2'-O-methyltransferase fibrillarin. PRO_0000148507
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). 
COMPBIAS   8    77  70     DMA/Gly-rich. 
BINDING   143   143        S-adenosyl-L-methionine (By similarity). 
BINDING   236   236        S-adenosyl-L-methionine (By similarity). 
MOD_RES   8     8        Asymmetric dimethylarginine (By similarity). 
MOD_RES   15    15        Asymmetric dimethylarginine (By similarity). 
MOD_RES   21    21        Asymmetric dimethylarginine (By similarity). 
MOD_RES   24    24        Asymmetric dimethylarginine (By similarity). 
MOD_RES   27    27        Asymmetric dimethylarginine (By similarity). 
MOD_RES   34    34        Asymmetric dimethylarginine (By similarity). 
MOD_RES   36    36        Asymmetric dimethylarginine (By similarity). 
MOD_RES   41    41        Asymmetric dimethylarginine (By similarity). 
MOD_RES   43    43        Asymmetric dimethylarginine (By similarity). 
MOD_RES   45    45        Asymmetric dimethylarginine (By similarity). 
MOD_RES   59    59        Asymmetric dimethylarginine (By similarity). 
MOD_RES   70    70        Asymmetric dimethylarginine (By similarity). 
MOD_RES   72    72        Asymmetric dimethylarginine (By similarity). 
MOD_RES   74    74        Asymmetric dimethylarginine (By similarity). 
MOD_RES   78    78        Asymmetric dimethylarginine (By similarity). 
CONFLICT   132   132        I -> F (in Ref. 1; AAA52453). 
STRAND   96    98  3      
STRAND   107   109  3      
STRAND   117   119  3      
STRAND   122   125  4      
STRAND   132   136  5      
TURN   139   141  3      
HELIX   143   149  7      
STRAND   162   166  5      
HELIX   172   181  10      
STRAND   186   190  5      
HELIX   194   206  13      
STRAND   210   213  4      
HELIX   220   226  7      
STRAND   230   235  6      
HELIX   242   253  12      
STRAND   254   265  12      
HELIX   266   269  4      
STRAND   271   273  3      
HELIX   275   284  10      
HELIX   285   289  5      
STRAND   291   298  8      
TURN   300   302  3      
STRAND   303   313  11      
Sequence information
Length: 321 AA [This is the length of the unprocessed precursor] Molecular weight: 33784 Da [This is the MW of the unprocessed precursor] CRC64: 2123F41E01EC557A [This is a checksum on the sequence]
        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 

P22087 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!