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Identification
HMDB Protein ID HMDBP01856
Secondary Accession Numbers
  • 7234
Name rRNA 2'-O-methyltransferase fibrillarin
Synonyms
  1. 34 kDa nucleolar scleroderma antigen
Gene Name FBL
Protein Type Unknown
Biological Properties
General Function Involved in RNA binding
Specific 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
Pathways Not Available
Reactions Not Available
GO Classification
Function
binding
catalytic activity
transferase activity
nucleic acid binding
transferase activity, transferring one-carbon groups
methyltransferase activity
rna binding
Process
rna metabolic process
ncrna metabolic process
trna metabolic process
trna processing
metabolic process
macromolecule metabolic process
cellular macromolecule metabolic process
rrna metabolic process
rrna processing
Cellular Location
  1. Nucleus
  2. nucleolus
Gene Properties
Chromosome Location Chromosome:1
Locus 19q13.1
SNPs FBL
Gene Sequence
>963 bp
ATGAAGCCAGGATTCAGTCCCCGTGGGGGTGGCTTTGGCGGCCGAGGGGGCTTTGGTGAC
CGTGGTGGTCGTGGAGGCCGAGGGGGCTTTGGCGGGGGCCGAGGTCGAGGCGGAGGCTTT
AGAGGTCGTGGACGAGGAGGAGGTGGAGGCGGCGGCGGCGGTGGAGGAGGAGGAAGAGGT
GGTGGAGGCTTCCATTCTGGTGGCAACCGGGGTCGTGGTCGGGGAGGAAAAAGAGGAAAC
CAGTCGGGGAAGAATGTGATGGTGGAGCCGCATCGGCATGAGGGTGTCTTCATTTGTCGA
GGAAAGGAAGATGCACTGGTCACCAAGAACCTGGTCCCTGGGGAATCAGTTTATGGAGAG
AAGAGAGTCTCGATTTCGGAAGGAGATGACAAAATTGAGTACCGAGCCTGGAACCCCTTC
CGCTCCAAGCTAGCAGCAGCAATCCTGGGTGGTGTGGACCAGATCCACATCAAACCGGGG
GCTAAGGTTCTCTACCTCGGGGCTGCCTCGGGCACCACGGTCTCCCATGTCTCTGACATC
GTTGGTCCGGATGGTCTAGTCTATGCAGTCGAGTTCTCCCACCGCTCTGGCCGTGACCTC
ATTAACTTGGCCAAGAAGAGGACCAACATCATTCCTGTGATCGAGGATGCTCGACACCCA
CACAAATACCGCATGCTCATCGCAATGGTGGATGTGATCTTTGCTGATGTGGCCCAGCCA
GACCAGACCCGGATTGTGGCCCTGAATGCCCACACCTTCCTGCGTAATGGAGGACACTTT
GTGATTTCCATTAAGGCCAACTGCATTGACTCCACAGCCTCAGCCGAGGCCGTGTTTGCC
TCCGAAGTGAAAAAGATGCAACAGGAGAACATGAAGCCGCAGGAGCAGTTGACCCTTGAG
CCATATGAAAGAGACCATGCCGTGGTCGTGGGAGTGTACAGGCCACCCCCCAAGGTGAAG
AAC
Protein Properties
Number of Residues 321
Molecular Weight 33784.1
Theoretical pI 10.81
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>rRNA 2'-O-methyltransferase fibrillarin
MKPGFSPRGGGFGGRGGFGDRGGRGGRGGFGGGRGRGGGFRGRGRGGGGGGGGGGGGGRG
GGGFHSGGNRGRGRGGKRGNQSGKNVMVEPHRHEGVFICRGKEDALVTKNLVPGESVYGE
KRVSISEGDDKIEYRAWNPFRSKLAAAILGGVDQIHIKPGAKVLYLGAASGTTVSHVSDI
VGPDGLVYAVEFSHRSGRDLINLAKKRTNIIPVIEDARHPHKYRMLIAMVDVIFADVAQP
DQTRIVALNAHTFLRNGGHFVISIKANCIDSTASAEAVFASEVKKMQQENMKPQEQLTLE
PYERDHAVVVGVYRPPPKVKN
GenBank ID Protein 197692469
UniProtKB/Swiss-Prot ID P22087
UniProtKB/Swiss-Prot Entry Name FBRL_HUMAN
PDB IDs Not Available
GenBank Gene ID AB451384
GeneCard ID FBL
GenAtlas ID FBL
HGNC ID HGNC:3599
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  3. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, 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, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, 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 SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, 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 TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed:15057824 ]
  4. Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. doi: 10.1021/ac801708p. [PubMed:19007248 ]
  5. 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. 2008 Dec;5(12):1011-7. [PubMed:19054851 ]
  6. Aris JP, Blobel G: cDNA cloning and sequencing of human fibrillarin, a conserved nucleolar protein recognized by autoimmune antisera. Proc Natl Acad Sci U S A. 1991 Feb 1;88(3):931-5. [PubMed:1846968 ]
  7. Jansen RP, Hurt EC, 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. 1991 May;113(4):715-29. [PubMed:2026646 ]
  8. Lischwe MA, Ochs RL, Reddy R, Cook RG, Yeoman LC, Tan EM, 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. 1985 Nov 15;260(26):14304-10. [PubMed:2414294 ]
  9. Baserga SJ, Yang XD, Steitz JA: 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. 1991 Sep;10(9):2645-51. [PubMed:1714385 ]
  10. 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. 2004 Jan 16;279(3):1607-14. Epub 2003 Oct 28. [PubMed:14583623 ]
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