Modomics - A Database of RNA Modifications

ID Card:

Full name: rRNA 2′-O-methyltransferase fibrillarin
Synonym: FIB1, FLRN, fibrillarin
GI: 12056465
COG: COG1889
UniProt: P22087
Structures: | 2IPX |
Alpha Fold Predicted Structure: AF-P22087-F1
Complex: C/D RNP
Enzyme type: methyltransferase
Position of modification - modification: many - Nm


PDB Structures:


2IPX

Structure Description:

Title:
Classification:
Technique:

Abstract of the PDB Structure's related Publication:



Download RCSB-PDB Structures:

Pdb Files   2IPX.pdb  
Pdbx/mmCIF Files   2IPX.cif  


Protein sequence:

MKPGFSPRGGGFGGRGGFGDRGGRGGRGGFGGGRGRGGGFRGRGRGGGGGGGGGGGGGRGGGGFHSGGNRGRGRGGKRGNQSGKNVMVEPHRHEGVFICRGKEDALVTKNLVPGESVYGEKRVSISEGDDKIEYRAWNPFRSKLAAAILGGVDQIHIKPGAKVLYLGAASGTTVSHVSDIVGPDGLVYAVEFSHRSGRDLINLAKKRTNIIPVIEDARHPHKYRMLIAMVDVIFADVAQPDQTRIVALNAHTFLRNGGHFVISIKANCIDSTASAEAVFASEVKKMQQENMKPQEQLTLEPYERDHAVVVGVYRPPPKVKN

Comments:

FBL (fibrillarin) is a catalytic subunit of a multiprotein C/D RNP complex and homologue of S. cerevisiae Nop1 protein. It requires snoRNA to identify the substrate. The core of the complex is made of 15.5kD, Nop56 and Nop58 proteins.




Reaction Substrate SubstrateType Position (Anti)Codon Modified (Anti)Codon Amino Acid Change Transcript Name Transcript Region Cellular Localization References
N:Nm undefined RNA ()   3'end

Alpha Fold Predicted Structure:






Clear Selection and Reset Camera

Protein sequence:

M K P G F S P R G G G F G G R G G F G D R G G R G G R G G F G G G R G R G G G F R G R G R G G G G G G G G G G G G G R G G G G F H S G G N R G R G R G G K R G N Q S G K N V M V E P H R H E G V F I C R G K E D A L V T K N L V P G E S V Y G E K R V S I S E G D D K I E Y R A W N P F R S K L A A A I L G G V D Q I H I K P G A K V L Y L G A A S G T T V S H V S D I V G P D G L V Y A V E F S H R S G R D L I N L A K K R T N I I P V I E D A R H P H K Y R M L I A M V D V I F A D V A Q P D Q T R I V A L N A H T F L R N G G H F V I S I K A N C I D S T A S A E A V F A S E V K K M Q Q E N M K P Q E Q L T L E P Y E R D H A V V V G V Y R P P P K V K N

Secondary Structure Alphabet

  • G: 3-turn helix (310helix)
  • H: α-helix
  • I: 𝝅-helix (5 - turn helix)
  • T: Hydrogen Bonded Turn
  • B: β-sheet
  • S: Bend
  • C: Coil (residues not present in any of the above conformations)
  • N: Not assigned

Download PDB Structures & DSSP Secondary Structures:

Alpha Fold Pdb Files   AF-P22087-F1.pdb  
Alpha Fold Pdbx/mmCIF Files   AF-P22087-F1.cif  
DSSP Secondary Structures   P22087.dssp  





Diseases connected to this enzyme:

Description Reaction Disease Name
Hypermethylation of 4506 in 28S subunit of the ribosome leads to ribosome biogenesis deregulation N:Nm
β-thalassemia
Loss of 2'-O-Me results in decreased leukemia self-renewal potential and reduced colony formation potential. N:Nm
Leukemia
Hypermethylation of 4506 in 28S subunit of the ribosome leads to ribosome biogenesis deregulation N:Nm
Hemoglobin E
Genetic associations and regulation of expression indicate an independent role for 14q32 snoRNAs in human cardiovascular disease. N:Nm
Cardiovascular disease
Methylation levels on 5.8S, 18S, and 28S rRNAs are slightly increasing in p53 knock-downs. N:Nm
Breast cancer

Publications:

Title Authors Journal Details PubMed Id DOI
Evolutionary conservation of the human nucleolar protein fibrillarin and its functional expression in yeast. Jansen RP, Hurt EC, Kern H, Lehtonen H, Carmo-Fonseca M, Lapeyre B, Tollervey D J Cell Biol [details] 2026646 -
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 SJ, Yang XD, Steitz JA EMBO J [details] 1714385 -
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 [details] 14583623 -
cDNA cloning and sequencing of human fibrillarin, a conserved nucleolar protein recognized by autoimmune antisera. Aris JP, Blobel G Proc Natl Acad Sci U S A [details] 1846968 -

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