PROSITE documentation PDOC00489
Fibrillarin signature


Fibrillarin [1] is a component of a nucleolar small nuclear ribonucleoprotein (SnRNP) particle thought to participate in the first step of the processing of pre-rRNA. In mammals, fibrillarin is associated with the U3, U8 and U13 small nuclear RNAs [2].

Fibrillarin is an extremely well conserved protein of about 320 amino acid residues. Structurally it consists of three different domains:

  • An N-terminal domain of about 80 amino acids which is very rich in glycine and contains a number of dimethylated arginine residues (DMA).
  • A central domain of about 90 residues which resembles that of RNA-binding proteins and contains an octameric sequence similar to the RNP-2 consensus found in such proteins.
  • A C-terminal α-helical domain.

A protein evolutionary related to fibrillarin has been found [3] in archaebacteria. This protein (gene flpA) is involved in pre-rRNA processing. It lacks the Gly/Arg-rich N-terminal domain.

As a signature pattern, we selected a region that start with and encompass the RNP-2 like octapeptide sequence.

Last update:

April 2006 / Pattern revised.


Technical section

PROSITE method (with tools and information) covered by this documentation:

FIBRILLARIN, PS00566; Fibrillarin signature  (PATTERN)


1AuthorsAris J.P. Blobel G.
TitlecDNA cloning and sequencing of human fibrillarin, a conserved nucleolar protein recognized by autoimmune antisera.
SourceProc. Natl. Acad. Sci. U.S.A. 88:931-935(1991).
PubMed ID1846968

2AuthorsBandziulis R.J. Swanson M.S. Dreyfuss G.
TitleRNA-binding proteins as developmental regulators.
SourceGenes Dev. 3:431-437(1989).
PubMed ID2470643

3AuthorsAgha-Amiri K.
SourceJ. Bacteriol. 176:2124-2127(1994).

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