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PROSITE documentation PDOC51183 [for PROSITE entry PS51183]

JmjN and JmjC domains profiles





Description

The JmjN and JmjC domains are two non-adjacent domains which have been identified in the jumonji family of transcription factors. Although it was originally suggested that the JmjN and JmjC domains always co-occur and might form a single functional unit within the folded protein, the JmjC domain was latter found without the JmjN domain in organisms from bacteria to human [1,2].

JmJC domains are predicted to be metalloenzymes that adopt the cupin fold (see <PDB:1H2K>), and are candidates for enzymes that regulate chromatin remodelling. The cupin fold is a flattened β-barrel structure containing two sheets of five antiparallel β strands that form the walls of a zinc-binding cleft. JmjC domains were identified in numerous eukaryotic proteins containing domains typical of transcription factors, such as PHD (see <PDOC50016>), C2H2 (see <PDOC00028>), ARID/BRIGHT and zinc fingers [2,3]. The JmjC has been shown to function in a histone demethylation mechanism that is conserved from yeast to human [4].

In addition to eukaryotic transcription factors of the jumonji family, a JmjC domain is also found in the following proteins:

  • Eukaryotic transcription factors of the jumonji family.
  • Mammalian hairless. In human, defects in HR are the cause of alopecia universalis congenita (ALUNC) [MIM:203655]. ALUNC is a rare autosomal recessive form of hair loss characterized by hair follicles without hair.
  • Mammalian F-box/LRR-repeat protein 10 (FBXL10) and 11 (FBXL11) or JmjC domain-containing histone demethylase 1B (JHDM1B) or 1A (JHDM1A).
  • Human retinoblastoma-binding protein 2.
  • Several putative chromatin-associated proteins.
  • Bacillus subtilis hypothetical protein yxbC.
  • Escherichia coli hypothetical protein ycfD.
  • Neisseria meningitidis Z2491 hypothetical protein NMA0679.

The profiles we developed cover the entire JmjN and JmjC domains.

Last update:

February 2006 / First entry.

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Technical section

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

JMJN, PS51183; JmjN domain profile  (MATRIX)

JMJC, PS51184; JmjC domain profile  (MATRIX)


References

1AuthorsBalciunas D. Ronne H.
TitleEvidence of domain swapping within the jumonji family of transcription factors.
SourceTrends. Biochem. Sci. 25:274-276(2000).
PubMed ID10838566

2AuthorsClissold P.M. Ponting C.P.
TitleJmjC: cupin metalloenzyme-like domains in jumonji, hairless and phospholipase A2beta.
SourceTrends. Biochem. Sci. 26:7-9(2001).
PubMed ID11165500

3AuthorsElkins J.M. Hewitson K.S. McNeill L.A. Seibel J.F. Schlemminger I. Pugh C.W. Ratcliffe P.J. Schofield C.J.
TitleStructure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1 alpha.
SourceJ. Biol. Chem. 278:1802-1806(2003).
PubMed ID12446723
DOI10.1074/jbc.C200644200

4AuthorsTsukada Y. Fang J. Erdjument-Bromage H. Warren M.E. Borchers C.H. Tempst P. Zhang Y.
TitleHistone demethylation by a family of JmjC domain-containing proteins.
SourceNature 439:811-816(2006).
PubMed ID16362057
DOI10.1038/nature04433



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