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PROSITE documentation PDOC51183JmjN and JmjC domains profiles
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PURL: https://purl.expasy.org/prosite/documentation/PDOC51183
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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PROSITE methods (with tools and information) covered by this documentation:
| 1 | Authors | Balciunas D. Ronne H. |
| Title | Evidence of domain swapping within the jumonji family of transcription factors. | |
| Source | Trends. Biochem. Sci. 25:274-276(2000). | |
| PubMed ID | 10838566 |
| 2 | Authors | Clissold P.M. Ponting C.P. |
| Title | JmjC: cupin metalloenzyme-like domains in jumonji, hairless and phospholipase A2beta. | |
| Source | Trends. Biochem. Sci. 26:7-9(2001). | |
| PubMed ID | 11165500 |
| 3 | Authors | Elkins J.M. Hewitson K.S. McNeill L.A. Seibel J.F. Schlemminger I. Pugh C.W. Ratcliffe P.J. Schofield C.J. |
| Title | Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1 alpha. | |
| Source | J. Biol. Chem. 278:1802-1806(2003). | |
| PubMed ID | 12446723 | |
| DOI | 10.1074/jbc.C200644200 |
| 4 | Authors | Tsukada Y. Fang J. Erdjument-Bromage H. Warren M.E. Borchers C.H. Tempst P. Zhang Y. |
| Title | Histone demethylation by a family of JmjC domain-containing proteins. | |
| Source | Nature 439:811-816(2006). | |
| PubMed ID | 16362057 | |
| DOI | 10.1038/nature04433 |
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