{PDOC51183}
{PS51183; JMJN}
{PS51184; JMJC}
{BEGIN}
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* JmjN and JmjC domains profiles *
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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 beta-barrel structure containing
two sheets  of  five  antiparallel beta 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.

-Sequences known to belong to this class detected by the first profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Sequences known to belong to this class detected by the second profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: February 2006 / First entry.

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

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