ID:KDM5C_HUMAN DESCRIPTION: RecName: Full=Lysine-specific demethylase 5C; EC=1.14.11.-; AltName: Full=Histone demethylase JARID1C; AltName: Full=Jumonji/ARID domain-containing protein 1C; AltName: Full=Protein SmcX; AltName: Full=Protein Xe169; FUNCTION: Histone demethylase that specifically demethylates 'Lys- 4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-4'. Participates in transcriptional repression of neuronal genes by recruiting histone deacetylases and REST at neuron-restrictive silencer elements. COFACTOR: Alpha-ketoglutarate. COFACTOR: Binds 1 Fe(2+) ion per subunit. SUBUNIT: Part of two distinct complexes, one containing E2F6, and the other containing REST. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Expressed in all tissues examined. Highest levels found in brain and skeletal muscle. DOMAIN: The first PHD-type zinc finger domain recognizes and binds H3-K9Me3. DOMAIN: Both the JmjC domain and the JmjN domain are required for enzymatic activity. DISEASE: Defects in KDM5C are the cause of mental retardation syndromic X-linked JARID1C-related (MRXSJ) [MIM:300534]. MRXSJ is characterized by significantly sub-average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period. MRXSJ patients manifest mental retardation associated with variable features such as slowly progressive spastic paraplegia, seizures, facial dysmorphism. MISCELLANEOUS: Escapes X-inactivation. SIMILARITY: Belongs to the JARID1 histone demethylase family. SIMILARITY: Contains 1 ARID domain. SIMILARITY: Contains 1 JmjC domain. SIMILARITY: Contains 1 JmjN domain. SIMILARITY: Contains 2 PHD-type zinc fingers. WEB RESOURCE: Name=GeneReviews; URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/JARID1C";
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on P41229
Front
Top
Side
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.
Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.