Linked Life Data

CPATH-123887

Source:http://cbio.mskcc.org/cpath#CPATH-123887

Statements in which the resource exists.
SubjectPredicateObjectContext
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cpath:CPATH-123887http://www.biopax.org/relea...Lysine-specific demethylase 4Alld:biogrid
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cpath:CPATH-123887http://www.biopax.org/relea...1.14.11.-lld:biogrid
cpath:CPATH-123887http://www.biopax.org/relea...Jumonji domain-containing protein 2Alld:biogrid
cpath:CPATH-123887http://www.biopax.org/relea...JmjC domain-containing histone demethylation protein 3Alld:biogrid
cpath:CPATH-123887http://www.biopax.org/relea...FUNCTION: Histone demethylase that specifically demethylates 'Lys- 9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate. Participates in transcriptional repression of ASCL2 and E2F-responsive promoters via the recruitment of histone deacetylases and NCOR1, respectively. COFACTOR: Binds 1 Fe(2+) ion per subunit. SUBUNIT: Interacts with histone deacetylase proteins HDAC1, HDAC2 and HDAC3. Interacts with RB and NCOR1. Interacts with HTLV-1 Tax protein. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Ubiquitous. DOMAIN: The 2 Tudor domains recognize and bind methylated histone H3 'Lys-4' residue. Double Tudor domain has an interdigitated structure and the unusual fold is required for its ability to bind methylated histone tails. Trimethylated H3 'Lys-4' is bound in a cage of 3 aromatic residues, 2 of which are from the Tudor domain 2, while the binding specificity is determined by side-chain interactions involving residues from the Tudor domain 1. The Tudor domains are able to bind trimethylated histone H3 'Lys-4', trimethylated histone H3 'Lys-9', di- and trimethylated H4 'Lys- 20'. SIMILARITY: Belongs to the JHDM3 histone demethylase family. SIMILARITY: Contains 1 JmjC domain. SIMILARITY: Contains 1 JmjN domain. SIMILARITY: Contains 2 PHD-type zinc fingers. SIMILARITY: Contains 2 Tudor domains. SEQUENCE CAUTION: Sequence=BAA31652.2; Type=Erroneous initiation; Note=Translation N-terminally shortened; GENE SYNONYMS: JHDM3A JMJD2 JMJD2A KIAA0677. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.lld:biogrid
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