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HDAC9 (Histone Deacetylase 9) catalyses the deacetylation of lysine residues on the core histones (H2A, H2B, H3 and H4). It belongs to the Class IIa HDAC family, which are key regulators of several developmental and differentiation processes such as cardiac growth. HDAC9 represses MEF2 (myocyte enhancer factor 2)-dependent transcription, playing an important role in cardiac hypertrophy. $n$nThe HDAC9 isoform MITR/HDRP lacks active site residues and is therefore catalytically inactive. It rep

Anillin, also known as scraps homolog, is an evolutionarily conserved Actin- binding protein required for cytokinesis that was first identified in Drosophila melanogaster. Anillin is a ubiquitously expressed protein with highest expression levels in the central nervous system. It is predominantly found in the nucleus and it localizes to the cleavage furrow during cytokinesis, forming a ring with the help of Rac GTPase. During cytokinesis, Anillin interacts with CD2AP and functions to concentr

Phosphodiesterases (PDE, also designated cyclic nucleotide phosphodiesterase) are important for the downregulation of the intracellular level of the second messenger cyclic adenosine monophosphate (cAMP) by hydrolyzing cAMP to 5'AMP. Phosphodiesterase type 3 isoforms, PDE3A and 3B, are expressed primarily in cardiovascular tissue and adipose tissue, respectively. PDE3A, is found in myocardium and platelets and PDE3B is found in lymphocytes. The PDE7A1 (HCP1) isozyme and the PDE7A2 protein

This gene encodes a transmembrane receptor that is associated with lysosomes. The encoded protein, also known as E3 protein, may play a role in hematopoiesis. [provided by RefSeq, Feb 2009]

KLC2 is a 622 amino acid protein that contains six TPR repeats and belongs to the kinesin light chain family. Existing in an oligomeric complex composed of two light and two heavy chain kinesin proteins, KLC2 plays a role in coupling organelle transport with ATPase activity. The gene encoding KLC2 maps to human chromosome 11, which houses over 1,400 genes and comprises nearly 4% of the human genome.

Apoptosis is mediated by death domain containing adapter molecules and a caspase family of proteases. Certain serine/threonine protein kinases, such as ASK1 and RIP, are mediators of apoptosis. Two novel serine/threonine kinases that induce apoptosis were recently identified and designated DRAK1 and DRAK2 (for DAP kinase related apoptosis inducing protein kinases). DRAKs contain an N terminal kinase domain and a C terminal regulation domain. Overexpression of DRAK2 induces apoptosis. DRAKs