HEAB is a 425 amino acid nuclear protein that belongs to the Clp1 family. Utilizing magnesium, manganese or nickel as cofactors, HEAB participates in the phosphorylation of the 5'-hydroxyl groups of double- and single- stranded RNA and DNA. HEAB is a member of the tRNA splicing endonuclease complex, in conjunction with TSEN2, TSEN15, TSEN34 and TSEN54, and is also a member of the pre-mRNA cleavage complex II. The gene encoding HEAB maps to human chromosome 11q12.1 and mouse chromosome 2 D

Contactin 4 is a 1,026 amino acid protein encoded by the human gene CNTN4. Contactin 4 belongs to the immunoglobulin superfamily and is a member of the Contactin family. Contactin 4 contains four fibronectin type-3 domains, six Ig-like C2-type domains, and has three isoforms (1,2,3). Defects in the CNTN4 gene are a cause of 3p deletion syndrome (3PDS). 3PDS is a rare contiguous gene disorder involving the loss of the telomeric portion of the short arm of chromosome 3 and is characterized by

This gene encodes a member of the oxysterol-binding protein (OSBP) family, a group of intracellular lipid receptors. Most members contain an N-terminal pleckstrin homology domain and a highly conserved C-terminal OSBP-like sterol-binding domain, although some members contain only the sterol-binding domain. Transcript variants derived from alternative promoter usage and/or alternative splicing exist; they encode different isoforms. [provided by RefSeq, Jul 2008]

The mammalian c-H-, c-K- and N-Ras proto-oncogenes encode ubiquitously expressed proteins (1,2). p21Ras can exist in either a physiologically quiescent GDP-binding state or a GTP-binding signal-emitting state (3). Oncogenic p21Ras proteins are trapped in the excited signal-emitting state because the mechanism normally employed to delimit their excitation period, hydrolysis of their bound GTP to GDP, is impaired as a result of specific mutations (3). Interaction of p21Ras with GTPase activating

IL15RA is a cytokine receptor that specifically binds IL15 with high affinity. It shares two subunits with the receptor of IL2, the IL2R beta and IL2R gamma chains. This forms the basis of many overlapping biological activities of IL15 and IL2. The IL2 receptor requires an additional IL2-specific alpha subunit for high affinity IL2 binding. This protein is structurally related to IL2R alpha, but is capable of binding IL15 with high affinity independent of other subunits, which suggests the di