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SHIP1 is a member of the inositol polyphosphate-5-phosphatase (INPP5) family and contains an N-terminal SH2 domain, an inositol phosphatase domain, and two C-terminal protein interaction domains. Expression of this protein is restricted to hematopoietic cells where its movement from the cytosol to the plasma membrane is mediated by tyrosine phosphorylation in response to multiple cytokine and B and T cell receptor activation. At the plasma membrane, the protein hydrolyzes the 5' phosphate

The Alpha-, Beta-, Gamma-, and Delta -catenins are proteins that bind to the highly conserved, intracellular cytoplasmic tail of E-cadherin. Together, the catenin/cadherin complexes play an important role mediating cellular adhesion. Alpha-catenin interacts with E-cadherin associated protein and also associates with other members of the cadherin family, such as N-cadherin and P-cadherin. Beta-catenin associates with the cytoplasmic portion of E-cadherin, which is necessary for the function o

SHIP1 is a member of the inositol polyphosphate-5-phosphatase (INPP5) family and contains an N-terminal SH2 domain, an inositol phosphatase domain, and two C-terminal protein interaction domains. Expression of this protein is restricted to hematopoietic cells where its movement from the cytosol to the plasma membrane is mediated by tyrosine phosphorylation in response to multiple cytokine and B and T cell receptor activation. At the plasma membrane, the protein hydrolyzes the 5' phosphate

Methylation is an important reaction in the metabolism of many drugs, other xenobiotics and endogenous molecules. A methyltransferase is a type of transferase enzyme that transfers a methyl group from a donor to an acceptor. INMT (indolethylamine N-methyltransferase), also known as Temt or aromatic alkylamine N-methyltransferase, is a 264 amino acid protein belonging to the NNMT/PNMT/TEMT family. Localized to the cytoplasm, INMT catalyzes the N-methylation of tryptamine and structurally relat

This gene encodes a mammalian peptidase that, at neutral pH, removes tripeptides from the N terminus of longer peptides. The protein has a specialized function that is essential for some MHC class I antigen presentation. The protein is a high molecular mass serine exopeptidase; the amino acid sequence surrounding the serine residue at the active site is similar to the peptidases of the subtilisin class rather than the trypsin class. [provided by RefSeq, Jul 2008]