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The protein encoded by this gene is a ubiquitin-like protein that is conjugated to intracellular target proteins upon activation by interferon-alpha and interferon-beta. Several functions have been ascribed to the encoded protein, including chemotactic activity towards neutrophils, direction of ligated target proteins to intermediate filaments, cell-to-cell signaling, and antiviral activity during viral infections. While conjugates of this protein have been found to be noncovalently attached

Endocannaboids such as arachidonoyl ethanolamide and 2-arachidonoyl glycerol function as short range modulators of cell and synaptic activity. Monoacylglycerol lipase hydrolyzes 2-arachidonoyl glycerol which terminates it's biological actions. Monoacylglycerol lipase also works consecutively with hormone sensitive lipase to mobilize fatty acids from triglyceride stores of adipocytes. Monoacylglycerol lipase is expressed in kidney, spleen, heart, liver, testis, stomach, brain and lung tissue

This gene encodes a member of the IQGAP family. The protein contains three IQ domains, one calponin homology domain, one Ras-GAP domain and one WW domain. It interacts with components of the cytoskeleton, with cell adhesion molecules, and with several signaling molecules to regulate cell morphology and motility. [provided by RefSeq, Jul 2008]

The protein encoded by this gene is a member of the Ser/Thr protein kinase family. This protein kinase is highly similar to the gene products of S. cerevisiae cdc28, and S. pombe cdc2. It is a catalytic subunit of the cyclin-dependent protein kinase complex, whose activity is restricted to the G1-S phase, and essential for cell cycle G1/S phase transition. This protein associates with and regulated by the regulatory subunits of the complex including cyclin A or E, CDK inhibitor p21Cip1 (CDKN

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