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PIM2 is a serine/threonine protein kinase which is a part of the CAMK family. PIM2 is expressed in various tissues mainly in spleen, thymus, testis and small intestine. PIM2 is implicated in tumor phenotypes and participates in the formation and preservation of Long-Term Potentiation (LTP). PIM2 is also involved in the positive regulation of chondrocyte survival and autophagy in the epiphyseal growth plate.

PIM1, which is a part of the Ser/Thr protein kinase family and PIM subfamily, is expressed primarily in B-lymphoid and myeloid cell lines, and is overexpressed in hematopoietic malignancies and in prostate cancer. PIM1 functions as Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation, consequently providing a selective advantage in tumorigenesis. Both human and orthologous mouse genes have been reported to encode two isoforms resulting from the use of alternative in-frame translation initiation codons, the upstream non-AUG (CUG) and downstream AUG codons.

p59-Fyn is a member of the protein-tyrosine kinase oncogene family. p59fyn is a membrane-associated non-receptor protein tyrosine kinase that belongs to the Src-family of kinases. p59-Fyn encodes a membrane-associated tyrosine kinase which is implicated in the control of cell growth. p59-Fyn associates with the p85 subunit of phosphatidylinositol 3-kinase and interacts with the fyn-binding protein. The unique N-terminal domain of p59fyn interacts with the CD3 and eta chains of the TcR. p59fyn can bind other proteins (p82 and p116) through its SH2 and SH3 domains, which may act as substrates or regulators of fyn activity. p59fyn is highly expressed in brain suggesting that it may have a role in the sensory nervous network and in myelination at early stages of CNS formation. Distinct isoforms exist due to alternative splicing.

LASP1 has a vital part in the regulation of dynamic actin-based, cytoskeletal activities. Agonist-dependent changes in LASP1 phosphorylation can additionally assist in regulation of actin-associated ion transport activities in the parietal cell and in several other F-actin-rich secretory epithelial cell types.

P85a functions as the regulatory subunit of the class IA PI3-kinase isoforms a, b, and d.
It contains two SH2 domains that bind to tyrosine-phosphorylated growth factor receptors or substrate adaptor proteins.
It also contains a BH (breakpoint cluster region homology) domain that shows GAP activity towards the small GTPases Rab4, Rab5, Cdc42, Rac1 and to a lesser extend towards Rab6 and Rab11.
It was shown that PI3Ka catalytic subunit mediated phosphorylation of the p85a adapter reduces the lipid kinase activity of the heterodimer and this gives hints for PI3K-dependent signaling events not requiring production of 3’-phosphorylated phosphoinositides.
PI3Ka protein kinase activity has been implicated in IRS-1 serine phosphorylation in insulin-treated adipocytes and in STAT3 and IRS-1 phosphorylation upon activation of the type 1 IFN receptor by IFN-a.

The Melanoma Inhibitory protein (MIA) was identified as an inhibitor of in vitro growth of malignant melanoma cells. The protein contains a SH3 domain. MIA acts as a potent tumor cell growth inhibitor for malignant melanoma cells and some other neuroectodermal tumors, including gliomas, in an autocrine fashion. In a study of human melanoma cell lines with different metastatic capacity MIA mRNA expression appeared to be inversely correlated with pigmentation. MIA has been shown to represent a very sensitive and specific serum marker for systemic malignant melanoma that might be useful for staging of primary melanomas, detection of progression from localized to metastatic disease during follow-up, and monitoring therapy of advanced melanomas.

DIRAS1 is a member of a distinct branch of the functionally diverse Ras superfamily of monomeric GTPases. DIRAS1 demonstrates low GTPase activity and exists mainly in the GTP-bound form. Ras proteins operate as binary molecular switches that control intracellular signaling networks. Ras-regulated signal pathways regulate such processes as actin cytoskeletal integrity, proliferation, differentiation, cell adhesion, apoptosis, and cell migration. Ras and ras-related proteins are frequently deregulated in cancers, leading to increased invasion and metastasis, and decreased apoptosis.

GADD45GIP1 is a nuclear protein which takes part in apoptosis control. GADD45GIP1 is expressed in several tissues, such as heart, thyroid, trachea, kidney, ovary, pancreas, testis and stomach and acts as a negative regulator of G1 to S phase cell cycle production by collaborating with GADD45 proteins to inhibit the activity of cyclin-dependent kinases.

The PI3Kb isoform can be activated by insulin via the insulin receptor to initiate a cascade of events that control cell growth and metabolism. The activation of
PI3Kb is mediated by the p85 regulatory subunit binding to tyrosine phosphorylated insulin receptor substrate (IRS) proteins (e.g. IRS-1 and IRS-2).
It was also shown that PI3Kb is involved in apoptosis in human colon carcinoma cells. Injection of neutralizing antibodies specific to p110b in WiDr,
HCT116 and CO 115 adenocarcinoma cells inhibited de novo DNA synthesis.
PI3Kb is the major PI3K isoform required for apoptotic cell and Fc-g receptor mediated phagocytosis shown for primary mouse macrophages and the Jurkat human leukemia T cell line.
It was shown by several research groups that the catalytic subunit of PI3Kb can be activated by Gbg subunits of G-protein coupled receptors.

Cyclin-dependent kinase inhibitors (CDKIs) are proteins that bind to and inhibit the activity of CDKs. Two major classes of CDK inhibitors have been identified. The p16 family (p15, p16, p18 and p19) binds to and inhibits the activities of CDK4 and CDK6. The p21 family (p21, p27, p28 and p57) can bind to broad range of CDK-cyclin complexes and inhibit their activities. CDKIs are capable of suppressing growth, and several lines of evidence strongly suggest that at least some CDKIs may be tumor suppressor proteins.

CINP is a member of the CINP family. CINP cooperates with the components of the replication complex and 2 kinases, CDK2 and CDC7, to provide a working and physical link between CDK2 and CDC7 throughout the firing of the origins of replication.

Cyclin-dependent kinase inhibitors (CDKIs) are proteins that bind to and inhibit the activity of CDKs. Two major classes of CDK inhibitors have been identified. The p16 family (p15, p16, p18 and p19) binds to and inhibits the activities of CDK4 and CDK6. The p21 family (p21, p27, p28 and p57) can bind to broad range of CDK-cyclin complexes and inhibit their activities. CDKIs are capable of suppressing growth, and several lines of evidence strongly suggest that at least some CDKIs may be tumor suppressor proteins.

IFN-gamma produced by lymphocytes activated by specific antigens or mitogens.
IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons.

Macrophage Inflammatory Proteins (MIP) belong to the family of chemotactic cytokines known as chemokines. In humans, there are two major forms, MIP-1a and MIP-1b that are now officially named CCL3 and CCL4 respectively. Both are major factors produced by macrophages after they are stimulated with bacterial endotoxins. They activate human granulocytes (neutrophils, eosinophils and basophils) which can lead to acute neutrophilic inflammation. They also induce the synthesis and release of other pro-inflammatory cytokines such as interleukin 1 (IL-1), IL-6 and TNF-a from fibroblasts and macrophages. The genes for CCL3 and CCL4 are both located on human chromosome 17.

Phosphatidylinositol transfer protein beta isoform (PITPNB) is found in the cytoplasm, where it catalyzes the transfer of phosphatidylinositol (PI) and phosphatidylcholine (PC) between membranes. PITPNB mobilizes PI from the endoplasmic reticulum and regulates its release from stored vesicles in the Golgi network. PITPNB is extensively expressed in various tissues.

Kirsten Rat Sarcoma Viral Oncogene, Isoform 2A (KRAS-2A) belongs to the small GTPase superfamily. The KRAS-2A protein is involved in a variety of malignancies, including lung adenocarcinoma, mucinous adenoma, ductal carcinoma of the pancreas and colorectal carcinoma. Ras family members impact cell growth and differentiation events in a subcellular membrane compartmentalization-based signaling system under normal conditions. Oncogenic Ras can deregulate processes which control both cell proliferation and apoptosis.

KIT, also known as KIT Proto-Oncogene Receptor Tyrosine, is a cytokine receptor which is expressed not only in hematopoietic stem cells but likewise in other cell types. KIT binds to receptor tyrosine kinase type III, which is a stem cell factor, also named a "rigid factor" or "c-kit ligand". Once this receptor binds to stem cell factor (SCF), it forms a dimer which activates intrinsic tyrosine kinase activity, which sequentially phosphorylates & activates signaling molecules which breed signals in cells. This receptor protects vascular smooth muscle cells from apoptosis in addition to restoring cardiac function after myocardial infarction.

RAB27A is part of the small GTPase superfamily, Rab family. RAB27A is membrane-bound and participates in protein transport and small GTPase mediated signal transduction. Mutations in this RAB27A are associated with Griscelli syndrome type 2. RAB27A is involved in cytotoxic granule exocytosis in lymphocytes.RAB27A is necessary for both granule maturation and granule docking and priming at the immunologic synapse.

RAP2A belongs to the RAS oncogene family and a Ras-like small G protein. The RAP2A protein shares 60% identity with Rap1A and exhibits a carboxy-terminal CAAX motif and 2 upstream cysteines similar to those of the H-Ras, K-Ras and N-Ras proteins. In contrast with Rap1A and Rap1B, overexpression of RAP2A doesn’t obstruct the Ras signaling pathway.

Zinc Finger Protein 689 (ZNF689) is a member of the krueppel C2H2-type zinc-finger protein family. The ZNF689 protein contains 12 C2H2-type zinc fingers and 1 KRAB domain. ZNF689 may be involved in transcriptional regulation.

FGFR1 oncogene partner (FGFR1OP) is a member of the FGFR1OP family. The FGFR1OP protein is an essentially hydrophilic protein proposed to be a leucine-rich protein family member. A t(6;8)(q27;p11) chromosomal translocation, fusing the FGFR1OP gene and the FGFR1 gene, is seen in cases of myeloproliferative disorder. The ensuing chimeric protein contains the N-terminal leucine-rich region of the FGFR1OP protein fused to the catalytic domain of FGFR1. The FGFR1OP gene is believed to play a significant role in normal proliferation and differentiation of the erythroid lineage.

Phosphatidylinositol transfer protein alpha (PITPNA) is found in the cytoplasm, where it catalyzes the transfer of phosphatidylinositol (PI) and phosphatidylcholine (PC) between membranes. PITPNA belongs to a family of lipid-binding proteins which transfer molecules of phosphatidylinositol or phosphatidylcholine between membrane surfaces. PITPNA is implicated in phospholipase C signaling and in the production of phosphatidylinositol 3, 4, 5-trisphosphate (PIP3) by phosphoinositide-3-kinase.