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Potassium Channel Tetramerisation Domain Containing 11 (KCTD11) is a 232 amino acid regulator of neuronal differentiation which induces growth arrest, apoptosis and the expression of p27 (cyclin-dependent kinase inhibitor). KCTD11 is expressed most highly in cerebellum. KCTD11 functions as an antagonist of the Hedgehog pathway and activator of the caspase cascade and among its related super-pathways are Melatonin Signaling and Activation of cAMP-Dependent PKA.

CCNH is part of the cyclin family that is known for its protein abundance through the cell cycle. Cyclins act as regulators of CDK kinases. CCNH forms a complex with CDK7 kinase and ring finger protein MAT1. The kinase complex is able to phosphorylate CDK2 and CDC2 kinases, therefore it functions as a CDK-activating kinase (CAK). CCNH and its kinase collaborator are components of TFIIH, as well as RNA polymerase II protein complexes.

UbcH12 is functional in in vitro NEDDylation reactions. It has been shown to form a thioester linkage with NEDD8 in the presence of the NEDD8 activating enzyme complex Uba3/APP-BP1. APP-BP1 binds to the amyloid precursor protein (APP) carboxy terminal domain and is important in conjunction with Uba3 and UbcH12 in driving cells through the S to M checkpoint. It was demonstrated to be the E2 responsible for the NEDDylation of the Cul-1 component of the SCF (?-TRCP) complex which is important as the E3-ligase in the ubiquitinylation of I?B?. NEDDylation of Cul-1 is essential for conjugation and processing of NF-?B p105 by SCF (?-TRCP) following phosphorylation of the complex. A dominant negative form of UbcH12, previously demonstrated to sequester NEDD8 and inhibit its conjugation, inhibits both conjugation and processing of p105, which is alleviated by wild-type UbcH12.

Ubiquitin-conjugating enzyme E2S (UBE2S) belongs to the ubiquitin-conjugating enzyme family. UBE2S is able to form a thiol ester linkage with ubiquitin in a ubiquitin activating enzyme-dependent manner, a typical property of ubiquitin carrier proteins. UBE2S catalyzes the covalent attachment of ubiquitin to other proteins. UBE2S acts as a crucial factor of the anaphase promoting complex/cyclosome (APC/C), which is a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. UBE2S acts by purposely elongating 'Lys-11'-linked polyubiquitin chains initiated by the E2 enzyme UBE2C/UBCH10 on APC/C substrates, augmenting the degradation of APC/C substrates by the proteasome and promoting mitotic exit. UBE2S also acts by elongating ubiquitin chains initiated by the E2 enzyme UBE2D1/UBCH5 in vitro; it is nevertheless uncertain whether UBE2D1/UBCH5 acts as an E2 enzyme for the APC/C in vivo. UBE2S is also involved in ubiquitination and consequent degradation of VHL, resulting in an accumulation of HIF1A.

Ubiquitin-Conjugating Enzyme E2G2 (UBE2G2) is a protein coding gene which is a part of the E2 ubiquitin-conjugating enzyme family. UBE2G2 accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to various proteins. UBE2G2 is ubiquitously expressed mainly in adult muscle. UBE2G2 also takes part in endoplasmic reticulum-associated degradation (ERAD).

FLT3 ligand is a receptor for the fl cytokine has a tyrosine-protein kinase activity & a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand synergizes with other CSFs and interleukins to induce growth and differentiation.

UBE2N belongs to the E2 ubiquitin-conjugating enzyme family. UBE2N catalyzes the ATP-dependent synthesis of non-canonical polyubiquitin chains, a process which doesn’t set in motion proteasomal degradation. UBE2N mediates the transcription of some target genes and is believed to have a role in cell cycle progression; cellular differentiation and DNA repair mechanisms which ensure cell survival after DNA damage.

BRCC3 is a subunit of the BRCA1-BRCA2-containing complex (BRCC), which is an E3 ubiquitin ligase. BRCC3 is also thought to be involved in the cellular response to ionizing radiation and progression through the G2/M checkpoint.

Kallikreins are a subgroup of serine proteases having various physiological functions. Many kallikreins are implicated in carcinogenesis and some have potential of becoming novel cancer and other disease biomarkers. Kallikrein-13 (KLK13) is one of the fifteen kallikrein subfamily members located in a cluster on chromosome 19. KLK13 gene expression is regulated by steroid hormones and may be useful as a marker for breast cancer.

FLT3 ligand is a receptor for the fl cytokine has a tyrosine-protein kinase activity & a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand synergizes with other CSFs and interleukins to induce growth and differentiation.

GZMK is a part of a group of related serine proteases from the cytoplasmic granules of cytotoxic lymphocytes. Cytolytic T lymphocytes and natural killer cells have the outstanding ability to bind, recognize and lyse specific target cells. They defend their host by lysing cells bearing on their surface 'nonself' antigens, usually peptides or proteins resulting from infection by intracellular pathogens.

Hexokinases phosphorylate glucose to produce glucose-6-phosphate, thus committing glucose to the glycolytic pathway. HK3 encodes hexokinase 3. Similar to hexokinases 1 and 2, this allosteric enzyme is inhibited by its product glucose-6-phosphate. Hexokinase3 lacks the hydrophobic N-terminal sequence critical for targeting to mitochondria. Hexpkinase3 may have anabolic functions, providing H6P for glycogen or lipid synthesis.

EPH Receptor A2 (EPHA2) is a member of the ephrin receptor subfamily of the protein-tyrosine kinase family. EPHA2 is a protein which binds ephrin-A ligands. EPH and EPH-related receptors are associated with mediating developmental events, particularly in the nervous system. Receptors in the EPH subfamily normally have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. The ephrin receptors are divided into two groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. EPHA2 gene mutations are the cause of certain genetically-related cataract disorders.

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.

Charged Multivesicular Body Protein 5 (CHMP5) is a member of the chromatin-modifying protein/charged multivesicular body protein (CHMP) family. These proteins comprise the ESCRT-III (endosomal sorting complex required for transport III), a complex involved in degradation of surface receptor proteins and development of endocytic multivesicular bodies (MVBs). Certain CHMPs have both nuclear and cytoplasmic/vesicular distributions, and one such CHMP the CHMP1A, is essential for both MVB formation and regulation of cell cycle progression.

Poly (ADP-Ribose) Polymerase 2 (PARP2) contains a catalytic domain which is homologous to that of poly (ADP-ribosyl) transferase but lacks an N-terminal DNA binding domain which activates the C-terminal catalytic domain of poly (ADP-ribosyl) transferase. PARP2 is capable of catalyzing a poly (ADP-ribosyl)ation reaction. The basic residues within the N-terminal area of this protein can bear potential DNA-binding properties, and can be engaged in the nuclear and/or nucleolar targeting of the protein. There has been found two alternatively spliced transcript variants encoding distinct isoforms.

RNH1 belongs to the proteinaceous cytoplasmic RNase inhibitors family which occur in many tissues and binds to both intracellular and extracellular RNases. In addition to control of intracellular RNases, the inhibitor may have a part in the regulation of angiogenin. The 50kDa RNH1 binds to ribonucleases and holds them in a latent form. Since neutral and alkaline ribonucleases possibly play a critical role in the turnover of RNA in eukaryotic cells, RNH1 may be vital for control of mRNA turnover; the interaction of eukaryotic cells with ribonuclease may be reversible in vivo.

EPH Receptor A2 (EPHA2) is a member of the ephrin receptor subfamily of the protein-tyrosine kinase family. EPHA2 is a protein which binds ephrin-A ligands. EPH and EPH-related receptors are associated with mediating developmental events, particularly in the nervous system. Receptors in the EPH subfamily normally have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. The ephrin receptors are divided into two groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. EPHA2 gene mutations are the cause of certain genetically-related cataract disorders.

Cathepsin D is synthesized as a 54kDa precursor, which is proteolytically processed to an intermediate 48kDa single chain, which matures into more stable 34kDa and 14kDa two chain form. It is an estrogen-regulated lysosomal protease that has been suggested to facilitate cancer cell migration and invasion by digesting the basement membrane, extracellular matrix, and xonnective tissue. Because of its mitogenic and proteolytic activities, it has been implicated as a prognostic marker in many tumor types. Cathepsin D is expressed in epithelial cells as well as in macrophages.

The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are at least seven isoforms that have been identified in mammals. The 14-3-3gamma, a subtype of the 14-3-3 family of proteins, was thought to be brain and neuron-specific. It has been shown to interact with RAF1 and protein kinase C, proteins involved in various signal transduction pathways.