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KCTD4 also known as Potassium Channel Tetramerisation Domain Containing 4 has an N-terminal homodimerization domain which contains multiple copies of kelch repeats and C2H2-type zinc fingers. Proteins which include BTB domains are consider being involved in transcriptional regulation through control of chromatin structure and function. In addition, KCTD4 is a 259 amino acid protein which contains one BTB domain, a possible role as a transcriptional regulator may be suggested.

KCTD15 protein is encoded in humans by the KCTD15 gene. KCTD15 is expressed at a high level in the brain and the hypothalamus. The potassium channel KCTD15 was identified as a genetic loci linked to higher than normal BMI in humans along with genes such as GNPDA2, MTCH2, FTO, and TMEM18. SNPs (Single nucleotide polymorphisms) in non-diabetic and diabetic patients showed that FTO was most strongly associated with obesity while MTCH2 and GNPDA2 were still notably associated with higher than normal BMI levels.

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.

BTB/POZ domain-containing protein KCTD5 (KCTD5), is a 234 amino acid protein which localizes mainly in the cytoplasm however translocates to the nucleus on interaction with REP proteins. The expression of KCTD5 is up regulated post-transcriptionally in peripheral blood lymphocytes stimulated via the T-cell receptor. KCTD5 interacts particularly with cullin3, attaches ubiquitinated proteins, and created oligomers through its BTB domain.

KCTD15 protein is encoded in humans by the KCTD15 gene. KCTD15 is expressed at a high level in the brain and the hypothalamus. The potassium channel KCTD15 was identified as a genetic loci linked to higher than normal BMI in humans along with genes such as GNPDA2, MTCH2, FTO, and TMEM18. SNPs (Single nucleotide polymorphisms) in non-diabetic and diabetic patients showed that FTO was most strongly associated with obesity while MTCH2 and GNPDA2 were still notably associated with higher than normal BMI levels.

KCTD15 protein is encoded in humans by the KCTD15 gene. KCTD15 is expressed at a high level in the brain and the hypothalamus. The potassium channel KCTD15 was identified as a genetic loci linked to higher than normal BMI in humans along with genes such as GNPDA2, MTCH2, FTO, and TMEM18. SNPs (Single nucleotide polymorphisms) in non-diabetic and diabetic patients showed that FTO was most strongly associated with obesity while MTCH2 and GNPDA2 were still notably associated with higher than normal BMI levels.

DCTD is an allosteric enzyme that exists as a homohexamer and is part of the cytidine and deoxycytidylate deaminase protein family. DTCD uses zinc as a cofactor to catalyze the deamination of dCMP to dUMP, thus making the nucleotide substrate (dUMP) that is used by thymidylate synthase.

KxDL Motif Containing 1 (KXD1) is a member of the KXD1 family. KXD1 is participating in endosomal cargo sorting. KXD1 contacts with the BLOC-1 complex and Interacts with BLOC1S1. KXD1 Interacts with DTNBP1/BLOC1S7 through coiled-coil domain.

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.

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.

CFD is an important component of the alternative pathway of complement activation. CFD cleaves and activates factor B when it binds C3b or a C3b-like protein such as C3 or CVF. CFD is a serine protease that exists as a mature protease, but it exhibits a highly restricted specificity and it appears to be substrate activated. CFD cleaves factor B bound to C3b leading to the release of the Ba fragment and leaving the Bb fragment bound to C3b. The C3b,Bb complex is called a C3 or C5 convertase because it converts these proteins to their active forms by cleaving off the small peptides C3a and C5a, respectively.

KH homology domain containing 1-like, also known as KHDC1L is a member of the KHDC1 family.KHDC1L is a protein-coding gene; an important paralog of this gene is KHDC1.

Formiminotransferase cyclodeaminase is an enzyme which catalyzes the conversion of formiminoglutamateand tetrahydrofolateinto formiminotetrahydrofolateand glutamate.
Formiminotransferase cyclodeaminase, a bifunctional enzyme of tetrahydrofolate synthesis, is the target antigen of anti-LC1 (liver cytosol antigen type 1) autoantibodies. Presence of LC1 autoantibodies is a marker for type 2 autoimmune hepatitis (for which anti-LKM 1/cytochrome P450 2D6 autoantibodies are a further marker).
Serum LC1 autoantibody concentrations appear to fluctuate in parallel with aminotransferase levels, a particularly intriguing observation that suggests a possible role of LC1 autoreactivity in the pathogenic mechanism leading to hepatocyte injury.

Branched-chain ?-keto acid dehydrogenase E1 component ? chain (BCKDHA) is a member of the BCKDHA family. The BCKD (branched-chain alpha-keto acid dehydrogenase) complex is an inner mitochondrial enzyme complex which catalyzes the second major step in the catabolism of the branched-chain amino acids leucine, isoleucine, and valine. This complex consists of 3 catalytic components: a heterotetrameric (alpha2-beta2) branched-chain alpha-keto acid decarboxylase (E1), a dihydrolipoyl transacylase (E2), and a dihydrolipoamide dehydrogenase (E3). Mutations in the BCKDHA gene result in maple syrup urine disease, type IA.

Kelch Domain Containing 8B, also known as KLHDC8B shapes a distinct beta-propeller protein structure of kelch domains which allow for protein-protein interactions. In addition,mutations in KLHDC8B have been connected with Hodgkin lymphoma.

KLRD1, also known as Killer Cell Lectin Like Receptor D1, is expressed on the surface of natural killer cells in the innate immune system. KLRD1 functions as a receptor for the recognition of MHC class I HLA-E molecules by NK cells and some cytotoxic T-cells. KLRD1 can create disulfide-bonded heterodimer with NKG2 family members. CD94 & NKG2 complex interacts with (HLA)-E, Human Leukocyte Antigen on target cells on the surface of natural killer cells.

Sclerostin Domain Containing 1 (SOSTDC1) belongs to the sclerostin family and an N-glycosylated, secreted protein with a C-terminal cystine knot-like domain. The SOSTDC1 protein acts as a bone morphogenetic protein (BMP) antagonist. Specifically, SOSTDC1 directly associates with BMPs, prohibiting them from binding their receptors, thus regulating BMP signaling throughout cellular proliferation, differentiation, and programmed cell death. SOSTDC1 may also be involved in the onset of endometrial receptivity for implantation/sensitization for the decidual cell reaction Enhances Wnt signaling and hinders TGF-beta signaling. In addition, SOSTDC1 directly antagonizes the activity of BMP2, BMP4, BMP6 and BMP7 in a dose-dependent manner.

Killer-cell immunoglobulin-like receptors (KIRs), are a family of cell surface glycoproteins found on Natural Killer (NK) Cells, which are important cells of the immune system. They control the killing function of these cells by interacting with MHC class I molecules, which are expressed on all cell types. This interaction allows them to identify virally infected cells or tumor cells that have a distinctive low level of Class I MHC on their surface. The majority of KIRs are inhibitory, which means that their recognition of MHC suppresses the cytotoxic activity of their NK cell. Only a limited number of KIRs have the capacity to activate cells.
The KIR genes are found in a cluster on chromosome 19q13.4 within the 1 Mb leukocyte receptor complex (LRC). KIR molecules are extremely polymorphic, meaning their gene sequences differ significantly between individuals, so that different individuals have different arrays/repertoires of KIR genes.
The KIR proteins are categorized by the number of extracellular immunoglobulin domains (2D or 3D) and by whether they have a long (L) or short (S) cytoplasmic domain. KIR proteins with the long cytoplasmic domain transduce inhibitory signals upon ligand binding via an immune tyrosine-based inhibitory motif (ITIM). Whereas KIR proteins with the short cytoplasmic domain lack the ITIM motif and instead associate with the TYRO protein tyrosine kinase binding protein to transduce activating signals.
KIR2DS4 is an activating Killer Cell Ig-like Receptor (KIR, previously called p50 KIR, p50.3, cl39, or KAR-K1), which may recognize class I MHC molecules. KIR2DS4 does not inhibit the activity of NK cells.

CCND2 is a member of the highly conserved cyclin family, whose members are characterized by a dramatic periodicity in protein abundance through the cell cycle. Cyclins serve as regulators of CDK kinases. Various cyclins demonstrate distinct expression and degradation patterns which contribute to the temporal coordination of each mitotic event. CCND2 forms a complex with and acts as a regulatory subunit of CDK4 or CDK6, whose activity is vital for cell cycle G1/S transition. CCND2 interacts with and is involved in the phosphorylation of tumor suppressor protein Rb. High level expression of the CCND2 protein is observed in ovarian and testicular tumors. In addition, knockout studies of the homologous gene in mouse suggest the vital roles of the CCND2 gene in ovarian granulosa and germ cell proliferation.

Killer-cell immunoglobulin-like receptors (KIRs), are a family of cell surface glycoproteins found on Natural Killer (NK) Cells, which are important cells of the immune system. They control the killing function of these cells by interacting with MHC class I molecules, which are expressed on all cell types. This interaction allows them to identify virally infected cells or tumor cells that have a distinctive low level of Class I MHC on their surface. The majority of KIRs are inhibitory, which means that their recognition of MHC suppresses the cytotoxic activity of their NK cell. Only a limited number of KIRs have the capacity to activate cells.
The KIR genes are found in a cluster on chromosome 19q13.4 within the 1 Mb leukocyte receptor complex (LRC). KIR molecules are extremely polymorphic, meaning their gene sequences differ significantly between individuals, so that different individuals have different arrays/repertoires of KIR genes.
The KIR proteins are categorized by the number of extracellular immunoglobulin domains (2D or 3D) and by whether they have a long (L) or short (S) cytoplasmic domain. KIR proteins with the long cytoplasmic domain transduce inhibitory signals upon ligand binding via an immune tyrosine-based inhibitory motif (ITIM). Whereas KIR proteins with the short cytoplasmic domain lack the ITIM motif and instead associate with the TYRO protein tyrosine kinase binding protein to transduce activating signals.
The three Ig-domain from of inhibitory killer cell Ig-like receptor 1(KIR3DL1, NKB1, nkat3, p70KIR) is a NK cell receptor for polymorphic HLA-B determinant. KIR3DLl recognizes the Bw4 determinant defined by sequence motifs at positions 77-83 of the HLA-B heavy chain. The cytoplasmic tail of KIR, which contains two immunoreceptor tyrosine-based inhibition motifs (ITIMs), mediates inhibitory signal transduction that prevents killer cell-mediated cytotoxicity. A His-tag fusion protein of KIR3DL1 cytoplasmic tail (361-444aa) was overexpressed as insoluble protein aggregates (inclusion bodies).

TKT is a thiamine-dependent enzyme that takes part in the channeling of leftover sugar phosphates to glycolysis in the pentose phosphate pathway. Multiple alternatively spliced variants are known that encode the same protein.

Glutamyl-TRNA Amidotransferase, Subunit C also known as GATC allows the formation of properly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction occurs in the attendance of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). In addition, GATC is subunit of the heterotrimeric GatCAB amidotransferase (AdT) complex, composed of A (QRSL1), B (PET112) and C (GATC) subunits.

Enoyl CoA hydratase domain containing 1 (ECHDC1) is a member of the enoyl-CoA hydratase/isomerase family. ECHDC1 is an enzyme which hydrates the double bond between the second and third carbons on acyl-CoA. The ECHDC1 enzyme is crucial to metabolizing fatty acids to supply both acetyl CoA and energy.

GCDH is part of the acyl-CoA dehydrogenase family. GCDH is localized in the mitochondrial matrix as a homotetramer of 45-kD subunits. GCDH catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and CO(2) in the degradative pathway of L-lysine, L-hydroxylysine, and L-tryptophan metabolism. GCDH uses electron transfer flavoprotein as its electron acceptor.