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Mitochondrial Ribosomal Protein L1 (MRPL1) exists as a component of the 39S ribosomal subunit and operates in conjunction with other MRPs to mediate protein synthesis. Mitochondrial ribosomes consist of a large 39S subunit and a small 28S subunit, both of which are consist of multiple mitochondrial ribosomal proteins (MRPs) that are encoded by nuclear genes and are vital for protein synthesis within mitochondria. MRPL1 exists as 2 isoforms produced by alternative splicing. Isoform 1 of MRPL1 is ubiquitously expressed while isoform 2 is particularly expressed in heart.

Nucleophosmin (NPM1) is a phosphoprotein which shuffles between the nucleus and the cytoplasm. NPM1 is assumed to be involved in a number of processes including regulation of the ARF/p53 pathway. Several genes fusion partners have been described, particularly the anaplastic lymphoma kinase gene on chromosome 2. NPM1 gene mutations are linked with acute myeloid leukemia.

TIGAR is a p53-inducible enzyme which catalyzes the hydrolysis of fructose-2-6 bisphosphate (F-2-6-BP) to fructose-6-phosphate and inorganic phosphate. F-2-6-BP is an influential activator of 6-phosphofructose-1 kinase (the rate limiting enzyme of glycolysis). By lowering the intracellular level of F-2-6-BP, TIGAR expression leads to increased glucose processing through the pentose phosphate pathway, the main cellular source for NADPH.

PECR is the main enzyme for a projected peroxisomal chain elongation pathway and is primarily expressed in kidney and liver.

CBR1 is one of numerous monomeric, NADPH-dependent oxidoreductases having ubiquistly specificity for carbonyl compounds. CBR1 is broadly distributed in human tissues. CBR1 metabolizes toxic environmental quinones and pharmacological relevant substrates. CBR1 converts prostaglandin E2 to prostaglandin F2-alpha.

Creatine Kinase, Mitochondrial 2 (CKMT2) is a member of the ATP:guanido phosphotransferase family. CKMT2 is responsible for the transfer of high energy phosphate from mitochondria to the cytosolic carrier, creatine. CKMT2 reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes have a principal role in energy transduction in tissues with large, variable energy demands, such as skeletal muscle, heart, brain and spermatozoa. Mitochondrial creatine kinase occurs in 2 different oligomeric forms: dimers and octamers, contrary to the exclusively dimeric cytosolic creatine kinase isoenzymes. The CKMT2 gene contains sequences homologous to a number of motifs which are shared among some nuclear genes encoding mitochondrial proteins and therefore may be crucial for the coordinated activation of these genes during mitochondrial biogenesis.

Mmitochondrial import receptor subunit TOMM20 homolog (TOMM20) is a member of the Tom20 family. The Tom machinery consists of import receptors for the initial binding of cytosolically synthesized preproteins and a general import pore (GIP) for the membrane translocation of various preproteins into the mitochondria. TOMM20 acts as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into the TOM40 translocation pore.

Synaptotagmin-11 (SYT11) protein may be involved in Ca2+-dependent exocytosis of secretory vesicles through Ca2+ and phospholipid binding to the C2 domain or may function as Ca2+ sensors in the process of vesicular trafficking and exocytosis.

ACADM enzyme is essential for the degradation a certain group of fats called medium-chain fatty acids. ACADM is essential for converting specific fatty acids to energy, mainly during fasting periods. ACADM functions in mitochondria, the energy-producing centers within cells. ACADM is localized in the mitochondria of numerous tissue types, predominantly the liver.

Synaptotagmin V, (SYT5) is a member of synaptotagmin family, which is a family of type III membrane proteins characterized by cytoplasmic repeats related to protein kinase C regulatory (C2) domains that are considered to bind calcium. Synaptotagmins function as negative regulators of vesicle fusion, allowing fusion in the attendance of calcium, and as calcium receptors or sensor molecules. Among the diseases associated with SYT5 are labyrinthitis, and thyroiditis.

PDE6H belongs to the rod/cone cGMP-PDE gamma subunit family, which selectively catalyze the hydrolysis of 3 cyclic phosphate bonds in adenosine and/or guanine 3,5 cyclic monophosphate (cAMP and/or cGMP). This family regulates the cellular levels, localization and duration of action of these second messengers by controlling the rate of their degradation. PDE6H is the inhibitory (or gamma) subunit of the cone-specific cGMP phosphodiesterase, which is atetramer composed of two catalytic chains (alpha and beta), and two inhibitory chains (gamma). PDE6H is particularly expressed in the retina, and is implicated in the transmission and amplification of the visual signal. Mutations in PDE6H have been associated with retinal cone dystrophy type 3A.

PSMA6 belongs to the peptidase T1A family, which is a 20S core alpha subunit. The proteasome is a multicatalytic proteinase complex with an extremely organized ring-shaped 20S core structure. The core structure consists of 4 rings of 28 non-identical subunits; 2 rings consist of 7 alpha subunits and 2 rings consist of 7 beta subunits. PSMA6 is spread all over eukaryotic cells in large quantities and cleave peptides in an ATP/ubiquitin-dependent procedure in a non-lysosomal pathway.

ECH1 is a member of the hydratase/isomerase superfamily. ECH1 demonstrates high sequence similarity to enoyl-coenzyme A (CoA) hydratases of more than a few species, mostly within a conserved domain characteristic of these proteins. ECH1 contains a C-terminal peroxisomal targeting sequence, localizes to both the peroxisome and the mitochondria. peroxisomal takes part in the auxiliary step of the fatty acid beta-oxidation pathway specifically functioning to catalyze the isomerization of 3-trans, 5-cis-dienoyl-CoA to 2-trans, 4-transdienoyl-CoA.

Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4 (PIN4) is a peptidyl-prolyl cis/trans isomerase (PPIase) which interacts with NIMA and is vital for cell cycle regulation. PIN4 has 2 different isoforms: PAR14 and PAR17. Furthermore, Pin4 protein binds to double-stranded DNA under physiological salt conditions.

IVD is a mitochondrial matrix enzyme that is part of the cyl-CoA dehydrogenase family which catalyzes the third step in leucine catabolism. The genetic deficiency of IVD leads to a buildup of isovaleric acid, which is toxic to the central nervous system and results in isovaleric acidemia. IVD is a homotetrameric flavoenzyme which catalyzes the conversion of isovaleryl-CoA to 3-methylcrotonyl-CoA.

PRDX3 is part of the peroxiredoxin family of antioxidant enzymes, that reduces hydrogen peroxide and alkyl hydroperoxides. PRDX3 is particularly located in the mitochondria and involved in the regulation of cellular redox status by serving as a primary line of defense against H2O2 produced during respiration. PRDX3 is a significant regulator of the abundance of mitochondrial H(2)O(2), which itself promotes apoptosis in cooperation with other mediators of apoptotic signaling. PRDX3 mitochondrial protein is significantly decreased in Alzheimer Disease and Down Syndrome.

Cyclin-Dependent Kinase 2 Associated Protein 2 (CDK2AP2) is a member of the CDK2AP family. CDK2-associated protein is assumed to negatively regulate CDK2 activity by sequestering monomeric CDK2, and targeting CDK2 for proteolysis. CDK2AP2 is implicated in the regulation of self-renewal of stem cells during early embryogenesis. CDK2AP2 is a regulator for self-renewal of mESCs (mouse embryonic stem cells) under permissive conditions, and cell survival during differentiation of the mESCs into terminally differentiated cell types.

Clathrin light chain B (CLTB) is a member of the clathrin light chain family. Clathrin is a protein that has a key role in the formation of coated vesicles. CLTB functions as the key structural component of the lattice-type cytoplasmic face of coated pits and vesicles which capture certain macromolecules during receptor-mediated endocytosis. CLTB forms a triskelion form comprised of 3 clathrin heavy chains and 3 light chains. When the triskelia interact they form a polyhedral pattern which encircles the vesicle. CME (Clathrin-mediated endocytosis) controls numerous cellular physiological processes such as the internalization of growth factors and receptors, entry of pathogens, and synaptic transmission.

C9orf103 is a member of the gluconokinase gntK/gntV family. C9orf103 takes part in carbohydrate acid metabolism and D-gluconate degradation.

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, β, γ, ε, σ, ζ, τ and η that have been identified in mammals. The 14-3-3 epsilon, 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 CDC25 phosphatases, RAF1 and IRS1 proteins, suggesting its role in diverse biochemical activities related to signal transduction, such as cell division and regulation of insulin sensitivity. It has also been implicated in the pathogenesis of small cell lung cancer.

Cyclophilin-G is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and speeds up the protein folding. PPIG catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and is involved in the folding, transport, and assembly of proteins. PPIG is localized to the nuclear speckles, a nuclear compartment rich in splicing factors, and cooperates with the splicing factors SC35 and pinin. Cyclophilin-G also takes part in the regulation of pre-mRNA splicing.

NFNB demonstrates the capability to reduce quinines. NFNB enzyme activates prodrugs in antibody directed enzyme prodrug therapy. NFNB reduces nitrofurazone, quinones and anti-tumor agent CB1954 (5-(aziridin-1-yl)-2,4-dinitrobenzamide). The reduction of CB1954 results in the generation of cytotoxic species.

L-threonine to glycine degradation consists of a two-step biochemical pathway which involvs the enzymes L-threonine dehydrogenase and 2-amino-3-ketobutyrate coenzyme A ligase. L-Threonine is initially converted into 2-amino-3-ketobutyrate by L-threonine dehydrogenase. Glycine C-Acetyltransferase (GCAT) is the 2nd enzyme in this pathway, which subsequently catalyzes the reaction between 2-amino-3-ketobutyrate and coenzyme A to form glycine and acetyl-CoA. The GCAT enzyme is regard as a class II pyridoxal-phosphate-dependent aminotransferase. GCAT is strongly expressed in the heart, brain, liver and pancreas. GCAT is also found in lung.

CISD1 protein holds a CDGSH iron-sulfur domain and is known to bind a redox-active [2Fe-2S] cluster. CISD1 is restricted to the outer membrane of mitochondria and takes part in oxidation regulation.