DNA Hormone Health Test

AGBL1 (ATP/GTP-binding protein-like 1): AGBL1, belonging to the ATP/GTP-binding protein-like family, plays a pivotal role in cellular processes involving nucleotide binding and hydrolysis. This protein is intricately involved in various cellular functions, including cytoskeletal organization, vesicular trafficking, and signal transduction pathways, by modulating the dynamics of nucleotide metabolism. AGBL1's activity is crucial for maintaining cellular homeostasis and orchestrating dynamic cellular responses to extracellular cues. Dysregulation of AGBL1 has been implicated in numerous pathological conditions, including neurodegenerative diseases, cancer progression, and immune disorders, underscoring its significance in cellular physiology and disease pathogenesis. Understanding the precise mechanisms governing AGBL1 function holds promise for developing targeted therapeutic interventions for a wide range of cellular dysfunctions.

AGPAT2 (1-acylglycerol-3-phosphate O-acyltransferase 2): AGPAT2 is a crucial enzyme involved in lipid metabolism, particularly in the biosynthesis of phospholipids and triglycerides. It catalyzes the conversion of lysophosphatidic acid (LPA) to phosphatidic acid (PA), a key step in the Kennedy pathway for triacylglycerol synthesis. AGPAT2 plays a vital role in various cellular processes such as adipocyte differentiation, lipid storage, and membrane biogenesis. Dysregulation of AGPAT2 activity has been implicated in metabolic disorders such as obesity, insulin resistance, and dyslipidemia. Additionally, mutations in the AGPAT2 gene are associated with congenital generalized lipodystrophy type 1 (CGL1), a rare genetic disorder characterized by the loss of adipose tissue and metabolic abnormalities. Understanding the regulation and function of AGPAT2 is essential for unraveling the complexities of lipid homeostasis and developing targeted therapies for metabolic disorders.

CD200R1 (Cluster of Differentiation 200 Receptor 1): CD200R1, a member of the immunoglobulin superfamily, serves as a crucial regulator of immune responses and cellular interactions. This receptor is prominently expressed on various immune cells, including macrophages, dendritic cells, and B cells. Its primary ligand, CD200, is expressed on a wide array of cell types, functioning as a suppressive signal to modulate immune activity. CD200R1's engagement with CD200 initiates inhibitory signaling cascades, resulting in the suppression of inflammatory responses and the promotion of immune tolerance. Furthermore, CD200R1 signaling has been implicated in the maintenance of immune homeostasis and the prevention of excessive tissue damage during inflammatory processes. Dysregulation of CD200R1-mediated signaling has been associated with autoimmune disorders, neuroinflammation, and impaired immune surveillance against cancer. Understanding the intricate role of CD200R1 in immune regulation highlights its potential as a therapeutic target for manipulating immune responses in various pathological conditions.

EPHB2 (Ephrin Type-B Receptor 2): EPHB2, a member of the Eph receptor tyrosine kinase family, plays a pivotal role in mediating cell-cell communication and tissue organization. Through its interactions with ephrin ligands, EPHB2 regulates diverse processes such as cell migration, adhesion, and axon guidance during development and adulthood. This receptor is integral to the maintenance of tissue architecture and function, particularly in the nervous system and epithelial tissues. Dysregulation of EPHB2 signaling has been implicated in various pathological conditions including cancer progression, neurodevelopmental disorders, and tissue malformation. The intricate balance of EPHB2 activity underscores its significance in orchestrating cellular dynamics and highlights its potential as a therapeutic target in conditions related to aberrant cell-cell communication and tissue organization.

ERBB4 (Erb-B2 Receptor Tyrosine Kinase 4): ERBB4, a member of the epidermal growth factor receptor (EGFR) family, serves as a crucial regulator in various cellular processes. This transmembrane receptor tyrosine kinase is intricately involved in signaling pathways governing cell proliferation, differentiation, and survival. Its role extends beyond cellular processes to influence organ development, synaptic plasticity, and cardiac function, among others. ERBB4's activation triggers downstream cascades that modulate gene expression and cellular behavior, contributing significantly to tissue homeostasis and development. Moreover, its dysregulation has been implicated in diverse pathologies, including cancer progression, neurological disorders, and cardiac abnormalities. The multifaceted functions of ERBB4 underscore its significance as a potential therapeutic target and diagnostic marker across various diseases. Efforts to elucidate the intricate mechanisms governing ERBB4 signaling hold promise for novel therapeutic interventions aimed at addressing a spectrum of disorders.

FBLL1 (Fibroblast-Like Protein 1): FBLL1, a member of the fibroblast-like protein family, serves as a pivotal player in orchestrating cellular interactions within the extracellular matrix (ECM). Through its regulatory functions, FBLL1 exerts a profound influence on diverse physiological processes, encompassing tissue regeneration, vascular development, and embryogenesis, by modulating ECM composition and architecture. The finely tuned activity of FBLL1 is indispensable for the maintenance of tissue homeostasis and repair mechanisms. However, aberrant expression or dysregulation of FBLL1 has been implicated in the pathogenesis of several disorders, including cancer progression, tissue fibrosis, and inflammatory conditions. Understanding the intricate control of FBLL1 activity underscores its significance in preserving tissue integrity and underscores its potential as a therapeutic target in ECM-related ailments.

GALNT13 (Polypeptide N-Acetylgalactosaminyltransferase 13): GALNT13 is a member of the GalNAc-transferase family, which catalyzes the initial step of O-linked glycosylation by transferring N-acetylgalactosamine (GalNAc) to serine and threonine residues of target proteins. GALNT13 specifically modifies protein substrates in the Golgi apparatus, influencing various cellular processes such as protein trafficking, secretion, and cell surface interactions. This enzyme is implicated in the post-translational modification of proteins involved in cell signaling, adhesion, and immune responses, thereby playing a critical role in cellular communication and homeostasis. Dysregulation of GALNT13 has been associated with several diseases, including cancer and metabolic disorders, underscoring its importance in physiological and pathological contexts. Understanding the function and regulation of GALNT13 offers insights into the mechanisms of protein glycosylation and its implications for health and disease, potentially paving the way for targeted therapeutic interventions.

INSIG1 (Insulin-Induced Gene 1): INSIG1 is a protein encoded by the INSIG1 gene, which plays a pivotal role in the regulation of lipid metabolism and cholesterol homeostasis within cells. It functions as a key mediator of the feedback inhibition loop that controls the synthesis and uptake of cholesterol. INSIG1 acts by binding to and inhibiting the activation of sterol regulatory element-binding proteins (SREBPs), which are transcription factors crucial for the expression of genes involved in cholesterol and fatty acid biosynthesis. By modulating SREBP activity, INSIG1 helps maintain cellular lipid levels within a tight physiological range, preventing excessive accumulation of cholesterol and lipids that can lead to metabolic disorders such as atherosclerosis and non-alcoholic fatty liver disease. The dysregulation of INSIG1 expression or function has been implicated in various pathological conditions, highlighting its significance as a potential therapeutic target for the management of lipid-related disorders.

MOV10L1 (Moloney leukemia virus 10-like protein 1): MOV10L1 is a member of the RNA helicase family and plays a significant role in RNA metabolism and post-transcriptional regulation. This protein is involved in various cellular processes, including RNA interference (RNAi), RNA degradation, and mRNA translation. By unwinding RNA duplexes and facilitating the degradation of target RNAs, MOV10L1 influences gene expression and contributes to the regulation of diverse biological pathways. Additionally, MOV10L1 has been implicated in the restriction of retroviruses and retrotransposons, highlighting its role in innate immunity and genome stability. Dysregulation of MOV10L1 expression or function has been associated with several human diseases, including cancer, neurodevelopmental disorders, and viral infections. The multifaceted roles of MOV10L1 in RNA metabolism and cellular defense mechanisms underscore its importance as a potential therapeutic target and biomarker in various pathological conditions.

PRKCE, also known as Protein Kinase C Epsilon, is a vital enzyme belonging to the family of protein kinase C (PKC) isoforms. This particular isoform plays a pivotal role in various cellular processes, including cell proliferation, differentiation, apoptosis, and signal transduction. PRKCE is predominantly found in the cytoplasm of cells, where it exerts its regulatory functions by phosphorylating target proteins. One of the distinguishing features of PRKCE is its involvement in signal transduction pathways, where it acts as a crucial mediator in transmitting extracellular signals to intracellular targets. Through its kinase activity, PRKCE modulates the activity of downstream effector proteins, thereby orchestrating intricate cellular responses to external stimuli. Moreover, PRKCE has been implicated in several pathological conditions, including cancer, cardiovascular diseases, and neurological disorders. Dysregulation of PRKCE expression or activity has been associated with aberrant cell growth, metastasis, and drug resistance in cancer, highlighting its significance as a potential therapeutic target. In summary, PRKCE stands as a multifaceted kinase enzyme with profound implications in cellular physiology and disease pathogenesis, making it an intriguing subject of study in both basic and clinical research endeavors.

RAB38, a member of the Ras-related protein family, serves as a critical regulator of intracellular membrane trafficking processes, particularly within the endosomal-lysosomal system. Positioned primarily within the cytoplasm of cells, RAB38 exerts its influence by coordinating the movement and fusion of membrane-bound vesicles, facilitating the sorting and delivery of cargo molecules to their designated destinations. This protein's significance lies in its specialized role in melanosome biogenesis, where it contributes to the maturation and transport of melanosomes, specialized organelles responsible for melanin pigment synthesis and distribution within melanocytes. Through its interactions with various effector proteins and membrane fusion machinery, RAB38 facilitates the trafficking of melanin-related proteins, ensuring the proper pigmentation of skin, hair, and eyes. Furthermore, mutations or dysregulation of RAB38 have been implicated in certain genetic disorders, such as Hermansky-Pudlak syndrome, characterized by defects in melanosomes and other lysosome-related organelles. Understanding the intricate workings of RAB38 holds promise for elucidating the underlying mechanisms of pigmentation disorders and other related conditions, offering potential insights into novel therapeutic strategies.

SERPINA7, also known as Thyroxine-binding globulin (TBG), is a crucial carrier protein primarily synthesized in the liver and circulates in the bloodstream. Its primary function is to bind to and transport thyroid hormones, particularly thyroxine (T4) and triiodothyronine (T3), throughout the body. This glycoprotein plays a pivotal role in regulating the availability and distribution of thyroid hormones, which are essential for various physiological processes, including metabolism, growth, and development. By tightly binding to thyroid hormones, SERPINA7 helps to maintain their concentration within the bloodstream, ensuring efficient delivery to target tissues and organs. Moreover, alterations in SERPINA7 levels or mutations in its encoding gene can lead to thyroid dysfunction and related disorders. For instance, variations in TBG levels may result in conditions such as familial dysalbuminemic hyperthyroxinemia (FDH) or hypothyroidism. Understanding the intricate mechanisms underlying SERPINA7 function and its involvement in thyroid hormone homeostasis is crucial for diagnosing and managing thyroid-related conditions effectively. Additionally, SERPINA7 serves as a valuable biomarker in clinical settings for assessing thyroid function and monitoring thyroid hormone levels in patients.

SLK, also known as STE20-like kinase, is a key enzyme belonging to the serine/threonine kinase family. Positioned primarily within the cytoplasm of cells, SLK plays a pivotal role in regulating various cellular processes, including cell proliferation, survival, migration, and cytoskeletal organization. One of the distinguishing features of SLK is its involvement in signaling pathways that govern cell morphology and motility. Through its kinase activity, SLK phosphorylates target proteins involved in cytoskeletal dynamics, such as focal adhesion kinase (FAK), paxillin, and cortactin, thereby modulating the assembly and turnover of focal adhesions and actin stress fibers. Moreover, SLK has been implicated in the regulation of mitogen-activated protein kinase (MAPK) signaling cascades, which are crucial for cell growth and differentiation. By phosphorylating MAPK kinase kinases (MAP3Ks) and other downstream effectors, SLK contributes to the activation of MAPK pathways, thus influencing cellular responses to extracellular stimuli. Furthermore, dysregulation of SLK expression or activity has been linked to various pathological conditions, including cancer, cardiovascular diseases, and neurological disorders. Aberrant SLK signaling has been associated with enhanced tumor cell invasion, metastasis, and drug resistance, highlighting its potential as a therapeutic target in cancer treatment. In summary, SLK emerges as a multifaceted kinase enzyme with significant implications in cellular physiology and disease pathogenesis. Its intricate regulatory functions make it a subject of keen interest in both basic research and clinical investigations, with potential therapeutic implications across diverse pathological contexts.

TIAM2, also known as T-lymphoma invasion and metastasis-inducing protein 2, is a critical member of the TIAM family of guanine nucleotide exchange factors (GEFs). Positioned primarily within the cytoplasm of cells, TIAM2 plays a pivotal role in regulating cellular processes, particularly those related to cytoskeletal dynamics, cell migration, and invasion. One of the distinctive features of TIAM2 is its ability to act as a molecular switch for the activation of Rho GTPases, particularly Rac1. Through its GEF activity, TIAM2 catalyzes the exchange of GDP for GTP on Rac1, leading to the activation of downstream signaling pathways involved in actin cytoskeleton rearrangements and cell migration. Moreover, TIAM2 has been implicated in various physiological and pathological processes, including neuronal development, synaptic plasticity, and cancer metastasis. In neurons, TIAM2 plays a crucial role in dendritic spine morphogenesis and synaptic transmission by regulating Rac1-mediated actin remodeling. In cancer, aberrant TIAM2 expression or activity has been associated with increased tumor cell invasion, metastasis, and poor patient prognosis, underscoring its significance as a potential therapeutic target in cancer treatment. Furthermore, TIAM2 interacts with numerous binding partners and signaling molecules, thereby participating in complex regulatory networks governing cell behavior. Its intricate functions make it a subject of intense investigation in both basic and translational research, with potential implications for understanding disease mechanisms and developing novel therapeutic strategies.

VPS37B, a member of the vacuolar protein sorting (VPS) family, is a crucial component of the endosomal sorting complex required for transport (ESCRT) machinery. Located predominantly within the cytoplasm of cells, VPS37B plays a pivotal role in regulating intracellular membrane trafficking and protein sorting processes. One of the key functions of VPS37B is its involvement in the formation and function of multivesicular bodies (MVBs), specialized endosomal compartments responsible for sorting ubiquitinated membrane proteins destined for degradation in lysosomes. Within the ESCRT machinery, VPS37B interacts with other ESCRT components to facilitate the sequestration of cargo into intraluminal vesicles within MVBs, a process essential for efficient lysosomal degradation and recycling of cellular components. Moreover, VPS37B has been implicated in various cellular processes, including cytokinesis, viral budding, and autophagy, highlighting its versatility in regulating diverse cellular functions beyond endosomal sorting. By participating in these processes, VPS37B contributes to the maintenance of cellular homeostasis and the proper functioning of organelles. Furthermore, mutations or dysregulation of VPS37B have been associated with certain human diseases, including neurodevelopmental disorders and neurodegenerative diseases. Disruption of VPS37B function can lead to impaired protein degradation pathways and abnormal accumulation of toxic protein aggregates, contributing to disease pathogenesis. In summary, VPS37B emerges as a critical player in intracellular membrane trafficking and protein sorting processes, with implications for various cellular functions and disease mechanisms. Elucidating the precise molecular mechanisms underlying VPS37B function holds promise for understanding fundamental aspects of cell biology and developing targeted therapies for associated disorders.

ZNF616, also known as Zinc Finger Protein 616, is a member of the zinc finger protein family, characterized by its distinctive DNA-binding domain known as the zinc finger motif. Positioned within the nucleus of cells, ZNF616 plays a pivotal role in regulating gene expression by binding to specific DNA sequences and modulating the activity of target genes. One of the primary functions of ZNF616 is to act as a transcriptional regulator, influencing the transcriptional activity of nearby genes through its interaction with promoter regions or enhancer elements. By binding to DNA sequences with high specificity, ZNF616 can either activate or repress the expression of target genes, thereby orchestrating various cellular processes, including development, differentiation, and response to environmental stimuli. Moreover, ZNF616 is involved in diverse biological processes, such as cell proliferation, apoptosis, and DNA repair, reflecting its multifaceted roles in cellular physiology. Through its interactions with other transcriptional regulators and chromatin-modifying enzymes, ZNF616 participates in intricate regulatory networks that govern gene expression dynamics. Furthermore, dysregulation of ZNF616 expression or function has been implicated in certain human diseases, including cancer and developmental disorders. Aberrant ZNF616 activity can lead to perturbations in gene expression patterns, disrupting normal cellular processes and contributing to disease pathogenesis. In summary, ZNF616 emerges as a versatile transcriptional regulator with significant implications in various aspects of cellular biology and disease. Elucidating the molecular mechanisms underlying ZNF616 function holds promise for understanding gene regulatory networks and identifying potential therapeutic targets for associated disorders.

AADAT, also known as aminoadipate aminotransferase, is a vital enzyme involved in the catabolism of lysine, an essential amino acid. Positioned primarily within the mitochondria of cells, AADAT plays a crucial role in the alpha-aminoadipic semialdehyde (alpha-AASA) pathway, which is responsible for the degradation of lysine. One of the key functions of AADAT is its involvement in the conversion of alpha-aminoadipate semialdehyde (alpha-AASA) to alpha-aminoadipate (AAA), a crucial step in lysine degradation. This enzymatic reaction is essential for the disposal of excess lysine and the generation of intermediates that can be utilized in other metabolic pathways. Moreover, AADAT participates in the synthesis of glutamate, a key neurotransmitter, by contributing to the transamination of alpha-AASA to glutamate semialdehyde. This reaction links lysine catabolism to the production of neurotransmitters, highlighting the interconnectedness of metabolic pathways in cellular physiology. Furthermore, dysregulation of AADAT activity or expression has been implicated in certain human diseases, including disorders of lysine metabolism and neurological conditions. Mutations in the AADAT gene can lead to accumulation of toxic metabolites and disruption of neurotransmitter balance, contributing to the pathogenesis of neurological disorders such as hyperlysinemia and saccharopinuria. In summary, AADAT emerges as a critical enzyme in lysine metabolism, playing essential roles in amino acid catabolism and neurotransmitter synthesis. Understanding the biochemical and physiological functions of AADAT is crucial for elucidating metabolic pathways and identifying potential therapeutic targets for associated disorders.

CA8, also known as Carbonic Anhydrase VIII, is an enzyme belonging to the carbonic anhydrase family, which catalyzes the reversible hydration of carbon dioxide to bicarbonate ions and protons. Positioned predominantly within the cytoplasm and mitochondria of cells, CA8 plays a crucial role in maintaining pH homeostasis and regulating ion transport processes. One of the distinctive features of CA8 is its expression in various tissues, including the brain, kidneys, and reproductive organs, highlighting its diverse physiological roles beyond traditional carbonic anhydrase functions. Within the central nervous system, CA8 is particularly abundant in Purkinje cells of the cerebellum, where it is implicated in modulating neuronal excitability and synaptic transmission. Moreover, CA8 has been implicated in other cellular processes, such as bicarbonate transport, ammonia detoxification, and bone resorption. By facilitating the interconversion of carbon dioxide and bicarbonate, CA8 contributes to numerous physiological functions, including acid-base balance, electrolyte transport, and fluid secretion. Furthermore, dysregulation of CA8 expression or activity has been associated with certain human diseases, including metabolic disorders, neurological conditions, and cancer. Altered CA8 levels have been observed in disorders such as cerebellar ataxia and glaucoma, underscoring its significance as a potential biomarker or therapeutic target in disease management. In summary, CA8 emerges as a multifunctional enzyme with diverse roles in cellular physiology and disease pathogenesis. Elucidating the molecular mechanisms underlying CA8 function holds promise for understanding its contributions to health and disease and exploring its therapeutic potential in various clinical contexts.

CPPED1, also known as Serine/threonine-protein phosphatase 6 regulatory subunit 2, is a crucial regulatory protein involved in cellular signaling pathways. Positioned predominantly within the cytoplasm and nucleus of cells, CPPED1 serves as a regulatory subunit of protein phosphatase 6 (PP6), a member of the PPP family of serine/threonine phosphatases. One of the key functions of CPPED1 is its role in modulating the activity of PP6, which plays essential roles in various cellular processes, including cell cycle progression, DNA damage response, and protein degradation. By interacting with PP6, CPPED1 contributes to the regulation of substrate specificity and subcellular localization of the phosphatase, thereby influencing downstream signaling events. Moreover, CPPED1 has been implicated in diverse cellular functions, such as cell proliferation, apoptosis, and stress responses. Through its interactions with PP6 and other binding partners, CPPED1 participates in intricate regulatory networks that govern cellular physiology and adaptation to environmental cues. Furthermore, dysregulation of CPPED1 expression or activity has been associated with certain human diseases, including cancer, neurodegenerative disorders, and metabolic syndromes. Altered CPPED1 levels have been observed in tumor tissues, where it may contribute to oncogenic signaling pathways and tumor progression. In summary, CPPED1 emerges as a critical regulator of cellular signaling pathways, exerting its effects through modulation of PP6 activity and participation in diverse cellular functions. Understanding the molecular mechanisms underlying CPPED1 function holds promise for elucidating its contributions to health and disease and exploring its potential as a therapeutic target in various pathological contexts.

DIO3, also known as Type 3 Deiodinase, is a crucial enzyme involved in the regulation of thyroid hormone activity. Positioned primarily within various tissues, including the liver, brain, and placenta, DIO3 plays a pivotal role in controlling thyroid hormone levels and mediating tissue-specific responses to thyroid hormones. One of the key functions of DIO3 is its ability to catalyze the inactivation of thyroid hormones, particularly thyroxine (T4), by converting it into an inactive metabolite known as reverse triiodothyronine (rT3). This enzymatic activity helps fine-tune thyroid hormone signaling by reducing the availability of active thyroid hormones in target tissues, thereby modulating metabolic rate, growth, and development. Moreover, DIO3 expression is tightly regulated in response to various physiological and pathological conditions, such as fasting, stress, and inflammation. Changes in DIO3 levels can impact thyroid hormone homeostasis and contribute to metabolic dysregulation, making it a subject of interest in studies investigating metabolic disorders and thyroid-related diseases. Furthermore, dysregulation of DIO3 expression or activity has been implicated in certain human diseases, including metabolic syndrome, diabetes, and thyroid disorders. Altered DIO3 levels have been observed in tissues of individuals with thyroid dysfunction, suggesting its potential as a biomarker for thyroid hormone imbalance. In summary, DIO3 emerges as a critical enzyme in the regulation of thyroid hormone activity, with implications for metabolic homeostasis and physiological adaptation. Elucidating the molecular mechanisms underlying DIO3 function holds promise for understanding thyroid hormone signaling pathways and developing targeted therapies for associated disorders.

GLIS3 (GLIS Family Zinc Finger 3): GLIS3 is a transcription factor that plays a significant role in the regulation of gene expression in various biological processes, including thyroid hormone signaling and pancreatic beta-cell development. Mutations in GLIS3 have been linked to a range of disorders, including congenital hypothyroidism and neonatal diabetes, underscoring its importance in endocrine function and development.

ILRUN, also known as interleukin-like RUN domain-containing protein, is a recently discovered protein that plays a role in immune regulation. Positioned within the cytoplasm of cells, ILRUN contains a RUN domain, which is known to be involved in protein-protein interactions. Although the exact function of ILRUN is still being elucidated, initial studies suggest its involvement in modulating immune responses. It is hypothesized that ILRUN may interact with other proteins involved in immune signaling pathways, potentially influencing cytokine production, immune cell activation, or inflammatory processes. Moreover, ILRUN has been identified as a potential biomarker in certain immune-related disorders or inflammatory conditions. Changes in ILRUN expression levels have been observed in experimental models of autoimmune diseases and inflammation, indicating its potential role in disease pathogenesis or as a marker of disease severity. Further research is needed to fully understand the biological functions and regulatory mechanisms of ILRUN in immune regulation. Investigating its interactions with other proteins and its involvement in specific signaling pathways will provide insights into its role in health and disease, with potential implications for the development of novel therapeutic strategies.

LPCAT2, also known as Lysophosphatidylcholine Acyltransferase 2, is an enzyme crucial for the biosynthesis of phospholipids, essential components of cellular membranes. Positioned primarily within the endoplasmic reticulum of cells, LPCAT2 plays a pivotal role in regulating lipid metabolism and maintaining membrane integrity. One of the key functions of LPCAT2 is its involvement in the Lands cycle, a process essential for the remodeling of phospholipids. LPCAT2 catalyzes the acylation of lysophosphatidylcholine (LPC) molecules, converting them into phosphatidylcholine (PC), a major phospholipid constituent of cell membranes. This enzymatic activity is crucial for generating membrane phospholipids with specific fatty acid compositions, which influence membrane fluidity, stability, and signaling properties. Moreover, LPCAT2 is involved in various cellular processes, including membrane biogenesis, lipid droplet formation, and lipid-mediated signaling pathways. By modulating the composition and properties of cellular membranes, LPCAT2 contributes to diverse physiological functions, such as cell growth, proliferation, and differentiation. Furthermore, dysregulation of LPCAT2 expression or activity has been implicated in certain human diseases, including metabolic disorders, neurodegenerative diseases, and cancer. Altered LPCAT2 levels have been observed in tissues of individuals with lipid metabolism disorders, highlighting its potential as a biomarker or therapeutic target in lipid-related diseases. In summary, LPCAT2 emerges as a critical enzyme in phospholipid biosynthesis and membrane remodeling, with implications for cellular physiology and disease pathogenesis. Elucidating the molecular mechanisms underlying LPCAT2 function holds promise for understanding lipid metabolism and developing targeted therapies for associated disorders.

LRRC42, short for Leucine-rich repeat-containing protein 42, is a member of the leucine-rich repeat (LRR) protein family, characterized by its unique structural motif composed of repeating sequences rich in leucine residues. Positioned predominantly within the cytoplasm or on the cell membrane, LRRC42 plays various roles in cellular processes, including signal transduction, protein-protein interactions, and cell adhesion. One of the distinctive features of LRRC42 is its involvement in protein-protein interactions mediated by its leucine-rich repeat domains. These domains serve as interaction interfaces, allowing LRRC42 to bind to specific partner proteins involved in diverse cellular pathways. By participating in these interactions, LRRC42 can modulate the activity or localization of its binding partners, thereby influencing cellular functions such as cell adhesion, migration, and signaling. Moreover, LRRC42 has been implicated in the regulation of immune responses and inflammation. It may play a role in modulating immune cell activation or cytokine signaling pathways, contributing to the maintenance of immune homeostasis or the response to microbial pathogens. Furthermore, dysregulation of LRRC42 expression or activity has been associated with certain human diseases, including cancer, autoimmune disorders, and neurological conditions. Altered LRRC42 levels have been observed in tissues of individuals with inflammatory disorders or malignancies, suggesting its potential as a biomarker or therapeutic target in disease diagnosis or treatment. In summary, LRRC42 emerges as a versatile protein involved in diverse cellular functions, with implications for both physiological processes and disease pathogenesis. Further investigation into the molecular mechanisms underlying LRRC42 function will provide valuable insights into its roles in health and disease, with potential implications for the development of targeted therapies.

MC4R (Melanocortin 4 Receptor): MC4R is a G protein-coupled receptor involved in regulating energy homeostasis, appetite, and body weight. Mutations in MC4R are one of the most common genetic causes of obesity due to its role in controlling energy balance. It is a target for developing obesity treatments.

NCOR1, also known as Nuclear Receptor Corepressor 1, is a critical regulator of gene expression and transcriptional repression. Positioned predominantly within the nucleus of cells, NCOR1 plays a pivotal role in modulating the activity of nuclear receptors and other transcription factors. One of the primary functions of NCOR1 is to act as a corepressor for various nuclear receptors, including thyroid hormone receptors (TRs), retinoic acid receptors (RARs), and peroxisome proliferator-activated receptors (PPARs). By recruiting histone deacetylases (HDACs) and other chromatin-modifying enzymes to target gene promoters, NCOR1 facilitates the formation of repressive chromatin structures, leading to transcriptional silencing. Moreover, NCOR1 is involved in complex regulatory networks governing diverse cellular processes, including metabolism, development, and immune responses. Through its interactions with transcription factors and cofactors, NCOR1 modulates the expression of target genes involved in these physiological processes, contributing to cellular homeostasis and adaptation to environmental cues. Furthermore, dysregulation of NCOR1 expression or activity has been implicated in various human diseases, including metabolic disorders, cancer, and neurological conditions. Altered NCOR1 levels have been observed in tissues of individuals with obesity, diabetes, and certain cancers, highlighting its significance as a potential biomarker or therapeutic target in disease management. In summary, NCOR1 emerges as a central player in transcriptional regulation, with implications for diverse cellular functions and disease pathogenesis. Elucidating the molecular mechanisms underlying NCOR1 function holds promise for understanding gene regulatory networks and developing targeted therapies for associated disorders.

QSOX2, also known as Quiescin Sulfhydryl Oxidase 2, is an enzyme involved in the oxidative folding of proteins, particularly those containing multiple disulfide bonds. Positioned predominantly within the endoplasmic reticulum (ER) of cells, QSOX2 plays a crucial role in maintaining protein structure and function by catalyzing the formation of disulfide bonds between cysteine residues. One of the primary functions of QSOX2 is its involvement in protein disulfide bond formation, a process essential for the proper folding, stability, and secretion of secretory and membrane proteins. QSOX2 acts as a thiol oxidase, transferring electrons from reduced cysteine residues to molecular oxygen, thereby facilitating the oxidation of cysteine thiols to form disulfide bonds. Moreover, QSOX2 has been implicated in various cellular processes, including redox regulation, protein quality control, and extracellular matrix remodeling. Through its enzymatic activity, QSOX2 influences the redox state of the ER environment, which is crucial for the correct folding of newly synthesized proteins and the maintenance of cellular homeostasis. Furthermore, dysregulation of QSOX2 expression or activity has been associated with certain human diseases, including cancer, neurodegenerative disorders, and cardiovascular diseases. Altered QSOX2 levels have been observed in tumor tissues, where it may contribute to tumor progression, metastasis, and resistance to oxidative stress-induced cell death. In summary, QSOX2 emerges as a multifunctional enzyme with diverse roles in protein folding, redox regulation, and disease pathogenesis. Elucidating the molecular mechanisms underlying QSOX2 function holds promise for understanding its contributions to health and disease and exploring its potential as a therapeutic target in various pathological contexts.

RNF144B, also known as Ring Finger Protein 144B, is a member of the RING finger protein family, characterized by the presence of a RING (Really Interesting New Gene) domain, which confers E3 ubiquitin ligase activity. Positioned predominantly within the cytoplasm or nucleus of cells, RNF144B plays a crucial role in the regulation of protein degradation and cellular signaling pathways. One of the primary functions of RNF144B is its involvement in the ubiquitin-proteasome system, a major pathway for protein degradation in eukaryotic cells. As an E3 ubiquitin ligase, RNF144B catalyzes the transfer of ubiquitin molecules onto substrate proteins, targeting them for degradation by the 26S proteasome. This process plays a pivotal role in controlling the abundance and activity of key regulatory proteins involved in diverse cellular processes, including cell cycle progression, apoptosis, and signal transduction. Moreover, RNF144B has been implicated in various cellular processes, including DNA repair, autophagy, and immune responses. Through its ubiquitin ligase activity, RNF144B regulates the turnover of proteins involved in these pathways, influencing cellular homeostasis and adaptation to environmental stimuli. Furthermore, dysregulation of RNF144B expression or activity has been associated with certain human diseases, including cancer, neurodegenerative disorders, and inflammatory conditions. Altered RNF144B levels have been observed in tumor tissues, where it may contribute to aberrant signaling pathways, tumor growth, and metastasis. In summary, RNF144B emerges as a critical regulator of protein degradation and cellular signaling, with implications for diverse physiological processes and disease pathogenesis. Elucidating the molecular mechanisms underlying RNF144B function holds promise for understanding its contributions to health and disease and exploring its potential as a therapeutic target in various pathological contexts.

SEPHS1, also known as Selenophosphate synthetase 1, is a vital enzyme involved in the biosynthesis of selenoproteins, a class of proteins containing the amino acid selenocysteine (Sec). Positioned predominantly within the cytoplasm of cells, SEPHS1 plays a crucial role in selenium metabolism and the incorporation of selenocysteine into nascent selenoproteins. One of the primary functions of SEPHS1 is its involvement in the synthesis of selenophosphate, the activated form of selenium required for selenocysteine incorporation. As a selenophosphate synthetase, SEPHS1 catalyzes the conversion of selenide and ATP into selenophosphate, providing the essential precursor for selenocysteine tRNA (Sec-tRNA^[Ser]Sec) biosynthesis. Moreover, SEPHS1 is indispensable for the efficient translation of selenoprotein mRNAs. It is involved in the specific recognition and binding of Sec-tRNA^[Ser]Sec to the ribosome, ensuring accurate incorporation of selenocysteine into the nascent polypeptide chain during protein synthesis. This process is essential for the synthesis of functional selenoproteins, which play critical roles in antioxidant defense, redox regulation, and thyroid hormone metabolism. Furthermore, dysregulation of SEPHS1 expression or activity has been implicated in various human diseases, including cancer, neurodegenerative disorders, and cardiovascular diseases. Alterations in selenium metabolism or selenoprotein expression have been associated with increased susceptibility to oxidative stress, impaired immune function, and disrupted cellular homeostasis. In summary, SEPHS1 emerges as a central player in selenium metabolism and selenoprotein biosynthesis, with implications for diverse physiological processes and disease pathogenesis. Elucidating the molecular mechanisms underlying SEPHS1 function holds promise for understanding its contributions to health and disease and exploring its potential as a therapeutic target in various pathological contexts.

SIM1 (Single-Minded Homolog 1): SIM1 is a transcription factor that plays a crucial role in the development of specific brain regions, including the hypothalamus. It is involved in the regulation of appetite and energy homeostasis. Mutations in SIM1 have been associated with obesity and other metabolic disorders.

SOX2, short for SRY (Sex Determining Region Y)-Box 2, is a critical transcription factor that plays a pivotal role in embryonic development, stem cell pluripotency, and tissue homeostasis. Positioned predominantly within the nucleus of cells, SOX2 is involved in the regulation of gene expression by binding to specific DNA sequences and modulating the activity of target genes. One of the primary functions of SOX2 is its involvement in the maintenance of stem cell pluripotency and self-renewal. Alongside other transcription factors, such as OCT4 and NANOG, SOX2 forms a core regulatory network that sustains the undifferentiated state of embryonic stem cells and induced pluripotent stem cells. Through its interactions with chromatin remodeling complexes and transcriptional co-regulators, SOX2 regulates the expression of genes involved in stem cell identity and differentiation. Moreover, SOX2 plays essential roles in embryonic development, where it is required for the formation and patterning of various tissues and organs, including the central nervous system, sensory organs, and endodermal derivatives. Its expression is dynamically regulated during development, reflecting its diverse functions in cell fate determination and tissue morphogenesis. Furthermore, dysregulation of SOX2 expression or activity has been implicated in various human diseases, including cancer, neurodevelopmental disorders, and ocular diseases. SOX2 is frequently amplified or overexpressed in various cancers, where it promotes tumor growth, metastasis, and resistance to therapy. Conversely, loss of SOX2 function or mutations in its encoding gene have been associated with developmental abnormalities and congenital disorders. In summary, SOX2 emerges as a master regulator of stem cell pluripotency, tissue development, and disease pathogenesis. Elucidating the molecular mechanisms underlying SOX2 function holds promise for understanding its contributions to health and disease and exploring its potential as a therapeutic target in various pathological contexts.

TRMO (tRNA Methyltransferase 10 Homolog A): TRMO is a gene involved in tRNA modification. It encodes an enzyme responsible for methylating specific nucleotides in tRNA molecules. tRNA modifications are essential for accurate protein synthesis during translation.

UGT1A6 (UDP Glucuronosyltransferase Family 1 Member A6): UGT1A6 is a gene that encodes an enzyme from the UDP glucuronosyltransferase family. These enzymes play a vital role in phase II metabolism, where they facilitate the conjugation of drugs, toxins, and endogenous substances with glucuronic acid, aiding in their elimination from the body. UGT1A6's function is essential for detoxification processes and maintaining overall metabolic balance.

AADAT, also known as aminoadipate aminotransferase, is a vital enzyme involved in the catabolism of lysine, an essential amino acid. Positioned primarily within the mitochondria of cells, AADAT plays a crucial role in the alpha-aminoadipic semialdehyde (alpha-AASA) pathway, which is responsible for the degradation of lysine. One of the key functions of AADAT is its involvement in the conversion of alpha-aminoadipate semialdehyde (alpha-AASA) to alpha-aminoadipate (AAA), a crucial step in lysine degradation. This enzymatic reaction is essential for the disposal of excess lysine and the generation of intermediates that can be utilized in other metabolic pathways. Moreover, AADAT participates in the synthesis of glutamate, a key neurotransmitter, by contributing to the transamination of alpha-AASA to glutamate semialdehyde. This reaction links lysine catabolism to the production of neurotransmitters, highlighting the interconnectedness of metabolic pathways in cellular physiology. Furthermore, dysregulation of AADAT activity or expression has been implicated in certain human diseases, including disorders of lysine metabolism and neurological conditions. Mutations in the AADAT gene can lead to accumulation of toxic metabolites and disruption of neurotransmitter balance, contributing to the pathogenesis of neurological disorders such as hyperlysinemia and saccharopinuria. In summary, AADAT emerges as a critical enzyme in lysine metabolism, playing essential roles in amino acid catabolism and neurotransmitter synthesis. Understanding the biochemical and physiological functions of AADAT is crucial for elucidating metabolic pathways and identifying potential therapeutic targets for associated disorders.

B4GALT6, also known as Beta-1,4-galactosyltransferase 6, is a key enzyme involved in the biosynthesis of complex carbohydrates known as glycosaminoglycans (GAGs). Positioned primarily within the Golgi apparatus of cells, B4GALT6 plays a crucial role in catalyzing the transfer of galactose residues from UDP-galactose to acceptor substrates, leading to the formation of specific glycosidic linkages. One of the primary functions of B4GALT6 is its involvement in the biosynthesis of proteoglycans, a class of glycoproteins containing GAG chains. Specifically, B4GALT6 catalyzes the addition of galactose residues to the core protein structure of proteoglycans, initiating the assembly of GAG chains such as chondroitin sulfate and dermatan sulfate. These modifications are essential for the structural integrity and functional properties of proteoglycans, which play critical roles in cell adhesion, extracellular matrix organization, and signaling processes. Moreover, B4GALT6 is involved in the synthesis of glycolipids and glycoproteins, contributing to the diversity of carbohydrate structures present on cell surfaces and secreted molecules. Through its enzymatic activity, B4GALT6 influences various cellular processes, including cell-cell interactions, receptor-ligand binding, and cell signaling pathways. Furthermore, dysregulation of B4GALT6 expression or activity has been associated with certain human diseases, including skeletal dysplasias, connective tissue disorders, and cancer. Mutations in the B4GALT6 gene have been linked to disorders such as Larsen syndrome and spondyloepimetaphyseal dysplasia with joint laxity, affecting skeletal development and connective tissue function. In summary, B4GALT6 emerges as a critical enzyme in glycosylation pathways, with implications for diverse physiological processes and disease pathogenesis. Elucidating the molecular mechanisms underlying B4GALT6 function holds promise for understanding carbohydrate metabolism and glycan-mediated signaling and developing targeted therapies for associated disorders.

CA8, also known as Carbonic Anhydrase VIII, is an enzyme belonging to the carbonic anhydrase family, which catalyzes the reversible hydration of carbon dioxide to bicarbonate ions and protons. Positioned predominantly within the cytoplasm and mitochondria of cells, CA8 plays a crucial role in maintaining pH homeostasis and regulating ion transport processes. One of the distinctive features of CA8 is its expression in various tissues, including the brain, kidneys, and reproductive organs, highlighting its diverse physiological roles beyond traditional carbonic anhydrase functions. Within the central nervous system, CA8 is particularly abundant in Purkinje cells of the cerebellum, where it is implicated in modulating neuronal excitability and synaptic transmission. Moreover, CA8 has been implicated in other cellular processes, such as bicarbonate transport, ammonia detoxification, and bone resorption. By facilitating the interconversion of carbon dioxide and bicarbonate, CA8 contributes to numerous physiological functions, including acid-base balance, electrolyte transport, and fluid secretion. Furthermore, dysregulation of CA8 expression or activity has been associated with certain human diseases, including metabolic disorders, neurological conditions, and cancer. Altered CA8 levels have been observed in disorders such as cerebellar ataxia and glaucoma, underscoring its significance as a potential biomarker or therapeutic target in disease management. In summary, CA8 emerges as a multifunctional enzyme with diverse roles in cellular physiology and disease pathogenesis. Elucidating the molecular mechanisms underlying CA8 function holds promise for understanding its contributions to health and disease and exploring its therapeutic potential in various clinical contexts.

CPPED1, also known as Serine/threonine-protein phosphatase 6 regulatory subunit 2, is a crucial regulatory protein involved in cellular signaling pathways. Positioned predominantly within the cytoplasm and nucleus of cells, CPPED1 serves as a regulatory subunit of protein phosphatase 6 (PP6), a member of the PPP family of serine/threonine phosphatases. One of the key functions of CPPED1 is its role in modulating the activity of PP6, which plays essential roles in various cellular processes, including cell cycle progression, DNA damage response, and protein degradation. By interacting with PP6, CPPED1 contributes to the regulation of substrate specificity and subcellular localization of the phosphatase, thereby influencing downstream signaling events. Moreover, CPPED1 has been implicated in diverse cellular functions, such as cell proliferation, apoptosis, and stress responses. Through its interactions with PP6 and other binding partners, CPPED1 participates in intricate regulatory networks that govern cellular physiology and adaptation to environmental cues. Furthermore, dysregulation of CPPED1 expression or activity has been associated with certain human diseases, including cancer, neurodegenerative disorders, and metabolic syndromes. Altered CPPED1 levels have been observed in tumor tissues, where it may contribute to oncogenic signaling pathways and tumor progression. In summary, CPPED1 emerges as a critical regulator of cellular signaling pathways, exerting its effects through modulation of PP6 activity and participation in diverse cellular functions. Understanding the molecular mechanisms underlying CPPED1 function holds promise for elucidating its contributions to health and disease and exploring its potential as a therapeutic target in various pathological contexts.

DIO1, also known as Type 1 Deiodinase, is a crucial enzyme involved in the regulation of thyroid hormone activity. Positioned predominantly within various tissues, including the liver, kidney, and thyroid gland, DIO1 plays a pivotal role in controlling thyroid hormone levels and mediating tissue-specific responses to thyroid hormones. One of the primary functions of DIO1 is its involvement in the activation of thyroid hormones through the conversion of thyroxine (T4), the inactive form of thyroid hormone, into triiodothyronine (T3), the active form. DIO1 accomplishes this by catalyzing the removal of an iodine atom from the outer ring of T4, generating T3, which binds to thyroid hormone receptors and regulates gene expression in target tissues. Moreover, DIO1 contributes to the local regulation of thyroid hormone levels within tissues by modulating the intracellular concentrations of T3. Through its enzymatic activity, DIO1 influences the availability of active thyroid hormone for target cells, thereby fine-tuning thyroid hormone signaling and metabolic responses in a tissue-specific manner. Furthermore, dysregulation of DIO1 expression or activity has been implicated in certain human diseases, including thyroid disorders, metabolic syndrome, and cardiovascular diseases. Alterations in DIO1 levels have been observed in tissues of individuals with thyroid dysfunction, suggesting its potential as a biomarker or therapeutic target in thyroid-related disorders. In summary, DIO1 emerges as a critical enzyme in thyroid hormone metabolism and signaling, with implications for diverse physiological processes and disease pathogenesis. Elucidating the molecular mechanisms underlying DIO1 function holds promise for understanding thyroid hormone regulation and developing targeted therapies for associated disorders.

DIO2, also known as Type 2 Deiodinase, is a vital enzyme involved in the regulation of thyroid hormone activity. Positioned predominantly within various tissues, including the thyroid gland, brain, and brown adipose tissue, DIO2 plays a pivotal role in controlling thyroid hormone levels and mediating tissue-specific responses to thyroid hormones. One of the primary functions of DIO2 is its involvement in the conversion of thyroxine (T4), the inactive form of thyroid hormone, into triiodothyronine (T3), the active form. DIO2 accomplishes this by catalyzing the removal of an iodine atom from the outer ring of T4, generating T3, which binds to thyroid hormone receptors and regulates gene expression in target tissues. Moreover, DIO2 contributes to the local regulation of thyroid hormone levels within tissues by modulating the intracellular concentrations of T3. Through its enzymatic activity, DIO2 influences the availability of active thyroid hormone for target cells, thereby fine-tuning thyroid hormone signaling and metabolic responses in a tissue-specific manner. Furthermore, DIO2 is involved in thermogenesis and energy metabolism, particularly in brown adipose tissue, where it regulates the expression of genes involved in adaptive thermogenesis and lipid metabolism. By converting T4 to T3 locally, DIO2 enhances the responsiveness of brown adipocytes to thyroid hormone stimulation, promoting energy expenditure and heat production. Dysregulation of DIO2 expression or activity has been implicated in various human diseases, including thyroid disorders, metabolic syndrome, and obesity. Alterations in DIO2 levels have been observed in tissues of individuals with thyroid dysfunction, suggesting its potential as a biomarker or therapeutic target in thyroid-related disorders. In summary, DIO2 emerges as a critical enzyme in thyroid hormone metabolism and signaling, with implications for diverse physiological processes and disease pathogenesis. Elucidating the molecular mechanisms underlying DIO2 function holds promise for understanding thyroid hormone regulation and developing targeted therapies for associated disorders.

DIO3, also known as Type 3 Deiodinase, is a crucial enzyme involved in the regulation of thyroid hormone activity. Positioned primarily within various tissues, including the liver, brain, and placenta, DIO3 plays a pivotal role in controlling thyroid hormone levels and mediating tissue-specific responses to thyroid hormones. One of the key functions of DIO3 is its ability to catalyze the inactivation of thyroid hormones, particularly thyroxine (T4), by converting it into an inactive metabolite known as reverse triiodothyronine (rT3). This enzymatic activity helps fine-tune thyroid hormone signaling by reducing the availability of active thyroid hormones in target tissues, thereby modulating metabolic rate, growth, and development. Moreover, DIO3 expression is tightly regulated in response to various physiological and pathological conditions, such as fasting, stress, and inflammation. Changes in DIO3 levels can impact thyroid hormone homeostasis and contribute to metabolic dysregulation, making it a subject of interest in studies investigating metabolic disorders and thyroid-related diseases. Furthermore, dysregulation of DIO3 expression or activity has been implicated in certain human diseases, including metabolic syndrome, diabetes, and thyroid disorders. Altered DIO3 levels have been observed in tissues of individuals with thyroid dysfunction, suggesting its potential as a biomarker for thyroid hormone imbalance. In summary, DIO3 emerges as a critical enzyme in the regulation of thyroid hormone activity, with implications for metabolic homeostasis and physiological adaptation. Elucidating the molecular mechanisms underlying DIO3 function holds promise for understanding thyroid hormone signaling pathways and developing targeted therapies for associated disorders.

GLIS3 (GLIS Family Zinc Finger 3): GLIS3 is a transcription factor that plays a significant role in the regulation of gene expression in various biological processes, including thyroid hormone signaling and pancreatic beta-cell development. Mutations in GLIS3 have been linked to a range of disorders, including congenital hypothyroidism and neonatal diabetes, underscoring its importance in endocrine function and development.

H2BC1 refers to Histone H2B type 1-C/E/F/G/I, a member of the histone H2B family, which is essential for the packaging of DNA into chromatin within the nucleus of eukaryotic cells. Histones, including H2B proteins, play a crucial role in regulating gene expression by modulating the accessibility of DNA to transcription factors and the transcriptional machinery. H2BC1 is specifically involved in forming the core structure of nucleosomes, the basic repeating units of chromatin. Within nucleosomes, H2B proteins, along with histones H2A, H3, and H4, form an octameric complex around which DNA is wrapped. This compacted structure helps to organize and condense the genome, facilitating various cellular processes such as DNA replication, transcription, and repair. Moreover, histone H2B proteins undergo various post-translational modifications, such as methylation, acetylation, and ubiquitination, which further regulate chromatin structure and gene expression. These modifications can influence the recruitment of transcriptional regulators and chromatin-modifying enzymes, thereby modulating gene activity in response to cellular signals and environmental cues. Furthermore, dysregulation of histone H2B expression or modifications has been implicated in various human diseases, including cancer, developmental disorders, and neurodegenerative diseases. Alterations in histone H2B levels or modifications can disrupt normal chromatin structure and gene regulation, leading to aberrant cellular processes and disease pathogenesis. In summary, H2BC1 is a crucial component of chromatin structure and gene regulation, with implications for diverse physiological processes and disease states. Elucidating the roles of H2BC1 and other histone proteins in chromatin dynamics holds promise for understanding gene expression regulation and developing targeted therapies for associated disorders.

ILRUN, also known as interleukin-like RUN domain-containing protein, is a recently discovered protein that plays a role in immune regulation. Positioned within the cytoplasm of cells, ILRUN contains a RUN domain, which is known to be involved in protein-protein interactions. Although the exact function of ILRUN is still being elucidated, initial studies suggest its involvement in modulating immune responses. It is hypothesized that ILRUN may interact with other proteins involved in immune signaling pathways, potentially influencing cytokine production, immune cell activation, or inflammatory processes. Moreover, ILRUN has been identified as a potential biomarker in certain immune-related disorders or inflammatory conditions. Changes in ILRUN expression levels have been observed in experimental models of autoimmune diseases and inflammation, indicating its potential role in disease pathogenesis or as a marker of disease severity. Further research is needed to fully understand the biological functions and regulatory mechanisms of ILRUN in immune regulation. Investigating its interactions with other proteins and its involvement in specific signaling pathways will provide insights into its role in health and disease, with potential implications for the development of novel therapeutic strategies.

MC4R (Melanocortin 4 Receptor): MC4R is a G protein-coupled receptor involved in regulating energy homeostasis, appetite, and body weight. Mutations in MC4R are one of the most common genetic causes of obesity due to its role in controlling energy balance. It is a target for developing obesity treatments.

NCOR1, also known as Nuclear Receptor Corepressor 1, is a critical regulator of gene expression and transcriptional repression. Positioned predominantly within the nucleus of cells, NCOR1 plays a pivotal role in modulating the activity of nuclear receptors and other transcription factors. One of the primary functions of NCOR1 is to act as a corepressor for various nuclear receptors, including thyroid hormone receptors (TRs), retinoic acid receptors (RARs), and peroxisome proliferator-activated receptors (PPARs). By recruiting histone deacetylases (HDACs) and other chromatin-modifying enzymes to target gene promoters, NCOR1 facilitates the formation of repressive chromatin structures, leading to transcriptional silencing. Moreover, NCOR1 is involved in complex regulatory networks governing diverse cellular processes, including metabolism, development, and immune responses. Through its interactions with transcription factors and cofactors, NCOR1 modulates the expression of target genes involved in these physiological processes, contributing to cellular homeostasis and adaptation to environmental cues. Furthermore, dysregulation of NCOR1 expression or activity has been implicated in various human diseases, including metabolic disorders, cancer, and neurological conditions. Altered NCOR1 levels have been observed in tissues of individuals with obesity, diabetes, and certain cancers, highlighting its significance as a potential biomarker or therapeutic target in disease management. In summary, NCOR1 emerges as a central player in transcriptional regulation, with implications for diverse cellular functions and disease pathogenesis. Elucidating the molecular mechanisms underlying NCOR1 function holds promise for understanding gene regulatory networks and developing targeted therapies for associated disorders.

RNF144B, also known as Ring Finger Protein 144B, is a member of the RING finger protein family, characterized by the presence of a RING (Really Interesting New Gene) domain, which confers E3 ubiquitin ligase activity. Positioned predominantly within the cytoplasm or nucleus of cells, RNF144B plays a crucial role in the regulation of protein degradation and cellular signaling pathways. One of the primary functions of RNF144B is its involvement in the ubiquitin-proteasome system, a major pathway for protein degradation in eukaryotic cells. As an E3 ubiquitin ligase, RNF144B catalyzes the transfer of ubiquitin molecules onto substrate proteins, targeting them for degradation by the 26S proteasome. This process plays a pivotal role in controlling the abundance and activity of key regulatory proteins involved in diverse cellular processes, including cell cycle progression, apoptosis, and signal transduction. Moreover, RNF144B has been implicated in various cellular processes, including DNA repair, autophagy, and immune responses. Through its ubiquitin ligase activity, RNF144B regulates the turnover of proteins involved in these pathways, influencing cellular homeostasis and adaptation to environmental stimuli. Furthermore, dysregulation of RNF144B expression or activity has been associated with certain human diseases, including cancer, neurodegenerative disorders, and inflammatory conditions. Altered RNF144B levels have been observed in tumor tissues, where it may contribute to aberrant signaling pathways, tumor growth, and metastasis. In summary, RNF144B emerges as a critical regulator of protein degradation and cellular signaling, with implications for diverse physiological processes and disease pathogenesis. Elucidating the molecular mechanisms underlying RNF144B function holds promise for understanding its contributions to health and disease and exploring its potential as a therapeutic target in various pathological contexts.

SEPHS1, also known as Selenophosphate synthetase 1, is a vital enzyme involved in the biosynthesis of selenoproteins, a class of proteins containing the amino acid selenocysteine (Sec). Positioned predominantly within the cytoplasm of cells, SEPHS1 plays a crucial role in selenium metabolism and the incorporation of selenocysteine into nascent selenoproteins. One of the primary functions of SEPHS1 is its involvement in the synthesis of selenophosphate, the activated form of selenium required for selenocysteine incorporation. As a selenophosphate synthetase, SEPHS1 catalyzes the conversion of selenide and ATP into selenophosphate, providing the essential precursor for selenocysteine tRNA (Sec-tRNA^[Ser]Sec) biosynthesis. Moreover, SEPHS1 is indispensable for the efficient translation of selenoprotein mRNAs. It is involved in the specific recognition and binding of Sec-tRNA^[Ser]Sec to the ribosome, ensuring accurate incorporation of selenocysteine into the nascent polypeptide chain during protein synthesis. This process is essential for the synthesis of functional selenoproteins, which play critical roles in antioxidant defense, redox regulation, and thyroid hormone metabolism. Furthermore, dysregulation of SEPHS1 expression or activity has been implicated in various human diseases, including cancer, neurodegenerative disorders, and cardiovascular diseases. Alterations in selenium metabolism or selenoprotein expression have been associated with increased susceptibility to oxidative stress, impaired immune function, and disrupted cellular homeostasis. In summary, SEPHS1 emerges as a central player in selenium metabolism and selenoprotein biosynthesis, with implications for diverse physiological processes and disease pathogenesis. Elucidating the molecular mechanisms underlying SEPHS1 function holds promise for understanding its contributions to health and disease and exploring its potential as a therapeutic target in various pathological contexts.

SIM1 (Single-Minded Homolog 1): SIM1 is a transcription factor that plays a crucial role in the development of specific brain regions, including the hypothalamus. It is involved in the regulation of appetite and energy homeostasis. Mutations in SIM1 have been associated with obesity and other metabolic disorders.

SLCO1B1, also known as Solute Carrier Organic Anion Transporter Family Member 1B1, is a membrane-bound transporter protein primarily found in the liver. It plays a crucial role in the uptake of various endogenous and exogenous compounds, including bile acids, hormones, drugs, and toxins, from the bloodstream into hepatocytes (liver cells). One of the primary functions of SLCO1B1 is its involvement in the hepatic uptake of bile acids, a process essential for bile acid homeostasis and bile formation. By transporting bile acids across the sinusoidal membrane of hepatocytes, SLCO1B1 facilitates their clearance from the bloodstream and their subsequent incorporation into bile, which is then secreted into the bile canaliculi and ultimately into the gastrointestinal tract. Moreover, SLCO1B1 is also responsible for the uptake of various drugs and xenobiotics into hepatocytes, where they may undergo metabolism, detoxification, or excretion. The transport activity of SLCO1B1 can significantly influence the pharmacokinetics and pharmacodynamics of drugs, impacting their efficacy, toxicity, and potential for drug-drug interactions. Furthermore, genetic variations in the SLCO1B1 gene have been associated with altered transporter activity and pharmacokinetics of certain drugs. For example, polymorphisms in SLCO1B1 have been linked to variability in statin response and the risk of statin-induced myopathy, a common adverse effect of statin therapy. In summary, SLCO1B1 is a critical transporter protein involved in the hepatic uptake of bile acids, drugs, and other compounds, with implications for bile acid metabolism, drug disposition, and clinical pharmacology. Understanding the role of SLCO1B1 in drug transport and metabolism is essential for optimizing drug therapy and minimizing the risk of adverse drug reactions.

SOX2, short for SRY (Sex Determining Region Y)-Box 2, is a critical transcription factor that plays a pivotal role in embryonic development, stem cell pluripotency, and tissue homeostasis. Positioned predominantly within the nucleus of cells, SOX2 is involved in the regulation of gene expression by binding to specific DNA sequences and modulating the activity of target genes. One of the primary functions of SOX2 is its involvement in the maintenance of stem cell pluripotency and self-renewal. Alongside other transcription factors, such as OCT4 and NANOG, SOX2 forms a core regulatory network that sustains the undifferentiated state of embryonic stem cells and induced pluripotent stem cells. Through its interactions with chromatin remodeling complexes and transcriptional co-regulators, SOX2 regulates the expression of genes involved in stem cell identity and differentiation. Moreover, SOX2 plays essential roles in embryonic development, where it is required for the formation and patterning of various tissues and organs, including the central nervous system, sensory organs, and endodermal derivatives. Its expression is dynamically regulated during development, reflecting its diverse functions in cell fate determination and tissue morphogenesis. Furthermore, dysregulation of SOX2 expression or activity has been implicated in various human diseases, including cancer, neurodevelopmental disorders, and ocular diseases. SOX2 is frequently amplified or overexpressed in various cancers, where it promotes tumor growth, metastasis, and resistance to therapy. Conversely, loss of SOX2 function or mutations in its encoding gene have been associated with developmental abnormalities and congenital disorders. In summary, SOX2 emerges as a master regulator of stem cell pluripotency, tissue development, and disease pathogenesis. Elucidating the molecular mechanisms underlying SOX2 function holds promise for understanding its contributions to health and disease and exploring its potential as a therapeutic target in various pathological contexts.

ZGRF1, also known as Zinc finger GRF-type containing 1, is a protein characterized by the presence of zinc finger domains, which are common protein motifs involved in nucleic acid binding and protein-protein interactions. Positioned within the nucleus of cells, ZGRF1 likely functions as a transcription factor or a regulator of gene expression. While specific details regarding the function of ZGRF1 are still being elucidated, proteins containing zinc finger domains often play crucial roles in diverse cellular processes, including gene transcription, RNA processing, and chromatin remodeling. Zinc finger proteins can act as transcriptional activators or repressors by binding to specific DNA sequences and recruiting transcriptional co-regulators to modulate gene expression. Moreover, zinc finger proteins like ZGRF1 are involved in various signaling pathways and developmental processes, contributing to cell fate determination, tissue morphogenesis, and organismal development. Through their interactions with other proteins and nucleic acids, zinc finger proteins can influence cellular proliferation, differentiation, and response to environmental cues. Furthermore, dysregulation of zinc finger proteins has been implicated in certain human diseases, including cancer, developmental disorders, and neurological conditions. Alterations in the expression or activity of zinc finger proteins like ZGRF1 can disrupt normal cellular functions and contribute to disease pathogenesis. In summary, while the specific function of ZGRF1 remains to be fully elucidated, its classification as a zinc finger protein suggests its potential involvement in transcriptional regulation and other cellular processes. Further research is needed to unravel the molecular mechanisms underlying ZGRF1 function and its significance in health and disease.

CDK17, also known as Cyclin-dependent kinase 17, is a member of the cyclin-dependent kinase (CDK) family, which plays crucial roles in cell cycle regulation, transcriptional control, and cellular differentiation. Positioned within the nucleus of cells, CDK17 functions as a serine/threonine protein kinase, phosphorylating target proteins to regulate their activity and function. One of the primary functions of CDK17 is its involvement in cell cycle progression. CDK17 activity is tightly regulated throughout the cell cycle, and it plays a role in promoting the transition from G1 phase to S phase, where DNA replication occurs. CDK17 phosphorylates various substrates involved in cell cycle regulation, including proteins that control the expression of genes required for DNA replication and cell division. Moreover, CDK17 has been implicated in the regulation of transcriptional processes. It can phosphorylate transcription factors and co-regulators, influencing their activity and ability to regulate gene expression. By modulating the activity of transcriptional machinery, CDK17 can impact cellular processes such as differentiation, proliferation, and response to environmental stimuli. Furthermore, dysregulation of CDK17 expression or activity has been associated with certain human diseases, including cancer and neurodegenerative disorders. Altered CDK17 levels have been observed in tumor tissues, where it may contribute to aberrant cell cycle progression, genomic instability, and tumor growth. In summary, CDK17 is a critical regulator of cell cycle progression and transcriptional control, with implications for diverse physiological processes and disease pathogenesis. Elucidating the molecular mechanisms underlying CDK17 function holds promise for understanding its contributions to health and disease and exploring its potential as a therapeutic target in various pathological contexts.

CERS6, also known as Ceramide Synthase 6, is an enzyme involved in the biosynthesis of ceramides, which are essential components of cell membranes and serve as signaling molecules in various cellular processes. Positioned within the endoplasmic reticulum (ER) of cells, CERS6 plays a crucial role in catalyzing the synthesis of ceramides by acylating sphingoid bases with fatty acyl-CoA substrates. One of the primary functions of CERS6 is its involvement in the generation of specific ceramide species with distinct acyl chain lengths and saturation levels. Ceramides produced by CERS6 can vary in their fatty acyl composition, which influences their biophysical properties and cellular functions. These ceramide species participate in various cellular processes, including cell growth, apoptosis, inflammation, and lipid metabolism. Moreover, ceramides generated by CERS6 serve as precursors for the synthesis of complex sphingolipids, such as sphingomyelin and glycosphingolipids, which are important constituents of cellular membranes and participate in cell signaling pathways. By regulating ceramide levels and composition, CERS6 influences the balance between different sphingolipid species and modulates cellular responses to environmental cues and stress stimuli. Furthermore, dysregulation of CERS6 expression or activity has been associated with certain human diseases, including metabolic disorders, neurodegenerative diseases, and cancer. Altered ceramide levels have been observed in tissues of individuals with obesity, insulin resistance, and neurodegeneration, highlighting the significance of ceramide metabolism in disease pathogenesis. In summary, CERS6 is a critical enzyme in ceramide biosynthesis, with implications for diverse physiological processes and disease states. Elucidating the molecular mechanisms underlying CERS6 function holds promise for understanding sphingolipid metabolism and developing targeted therapies for associated disorders.

FOXA2 (Forkhead Box A2): FOXA2 is a transcription factor that plays a pivotal role in the development of various tissues, including the liver, pancreas, and lung. This transcription factor is involved in the regulation of genes related to metabolism, development, and differentiation. In the pancreas, FOXA2 is crucial for the development and function of insulin-producing beta cells. It plays a key role in maintaining glucose homeostasis by regulating the expression of genes involved in insulin secretion and glucose metabolism.

LRRC6 (Leucine-Rich Repeat-Containing Protein 6): LRRC6 encodes a protein that is part of the ciliary structure in cells. Cilia are important for cellular motility and signaling. Mutations in LRRC6 can lead to ciliopathies, a group of genetic disorders characterized by ciliary dysfunction and various clinical manifestations.

MAF (MAF BZIP Transcription Factor): MAF encodes a transcription factor that is involved in the development and differentiation of various tissues, including the lens of the eye and pancreatic beta cells. It plays a role in regulating gene expression and cell fate determination. Mutations in MAF can lead to developmental abnormalities and diseases.

NFIA, or Nuclear Factor I A, is a transcription factor that plays crucial roles in the regulation of gene expression, cellular differentiation, and development. Positioned predominantly within the nucleus of cells, NFIA belongs to the Nuclear Factor I (NFI) family, which consists of highly conserved DNA-binding proteins involved in the transcriptional control of various genes. One of the primary functions of NFIA is its involvement in the regulation of gene expression through binding to specific DNA sequences, known as NFIA recognition elements, within the promoter regions of target genes. By interacting with transcriptional co-regulators and chromatin-modifying enzymes, NFIA can either activate or repress the transcription of target genes, depending on cellular context and environmental cues. Moreover, NFIA has been implicated in various cellular processes, including cell proliferation, differentiation, and survival. It plays critical roles in the development and function of multiple tissues and organs, including the central nervous system, liver, and adipose tissue. NFIA is particularly important for the development of the central nervous system, where it regulates the formation and differentiation of neural progenitor cells and the specification of neuronal and glial cell lineages. Furthermore, dysregulation of NFIA expression or activity has been associated with certain human diseases and developmental disorders. Altered NFIA levels have been observed in various cancers, where it may contribute to tumor progression, metastasis, and drug resistance. Additionally, mutations in the NFIA gene have been linked to congenital abnormalities, such as brain malformations and developmental delays. In summary, NFIA is a critical transcription factor involved in the regulation of gene expression and cellular differentiation, with implications for development, tissue homeostasis, and disease pathogenesis. Elucidating the molecular mechanisms underlying NFIA function holds promise for understanding its roles in health and disease and exploring its potential as a therapeutic target in various pathological contexts.

NKX2-1, also known as thyroid transcription factor 1 (TTF-1), is a protein that functions as a transcription factor, meaning it regulates the expression of genes by binding to specific DNA sequences. It is a member of the NKX family of homeodomain-containing transcription factors and plays a critical role in the development and function of several organs, particularly the thyroid, lung, and brain. One of the primary functions of NKX2-1 is its role in the development of the thyroid gland. NKX2-1 is expressed in the thyroid primordium during embryonic development and is essential for the specification and differentiation of thyroid follicular cells. It regulates the expression of genes involved in thyroid organogenesis, thyroid hormone synthesis, and thyroid-specific functions, such as thyroglobulin and thyroperoxidase. Moreover, NKX2-1 is involved in lung development and function. It is expressed in the developing lung epithelium and regulates the expression of genes involved in lung morphogenesis, including surfactant proteins and Clara cell secretory proteins. NKX2-1 plays a crucial role in the formation of pulmonary epithelial cells and the differentiation of alveolar type II cells, which produce surfactant to reduce surface tension in the alveoli and facilitate gas exchange. Furthermore, NKX2-1 is implicated in brain development, particularly in the differentiation of neurons in the basal ganglia and hypothalamus. It regulates the expression of genes involved in neurotransmitter synthesis and signaling pathways, contributing to neuronal function and connectivity in these brain regions. Additionally, NKX2-1 has been associated with various diseases and disorders. Mutations or dysregulation of NKX2-1 expression have been implicated in congenital hypothyroidism, thyroid dysgenesis, respiratory distress syndrome, lung adenocarcinoma, and neurodevelopmental disorders such as chorea and cognitive impairment. In summary, NKX2-1 is a transcription factor that plays critical roles in the development and function of the thyroid, lung, and brain. Its functions in regulating gene expression during organogenesis and tissue differentiation are essential for normal development and physiology. Dysregulation of NKX2-1 expression or activity can lead to various developmental abnormalities and diseases, highlighting its significance in human health and development.

NR3C2, also known as Nuclear Receptor Subfamily 3 Group C Member 2 or mineralocorticoid receptor (MR), is a nuclear receptor protein that plays a crucial role in the regulation of electrolyte balance and blood pressure homeostasis. Positioned predominantly within the cytoplasm of target cells, NR3C2 functions as a ligand-activated transcription factor that mediates the effects of mineralocorticoid hormones, such as aldosterone. One of the primary functions of NR3C2 is its involvement in the regulation of sodium and potassium ion transport in the kidney, colon, and salivary glands. Upon binding to aldosterone, NR3C2 undergoes a conformational change and translocates into the nucleus, where it regulates the expression of target genes encoding ion channels, pumps, and transporters. Through its transcriptional activity, NR3C2 promotes sodium reabsorption and potassium excretion, thereby modulating extracellular fluid volume and blood pressure. Moreover, NR3C2 is also involved in the regulation of other physiological processes, including cardiac function, vascular tone, and inflammation. It influences the expression of genes involved in cardiac remodeling, endothelial function, and immune cell activation, contributing to cardiovascular health and immune responses. Furthermore, dysregulation of NR3C2 expression or activity has been associated with various cardiovascular disorders, including hypertension, heart failure, and electrolyte imbalances. Mutations in the NR3C2 gene can lead to aldosterone resistance, a condition characterized by impaired sodium retention and potassium excretion, resulting in hypertension and electrolyte abnormalities. In summary, NR3C2 is a critical regulator of electrolyte balance and blood pressure homeostasis, with implications for cardiovascular health and disease. Elucidating the molecular mechanisms underlying NR3C2 function holds promise for understanding its roles in health and disease and exploring its potential as a therapeutic target in cardiovascular disorders and hypertension.

PDE8B (Phosphodiesterase 8B): PDE8B is another gene that encodes a phosphodiesterase enzyme, specifically phosphodiesterase 8B. Like PDE10A, it regulates cyclic nucleotide signaling, but its functions may vary across different tissues and cell types. PDE8B may have implications in various physiological processes.

PDE10A (Phosphodiesterase 10A): PDE10A encodes an enzyme called phosphodiesterase 10A, which regulates intracellular signaling by hydrolyzing cyclic nucleotides, particularly cAMP and cGMP. PDE10A is primarily expressed in the brain and is involved in neuronal signaling. It has been implicated in neurological and psychiatric disorders.

TNP1, or Transition Protein 1, is a protein primarily found in the nuclei of developing spermatids, the immature male germ cells, during spermiogenesis—the final stage of spermatogenesis where round spermatids differentiate into mature spermatozoa. TNP1 is a member of a family of small, highly basic proteins known as transition proteins, which are involved in the chromatin remodeling process that occurs during spermiogenesis. One of the primary functions of TNP1 is its role in the replacement of histones with protamines, specialized proteins that condense and package DNA into a highly compacted form within the sperm nucleus. During spermiogenesis, TNP1 binds to histones in the chromatin and facilitates their displacement, allowing for the subsequent incorporation of protamines. This process results in the formation of a highly condensed and stable nucleus in mature sperm, essential for protecting the paternal DNA during fertilization and ensuring proper sperm function. Moreover, TNP1 contributes to the compaction and stabilization of sperm chromatin, which is crucial for sperm motility, DNA integrity, and fertilization success. It helps to establish the unique chromatin structure characteristic of spermatozoa, which is essential for efficient sperm function and successful transmission of genetic material to the oocyte during fertilization. Furthermore, alterations in TNP1 expression or function have been associated with male infertility and reproductive disorders. Dysregulation of chromatin remodeling processes during spermiogenesis, including abnormalities in TNP1 expression or localization, can lead to defects in sperm chromatin structure and function, impairing fertility and reducing the chances of successful fertilization. In summary, TNP1 is a critical component of the chromatin remodeling process during spermiogenesis, playing essential roles in the condensation and stabilization of sperm chromatin. Understanding the molecular mechanisms underlying TNP1 function is crucial for elucidating the processes involved in sperm development and fertilization and for diagnosing and treating male infertility and reproductive disorders.

TBX2 (T-Box Transcription Factor 2): TBX2 encodes a transcription factor that belongs to the T-box family. It plays a role in embryonic development and tissue differentiation, particularly in the development of the heart and limb formation.

VAV3 (Vav Guanine Nucleotide Exchange Factor 3): VAV3 encodes a guanine nucleotide exchange factor that is involved in intracellular signaling pathways related to cell proliferation and cytoskeletal rearrangement. It plays a role in immune cell activation and may have implications in immune responses and cancer.

VEGFC, or Vascular Endothelial Growth Factor C, is a crucial protein involved in the regulation of lymphangiogenesis, the formation of lymphatic vessels, and angiogenesis, the formation of blood vessels. As a member of the vascular endothelial growth factor (VEGF) family, VEGFC plays diverse roles in physiological and pathological processes, including embryonic development, tissue repair, and tumor progression. One of the primary functions of VEGFC is its ability to stimulate the growth and proliferation of lymphatic endothelial cells, promoting the formation and remodeling of lymphatic vessels. VEGFC binds to and activates its receptors, primarily VEGFR-3 (vascular endothelial growth factor receptor 3), initiating signaling cascades that promote lymphatic vessel sprouting and branching. This process is essential for maintaining tissue fluid balance, immune cell trafficking, and the absorption of dietary fats from the intestine. Moreover, VEGFC is involved in angiogenesis, where it can also stimulate the growth and branching of blood vessels, particularly in the context of wound healing and tissue repair. By binding to its receptors, including VEGFR-2, VEGFC promotes endothelial cell proliferation, migration, and survival, contributing to the formation of new blood vessels from pre-existing ones. Furthermore, dysregulation of VEGFC expression or activity has been implicated in various human diseases, including cancer, lymphedema, and inflammatory disorders. Overexpression of VEGFC is often observed in tumor tissues, where it can promote tumor angiogenesis and lymphangiogenesis, facilitating tumor growth, metastasis, and resistance to therapy. In contrast, deficiencies in VEGFC signaling can lead to impaired lymphatic vessel formation and lymphedema, a condition characterized by abnormal accumulation of lymph fluid in tissues. In summary, VEGFC is a critical regulator of lymphangiogenesis and angiogenesis, with implications for tissue homeostasis, wound healing, and disease pathogenesis. Elucidating the molecular mechanisms underlying VEGFC function holds promise for understanding its roles in health and disease and for developing targeted therapies for associated disorders, such as cancer and lymphedema.

INSR, or Insulin Receptor, is a transmembrane receptor protein that plays a crucial role in mediating the biological effects of insulin, a hormone involved in the regulation of glucose metabolism, lipid metabolism, and cellular growth. INSR is primarily found on the surface of target cells, such as adipocytes, hepatocytes, and skeletal muscle cells. One of the primary functions of INSR is its involvement in insulin signaling pathways. Upon binding of insulin to the extracellular domain of INSR, the receptor undergoes conformational changes, leading to autophosphorylation of tyrosine residues in its intracellular domain. This phosphorylation event activates the receptor's tyrosine kinase activity, initiating a cascade of downstream signaling events that regulate cellular processes such as glucose uptake, glycogen synthesis, protein synthesis, and gene expression. Moreover, INSR plays a critical role in glucose homeostasis by promoting the uptake of glucose from the bloodstream into insulin-sensitive tissues, such as skeletal muscle and adipose tissue. Activation of INSR stimulates the translocation of glucose transporter proteins, such as GLUT4, to the cell membrane, facilitating the uptake of glucose into the cell for energy production or storage. Furthermore, dysregulation of INSR expression or activity has been implicated in various metabolic disorders, including type 2 diabetes mellitus and insulin resistance. Reduced sensitivity or impaired signaling through INSR can lead to elevated blood glucose levels, insulin resistance, and metabolic abnormalities associated with diabetes and obesity. In summary, INSR is a critical mediator of insulin action, playing essential roles in glucose metabolism, lipid metabolism, and cellular growth. Understanding the molecular mechanisms underlying INSR function is essential for elucidating the pathophysiology of metabolic disorders and developing targeted therapies for diabetes and related conditions.

ATP1B2, also known as Sodium/potassium-transporting ATPase subunit beta-2, is a protein that serves as a subunit of the sodium-potassium ATPase (Na+/K+-ATPase) pump. This pump is crucial for maintaining the electrochemical gradients of sodium and potassium ions across cell membranes, a process essential for numerous physiological functions, including nerve conduction, muscle contraction, and regulation of cell volume. As a subunit of the Na+/K+-ATPase pump, ATP1B2 plays an indispensable role in the assembly, stability, and function of the pump complex. It interacts with the catalytic alpha subunit of the pump, ATP1A1 or ATP1A2, and helps to anchor the complex to the cell membrane. Additionally, ATP1B2 contributes to the regulation of pump activity and trafficking, influencing the rate of sodium and potassium ion transport across the membrane. Moreover, ATP1B2 is involved in the maintenance of cellular ion homeostasis and osmotic balance. By actively transporting sodium ions out of the cell and potassium ions into the cell against their respective electrochemical gradients, the Na+/K+-ATPase pump powered by ATP1B2 establishes and maintains the membrane potential necessary for cellular excitability and function. Furthermore, dysregulation of ATP1B2 expression or activity has been implicated in various human diseases, including cardiovascular disorders, neurological disorders, and renal diseases. Mutations in ATP1B2 or alterations in Na+/K+-ATPase function can lead to disturbances in ion homeostasis, impaired cellular signaling, and dysfunction of tissues and organs affected by these conditions. In summary, ATP1B2 is a critical subunit of the Na+/K+-ATPase pump, playing essential roles in ion transport, cellular excitability, and osmotic regulation. Elucidating the molecular mechanisms underlying ATP1B2 function is crucial for understanding its contributions to health and disease and for developing targeted therapies for disorders associated with Na+/K+-ATPase dysfunction.

BAIAP2L1, also known as Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 1, is a protein encoded by the BAIAP2L1 gene. It belongs to the I-BAR domain-containing protein family and is involved in various cellular processes, including actin cytoskeleton remodeling, membrane dynamics, and cell signaling. One of the primary functions of BAIAP2L1 is its role in regulating actin dynamics and cytoskeletal organization. It contains an I-BAR (inverse Bin-Amphiphysin-Rvs) domain, which allows it to bind to and induce curvature in membranes, particularly at sites of membrane protrusions such as filopodia and lamellipodia. Through its ability to interact with actin filaments and membrane phospholipids, BAIAP2L1 participates in the formation and stabilization of actin-rich structures involved in cell migration, adhesion, and morphogenesis. Moreover, BAIAP2L1 is implicated in the regulation of synaptic structure and function in neurons. It interacts with various synaptic proteins and cytoskeletal regulators, contributing to the organization and plasticity of synapses. BAIAP2L1 has been shown to modulate dendritic spine morphology, synaptic transmission, and synaptic plasticity, processes essential for learning and memory. Furthermore, dysregulation of BAIAP2L1 expression or function has been associated with neurological disorders, including schizophrenia, autism spectrum disorders, and intellectual disabilities. Altered BAIAP2L1 levels have been observed in the brains of individuals with these conditions, suggesting its potential involvement in disease pathogenesis. In summary, BAIAP2L1 is a multifunctional protein involved in actin cytoskeleton remodeling, membrane dynamics, and synaptic function. Elucidating the molecular mechanisms underlying BAIAP2L1 function is crucial for understanding its roles in cellular physiology and neurological disorders, and for developing targeted therapies for associated conditions.

DGKB (Diacylglycerol Kinase Beta): DGKB is an enzyme that converts diacylglycerol into phosphatidic acid, playing a critical role in lipid signaling pathways. It's involved in various cellular processes, including insulin sensitivity, and neurotransmitter signaling. Dysregulation of DGKB has been associated with metabolic disorders and is of interest in the study of diseases like diabetes and obesity.

EDA2R, also known as Ectodysplasin A2 receptor, is a protein encoded by the EDA2R gene. It belongs to the tumor necrosis factor receptor (TNFR) superfamily and serves as a receptor for ectodysplasin A2 (EDA-A2), a signaling molecule involved in the development of ectodermal tissues such as hair, teeth, and sweat glands. One of the primary functions of EDA2R is its role in mediating the effects of EDA-A2 signaling during embryonic development. EDA-A2, also known as ectodysplasin A2 or EDA2, is a ligand that binds to EDA2R, initiating signaling cascades that regulate the formation and patterning of ectodermal structures. This signaling pathway plays a critical role in the development of hair follicles, teeth, and other appendages derived from the ectoderm. Moreover, EDA2R signaling is essential for the maintenance and regeneration of ectodermal tissues in adults. It contributes to the regulation of hair follicle cycling, sweat gland function, and tooth development throughout life. Dysregulation of EDA2R signaling can lead to developmental abnormalities or disorders affecting ectodermal tissues, such as hypohidrotic ectodermal dysplasia (HED), a genetic condition characterized by abnormal development of hair, teeth, and sweat glands. Furthermore, EDA2R has been implicated in immune responses and inflammatory processes. It is expressed in immune cells such as dendritic cells and macrophages, where it may modulate immune cell function and cytokine production. Additionally, dysregulation of EDA2R signaling has been associated with inflammatory skin conditions and autoimmune diseases. In summary, EDA2R is a critical receptor involved in the development and maintenance of ectodermal tissues, as well as in immune responses and inflammatory processes. Elucidating the molecular mechanisms underlying EDA2R signaling is crucial for understanding its roles in development, physiology, and disease, and for developing targeted therapies for conditions associated with ectodermal dysplasia and immune dysfunction.

FAM9A, or Family with Sequence Similarity 9 Member A, is a protein-coding gene that belongs to a family of genes with sequence similarity. While specific functions of FAM9A are still under investigation and not extensively characterized, it is known to be expressed in various tissues, including the brain, testis, and ovaries, suggesting potential roles in cellular processes in these organs. The designation "FAM" typically denotes a gene family whose members share sequence similarity but may have diverse functions. Often, genes within the FAM family are involved in various cellular processes, such as cell signaling, transcriptional regulation, or protein-protein interactions. Although the exact function of FAM9A remains to be fully elucidated, understanding its expression patterns and potential interactions with other cellular components may provide insights into its biological roles. Further experimental studies are required to uncover the specific functions of FAM9A and its contributions to cellular physiology and pathology. In summary, FAM9A is a gene within a family of genes with sequence similarity, and its precise function is yet to be determined. Further research is needed to elucidate its biological roles and significance in cellular processes.

FKBP4, also known as FK506-binding protein 4 or FKBP52, is a member of the FK506-binding protein (FKBP) family, which are peptidyl-prolyl cis-trans isomerases (PPIases) that function as molecular chaperones. FKBP4 is primarily found in the cytoplasm and nucleus of cells and is involved in regulating protein folding, trafficking, and signal transduction. One of the primary functions of FKBP4 is its role as a co-chaperone for steroid hormone receptors, including the glucocorticoid receptor (GR) and androgen receptor (AR). FKBP4 interacts with these receptors in the cytoplasm, facilitating their proper folding and assembly into functional complexes with heat shock proteins (HSPs). Upon ligand binding, FKBP4 dissociates from the receptor, allowing it to translocate to the nucleus and regulate gene transcription. Moreover, FKBP4 is implicated in the regulation of various cellular processes, including cell growth, differentiation, and apoptosis. It interacts with a diverse range of protein partners, including kinases, phosphatases, and transcription factors, influencing their activity and function. FKBP4 has been shown to modulate signaling pathways involved in cell survival, stress response, and immune regulation. Furthermore, dysregulation of FKBP4 expression or activity has been associated with certain human diseases, including cancer, neurodegenerative disorders, and metabolic syndrome. Altered FKBP4 levels have been observed in tumor tissues, where it may contribute to tumor progression, metastasis, and resistance to therapy. Additionally, FKBP4 polymorphisms have been linked to susceptibility to neurodegenerative diseases and metabolic disorders. In summary, FKBP4 is a multifunctional protein involved in protein folding, chaperone activity, and signal transduction, with implications for diverse physiological processes and disease states. Elucidating the molecular mechanisms underlying FKBP4 function is crucial for understanding its roles in health and disease and for developing targeted therapies for associated disorders.

GNGT2, also known as Guanine nucleotide-binding protein G(t) subunit gamma-T2, is a protein that belongs to the family of guanine nucleotide-binding proteins (G proteins). GNGT2 is a subunit of the transducin complex, which plays a critical role in signal transduction in photoreceptor cells of the retina. One of the primary functions of GNGT2 is its involvement in the phototransduction cascade, a process by which light stimuli are converted into electrical signals that can be interpreted by the brain. In the retina, photoreceptor cells contain light-sensitive proteins called opsins, which undergo a conformational change upon absorbing photons. This change activates the associated G protein, transducin, composed of alpha (GNAT1) and beta-gamma (GNGT1/GNGT2) subunits. GNGT2 plays a crucial role in transducing the signal from activated rhodopsin (the opsin in rod cells) or cone opsins (the opsins in cone cells) to downstream effector molecules, ultimately leading to changes in membrane potential and neurotransmitter release. By modulating the activity of effector enzymes such as phosphodiesterase and guanylate cyclase, the transducin complex regulates the levels of intracellular messengers, such as cyclic guanosine monophosphate (cGMP), which mediate the response to light stimuli. Furthermore, GNGT2 is involved in the regulation of visual sensitivity and adaptation to varying light conditions. Through its interactions with other signaling proteins in the photoreceptor cells, GNGT2 helps to modulate the sensitivity of the phototransduction cascade, allowing the visual system to adjust to changes in ambient light intensity and maintain optimal visual function. In summary, GNGT2 is a critical component of the transducin complex in photoreceptor cells, where it mediates the transduction of light signals into electrical signals. Elucidating the molecular mechanisms underlying GNGT2 function is essential for understanding visual signal transduction and for elucidating the pathophysiology of retinal diseases associated with G protein dysfunction.

GPR139, also known as G protein-coupled receptor 139, is a protein that belongs to the G protein-coupled receptor (GPCR) superfamily. It is primarily expressed in the central nervous system, particularly in regions associated with the regulation of neurotransmitter systems and neuronal activity. Although the specific functions of GPR139 are still being elucidated, it is believed to play a role in modulating neurotransmission, particularly in the regulation of dopamine and glutamate signaling. Studies have suggested that GPR139 may function as an inhibitory receptor, as its activation leads to decreased cAMP (cyclic adenosine monophosphate) levels and reduced neuronal excitability. Moreover, GPR139 has been implicated in the regulation of various physiological processes, including appetite and metabolism. Preclinical studies have shown that GPR139 agonists can decrease food intake and body weight in animal models, suggesting a potential role in the control of energy balance and food intake regulation. Furthermore, GPR139 has gained attention as a potential therapeutic target for the treatment of neuropsychiatric and metabolic disorders. Dysregulation of GPR139 signaling has been associated with conditions such as schizophrenia, depression, and obesity, highlighting its importance in maintaining normal physiological function. In summary, GPR139 is a G protein-coupled receptor expressed in the central nervous system, involved in modulating neurotransmission, appetite, and metabolism. Further research into the signaling pathways and physiological functions of GPR139 may provide insights into its role in health and disease and its potential as a therapeutic target for various disorders.

HSD17B13, also known as Hydroxysteroid 17-beta dehydrogenase 13, is an enzyme primarily found in the liver and is involved in the metabolism of steroid hormones and fatty acids. It belongs to the hydroxysteroid (17-beta) dehydrogenase (HSD17B) family, which catalyzes the conversion of hydroxysteroids to ketosteroids and vice versa. One of the primary functions of HSD17B13 is its role in fatty acid metabolism, particularly in the oxidation of long-chain fatty acids. HSD17B13 is localized to the peroxisomes, cellular organelles involved in fatty acid metabolism, where it catalyzes the conversion of long-chain fatty acyl-CoAs to the corresponding 3-ketoacyl-CoAs. This enzymatic activity is essential for the breakdown of fatty acids to generate energy through beta-oxidation, a process that occurs in the mitochondria and peroxisomes. Moreover, HSD17B13 has been implicated in the regulation of lipid homeostasis and the development of metabolic disorders such as non-alcoholic fatty liver disease (NAFLD) and alcoholic liver disease (ALD). Genetic variations in the HSD17B13 gene have been associated with susceptibility to NAFLD and ALD, suggesting a potential role for HSD17B13 in the pathogenesis of these conditions. Additionally, HSD17B13 may modulate hepatic lipid accumulation and inflammation, thereby influencing the progression of liver diseases. Furthermore, recent studies have suggested that HSD17B13 may have additional functions beyond fatty acid metabolism. It has been proposed to interact with other proteins and signaling pathways involved in cellular processes such as apoptosis, fibrosis, and inflammation. However, further research is needed to elucidate the molecular mechanisms underlying these potential functions of HSD17B13 and their implications in health and disease. In summary, HSD17B13 is an enzyme involved in fatty acid metabolism and lipid homeostasis, primarily localized to the liver. Its roles in fatty acid oxidation and hepatic lipid metabolism make it a potentially important player in the development of metabolic disorders, particularly NAFLD and ALD. Further research on HSD17B13 and its regulatory mechanisms may provide insights into its physiological functions and therapeutic potential in liver diseases and metabolic disorders.

JHY (Jellybean Homologue Y): JHY, analogous to its namesake in the Matrix Metallopeptidase family, is a pivotal player in cellular processes, albeit in a distinct context. This protein is fundamental in orchestrating intracellular signaling cascades that regulate crucial aspects of cell behavior and function. Through its involvement in signal transduction pathways, JHY influences diverse physiological phenomena, ranging from cell proliferation and differentiation to cell migration and survival. The intricate control exerted by JHY on cellular activities underscores its significance in maintaining proper cellular homeostasis. However, aberrations in JHY expression or function have been implicated in various pathological conditions, including cancer progression, neurodegenerative disorders, and immune dysregulation. Unraveling the intricate mechanisms governing JHY's role in cellular signaling may offer promising avenues for therapeutic intervention, particularly in diseases characterized by dysregulated cellular behaviors.

KANSL1, also known as KAT8 Regulatory NSL Complex Subunit 1, is a protein that plays a crucial role in chromatin regulation and gene expression. It is a component of the Non-Specific Lethal (NSL) histone acetyltransferase (HAT) complex, which is responsible for acetylating histone proteins, specifically histone H4 at lysine 16 (H4K16ac), a modification associated with transcriptional activation and chromatin remodeling. One of the primary functions of KANSL1 within the NSL complex is its role in regulating gene expression by modifying chromatin structure. The NSL complex targets specific genomic loci and catalyzes the acetylation of histone proteins, leading to an open chromatin configuration that facilitates transcriptional activation. This process allows for the efficient expression of genes involved in various cellular processes, including development, differentiation, and proliferation. Moreover, KANSL1 has been implicated in the regulation of neuronal development and function. Mutations in the KANSL1 gene have been associated with Koolen-De Vries syndrome (KdVS), a rare genetic disorder characterized by intellectual disability, developmental delay, and distinctive facial features. KANSL1 haploinsufficiency, where one copy of the gene is lost or mutated, is thought to contribute to the neurodevelopmental abnormalities observed in individuals with KdVS. Furthermore, KANSL1 is involved in DNA repair mechanisms and maintenance of genomic stability. It interacts with other proteins involved in DNA damage response pathways, suggesting a role in the cellular response to DNA damage and maintenance of genome integrity. In summary, KANSL1 is a critical component of the NSL histone acetyltransferase complex, involved in chromatin regulation, gene expression, and maintenance of genomic stability. Dysregulation of KANSL1 function has been linked to neurodevelopmental disorders, highlighting its importance in normal brain development and function. Further research into the molecular mechanisms underlying KANSL1 function may provide insights into its roles in health and disease

MYPOP (Myb-related transcription factor partner): Similar to MMP15's role in the extracellular matrix (ECM), MYPOP serves as a crucial regulator within the intricate network of transcriptional control. As a partner to Myb-related transcription factors, MYPOP plays a vital role in modulating gene expression patterns essential for various cellular processes, including proliferation, differentiation, and cell cycle progression. Through its involvement in transcriptional regulation, MYPOP influences diverse physiological phenomena, such as tissue development, immune response, and homeostasis maintenance. Dysregulation of MYPOP expression or activity has been implicated in numerous pathological conditions, including cancer, developmental disorders, and immune-related diseases. The precise orchestration of MYPOP-mediated transcriptional control underscores its significance in cellular function and its potential as a therapeutic target for diseases involving aberrant gene expression patterns.

NR2F2 (Nuclear Receptor Subfamily 2 Group F Member 2): NR2F2, also known as COUP-TFII, is a transcription factor involved in the development and function of several organs, including the heart and vascular system. It regulates genes involved in angiogenesis (formation of new blood vessels) and metabolic processes. Abnormal NR2F2 function has implications in developmental disorders and various cancers, where it can influence tumor growth and metastasis.

NRBF2, also known as Nuclear Receptor Binding Factor 2, is a protein involved in autophagy, a cellular process responsible for degrading and recycling damaged or unnecessary cellular components. NRBF2 plays a crucial role in the regulation of autophagy by facilitating the formation of autophagosomes, double-membraned vesicles that engulf and sequester cellular cargo for degradation. One of the primary functions of NRBF2 is its interaction with the autophagy-initiating kinase complex, ULK1 (Unc-51 Like Autophagy Activating Kinase 1) complex. NRBF2 binds to the ULK1 complex, which consists of ULK1, ATG13, FIP200, and ATG101, and promotes its stability and activity. This interaction is essential for the activation of ULK1 kinase activity, which phosphorylates downstream targets involved in autophagosome formation and maturation. Moreover, NRBF2 participates in the regulation of various cellular processes associated with autophagy, including nutrient sensing, energy homeostasis, and cellular stress responses. It acts as a scaffold protein, mediating protein-protein interactions within the autophagy machinery and coordinating the assembly of autophagosomal membranes. Furthermore, dysregulation of NRBF2 expression or function has been implicated in various human diseases, including cancer, neurodegenerative disorders, and metabolic disorders. Altered NRBF2 levels or mutations in NRBF2 have been associated with defects in autophagy regulation, leading to abnormal accumulation of protein aggregates, dysfunctional organelles, and impaired cellular homeostasis. In summary, NRBF2 is a critical regulator of autophagy, facilitating the formation of autophagosomes and coordinating the autophagic process. Elucidating the molecular mechanisms underlying NRBF2 function is essential for understanding its roles in health and disease and for developing targeted therapies for autophagy-related disorders.

PNPLA3 (Patatin-Like Phospholipase Domain Containing 3): PNPLA3 encodes an enzyme called adiponutrin or patatin-like phospholipase domain-containing protein 3 (PNPLA3). It is involved in lipid metabolism and the hydrolysis of triglycerides in adipocytes. Genetic variations in PNPLA3 are associated with liver diseases, including non-alcoholic fatty liver disease (NAFLD).

SERPINA1 (Serpin Family A Member 1): SERPINA1, also known as alpha-1-antitrypsin, is a major protease inhibitor, primarily produced in the liver, and plays a vital role in protecting the lungs from neutrophil elastase. Deficiency in SERPINA1 can lead to alpha-1 antitrypsin deficiency, a genetic disorder that causes lung diseases like emphysema and chronic obstructive pulmonary disease (COPD), as well as liver diseases. It is crucial in maintaining the balance of proteolytic activity in lung tissues.

SLCO1B1, also known as Solute Carrier Organic Anion Transporter Family Member 1B1, is a membrane-bound transporter protein primarily found in the liver. It plays a crucial role in the uptake of various endogenous and exogenous compounds, including bile acids, hormones, drugs, and toxins, from the bloodstream into hepatocytes (liver cells). One of the primary functions of SLCO1B1 is its involvement in the hepatic uptake of bile acids, a process essential for bile acid homeostasis and bile formation. By transporting bile acids across the sinusoidal membrane of hepatocytes, SLCO1B1 facilitates their clearance from the bloodstream and their subsequent incorporation into bile, which is then secreted into the bile canaliculi and ultimately into the gastrointestinal tract. Moreover, SLCO1B1 is also responsible for the uptake of various drugs and xenobiotics into hepatocytes, where they may undergo metabolism, detoxification, or excretion. The transport activity of SLCO1B1 can significantly influence the pharmacokinetics and pharmacodynamics of drugs, impacting their efficacy, toxicity, and potential for drug-drug interactions. Furthermore, genetic variations in the SLCO1B1 gene have been associated with altered transporter activity and pharmacokinetics of certain drugs. For example, polymorphisms in SLCO1B1 have been linked to variability in statin response and the risk of statin-induced myopathy, a common adverse effect of statin therapy. In summary, SLCO1B1 is a critical transporter protein involved in the hepatic uptake of bile acids, drugs, and other compounds, with implications for bile acid metabolism, drug disposition, and clinical pharmacology. Understanding the role of SLCO1B1 in drug transport and metabolism is essential for optimizing drug therapy and minimizing the risk of adverse drug reactions.

TNFSF12, also known as Tumor Necrosis Factor Ligand Superfamily Member 12 or TWEAK (TNF-like weak inducer of apoptosis), is a cytokine belonging to the tumor necrosis factor (TNF) superfamily. It plays diverse roles in inflammation, immunity, tissue homeostasis, and cell death regulation. One of the primary functions of TNFSF12 is its role in modulating immune responses and inflammation. TNFSF12 can act as both a pro-inflammatory and anti-inflammatory cytokine, depending on the cellular context and signaling pathways involved. It promotes the production of inflammatory cytokines and chemokines, recruits immune cells to sites of inflammation, and stimulates the activation of endothelial cells and fibroblasts. Moreover, TNFSF12 is involved in the regulation of tissue remodeling and repair processes. It promotes the proliferation, migration, and activation of various cell types, including fibroblasts, endothelial cells, and mesenchymal stem cells, contributing to tissue regeneration and wound healing. Additionally, TNFSF12 can induce apoptosis or cell death in certain cell types, particularly cancer cells, through activation of pro-apoptotic signaling pathways. Furthermore, dysregulation of TNFSF12 expression or signaling has been implicated in various human diseases, including autoimmune diseases, inflammatory disorders, and cancer. Altered TNFSF12 levels or aberrant TNFSF12 signaling pathways can contribute to chronic inflammation, tissue damage, and tumor progression. In summary, TNFSF12 is a multifunctional cytokine involved in immune regulation, inflammation, tissue repair, and cell death. Elucidating the molecular mechanisms underlying TNFSF12 function is essential for understanding its roles in health and disease and for developing targeted therapies for inflammatory and autoimmune disorders, as well as cancer.

UBQLN2, also known as Ubiquilin-2, is a protein involved in the ubiquitin-proteasome system (UPS), a crucial pathway for protein degradation within cells. It belongs to the ubiquilin family of proteins, which are characterized by containing ubiquitin-like (UBL) and ubiquitin-associated (UBA) domains that facilitate interactions with ubiquitinated proteins and proteasome components. One of the primary functions of UBQLN2 is its role in protein quality control and degradation. UBQLN2 acts as a shuttle factor, facilitating the delivery of ubiquitinated proteins to the proteasome for degradation. It binds to ubiquitinated proteins through its UBA domain and interacts with components of the proteasome, promoting the efficient degradation of misfolded or damaged proteins. Moreover, UBQLN2 is implicated in the regulation of protein aggregation and clearance, particularly in the context of neurodegenerative diseases. Mutations in the UBQLN2 gene have been associated with amyotrophic lateral sclerosis (ALS) and other neurodegenerative disorders characterized by the accumulation of protein aggregates, such as Alzheimer's disease and Parkinson's disease. Dysfunctional UBQLN2 may impair the clearance of misfolded proteins, leading to their aggregation and the formation of pathological inclusions in neurons. Furthermore, UBQLN2 is involved in various cellular processes, including transcriptional regulation, DNA repair, and cell signaling. It interacts with a diverse range of protein partners and is implicated in the regulation of protein-protein interactions and cellular responses to stress and environmental cues. In summary, UBQLN2 is a multifunctional protein involved in protein quality control, degradation, and cellular homeostasis. Dysregulation of UBQLN2 function has been implicated in neurodegenerative diseases and other disorders associated with protein aggregation, highlighting its importance in maintaining protein homeostasis and cellular function. Further research into the molecular mechanisms underlying UBQLN2 function may provide insights into its roles in health and disease and potential therapeutic strategies for associated conditions.

XDH, or Xanthine dehydrogenase, is an enzyme that plays a crucial role in purine metabolism, a pathway responsible for the synthesis and degradation of purine nucleotides such as adenine and guanine. XDH catalyzes the conversion of hypoxanthine to xanthine and xanthine to uric acid, the final product of purine degradation in humans. One of the primary functions of XDH is its involvement in the breakdown of purines to uric acid, a process essential for the elimination of excess purines from the body. Purines are derived from dietary sources and the breakdown of nucleic acids, and their metabolism is tightly regulated to maintain purine homeostasis. XDH helps to convert xanthine, an intermediate in purine catabolism, to uric acid, which is then excreted from the body via the kidneys. Moreover, XDH is a key enzyme in the generation of reactive oxygen species (ROS) and reactive nitrogen species (RNS) in cells. During the conversion of hypoxanthine and xanthine to uric acid, XDH generates superoxide radicals and hydrogen peroxide as byproducts. While ROS and RNS can serve as signaling molecules in cellular processes, excessive production can lead to oxidative stress and cellular damage. Furthermore, dysregulation of XDH activity or expression has been implicated in various human diseases, including gout and ischemia-reperfusion injury. Gout is characterized by the deposition of uric acid crystals in joints due to elevated levels of uric acid in the blood, often resulting from impaired XDH activity or increased purine intake. Ischemia-reperfusion injury occurs when tissues are deprived of oxygen (ischemia) and then reperfused, leading to oxidative damage mediated by XDH-generated ROS. In summary, XDH is a critical enzyme involved in purine metabolism, catalyzing the conversion of hypoxanthine and xanthine to uric acid. Understanding the regulation of XDH activity and its roles in health and disease is essential for elucidating purine metabolism pathways and developing therapies for purine-related disorders.

ABT1, also known as Activator of Basal Transcription 1, is a protein that plays a critical role in the regulation of gene expression by promoting the initiation of transcription. It is a component of the RNA polymerase I (Pol I) transcription machinery, which is responsible for transcribing ribosomal RNA (rRNA) genes to generate ribosomal RNA transcripts. One of the primary functions of ABT1 is its role as a transcription factor that binds to specific DNA sequences within the promoter regions of rRNA genes. By binding to these promoter sequences, ABT1 recruits other transcription factors and the RNA polymerase I complex to initiate transcription of rRNA genes. This process is essential for the production of ribosomal RNA, which is a fundamental component of ribosomes, the cellular machinery responsible for protein synthesis. Moreover, ABT1 is involved in the regulation of ribosomal RNA transcription in response to various cellular signals and environmental cues. It may interact with other proteins and regulatory factors to modulate the activity of RNA polymerase I and the rate of rRNA synthesis in cells. Additionally, ABT1 has been implicated in coordinating ribosome biogenesis with cell growth and proliferation, ensuring proper cellular function and homeostasis. Furthermore, dysregulation of ABT1 expression or activity has been associated with certain diseases and disorders, including cancer. Alterations in ABT1 levels or function may disrupt ribosomal RNA transcription and ribosome biogenesis, leading to aberrant protein synthesis and cell growth. Thus, ABT1 may serve as a potential target for therapeutic interventions aimed at modulating cellular proliferation and tumor growth in cancer. In summary, ABT1 is a transcription factor involved in the regulation of ribosomal RNA transcription and ribosome biogenesis. Its role in coordinating ribosomal RNA synthesis with cellular growth and proliferation underscores its importance in cellular physiology and its potential implications in disease pathogenesis, particularly in cancer. Further research on ABT1 and its regulatory mechanisms may provide insights into its roles in health and disease and its potential as a therapeutic target.

CYP19A1, also known as aromatase, is an enzyme that catalyzes the conversion of androgens (such as testosterone) into estrogens (such as estradiol). This process is crucial in the biosynthesis of estrogen, which plays essential roles in various physiological processes, including sexual development, reproduction, bone metabolism, and cardiovascular health. One of the primary functions of CYP19A1 is its role in the synthesis of estrogen from androgens. It is expressed in various tissues, including the ovaries, testes, placenta, adipose tissue, and brain. In females, CYP19A1 is primarily responsible for estrogen production in the ovaries, where it converts androgens produced by the adrenal glands into estrogens. In males, CYP19A1 is expressed in the testes and converts androgens into estrogens, contributing to local estrogen synthesis. Moreover, CYP19A1 expression and activity are regulated by various factors, including hormonal signals, growth factors, and environmental factors. Hormonal regulation of CYP19A1 is particularly important in the menstrual cycle, pregnancy, and menopause, where fluctuations in estrogen levels play key roles in reproductive physiology and health. Furthermore, dysregulation of CYP19A1 expression or activity has been implicated in various human diseases and conditions. Abnormalities in estrogen synthesis due to mutations in the CYP19A1 gene or alterations in its regulation have been associated with disorders of sexual development, infertility, hormone-dependent cancers (such as breast and prostate cancer), and osteoporosis. In summary, CYP19A1 is a critical enzyme involved in estrogen biosynthesis, catalyzing the conversion of androgens into estrogens. Understanding the regulation and function of CYP19A1 is essential for elucidating the role of estrogen in health and disease and for developing targeted therapies for estrogen-related disorders.

DGKB (Diacylglycerol Kinase Beta): DGKB is an enzyme that converts diacylglycerol into phosphatidic acid, playing a critical role in lipid signaling pathways. It's involved in various cellular processes, including insulin sensitivity, and neurotransmitter signaling. Dysregulation of DGKB has been associated with metabolic disorders and is of interest in the study of diseases like diabetes and obesity.

EIF4A1, also known as Eukaryotic Translation Initiation Factor 4A1, is a highly conserved RNA helicase enzyme involved in the initiation of translation, a fundamental process in protein synthesis. It is a member of the DEAD-box RNA helicase family and plays a crucial role in unwinding secondary structures within mRNA molecules, enabling ribosomes to access the initiation codon and begin protein synthesis. One of the primary functions of EIF4A1 is its role in the assembly of the eukaryotic translation initiation complex. In conjunction with other eukaryotic initiation factors, EIF4A1 binds to the 5' untranslated region (UTR) of mRNA and scans along the mRNA molecule until it encounters the initiation codon. During this process, EIF4A1 utilizes ATP hydrolysis to unwind RNA secondary structures, facilitating the recruitment of the small ribosomal subunit and the initiation of translation. Moreover, EIF4A1 is involved in the regulation of gene expression and protein synthesis in response to various cellular signals and environmental cues. It interacts with regulatory proteins and signaling pathways that modulate translation initiation, thereby controlling the rate and efficiency of protein synthesis in cells. Dysregulation of EIF4A1 activity or expression has been implicated in various diseases, including cancer, where aberrant translation initiation contributes to tumor growth, metastasis, and drug resistance. Furthermore, EIF4A1 has been identified as a potential therapeutic target for the development of anticancer therapies. Inhibition of EIF4A1 activity or expression has been shown to suppress tumor cell proliferation and induce apoptosis in preclinical studies, highlighting its importance as a target for cancer treatment. In summary, EIF4A1 is a critical component of the eukaryotic translation initiation machinery, playing a central role in the unwinding of mRNA secondary structures and the initiation of protein synthesis. Elucidating the molecular mechanisms underlying EIF4A1 function is essential for understanding its roles in normal cellular physiology and disease pathology, and for developing targeted therapies for conditions associated with dysregulated translation initiation.

ESR1, also known as Estrogen Receptor Alpha, is a protein that belongs to the nuclear hormone receptor family and acts as a transcription factor. It plays a pivotal role in mediating the effects of estrogen, a steroid hormone, in various tissues throughout the body. One of the primary functions of ESR1 is its role in regulating gene expression in response to estrogen binding. In the absence of estrogen, ESR1 resides in the cytoplasm in an inactive state, bound to heat shock proteins. Upon binding of estrogen, ESR1 undergoes a conformational change, dissociates from the heat shock proteins, and translocates to the nucleus. In the nucleus, ESR1 binds to specific DNA sequences known as estrogen response elements (EREs) within the regulatory regions of target genes, thereby modulating their transcription. Moreover, ESR1 is involved in regulating numerous physiological processes, including but not limited to, reproductive development, bone metabolism, cardiovascular function, and cognitive function. In the reproductive system, ESR1 plays a central role in the development and maintenance of female secondary sexual characteristics, regulation of the menstrual cycle, and maintenance of pregnancy. Additionally, ESR1 is essential for the regulation of bone density and strength, with estrogen signaling through ESR1 protecting against osteoporosis and bone fractures. Furthermore, dysregulation of ESR1 signaling has been implicated in various diseases, particularly hormone-related cancers such as breast cancer. In breast cancer, aberrant ESR1 signaling can drive tumor growth and progression. Therapeutic strategies targeting ESR1, such as selective estrogen receptor modulators (SERMs) or estrogen receptor downregulators (ERDs), are commonly used in the treatment of estrogen receptor-positive breast cancer to block ESR1 activity or reduce its expression. In summary, ESR1 is a key regulator of estrogen signaling and gene expression, with diverse roles in multiple physiological processes and disease states. Understanding the molecular mechanisms underlying ESR1 function is essential for elucidating its roles in health and disease and for developing targeted therapies for conditions associated with dysregulated estrogen signaling, particularly hormone-related cancers.

FAM9A, or Family with Sequence Similarity 9 Member A, is a protein-coding gene that belongs to a family of genes with sequence similarity. While specific functions of FAM9A are still under investigation and not extensively characterized, it is known to be expressed in various tissues, including the brain, testis, and ovaries, suggesting potential roles in cellular processes in these organs. The designation "FAM" typically denotes a gene family whose members share sequence similarity but may have diverse functions. Often, genes within the FAM family are involved in various cellular processes, such as cell signaling, transcriptional regulation, or protein-protein interactions. Although the exact function of FAM9A remains to be fully elucidated, understanding its expression patterns and potential interactions with other cellular components may provide insights into its biological roles. Further experimental studies are required to uncover the specific functions of FAM9A and its contributions to cellular physiology and pathology. In summary, FAM9A is a gene within a family of genes with sequence similarity, and its precise function is yet to be determined. Further research is needed to elucidate its biological roles and significance in cellular processes.

FKBP4, also known as FK506-binding protein 4 or FKBP52, is a member of the FK506-binding protein (FKBP) family, which are peptidyl-prolyl cis-trans isomerases (PPIases) that function as molecular chaperones. FKBP4 is primarily found in the cytoplasm and nucleus of cells and is involved in regulating protein folding, trafficking, and signal transduction. One of the primary functions of FKBP4 is its role as a co-chaperone for steroid hormone receptors, including the glucocorticoid receptor (GR) and androgen receptor (AR). FKBP4 interacts with these receptors in the cytoplasm, facilitating their proper folding and assembly into functional complexes with heat shock proteins (HSPs). Upon ligand binding, FKBP4 dissociates from the receptor, allowing it to translocate to the nucleus and regulate gene transcription. Moreover, FKBP4 is implicated in the regulation of various cellular processes, including cell growth, differentiation, and apoptosis. It interacts with a diverse range of protein partners, including kinases, phosphatases, and transcription factors, influencing their activity and function. FKBP4 has been shown to modulate signaling pathways involved in cell survival, stress response, and immune regulation. Furthermore, dysregulation of FKBP4 expression or activity has been associated with certain human diseases, including cancer, neurodegenerative disorders, and metabolic syndrome. Altered FKBP4 levels have been observed in tumor tissues, where it may contribute to tumor progression, metastasis, and resistance to therapy. Additionally, FKBP4 polymorphisms have been linked to susceptibility to neurodegenerative diseases and metabolic disorders. In summary, FKBP4 is a multifunctional protein involved in protein folding, chaperone activity, and signal transduction, with implications for diverse physiological processes and disease states. Elucidating the molecular mechanisms underlying FKBP4 function is crucial for understanding its roles in health and disease and for developing targeted therapies for associated disorders.

GOLT1A, also known as Golgi transport 1A protein, is a member of the Golgi transport family involved in the regulation of vesicular trafficking within cells, particularly in the context of the Golgi apparatus. The Golgi apparatus is a vital organelle responsible for processing, sorting, and modifying proteins and lipids synthesized in the endoplasmic reticulum (ER) before they are transported to their final destinations. While specific details about GOLT1A are limited, proteins within the Golgi transport family are often involved in mediating the movement of cargo vesicles between different compartments of the Golgi apparatus and between the Golgi apparatus and other cellular organelles. This process is essential for maintaining the structural and functional integrity of the Golgi apparatus and for regulating the secretion of proteins and lipids to the extracellular space or other cellular compartments. Moreover, Golgi transport proteins like GOLT1A may participate in the sorting and packaging of cargo molecules into transport vesicles, as well as in the fusion of vesicles with target membranes. By coordinating these processes, Golgi transport proteins contribute to the proper localization and secretion of proteins and lipids, which are crucial for various cellular functions, including cell signaling, cell adhesion, and immune response. Furthermore, dysregulation of Golgi transport proteins, including GOLT1A, has been implicated in various human diseases, such as neurodegenerative disorders, cancer, and genetic syndromes affecting Golgi function. Dysfunction of vesicular trafficking processes can disrupt cellular homeostasis, impair protein secretion, and contribute to disease pathogenesis. In summary, GOLT1A is a member of the Golgi transport protein family involved in regulating vesicular trafficking within cells, particularly within the Golgi apparatus. Further research is needed to elucidate the specific roles of GOLT1A and its contribution to cellular physiology and disease processes.

GPR139, also known as G protein-coupled receptor 139, is a protein that belongs to the G protein-coupled receptor (GPCR) superfamily. It is primarily expressed in the central nervous system, particularly in regions associated with the regulation of neurotransmitter systems and neuronal activity. Although the specific functions of GPR139 are still being elucidated, it is believed to play a role in modulating neurotransmission, particularly in the regulation of dopamine and glutamate signaling. Studies have suggested that GPR139 may function as an inhibitory receptor, as its activation leads to decreased cAMP (cyclic adenosine monophosphate) levels and reduced neuronal excitability. Moreover, GPR139 has been implicated in the regulation of various physiological processes, including appetite and metabolism. Preclinical studies have shown that GPR139 agonists can decrease food intake and body weight in animal models, suggesting a potential role in the control of energy balance and food intake regulation. Furthermore, GPR139 has gained attention as a potential therapeutic target for the treatment of neuropsychiatric and metabolic disorders. Dysregulation of GPR139 signaling has been associated with conditions such as schizophrenia, depression, and obesity, highlighting its importance in maintaining normal physiological function. In summary, GPR139 is a G protein-coupled receptor expressed in the central nervous system, involved in modulating neurotransmission, appetite, and metabolism. Further research into the signaling pathways and physiological functions of GPR139 may provide insights into its role in health and disease and its potential as a therapeutic target for various disorders.

JHY (Jellybean Homologue Y): JHY, analogous to its namesake in the Matrix Metallopeptidase family, is a pivotal player in cellular processes, albeit in a distinct context. This protein is fundamental in orchestrating intracellular signaling cascades that regulate crucial aspects of cell behavior and function. Through its involvement in signal transduction pathways, JHY influences diverse physiological phenomena, ranging from cell proliferation and differentiation to cell migration and survival. The intricate control exerted by JHY on cellular activities underscores its significance in maintaining proper cellular homeostasis. However, aberrations in JHY expression or function have been implicated in various pathological conditions, including cancer progression, neurodegenerative disorders, and immune dysregulation. Unraveling the intricate mechanisms governing JHY's role in cellular signaling may offer promising avenues for therapeutic intervention, particularly in diseases characterized by dysregulated cellular behaviors.

KCNIP4, also known as Kv channel-interacting protein 4, belongs to the family of Kv channel-interacting proteins (KCNIPs), also known as Kv channel regulatory proteins (KCHIPs). These proteins are associated with voltage-gated potassium (Kv) channels and modulate their function. One of the primary functions of KCNIP4 is its role in regulating the properties of Kv channels. Kv channels are integral membrane proteins that play a crucial role in controlling the electrical activity of cells by regulating the flow of potassium ions across cell membranes. KCNIP4 interacts with Kv channels and modulates their gating kinetics, voltage dependence, and trafficking to the cell membrane, thereby influencing the duration and amplitude of action potentials and the excitability of cells. Moreover, KCNIP4 is expressed in various tissues, including the brain, heart, and skeletal muscle, where Kv channels play essential roles in regulating neuronal excitability, cardiac repolarization, and muscle contraction. In the brain, KCNIP4 is particularly abundant in regions involved in learning and memory, suggesting its involvement in neuronal plasticity and cognitive functions. Furthermore, dysregulation of KCNIP4 expression or function has been implicated in various neurological and cardiovascular disorders. Altered Kv channel activity due to dysregulated KCNIP4 levels or mutations in the KCNIP4 gene can disrupt neuronal excitability and synaptic transmission, contributing to conditions such as epilepsy, schizophrenia, and Alzheimer's disease. Additionally, abnormalities in cardiac Kv channel function associated with KCNIP4 dysfunction may lead to arrhythmias and sudden cardiac death. In summary, KCNIP4 is a regulatory protein that modulates the function of Kv channels, influencing the electrical excitability of cells in various tissues. Elucidating the molecular mechanisms underlying KCNIP4-Kv channel interactions is crucial for understanding their roles in normal physiology and disease pathogenesis, and for developing targeted therapies for disorders associated with aberrant Kv channel function.

LIN28B is a highly conserved RNA-binding protein that plays diverse and crucial roles in regulating various cellular processes, including stem cell maintenance, development, metabolism, and oncogenesis. It belongs to the LIN28 family, which also includes LIN28A. One of the primary functions of LIN28B is its involvement in post-transcriptional regulation of gene expression through binding to specific mRNA targets. LIN28B primarily acts as a translational repressor, inhibiting the translation of its target mRNAs by blocking the recruitment of ribosomes. Additionally, LIN28B can also influence mRNA stability and processing through interactions with RNA-binding proteins and microRNAs (miRNAs). Moreover, LIN28B is a key regulator of stem cell pluripotency and differentiation. It represses the biogenesis of let-7 miRNAs, which are crucial regulators of cellular differentiation and development, thereby promoting the maintenance of pluripotent stem cells. In addition to its role in stem cells, LIN28B is also involved in tissue development and regeneration, as well as metabolic processes such as glucose metabolism and insulin sensitivity. Furthermore, dysregulation of LIN28B expression or activity has been implicated in various human diseases, particularly cancer. LIN28B is frequently overexpressed in various cancer types and is associated with tumor progression, metastasis, and chemoresistance. It promotes tumorigenesis by inhibiting let-7 miRNA activity, leading to derepression of oncogenic pathways and enhanced cell proliferation, survival, and invasion. In summary, LIN28B is a multifunctional RNA-binding protein involved in regulating diverse cellular processes, including stem cell maintenance, development, metabolism, and oncogenesis. Elucidating the molecular mechanisms underlying LIN28B function is crucial for understanding its roles in normal physiology and disease pathogenesis, and for developing targeted therapies for diseases associated with LIN28B dysregulation, particularly cancer.

MANBA (Mannosidase Beta): MANBA encodes a lysosomal enzyme that is involved in the degradation of N-linked glycoproteins. It catalyzes the hydrolysis of the beta-linked mannose residues in glycoproteins, playing a crucial role in the glycoprotein degradation pathway. Deficiencies in MANBA activity can lead to lysosomal storage disorders, characterized by the accumulation of undegraded glycoproteins, affecting cellular function and leading to clinical manifestations.

MME, also known as Membrane Metallo-Endopeptidase, or neprilysin, is a zinc-dependent metalloprotease enzyme that plays a critical role in the regulation of peptide signaling molecules, particularly in the degradation of biologically active peptides. It is primarily found anchored to the cell membrane of various cell types, including neurons, endothelial cells, and immune cells. One of the primary functions of MME is its role in the degradation of peptides involved in the regulation of blood pressure, such as bradykinin and atrial natriuretic peptide (ANP). MME cleaves these peptides into inactive fragments, thereby regulating their physiological effects and maintaining blood pressure homeostasis. Additionally, MME is involved in the degradation of other peptides, including enkephalins, substance P, and amyloid beta (Aβ), which are implicated in pain perception, inflammation, and Alzheimer's disease, respectively. Moreover, MME is involved in modulating the activity of peptide hormones and neurotransmitters in the central nervous system. It participates in the metabolism of neuropeptides and regulates the levels of peptides involved in neurotransmission, synaptic plasticity, and neuronal survival. Dysregulation of MME activity or expression has been associated with various neurological disorders, including Alzheimer's disease, Parkinson's disease, and epilepsy. Furthermore, MME has been identified as a potential therapeutic target for the treatment of cardiovascular diseases, neurodegenerative disorders, and pain management. Strategies aimed at enhancing MME activity or expression, or inhibiting the degradation of specific peptides by MME, have shown promise in preclinical studies for modulating peptide signaling pathways and alleviating disease symptoms. In summary, MME is a multifunctional enzyme involved in the regulation of peptide signaling molecules, with roles in blood pressure regulation, neurotransmission, and the pathophysiology of various diseases. Understanding the molecular mechanisms underlying MME function is essential for elucidating its roles in health and disease and for developing targeted therapeutic approaches for conditions associated with dysregulated peptide metabolism.

ORM1, also known as Orosomucoid 1 or Alpha-1-acid glycoprotein 1, is a glycoprotein primarily synthesized in the liver and secreted into the bloodstream. It belongs to the acute phase reactant proteins, which are produced in response to inflammation, infection, or tissue injury. One of the primary functions of ORM1 is its role in modulating the immune response and inflammation. During acute-phase reactions, the production of ORM1 is upregulated by pro-inflammatory cytokines, such as interleukin-6 (IL-6) and tumor necrosis factor-alpha (TNF-α). ORM1 plays a regulatory role in inflammation by binding to various substances, including drugs, hormones, and lipids, and modulating their distribution and activity. Additionally, ORM1 can interact with immune cells and cytokines, influencing their function and the overall inflammatory response. Moreover, ORM1 is involved in transporting and delivering hydrophobic molecules, such as drugs and hormones, in the bloodstream. It binds to these molecules, thereby increasing their solubility and stability in the aqueous environment of the blood. This function of ORM1 is crucial for regulating the pharmacokinetics and pharmacodynamics of drugs, as well as the distribution and bioavailability of hormones and other bioactive molecules. Furthermore, ORM1 levels can serve as biomarkers for various disease states and conditions. Changes in ORM1 concentration in the bloodstream are associated with inflammatory diseases, infections, cancer, and certain metabolic disorders. Monitoring ORM1 levels can provide valuable information about the severity of inflammation or disease activity and may aid in diagnosis, prognosis, and treatment monitoring. In summary, ORM1 is an acute-phase reactant glycoprotein involved in modulating the immune response, inflammation, and the transport of hydrophobic molecules in the bloodstream. Understanding the roles of ORM1 in health and disease is essential for elucidating its diagnostic and therapeutic potential and for developing strategies to modulate its activity in various pathological conditions.

PPP2R3C (Protein Phosphatase 2 Regulatory Subunit B''Gamma): This gene encodes a regulatory subunit of the protein phosphatase 2 (PP2A) complex, which is a serine/threonine phosphatase involved in the control of cell growth and division. PPP2R3C modulates the activity of PP2A, influencing various signaling pathways related to cellular stress responses, DNA damage repair, and apoptosis. Its role is critical in maintaining cellular homeostasis and in the regulation of cell cycle checkpoints.

SRD5A2, or 5-alpha-reductase 2, is an enzyme that catalyzes the conversion of testosterone into dihydrotestosterone (DHT), a more potent androgen. It is primarily expressed in androgen-sensitive tissues, including the prostate gland, hair follicles, and external genitalia. One of the primary functions of SRD5A2 is its role in androgen metabolism and the regulation of androgen signaling. Testosterone, synthesized primarily in the testes, adrenal glands, and ovaries, serves as the precursor for DHT. SRD5A2 converts testosterone into DHT by reducing the 4,5 double bond of the A ring, which increases the affinity of the androgen receptor (AR) for DHT. DHT binding to AR leads to the activation of androgen-responsive genes, mediating the physiological effects of androgens in target tissues. Moreover, SRD5A2-mediated conversion of testosterone to DHT is crucial for the development and maintenance of male secondary sexual characteristics, including facial and body hair growth, deepening of the voice, and the development of the prostate gland and external genitalia. Additionally, DHT is implicated in the regulation of sebum production in the skin and the growth of scalp hair follicles. Furthermore, dysregulation of SRD5A2 activity or expression has been associated with various androgen-related disorders. Mutations in the SRD5A2 gene can lead to 5-alpha-reductase deficiency, a condition characterized by impaired DHT production and masculinization in individuals with male chromosomes (XY) but ambiguous genitalia or female external genitalia. Additionally, aberrant DHT signaling has been implicated in conditions such as benign prostatic hyperplasia (BPH), androgenetic alopecia (male-pattern baldness), and prostate cancer. In summary, SRD5A2 is a key enzyme involved in androgen metabolism, catalyzing the conversion of testosterone to DHT. Understanding the regulation and function of SRD5A2 is essential for elucidating its roles in normal physiology and disease pathogenesis and for developing targeted therapies for androgen-related disorders.

AKR1E2 (Aldo-Keto Reductase Family 1 Member E2): AKR1E2 is part of the aldo-keto reductase family, which is involved in the detoxification of aldehydes and ketones. The specific function of AKR1E2 is not fully understood, but members of this family play roles in metabolism and the response to oxidative stress. Research into AKR1E2 could provide insights into metabolic disorders and cellular responses to environmental stressors.

ARL14EP (ADP-ribosylation factor-like protein 14E): ARL14EP, a member of the ADP-ribosylation factor-like (ARL) protein family, serves as a crucial regulator in various cellular processes, primarily by modulating intracellular vesicular trafficking and membrane dynamics. This protein plays a pivotal role in directing the movement of vesicles within cells, thus influencing processes such as protein secretion, endocytosis, and organelle organization. Additionally, ARL14EP is implicated in cell signaling pathways and cytoskeletal regulation, further underscoring its significance in cellular function. Dysregulation of ARL14EP expression or activity has been associated with several pathological conditions, including neurodegenerative disorders, cancer progression, and metabolic diseases. Understanding the precise mechanisms underlying ARL14EP function may offer insights into disease pathogenesis and could potentially lead to the development of therapeutic interventions targeting aberrant vesicular trafficking and cellular signaling pathways.

ASB13, also known as Ankyrin repeat and SOCS box protein 13, is a member of the ASB family of proteins, which are characterized by the presence of ankyrin repeat domains and a SOCS box domain. These proteins are involved in the regulation of protein degradation and signal transduction pathways within cells. One of the primary functions of ASB13 is its role as an E3 ubiquitin ligase, facilitating the ubiquitination and subsequent degradation of specific protein targets. The SOCS box domain of ASB13 interacts with components of the ubiquitin-proteasome system, including E2 ubiquitin-conjugating enzymes and Cullin-RING ligase (CRL) complexes, allowing ASB13 to catalyze the transfer of ubiquitin molecules onto target proteins. This process targets the tagged proteins for degradation by the proteasome, thereby regulating their abundance and activity within the cell. Moreover, ASB13 has been implicated in the regulation of various cellular processes and signaling pathways. It may interact with specific protein substrates involved in cell cycle progression, apoptosis, cell migration, and differentiation, thereby influencing cell behavior and physiology. Additionally, ASB13-mediated ubiquitination and degradation of certain signaling molecules may modulate the activity of signaling pathways implicated in development, immunity, and disease. Furthermore, ASB13 expression patterns and functions may vary across different tissues and cell types, reflecting its diverse roles in cellular homeostasis and function. Dysregulation of ASB13 expression or activity has been associated with various pathological conditions, including cancer, cardiovascular disease, and neurological disorders, highlighting its potential significance in disease pathogenesis. In summary, ASB13 is an E3 ubiquitin ligase protein involved in the regulation of protein degradation and signal transduction pathways. Its diverse functions and interactions with specific protein targets make it a crucial regulator of cellular processes and physiology. Further elucidation of ASB13's molecular mechanisms and roles in health and disease may provide insights into its potential as a therapeutic target in various pathological conditions.

CACNB2, also known as Calcium Channel Voltage-Dependent Beta 2 Subunit, is a protein that plays a crucial role in the functioning of voltage-gated calcium channels (VGCCs). These channels are responsible for regulating calcium influx into cells in response to changes in membrane potential, thereby controlling various physiological processes such as neurotransmitter release, muscle contraction, and gene expression. One of the primary functions of CACNB2 is its role as a regulatory subunit of VGCCs. It interacts with the pore-forming alpha subunits of VGCCs, modulating their biophysical properties, including voltage sensitivity, kinetics of channel opening and closing, and calcium conductance. CACNB2 helps regulate the activity and localization of VGCCs in different cell types and tissues, thereby fine-tuning calcium signaling and cellular responses. Moreover, CACNB2 is involved in mediating synaptic transmission and plasticity in neurons. It regulates calcium influx into presynaptic terminals, influencing neurotransmitter release and synaptic strength. Additionally, CACNB2 is implicated in postsynaptic signaling cascades, where it modulates calcium entry into dendritic spines and contributes to synaptic plasticity processes such as long-term potentiation (LTP) and long-term depression (LTD), which are fundamental for learning and memory. Furthermore, genetic variations or mutations in the CACNB2 gene have been associated with various neurological and neuropsychiatric disorders, including epilepsy, autism spectrum disorders, and schizophrenia. Dysregulation of calcium signaling mediated by CACNB2 dysfunction can disrupt neuronal excitability, synaptic transmission, and network activity, contributing to the pathophysiology of these disorders. In summary, CACNB2 is a critical regulatory subunit of VGCCs, involved in modulating calcium influx and signaling in neurons and other cell types. Understanding the molecular mechanisms underlying CACNB2 function is essential for elucidating its roles in normal physiology and disease pathogenesis and for developing targeted therapies for disorders associated with dysregulated calcium signaling.

CYP19A1, also known as aromatase, is an enzyme that catalyzes the conversion of androgens (such as testosterone) into estrogens (such as estradiol). This process is crucial in the biosynthesis of estrogen, which plays essential roles in various physiological processes, including sexual development, reproduction, bone metabolism, and cardiovascular health. One of the primary functions of CYP19A1 is its role in the synthesis of estrogen from androgens. It is expressed in various tissues, including the ovaries, testes, placenta, adipose tissue, and brain. In females, CYP19A1 is primarily responsible for estrogen production in the ovaries, where it converts androgens produced by the adrenal glands into estrogens. In males, CYP19A1 is expressed in the testes and converts androgens into estrogens, contributing to local estrogen synthesis. Moreover, CYP19A1 expression and activity are regulated by various factors, including hormonal signals, growth factors, and environmental factors. Hormonal regulation of CYP19A1 is particularly important in the menstrual cycle, pregnancy, and menopause, where fluctuations in estrogen levels play key roles in reproductive physiology and health. Furthermore, dysregulation of CYP19A1 expression or activity has been implicated in various human diseases and conditions. Abnormalities in estrogen synthesis due to mutations in the CYP19A1 gene or alterations in its regulation have been associated with disorders of sexual development, infertility, hormone-dependent cancers (such as breast and prostate cancer), and osteoporosis. In summary, CYP19A1 is a critical enzyme involved in estrogen biosynthesis, catalyzing the conversion of androgens into estrogens. Understanding the regulation and function of CYP19A1 is essential for elucidating the role of estrogen in health and disease and for developing targeted therapies for estrogen-related disorders.

ECHDC3, also known as Enoyl-CoA Hydratase Domain-Containing Protein 3, is an enzyme involved in fatty acid metabolism. Specifically, ECHDC3 contains a domain characteristic of enoyl-CoA hydratases, which catalyze the hydration of enoyl-CoA intermediates in the β-oxidation pathway of fatty acid degradation. One of the primary functions of ECHDC3 is its role in fatty acid β-oxidation, a metabolic process that occurs in the mitochondria and peroxisomes and is essential for energy production. During β-oxidation, fatty acids are broken down into acetyl-CoA molecules, which can enter the citric acid cycle to generate ATP, the primary energy currency of the cell. ECHDC3 participates in the hydration step of β-oxidation, converting enoyl-CoA intermediates into β-hydroxyacyl-CoA compounds, which can be further processed to produce energy. Moreover, ECHDC3 may play additional roles in cellular metabolism and lipid homeostasis beyond fatty acid β-oxidation. It may participate in the metabolism of other lipid species or interact with proteins involved in lipid synthesis, storage, or transport. Furthermore, dysregulation of ECHDC3 expression or activity has been associated with certain metabolic disorders, including obesity, insulin resistance, and dyslipidemia, although the specific mechanisms underlying these associations remain to be elucidated. In summary, ECHDC3 is an enzyme involved in fatty acid metabolism, particularly in the β-oxidation pathway. Its role in catalyzing the hydration of enoyl-CoA intermediates contributes to energy production and lipid homeostasis in cells. Further research on ECHDC3 and its functions may provide insights into its roles in health and disease, as well as its potential as a therapeutic target in metabolic disorders.

FSHR, or Follicle-Stimulating Hormone Receptor, is a G protein-coupled receptor (GPCR) primarily expressed on the surface of ovarian granulosa cells in females and Sertoli cells in males. It plays a crucial role in the regulation of reproductive function by mediating the effects of follicle-stimulating hormone (FSH), a glycoprotein hormone secreted by the anterior pituitary gland. One of the primary functions of FSHR is its role in folliculogenesis, the process by which ovarian follicles develop and mature. In females, FSH binds to FSHR on granulosa cells within ovarian follicles, leading to a cascade of intracellular signaling events that promote follicle growth, proliferation, and differentiation. FSHR activation stimulates granulosa cell proliferation, aromatase expression, and estradiol production, which are essential for follicle maturation and ovulation. Moreover, FSHR is involved in spermatogenesis, the process of sperm production, in males. FSH binds to FSHR on Sertoli cells within the seminiferous tubules of the testes, stimulating Sertoli cell proliferation and function. FSHR activation in Sertoli cells promotes the production of factors necessary for spermatogenesis, including androgen-binding protein (ABP) and inhibin, which regulate the development and maturation of sperm cells. Furthermore, dysregulation of FSHR signaling has been implicated in various reproductive disorders and conditions. Mutations in the FSHR gene can lead to abnormal FSHR function and result in conditions such as primary ovarian insufficiency (POI) in females or impaired spermatogenesis and infertility in males. Additionally, FSHR expression and activity are regulated by various factors, including gonadal steroids, gonadotropins, and intraovarian and intratesticular factors, which influence reproductive function and fertility. In summary, FSHR is a critical receptor involved in the regulation of reproductive function, mediating the effects of FSH in ovarian follicles and testicular Sertoli cells. Understanding the molecular mechanisms underlying FSHR signaling is essential for elucidating its roles in fertility and reproduction and for developing targeted therapies for reproductive disorders and infertility.

GAD2 (Glutamate Decarboxylase 2): GAD2 is crucial for the synthesis of gamma-aminobutyric acid (GABA), an important neurotransmitter in the brain. It plays a role in the regulation of neuronal excitability and has been implicated in disorders such as epilepsy and anxiety disorders.

GATA3 (GATA Binding Protein 3): GATA3 is a transcription factor that plays a key role in the development and differentiation of various cell types, including T cells and mammary gland cells. It is essential for immune responses and breast tissue development. Mutations in GATA3 can lead to immunodeficiency and breast cancer.

KLF6, or Krüppel-Like Factor 6, is a transcription factor that belongs to the Krüppel-like family of zinc finger proteins. It plays crucial roles in the regulation of gene expression, cell proliferation, differentiation, apoptosis, and various biological processes involved in development, tissue homeostasis, and disease pathogenesis. One of the primary functions of KLF6 is its role as a transcriptional regulator. It binds to specific DNA sequences within the regulatory regions of target genes, known as Krüppel-like factor binding sites, thereby modulating their transcriptional activity. KLF6 can act as both a transcriptional activator and a repressor, depending on the cellular context and the specific target genes involved. Through its transcriptional activity, KLF6 regulates the expression of genes involved in diverse cellular processes, including cell cycle control, apoptosis, angiogenesis, and tissue remodeling. Moreover, KLF6 is implicated in various physiological and pathological processes. It plays critical roles in the development and differentiation of tissues and organs during embryogenesis. In adults, KLF6 is involved in tissue homeostasis, wound healing, and response to cellular stress. Dysregulation of KLF6 expression or activity has been associated with various human diseases, including cancer, cardiovascular disease, liver disease, and metabolic disorders. Furthermore, KLF6 has emerged as a potential tumor suppressor in several types of cancer. It regulates the expression of genes involved in cell cycle progression, apoptosis, and metastasis, thereby inhibiting tumor growth and progression. Loss of KLF6 expression or function due to genetic alterations, epigenetic modifications, or dysregulated signaling pathways is observed in many cancers and is associated with aggressive tumor behavior, poor prognosis, and resistance to therapy. In summary, KLF6 is a versatile transcription factor with diverse roles in gene regulation and cellular physiology. Understanding the molecular mechanisms underlying KLF6 function is essential for elucidating its roles in normal development and disease pathogenesis and for developing targeted therapies for diseases associated with dysregulated KLF6 signaling, particularly cancer.

OR2B6 belongs to the olfactory receptor (OR) gene family, which is responsible for detecting and recognizing odor molecules in the environment. These receptors are located on the surface of olfactory sensory neurons in the olfactory epithelium of the nasal cavity. One of the primary functions of OR2B6, like other olfactory receptors, is its role in odor detection and olfactory signal transduction. OR2B6 specifically binds to certain odor molecules present in the surrounding air, triggering a signaling cascade within the olfactory sensory neuron. This cascade ultimately leads to the generation of electrical signals that are transmitted to the brain, where they are interpreted as specific odors. Moreover, OR2B6, along with other olfactory receptors, contributes to the incredible diversity of odor recognition abilities in humans. The human olfactory system is capable of distinguishing a vast array of different odors, each corresponding to specific combinations of odorant molecules and olfactory receptors. This ability to discern a wide range of odors is crucial for various physiological processes, including food detection, environmental sensing, and social interactions. Furthermore, variations in OR2B6 and other olfactory receptor genes can contribute to differences in odor perception among individuals. Genetic polymorphisms in these genes may affect the sensitivity or specificity of olfactory receptors, influencing an individual's ability to detect certain odors or perceive them differently from others. In summary, OR2B6 is an olfactory receptor gene involved in odor detection and olfactory signal transduction. Understanding the function and diversity of olfactory receptors like OR2B6 is essential for unraveling the complexities of human olfaction and its role in various physiological and behavioral processes.

PFKFB3, or 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 3, is an enzyme that plays a crucial role in cellular energy metabolism, particularly in glycolysis, the process by which glucose is metabolized to produce energy. PFKFB3 regulates the levels of fructose-2,6-bisphosphate (F2,6BP), a potent allosteric regulator of 6-phosphofructo-1-kinase (PFK-1), a key enzyme in glycolysis. One of the primary functions of PFKFB3 is its role in promoting glycolysis by synthesizing F2,6BP. F2,6BP allosterically activates PFK-1, which catalyzes the conversion of fructose-6-phosphate (F6P) to fructose-1,6-bisphosphate (F1,6BP), a critical regulatory step in glycolysis. By increasing F2,6BP levels, PFKFB3 stimulates PFK-1 activity, enhancing the flux of glucose through the glycolytic pathway and promoting ATP production. Moreover, PFKFB3 has been implicated in various cellular processes beyond glycolysis. It plays roles in cell proliferation, survival, and angiogenesis, processes that require high levels of energy and metabolites to support rapid growth and division. PFKFB3 expression is often upregulated in cancer cells and is associated with increased glycolytic metabolism, tumor growth, and resistance to apoptosis. Furthermore, PFKFB3 is a potential target for cancer therapy and metabolic diseases. Inhibition of PFKFB3 activity or expression can suppress glycolysis, impair cancer cell proliferation, and induce apoptosis in preclinical models. Additionally, targeting PFKFB3 may have therapeutic benefits in other pathological conditions characterized by dysregulated metabolism, such as diabetes and cardiovascular diseases. In summary, PFKFB3 is a key regulator of glycolysis and cellular metabolism, with important roles in energy production, cell proliferation, and disease pathogenesis. Understanding the molecular mechanisms underlying PFKFB3 function is essential for elucidating its roles in health and disease and for developing targeted therapies for conditions associated with dysregulated metabolism, particularly cancer and metabolic disorders.

UBE3A (Ubiquitin Protein Ligase E3A): UBE3A encodes an E3 ubiquitin ligase enzyme that plays a role in protein degradation via the ubiquitin-proteasome pathway. Mutations in UBE3A are associated with Angelman syndrome, a neurodevelopmental disorder characterized by intellectual disability and developmental delay.

UCN3, also known as Urocortin 3, is a peptide hormone belonging to the corticotropin-releasing factor (CRF) family. It is primarily expressed in the central nervous system, particularly in regions of the brain involved in stress response regulation, such as the hypothalamus, amygdala, and brainstem. One of the primary functions of UCN3 is its role in modulating the stress response and anxiety-related behaviors. Like other members of the CRF family, UCN3 acts as a neuromodulator, influencing the activity of neurons and circuits involved in the physiological and behavioral responses to stress. UCN3 binds to and activates specific receptors, including CRF receptor type 2 (CRF2), leading to downstream signaling cascades that regulate neurotransmitter release, neuronal excitability, and synaptic plasticity. Moreover, UCN3 is involved in the regulation of various physiological processes beyond the stress response. It plays roles in regulating appetite, energy balance, cardiovascular function, and gastrointestinal motility. UCN3 signaling is also implicated in modulating mood and affective states, with potential implications for mood disorders such as depression and anxiety disorders. Furthermore, dysregulation of UCN3 expression or signaling has been associated with various psychiatric and neurological disorders. Alterations in UCN3 levels or CRF2 receptor activity have been reported in conditions such as depression, anxiety disorders, post-traumatic stress disorder (PTSD), and irritable bowel syndrome (IBS), suggesting a potential role for UCN3 dysregulation in the pathophysiology of these disorders. In summary, UCN3 is a peptide hormone that plays crucial roles in modulating stress responses, anxiety-related behaviors, and various physiological processes. Further understanding of UCN3 signaling mechanisms and its interactions with other neurotransmitter systems may provide insights into its roles in health and disease, and may lead to the development of novel therapeutic strategies for stress-related and neuropsychiatric disorders.

ZNF438, also known as Zinc Finger Protein 438, is a member of the zinc finger protein family, which is characterized by the presence of zinc finger domains that mediate DNA binding and protein-protein interactions. These proteins are involved in various cellular processes, including transcriptional regulation, chromatin remodeling, and RNA processing. One of the primary functions of ZNF438 is its role as a transcription factor or regulator of gene expression. Through its zinc finger domains, ZNF438 binds to specific DNA sequences within the genome, thereby modulating the transcription of target genes. By interacting with other transcriptional regulators, chromatin-modifying enzymes, or transcriptional co-factors, ZNF438 can either activate or repress the expression of its target genes, depending on the cellular context and the specific target genes involved. Moreover, ZNF438 has been implicated in various biological processes and pathways. It may play roles in cell proliferation, differentiation, apoptosis, and development, as well as in the response to cellular stress or environmental stimuli. Dysregulation of ZNF438 expression or function has been associated with certain diseases or conditions, including cancer, developmental disorders, and neurological disorders, although the specific mechanisms underlying these associations remain to be elucidated. Furthermore, ZNF438 may participate in protein-protein interactions or protein complexes involved in other cellular processes beyond transcriptional regulation. It may interact with other proteins to form multiprotein complexes involved in chromatin remodeling, RNA processing, or protein degradation, thereby contributing to the regulation of additional cellular functions. In summary, ZNF438 is a zinc finger protein involved in transcriptional regulation and potentially other cellular processes. Further research is needed to elucidate the specific target genes and pathways regulated by ZNF438, as well as its roles in normal physiology and disease pathogenesis. Understanding the molecular mechanisms underlying ZNF438 function may provide insights into its biological significance and potential therapeutic applications.

PTER (Phosphotriesterase-related protein): Analogous to MMP15's involvement in extracellular matrix (ECM) remodeling, PTER plays a crucial role in cellular detoxification and metabolism regulation. As a member of the phosphotriesterase-related protein family, PTER is involved in the breakdown of various chemical compounds, including organophosphate pesticides and nerve agents. Its enzymatic activity contributes to the detoxification of these harmful substances, thereby protecting cells from chemical damage. Additionally, PTER has been implicated in cellular signaling pathways and metabolic processes, suggesting broader roles beyond detoxification. Dysregulation of PTER expression or activity can have detrimental effects, leading to increased susceptibility to chemical toxicity and metabolic disorders. Understanding the precise mechanisms underlying PTER-mediated detoxification and metabolic regulation may offer insights into disease pathogenesis and potential therapeutic strategies for chemical exposure-related disorders.

AKT3, also known as Protein Kinase B (PKB) gamma, is a serine/threonine protein kinase that plays a crucial role in various cellular processes, including cell survival, proliferation, metabolism, and growth. It is a member of the AKT family of kinases, which also includes AKT1 and AKT2. One of the primary functions of AKT3 is its role in the regulation of cell survival and apoptosis. AKT3 is activated in response to growth factors, cytokines, and other extracellular signals that stimulate cell growth and survival. Upon activation, AKT3 phosphorylates downstream targets involved in apoptotic regulation, such as BAD and caspase-9, leading to their inhibition and promoting cell survival. Moreover, AKT3 is involved in the regulation of cell proliferation and growth. It phosphorylates and activates proteins involved in cell cycle progression, such as cyclin-dependent kinase inhibitors (e.g., p21 and p27), leading to cell cycle progression and proliferation. Additionally, AKT3 promotes cell growth by activating the mammalian target of rapamycin (mTOR) pathway, which regulates protein synthesis and cell growth in response to nutrient availability and growth factors. Furthermore, AKT3 is implicated in various physiological processes and diseases. It plays roles in neuronal development, synaptic plasticity, and brain function, particularly during embryonic development and in the adult brain. Dysregulation of AKT3 signaling has been implicated in neurological disorders, including epilepsy, autism spectrum disorders, and neurodevelopmental disorders. Additionally, AKT3 is implicated in cancer progression and metastasis. Dysregulated AKT3 signaling is observed in various types of cancer, where it promotes cell survival, proliferation, and metastasis. AKT3 activation can occur through various mechanisms, including genetic alterations, oncogene activation, and dysregulated signaling pathways, making it an attractive target for cancer therapy. In summary, AKT3 is a critical regulator of cell survival, proliferation, and growth, with important roles in normal physiology and disease pathogenesis. Further understanding of AKT3 signaling mechanisms and its interactions with other cellular pathways may provide insights into its biological significance and therapeutic potential in various diseases, including cancer and neurological disorders.

ALX4 (ALX Homeobox 4): ALX4 is a transcription factor involved in skull and limb development. Mutations in this gene can lead to craniofacial malformations and skeletal abnormalities, highlighting its importance in bone development and morphogenesis.

BANK1, also known as B-cell scaffold protein with ankyrin repeats 1, is a protein predominantly expressed in B lymphocytes, a type of white blood cell crucial for adaptive immunity. BANK1 plays a significant role in modulating B-cell receptor (BCR) signaling, a pivotal process in the activation and differentiation of B cells. One of the primary functions of BANK1 is its involvement in BCR signaling pathway regulation. BANK1 acts as a scaffold protein, facilitating the assembly of signaling complexes upon BCR engagement. It interacts with various signaling molecules, including kinases, phosphatases, and adapter proteins, thereby modulating downstream signaling cascades. Through its scaffolding function, BANK1 regulates key cellular processes such as B-cell activation, proliferation, differentiation, and antibody production. Moreover, BANK1 has been implicated in the pathogenesis of autoimmune diseases, particularly systemic lupus erythematosus (SLE) and rheumatoid arthritis (RA). Genome-wide association studies (GWAS) have identified genetic variants in the BANK1 gene associated with increased susceptibility to autoimmune disorders. Dysregulated BANK1 signaling may contribute to aberrant B-cell activation, autoantibody production, and inflammation observed in these conditions. Furthermore, BANK1 is involved in other cellular processes beyond B-cell signaling. It has been reported to play roles in innate immunity, Toll-like receptor (TLR) signaling, and regulation of T-cell responses. Additionally, BANK1 expression is not limited to B cells; it is also found in other immune cell types and non-immune tissues, suggesting broader functions beyond its originally identified role in B cells. In summary, BANK1 is a critical regulator of B-cell signaling and function, with implications in both normal immune responses and autoimmune diseases. Further elucidation of BANK1's molecular mechanisms and interactions with other signaling pathways may provide insights into its roles in health and disease and could potentially lead to the development of novel therapeutic strategies for autoimmune disorders.

BRINP1, or BMP/retinoic acid-inducible neural-specific protein 1, is a member of the BRINP (BMP/retinoic acid-inducible neural-specific) family of proteins. It is predominantly expressed in the brain and has been implicated in various neuronal processes, including neurodevelopment, synaptic plasticity, and neuronal survival. One of the primary functions of BRINP1 is its involvement in neural development. It is induced by factors such as bone morphogenetic proteins (BMPs) and retinoic acid during early neural development, suggesting a role in patterning and differentiation of neural progenitor cells. BRINP1 expression is spatially and temporally regulated in the developing brain, suggesting its involvement in processes such as neurogenesis, neuronal migration, and axon guidance. Moreover, BRINP1 has been implicated in synaptic plasticity, the process by which synapses undergo activity-dependent changes in strength and connectivity. It is expressed in regions of the brain associated with synaptic plasticity, such as the hippocampus and cortex. BRINP1 expression levels have been shown to be altered in response to synaptic activity and neurotransmitter signaling, suggesting a role in synaptic function and plasticity. Furthermore, BRINP1 may play a role in neuronal survival and protection against neurodegeneration. It has been reported to have anti-apoptotic properties and may protect neurons from various insults, including oxidative stress and excitotoxicity. Dysregulation of BRINP1 expression or function has been implicated in neurodevelopmental disorders, such as autism spectrum disorders, as well as neurodegenerative diseases, including Alzheimer's disease and Parkinson's disease. In summary, BRINP1 is a neural-specific protein involved in various aspects of neuronal development, synaptic plasticity, and neuroprotection. Further elucidation of its molecular functions and interactions with other neuronal proteins may provide insights into its roles in normal brain function and its potential implications in neurological disorders.

CNTNAP2, also known as Contactin Associated Protein-Like 2, is a cell adhesion molecule that belongs to the neurexin superfamily. It plays a crucial role in the development and function of the nervous system, particularly in neuronal migration, axon guidance, synaptic formation, and signal transduction. One of the primary functions of CNTNAP2 is its role in neuronal migration and axon guidance during brain development. It is predominantly expressed in the developing nervous system, where it interacts with other cell adhesion molecules, extracellular matrix proteins, and signaling molecules to regulate neuronal migration and axonal pathfinding. Dysregulation of CNTNAP2 expression or function has been implicated in various neurodevelopmental disorders, including autism spectrum disorders (ASD), intellectual disabilities, epilepsy, and schizophrenia. Moreover, CNTNAP2 is involved in synaptic formation and function. It is localized to the pre- and postsynaptic regions of neurons, where it interacts with presynaptic neurexins and postsynaptic proteins, such as PSD-95 and gephyrin. Through its interactions with these proteins, CNTNAP2 plays a role in synapse development, maturation, and plasticity, influencing neurotransmitter release, synaptic strength, and connectivity within neural circuits. Furthermore, CNTNAP2 is implicated in language and cognitive development. Genetic variations or mutations in the CNTNAP2 gene have been associated with language-related traits, such as speech and language impairments, verbal fluency, and reading abilities. Dysfunction of CNTNAP2 signaling pathways may disrupt neural circuits involved in language processing and communication, contributing to language-related disorders such as specific language impairment (SLI) and developmental dyslexia. In summary, CNTNAP2 is a cell adhesion molecule that plays critical roles in neuronal development, synaptic function, and cognitive processes. Further understanding of CNTNAP2's molecular mechanisms and interactions with other proteins may provide insights into its roles in normal brain development and function and its contributions to neurodevelopmental and neuropsychiatric disorders.

MAF (MAF BZIP Transcription Factor): MAF encodes a transcription factor that is involved in the development and differentiation of various tissues, including the lens of the eye and pancreatic beta cells. It plays a role in regulating gene expression and cell fate determination. Mutations in MAF can lead to developmental abnormalities and diseases.

PAX5, also known as Paired Box 5, is a transcription factor that plays a crucial role in the regulation of B-cell development and differentiation. It belongs to the PAX family of transcription factors, characterized by the presence of a conserved paired box domain, which is involved in DNA binding and protein-protein interactions. One of the primary functions of PAX5 is its role in specifying B-cell lineage commitment during hematopoiesis, the process by which blood cells are formed. PAX5 is expressed in progenitor cells committed to the B-cell lineage and is essential for the development of B cells from hematopoietic stem cells. It regulates the expression of genes involved in B-cell fate determination, including those encoding immunoglobulin (Ig) genes, B-cell receptor components, and other key regulators of B-cell development. Moreover, PAX5 plays a critical role in maintaining the identity and function of mature B cells. It is required for the expression of genes associated with B-cell activation, proliferation, and antibody production. PAX5 regulates the transcriptional program that governs B-cell responses to antigen stimulation, ensuring proper immune responses against pathogens and foreign antigens. Furthermore, PAX5 has been implicated in the pathogenesis of B-cell malignancies, particularly B-cell acute lymphoblastic leukemia (B-ALL) and diffuse large B-cell lymphoma (DLBCL). Dysregulation of PAX5 expression or function, often due to chromosomal translocations, gene mutations, or altered signaling pathways, can lead to aberrant B-cell development, proliferation, and survival, contributing to the development of B-cell lymphomas. In summary, PAX5 is a critical transcription factor involved in the regulation of B-cell development, differentiation, and function. Its roles in B-cell lineage commitment, maintenance of B-cell identity, and contribution to B-cell malignancies highlight its significance in normal immune function and disease pathogenesis. Further understanding of PAX5's molecular mechanisms and interactions with other transcriptional regulators may provide insights into its roles in health and disease, as well as potential therapeutic strategies for B-cell-related disorders.

TRMT6, also known as tRNA methyltransferase 6 homolog, is an enzyme involved in the post-transcriptional modification of transfer RNA (tRNA). Specifically, TRMT6 belongs to the class I-like SAM (S-adenosylmethionine)-dependent methyltransferase superfamily and catalyzes the methylation of specific nucleotides within tRNA molecules. One of the primary functions of TRMT6 is its role in the modification of adenosine residues at the wobble position of certain tRNA molecules. This modification is crucial for ensuring accurate and efficient translation of mRNA into protein during the process of protein synthesis. Methylation at the wobble position of tRNA helps stabilize codon-anticodon interactions and contributes to the fidelity of translation by preventing errors such as frameshifts and misreading of the genetic code. Moreover, TRMT6-mediated tRNA modification has been implicated in various cellular processes, including protein synthesis, cell proliferation, and response to environmental stress. Proper tRNA modification is essential for maintaining cellular homeostasis and viability, as defects in tRNA modification pathways can lead to impaired protein synthesis, protein misfolding, and cellular dysfunction. Furthermore, dysregulation of TRMT6 expression or activity has been associated with certain human diseases and disorders. Mutations in genes encoding tRNA methyltransferases, including TRMT6, have been linked to neurodegenerative diseases such as amyotrophic lateral sclerosis (ALS) and intellectual disabilities, highlighting the importance of proper tRNA modification in neuronal function and health. In summary, TRMT6 is a tRNA methyltransferase enzyme involved in the post-transcriptional modification of tRNA molecules. Its role in catalyzing methylation at the wobble position of tRNA contributes to accurate and efficient protein synthesis and is essential for cellular function and viability. Further research on TRMT6 and its role in tRNA modification pathways may provide insights into its biological significance and potential implications in health and disease.

BRK1 (Breakpoint cluster region kinase 1): Similar to MMP15's pivotal role in extracellular matrix (ECM) remodeling, BRK1 is a crucial player in cellular signaling pathways that regulate cell proliferation, differentiation, and migration. As a member of the breakpoint cluster region kinase family, BRK1 modulates intracellular signaling cascades, influencing various physiological processes such as cell cycle progression, cytoskeletal organization, and cell adhesion. Additionally, BRK1 has been implicated in the regulation of immune responses and oncogenic signaling pathways, highlighting its significance in both normal physiological functions and disease pathogenesis. Dysregulation of BRK1 expression or activity has been associated with cancer progression, inflammatory disorders, and developmental abnormalities. Elucidating the precise mechanisms underlying BRK1-mediated signaling may provide valuable insights into disease mechanisms and therapeutic strategies targeting aberrant cellular signaling pathways.

EPDR1 (Epidermal growth factor receptor pathway substrate 15-related protein 1): Similar to MMP15's role in extracellular matrix (ECM) dynamics, EPDR1 is implicated in cellular signaling pathways that regulate various physiological processes, including cell proliferation, survival, and differentiation. As a member of the epidermal growth factor receptor (EGFR) pathway substrate family, EPDR1 interacts with key signaling molecules involved in growth factor signaling cascades, modulating downstream signaling events. This protein plays a critical role in mediating cellular responses to extracellular stimuli, such as growth factors and cytokines, thereby influencing cell fate decisions and tissue homeostasis. Dysregulation of EPDR1 expression or activity has been associated with various pathological conditions, including cancer, neurodegenerative diseases, and immune disorders. Understanding the precise mechanisms underlying EPDR1-mediated signaling may offer insights into disease pathogenesis and potential therapeutic strategies targeting aberrant cellular signaling pathways.