Persius/hicric huggingface dataset:
MYF6
Myogenic factor 6 (herculin) is a protein that in humans is encoded by the MYF6 gene.
Also known in the medical literature as MRF4 and herculin), MYF6 is a myogenic regulatory factor (MRF) in the process known as myogenesis.

# Function
MYF6 is a member of the myogenic factors (MYF) family that regulate myogenesis and muscle regeneration. Myogenics factor are basic helix-loop-helix (bHLH) transcription factors.
MYF-6 is a gene that encodes a protein involved in the regulation of myogenesis. Specifically, it induces the maturation of myotubes into myofibers.  The portion of the protein integral to myogenesis regulation is a basic helix-loop-helix (bHLH) domain that is conserved among all of the genes in the MRF family.
MYF-6 is expressed exclusively in skeletal muscle, and it is expressed at a higher levels in adult skeletal muscle than all of the other genes in the muscle regulatory factor factor gene family.  MYF-6 is different from the other myogenic regulatory factor genes due to its two-phase expression.  Initially, MYF-6 is transiently expressed along with MYF-5 in the somites during the early stages of myogenesis. However, it is primarily expressed postnatally. This suggests that it serves an important role in the maintenance and repair of adult skeletal muscle. The role of MYF-6 expression in the somites during embryogenesis is currently unknown.
The MYF-6 gene is physically linked to the MYF-5 gene on chromosome 12, and mutations in the MYF-6 gene typically exhibit reduced levels of MYF-5. Despite reductions in muscle mass of the back, MYF6 mutants still exhibit fairly normal skeletal muscle.  While this demonstrates that MYF-6 might not be essential for the formation of myofibers, it is thought that myogenin compensates for the absence of functional MYF-6.

# Clinical significance
Mutations in the MYF6 gene are associated with autosomal dominant centronuclear myopathy (ADCNM) and Becker's muscular dystrophy.
MYH7
MYH7 is a gene encoding a myosin heavy chain beta (MHC-) isoform (slow twitch) expressed primarily in the heart, but also in skeletal muscles (type I fibers). This isoform is distinct from the fast isoform of cardiac myosin heavy chain, MYH6, referred to as MHC-. MHC- is the major protein comprising the thick filament in cardiac muscle and plays a major role in cardiac muscle contraction.

# Structure
MHC- is a 223 kDa protein composed of 1935 amino acids. MHC- is a hexameric, asymmetric motor forming the bulk of the thick filament in cardiac muscle. MHC- is composed of N-terminal globular heads (20 nm) that project laterally, and alpha helical tails (130 nm) that dimerize and multimerize into a coiled-coil motif to form the light meromyosin (LMM), thick filament rod. The 9 nm alpha-helical neck region of each MHC- head non-covalently binds two light chains, essential light chain (MYL3) and regulatory light chain (MYL2).  Approximately 300 myosin molecules constitute one thick filament. There are two isoforms of cardiac MHC,  and , which display 93% homology. MHC- and MHC- display significantly different enzymatic properties, with  having 150-300% the contractile velocity and 60-70% actin attachment time as that of . MHC- is predominately expressed in the human ventricle, while MHC- is predominantly expressed in human atria.

# Function
It is the enzymatic activity of the ATPase in the myosin head that cyclically hydrolyzes ATP, fueling the myosin power stroke. This process converts chemical to mechanical energy, and propels shortening of the sarcomeres in order to generate intraventricular pressure and power. An accepted mechanism for this process is that ADP-bound myosin attaches to actin while thrusting tropomyosin inwards, then the S1-S2 myosin lever arm rotates ~70 about the converter domain and drives actin filaments towards the M-line.

# Clinical significance
Several mutations in MYH7 have been associated with inherited cardiomyopathies. Lowrance et al. were the first to identify the causative mutation Arg403Gln for hypertrophic cardiomyopathy (HCM) in the MYH7 gene. Studies have since identified several more MYH7 mutations, that are estimated to be causal in approximately 40% of HCM cases. This condition is an autosomal-dominant disease, in which a single copy of the variant gene causes enlargement of the left ventricle of the heart.  Disease onset usually occurs later in life, perhaps triggered by changes in thyroid hormone function and/or physical stress.
Another condition associated to mutations in this gene is paraspinal and proximal muscle atrophy.
MYL3
Myosin essential light chain (ELC), ventricular/cardiac isoform is a protein that in humans is encoded by the MYL3 gene. This cardiac ventricular/slow skeletal ELC isoform is distinct from that expressed in fast skeletal muscle (MYL1) and cardiac atrial muscle (MYL4). Ventricular ELC is part of the myosin molecule and is important in modulating cardiac muscle contraction.

# Structure
Cardiac, ventricular ELC is 21.9 kDa and composed of 195 amino acids (See human MYL3 sequences features here). Cardiac ELC and the second light chain, regulatory light chain (RLC, MYL2), are non-covalently bound to IQXXXRGXXXR motifs in the 9 nm S1-S2 lever arm of the myosin head, both alpha (MYH6) and beta (MYH7) isoforms. Both light chains are members of the EF-hand superfamily of proteins, which possess helix-loop-helix motifs in two globular domains connected by an alpha-helical linker. Though EF hand motifs are specialized to bind divalent ions such as calcium, cardiac ELC does not bind calcium at physiological levels. The N-terminal region of cardiac ELC is functionlly unique in that it is positively charged, being rich in Lysine residues (amino acids 4-14), with subsequent unique structure governed by Proline-Alanine repeats (amino acids 15-36).

# Function
Studies have provided evidence for ELC as modulator of myosin crossbrige kinetics. Treating cardiac myofibrils with the Lysine-rich N-terminal peptide (amino acids 5-14) evoked a supramaximal increase in cardiac myofibrillar MgATPase activity at submaximal calcium concentrations, and further studies demonstrated that this region of ELC modulates the affinity of myosin for actin.

# Clinical significance
Mutations in MYL3 have been identified as a cause of familial hypertrophic cardiomyopathy, and associated with a mid-left ventricular chamber type hypertrophy. Five mutations in MYL3 have been identified to date: M149V, R154H, E56G, A57G and E143K. All of these cluster around two of the four EF-hand domains, suggesting that proper conformation in these regions is necessary for normal cardiac function.
MYOT
Myotilin is a protein that in humans is encoded by the MYOT gene. Myotilin (myofibrillar titin-like protein) also known as TTID (TiTin Immunoglobulin Domain) is a muscle protein that is found within the Z-disc of sarcomeres.

# Structure
Myotilin is a 55.3 kDa protein composed of 496 amino acids. Myotilin was originally identified as a novel alpha-actinin binding partner with two Ig-like domains, that localized to the Z-disc. The C2-type Ig-like domains reside at the C-terminal half, and are most homologous to Ig domains 2-3 of palladin and Ig domains 4-5 of myopalladin and more distantly related to Z-disc Ig domains 7 and 8 of titin. The C-terminal region hosts the binding sites for Z-band proteins, and 2 Ig domains are the site of homodimerization for myotilin. By contrast, the N-terminal part of myotilin is unique, consisting of a serine-rich region with no homology to known proteins. Several disease-associated mutations involve serine residues within the serine-rich domain. Myotilin expression in human tissues is mainly restricted to striated muscles and nerves. In muscles, myotilin is predominantly found within the Z-discs. Myotilin forms homodimers and binds alpha-actinin, actin, Filamin C, FATZ-1, FATZ-2  and ZASP.

# Function
Myotilin is a structural protein that, along with titin and alpha-actinin give structural integrity to sarcomeres at Z-discs in striated muscle. Myotilin induces the formation of actin bundles in vitro and in non-muscle cells. A ternary complex myotilin/actin/alpha-actinin can be observed in vitro and actin bundles formed under these conditions appear more tightly packed than those induced by alpha-actinin alone. It was demonstrated that myotilin stabilizes F-actin by slowing down the disassembly rate. Ectopic overexpression of truncated myotilin causes the disruption of nascent myofibrils and the co-accumulation of myotilin and titin in amorphous cytoplasmic precipitates. In mature sarcomeres, wild-type myotilin colocalizes with alpha-actinin and Z-disc titin, showing the striated pattern typical of sarcomeric proteins. Targeted disruption of the myotilin gene in mice does not cause significant alterations in muscle function. On the other hand, transgenic mice with mutated myotilin develop muscle dystrophy.

# Clinical significance
Myotilin is mutated in various forms of muscular dystrophy: Limb-Girdle Muscular Dystrophy type 1A (LGMD1A), Myofibrillar Myopathy (MFM), Spheroid Body Myopathy and Distal Myopath. The mechanism underlying the pathology is still under investigation. It has been shown that actin binding properties of myotilin housing pathogenic mutations (Ser55Phe, Thr57Ile, Ser60Cys, and Ser95Ile) are normal, albeit with a slower rate of degradation. Surprisingly, YFP-fusion constructs of myotilin mutants (Ser55Phe, Ser55Ile, Thr57Ile, Ser60Cys, Ser60Phe, Ser95Ile, Arg405Lys) localized normally to Z-discs and exhibited normal dynamics in muscle cells.
MYPN
Myopalladin is a protein that in humans is encoded by the MYPN gene. Myopalladin is a muscle protein responsible for tethering proteins at the Z-disc and for communicating between the sarcomere and the nucleus in cardiac and skeletal muscle

# Structure
Myopalladin is a 145.2 kDa protein composed of 1320 amino acids. Myopalladin has five Ig-like repeats within the protein, and a proline-rich domain. Myopalladin binds the Src homology domain of nebulette and nebulin and tethers it to alpha-actinin via its C-terminal domain binding to the EF hand domains of alpha-actinin. The N-terminal region of myopalladin binds to the nuclear protein CARP, known to regulate gene expression in muscle. It also has been shown to bind ANKRD23.

# Function
Myopalladin has dual subcellular localization, residing in both the nucleus and sarcomere/I-bands in muscle. Accordingly, myopalladin has functions in both sarcomere assembly and in control of gene expression. Specifics of these functions were gleaned from studies involving MYPN mutants associated with various cardiomyopathies. The Q529X myopalladin mutant demonstrated incompetence in recruiting key binding partners such as desmin, alpha-actinin and CARP to the Z-disc during myofibrilogenesis. In contrast, the Y20C mutant resulted in decreased expression of binding partners.

# Clinical significance
Mutations in MYPN have been linked to dilated cardiomyopathy, hypertrophic cardiomyopathy and restrictive cardiomyopathy.
MYT1
Myelin transcription factor 1 is a protein that in humans is encoded by the MYT1 gene.

# Function
The protein encoded by this gene is a member of a family of neural specific, zinc finger-containing DNA-binding proteins. The protein binds to the promoter regions of proteolipid proteins of the central nervous system and plays a role in the developing nervous system.

# Interactive pathway map
Click on genes, proteins and metabolites below to visit related articles. 
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# Interactions
MYT1 has been shown to interact with PIN1.
Mesh
Mesh products are similar to fabric or a web in that it has many connected or woven strands. In clothing, a mesh is often defined as a loosely woven fabric that has a large number of closely-spaced holes, frequently used for modern sports jerseys and other clothing.

# Types of mesh
- A plastic mesh is extruded, oriented, expanded or tubular Plastic mesh can be made from polypropylene, polyethylene, nylon, PVC or PTFE.
- A metal mesh can be woven, welded, expanded, photo-chemically etched or electroformed (screen filter) from steel or other metals.

# Uses of meshes
- Meshes are often used to screen out unwanted things, such as insects. Wire screens on windows and mosquito netting can be considered as types of meshes.
- Wire screens can be used to shield against radio frequency radiation, e.g. in microwave ovens and Faraday cages.
- On a larger scale, in terms of the spaces in between, chicken wire and chain-link fences can also be considered a type of mesh.
- Metal and nylon wire mesh filters are used in water filtration.
- Wire Mesh is used in guarding for secure areas and as protection in the form of Vandal Screens.
- Wire Mesh can be fabricated to produce Park Benches, Waste Baskets and other baskets for Material Handling.
- Wire Mesh is the separation media in Vibratory Screening Units.
Mite
Mites, along with ticks, belong to the subclass Acarina (also known as Acari) and the class Arachnida. Mites are among the most diverse and successful of all the invertebrate groups. They have exploited an incredible array of habitats, and because of their small size (most are microscopic) most go totally unnoticed. Many live freely in the soil or water, but there are also a large number of species that live as parasites on plants or animals and even some that feed on mold.
Some of the plant pests include the so called spider mites (family Tetranychidae), thread-footed mites (family Tarsonemidae), and the gall mites (family Eriophyidae). Among the species that attack animals are members of the Sarcoptic Mange mites (family Sarcoptidae), which burrow under the skin. Demodex mites (family Demodicidae) are parasites that live in or near the hair follicles of mammals, including humans. Perhaps the best-known mite, though, is the house dust mite (family Pyroglyphidae).
Insects may also have parasitic mites. Examples are Varroa destructor which attaches to the body of the honeybee, and Acarapis woodi (family Tarsonemidae), which lives in the tracheae of honey bees. There are hundreds of species of mites associated with other bee species, and most are poorly described and understood. Some are thought to be parasites, while others beneficial symbionts.
There are over 45,000 described species of mites. Scientists believe that we have only found 5% of the total diversity of mites. Mites are believed to have existed for around 400 million years.
The scientific discipline devoted to the study of ticks and mites is called acarology.
The tropical species Archegozetes longisetosus is one of the strongest animals in the world, relative to its mass (100 g): It lifts up to 1182 times its own weight, over five times more than would be expected of such a minute animal (Heethoff & Koerner 2007).

# Systematics
For the systematics of mites, see Acarina.

# Allergy
Mites cause several forms of allergic diseases, including hay fever, asthma and eczema and also aggrevates atopic dermatitis.  Mites are usually found in warm and humid locations, including beds. It is thought that inhalation of mites during sleep exposes the human body to some antigens which eventually induce hypersensitivity reaction. Dust mite allergens are thought to be among the heaviest dust allergens.
Like most of the other types of allergy, treatment of mite allergy starts with avoidance. There is a strong body of evidence showing that avoidance should be helpful in patients with atopic dermatitis triggered by exposure to mites. Regular washing of mattresses and blankets with hot water can help in this regard. Antihistamines are also useful; Cetirizine, for example, is shown to reduce allergic symptoms of patients.
NAB2
NGFI-A-binding protein 2 also known as EGR-1-binding protein 2 or melanoma-associated delayed early response protein (MADER) is a protein that in humans is encoded by the NAB2 gene.

# Function
This gene encodes a member of the family of NGFI-A binding (NAB) proteins, which function in the nucleus to repress or activate transcription induced by some members of the EGR (early growth response) family of transactivators. NAB proteins can homo- or hetero-multimerize with other EGR or NAB proteins through a conserved N-terminal domain, and repress transcription through two partially redundant C-terminal domains. Transcriptional repression by the encoded protein is mediated in part by interactions with the nucleosome remodeling and deactylase (NuRD) complex. Alternatively spliced transcript variants have been described, but their biological validity has not been determined.

# Pathology
Recurrent somatic fusions of the two genes, NGFI-Abinding protein 2 (NAB2) and STAT6, located at chromosomal region 12q13, have been identified in solitary fibrous tumors.
NANS
Sialic acid synthase is an enzyme that in humans is encoded by the NANS gene.
This gene encodes an enzyme that functions in the biosynthetic pathways of sialic acids. In vitro, the encoded protein uses N-acetylmannosamine 6-phosphate and mannose 6-phosphate as substrates to generate phosphorylated forms of N-acetylneuraminic acid (Neu5Ac) and 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN), respectively. However, it exhibits much higher activity toward the Neu5Ac phosphate product. 
In insect cells, expression of this gene results in Neu5Ac and KDN production. This gene is related to the E. coli sialic acid synthase gene neuB, and it can partially restore sialic acid synthase activity in an E. coli neuB-negative mutant.
NCDN
Neurochondrin (also known as its murine homologue, Norbin) is a protein that in humans is encoded by the NCDN gene.
This gene encodes a leucine-rich cytoplasmic protein, which is highly similar to a mouse protein norbin that negatively regulates Ca/calmodulin-dependent protein kinase II phosphorylation and may be essential for spatial learning processes. Several alternatively spliced transcript variants of this gene have been described.
Norbin can modulate signaling activity and expression of metabotropic glutamate receptor 5; modulating  mice with targeted deletion of NCDN in the brain have phenotypic traits usually found in the rodent models of schizophrenia, including disruptions in prepulse inhibition. Furthermore, norbin protein expression is altered in the schizophrenia brain.
NEK6
Serine/threonine-protein kinase Nek6 is an enzyme that in humans is encoded by the NEK6 gene.

# Function
The Aspergillus nidulans 'never in mitosis A' (NIMA) gene encodes a serine/threonine kinase that controls initiation of mitosis. NIMA-related kinases (NEKs) are a group of protein kinases that are homologous to NIMA. Evidence suggests that NEKs perform functions similar to those of NIMA.
It is a protein kinase which plays an important role in mitotic cell cycle progression. Required for chromosome segregation at metaphase-anaphase transition, robust mitotic spindle formation and cytokinesis. Phosphorylates ATF4, CIR1, PTN, RAD26L, RBBP6, RPS7, RPS6KB1, TRIP4, STAT3 and histones H1 and H3. Phosphorylates KIF11 to promote mitotic spindle formation. Involved in G2/M phase cell cycle arrest induced by DNA damage. Inhibition of activity results in apoptosis. May contribute to tumorigenesis by suppressing p53/TP53-induced cancer cell senescence.

# Interactions
NEK6 has been shown to interact with NEK9.
NEU1
Sialidase 1 (lysosomal sialidase), also known as NEU1 is a mammalian lysosomal neuraminidase enzyme which in humans is encoded by the NEU1 gene.

# Function
The protein encoded by this gene encodes the lysosomal enzyme, which cleaves terminal sialic acid residues from substrates such as glycoproteins and glycolipids. In the lysosome, this enzyme is part of a heterotrimeric complex together with beta-galactosidase and cathepsin A (the latter also referred to as 'protective protein'). Mutations in this gene can lead to sialidosis.

# Clinical significance
Deficiencies in the human enzyme NEU1 leads to sialidosis, a rare lysosomal storage disease. Sialidase has also been shown to enhance recovery from spinal cord contusion injury when injected in rats.

# Interactions
NEU1 has been shown to interact with Cathepsin A.
NFYA
Nuclear transcription factor Y subunit alpha is a protein that in humans is encoded by the NFYA gene.

# Function
The protein encoded by this gene is one subunit of a trimeric complex, forming a highly conserved transcription factor that binds to CCAAT motifs in the promoter regions in a variety of genes. Subunit A associates with a tight dimer composed of the B and C subunits, resulting in a trimer that binds to DNA with high specificity and affinity. The sequence specific interactions of the complex are made by the A subunit, suggesting a role as the regulatory subunit. In addition, there is evidence of post-transcriptional regulation in this gene product, either by protein degradation or control of translation. Further regulation is represented by alternative splicing in the glutamine-rich activation domain, with clear tissue-specific preferences for the two isoforms.

# Interactions
NFYA has been shown to interact with Serum response factor and ZHX1. NFYA, NFYB and NFYC form the NFY complex and it has been shown that the NFY complex serves as a pioneer factor by promoting chromatin accessibility to facilitate other co-localizing cell type-specific transcription factors.
NFYC
Nuclear transcription factor Y subunit gamma is a protein that in humans is encoded by the NFYC gene.

# Function
The protein encoded by this gene is one subunit of a trimeric complex, forming a highly conserved transcription factor that binds with high specificity to CCAAT motifs in the promoter regions in a variety of genes. This gene product, subunit C, forms a tight dimer with the B subunit (NFYB), a prerequisite for subunit A (NFYA) association. The resulting trimer binds to DNA with high specificity and affinity. Subunits B and C each contain a histone-like motif. Observation of the histone nature of these subunits is supported by two types of evidence; protein sequence alignments and experiments with mutants. Additional regulation, preliminarily supported by the EST database, may be represented by alternative splicing in this subunit.
Two microRNAs; miR-30c and miR-30e are located within introns of the nfyc gene.  These microRNAs are actively transcribed in human insulin-producing beta cells in the pancreatic islets that also show high expression of nfyc and CDH1 genes.  The expression of these intronic microRNAs is essential for maintaining the differentiated phenotype of human islet beta cells.  Inhibition of miR-30 family microRNAs induces epithelial-mesenchymal transition of human pancreatic islet cells.

# Interactions
NFYC has been shown to interact with Myc.