Persius/hicric huggingface dataset:
MYO10
Myosin X, also known as MYO10, is a protein that in humans is encoded by the MYO10 gene.
Myosin X is an actin-based motor protein known to associate at the tips of filopodia.

# Model organisms
Model organisms have been used in the study of MYO10 function. A conditional knockout mouse line called Myo10tm2(KOMP)Wtsi was generated at the Wellcome Trust Sanger Institute. Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Additional screens performed:  - In-depth immunological phenotyping
MYO5A
Myosin-Va is a protein that in humans is encoded by the MYO5A gene.

# Interactions
MYO5A has been shown to interact with DYNLL1, RAB27A, DYNLL2 and RPGRIP1L.

# Clinical significance
Defects are associated with Griscelli syndrome type 1, also known as Elejalde syndrome.

# Model organisms
Model organisms have been used in the study of MYO5A function. A conditional knockout mouse line, called Myo5atm1e(KOMP)Wtsi was generated as part of the International Knockout Mouse Consortium programa high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Twenty five tests were carried out on mutant mice and three significant abnormalities were observed. Male homozygous mutants had abnormal hair cycles, coat colouration and an increased susceptibility to bacterial infection.
MYO5B
Myosin-Vb is a protein that in humans is encoded by the MYO5B gene.
Recent evidence suggests that Myosin VB is related to the creation of memories by actin-dependent trafficking of AMPA receptor containing recycling endosomes in dendritic spines.
Mutations of MYO5B cause microvillus inclusion disease and have been associated with bipolar disorder.

# Interactions
MYO5B has been shown to interact with RAB11FIP2.
MYO7A
Myosin VIIA is protein that in humans is encoded by the MYO7A gene.  Myosin VIIA is a member of the unconventional myosin superfamily of proteins. Myosins are actin binding molecular motors that use the enzymatic conversion of ATP - ADP + inorganic phosphate (Pi) to provide the energy for movement.
Myosins are mechanochemical proteins characterized by the presence of a motor domain, an actin-binding domain, a neck domain that interacts with other proteins, and a tail domain that serves as an anchor. Myosin VIIA is an unconventional myosin with a very short tail. Unconventional myosins have diverse functions in eukaryotic cells and are primarily thought to be involved in the movement or linkage of intra-cellular membranes and organelles to the actin cytoskeleton via interactions mediated by their highly divergent tail domains.
MYO7A is expressed in a number of mammalian tissues, including testis, kidney, lung, inner ear, retina and the ciliated epithelium of the nasal mucosa.

# Clinical significance
Mutations in the MYO7A gene cause the Usher syndrome type 1B, a combined deafness/blindness disorder. Affected individuals are typically profoundly deaf at birth and then undergo progressive retinal degeneration.

# Model organisms
Model organisms have been used in the study of MYO7A function. A spontaneous mutant mouse line, called Myo7ash1-6J was generated. Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Twenty three tests were carried out on mutant mice and ten significant abnormalities were observed. Male homozygous mutant mice displayed a decreased body weight, a decrease in body fat, improved glucose tolerance and abnormal pelvic girdle bone morphology. Homozygous mutant mice of both sex displayed various abnormalities in a modified SHIRPA test, including abnormal gait, tail dragging and an absence of pinna reflex, a decrease in grip strength, an increased thermal pain threshold, severe hearing impairment and a number of abnormal indirect calorimetry and clinical chemistry parameters.
MYOM1
Myomesin-1 is a protein that in humans is encoded by the MYOM1 gene. Myomesin-1 is expressed in muscle cells and functions to stabilize the three-dimensional conformation of the thick filament. Embryonic forms of Myomesin-1 have been detected in dilated cardiomyopathy.

# Structure
Alternatively spliced variants of MYOM1, including EH-myomesin, Skelemin and Myomesin-1 have been identified; with Skelemin having an additional 96 amino acids rich in serine and proline residues. Myomesin-1, like myomesin 2 and titin, is a member of a family of myosin-associated proteins containing structural modules with strong homology to either fibronectin type III (motif I) or immunoglobulin C2 (motif II) domains. Myomesin-1 bears uniqueness within this family in that it has intermediate filament core-like motifs, one near each terminus. Myomesin-1 and Myomesin-2 each have a unique N-terminal region followed by 12 modules of motif I or motif II, in the arrangement II-II-I-I-I-I-I-II-II-II-II-II. The two proteins share 50% sequence identity in this repeat-containing region. The head structure formed by these 2 proteins on one end of the titin string extends into the center of the M band. Alternatively spliced, tissue-specific transcript variants encoding different isoforms have been identified. Myomesin-1 can dimerize in an anti-parallel fashion via its C-terminal region.

# Function
Titin, together with its associated proteins, interconnects the major structure of sarcomeres, the M bands and Z discs. The C-terminal end of the titin string extends into the M line, where it binds tightly to Myomesin-1 and myomesin 2. Skelemin/Myomesin-1 is concentrated at peripheral regions of M-bands, and is postulated to link myofibrils with the intermediate filament cytoskeleton. Skelemin/Myomesin-1 has been detected in the nucleus as well as the cytoskeletal, suggesting that it may play a role in gene expression. Myomesin-1 functions to mediate stretch-induced signaling, and the EH-myomesin splice variant, expressed in embryonic hearts and in dilated cardiomyopathy, can modulate its elasticity.

# Clinical Significance
The fetal EH-myomesin alternatively spliced form of MYOM1 has been shown to be reexpressed at an early timepoint in the progression of dilated cardiomyopathy, coincident with isoform switches in titin.
MYOM1 has also been shown to be abnormally spliced in patients with myotonic dystrophy type I; specifically, exon 17a.

# Interactions
Skelemin/Myomesin-1 has been shown to interact with:
- ITGB1
- ITGB3
- ITGA2B
- MYH7
- Titin
- PNKD
MYOZ2
Myozenin-2, also referred to as Calsarcin-1, is a protein that in humans is encoded by the MYOZ2 gene. The Calsarcin-1 isoform is a muscle protein expressed in cardiac muscle and slow-twitch skeletal muscle, which functions to tether calcineurin to alpha-actinin at Z-discs, and inhibit the pathological cardiac hypertrophic response. This differs from the fast-skeletal muscle isoform, calsarcin-2.

# Structure
Calsarcin-1 is a 29.9 kDa protein composed of 264 amino acids. Calsarcin-1 and calsarcin-2 are only 31% homologous (94 identical amino acids), exhibiting the highest homology at N- and C-termini. Calsarcin-1 binds to alpha-actinin, gamma-filamin,  telethonin, ZASP/Cypher and calcineurin. The binding region of calsarcin-1 to alpha-actinin is localized to amino acids 153-200, and that of calsarcin-1 to calcineurin is amino acids 217-240.

# Function
The function of calsarcin-1 in cardiac and slow-skeletal muscle has been illuminated through studies in transgenic animals. Mice lacking the MYOZ2 gene (MYOZ2-/-) are generally sensitized to calcineurin signaling in both muscle types. In slow-skeletal muscle, MYOZ2-/- show increased slow-twitch muscle fibers. In cardiac, MYOZ2-/- show induction of the fetal gene program typical of pathologic hypertrophy, however there was no evidence of hypertrophied morphometry at baseline. However, upon calcineurin activation or pressure overload-induced pathologic hypertrophy, MYOZ2-/- exhibited exaggerated cardiac hypertrophy, demonstrating that calsarcin-1 negatively modulates the function of calcineurin during pathologic hypertrophic remodeling. Additional studies supported these findings in demonstrating that adenoviral overexpression of calsarcin-1 attenuated Gq alpha subunit-stimuated hypertrophy and ANP induction, by Angiotensin II, phenylephrine and endothelin-1 agonists in neonatal cardiomyocytes. Overexpression of calsarcin-1 in mice (CS1Tg) was protective against Angiotensin II-induced pathologic cardiac hypertrophy, evidenced by preserved fractional shortening and contractility, as well as a blunted induction of the fetal hypertrophic gene program and significantly reduced expression of calcineurin-stimulated MCIP1.4 gene expression. Taken together, these studies strongly support a role for calsarcin-1 in suppressing pathologic cardiac hypertrophy.

# Clinical Significance
Two missense mutations in MYOZ2, Ser48Pro and Ile246Met, have been shown to be causal for rare forms of familial hypertrophic cardiomyopathy.
Mamba

# Overview
Mambas, of the genus Dendroaspis, are fast-moving tree-dwelling snakes of Africa.  ("Dendroaspis" is literally "tree snake".) They belong to the family of Elapidae which includes cobras, coral snakes, kraits and, debatably, sea snakes, all of which can be extremely deadly. The black mamba is the longest venomous snake in Africa, with an extremely potent neurotoxic venom that attacks the nervous system, and cardiotoxins which attack the heart; the bite is often fatal to humans without access to proper first aid and subsequent antivenin treatment, because it shuts down the lungs and heart. Prior to the availability of antivenom, envenomations by members of this genus carried a nearly 100% fatality rate. However, with antivenom being much more available today, fatalities have become much more rare.
The Western green mamba (D. viridis) and Eastern green mamba, (D. angusticeps), possess venom that is roughly equal in potency to that of the Black mamba (D. polylepis). However, they are not nearly as aggressive. 
They are slightly smaller, and are arboreal, whereas the latter is primarily terrestrial.
The black mamba is not named for the colour of its body (which is usually a shade of grey or charcoal), but for the highly pigmented interior of its mouth, which it will display to the predator in hopes it will leave it alone. Many people believe that the Black Mamba will actually chase and attack humans. This is a myth, and is probably fueled by the great speed with which this species can move. Humans are actually their predators, rather than their prey. For that reason, mambas generally avoid contact with humans. However, if a mamba feels threatened by a human, it may defend itself fiercely.
In contrast to all other species in this genus, which are arboreal, black mambas reside in hollow insect mounds, abandoned burrows, and rock crevices. They are diurnal.  During the day they actively hunt their prey of small mammals, birds and lizards. They return to the same lair nightly.
Mambas are related to the cobras (Elapids), as can be seen during their threat display, when they stretch a slightly smaller 'hood' while gaping their mouth. Unlike most other snakes mambas will strike repeatedly if cornered, and have been reported to bring down a giraffe and a lion with their venom.

# Mamba toxin
Mamba toxin is in fact several components, with different targets. Examples are:
- Mamba toxin 3, which inhibits M4 receptors. 
- Mamba toxin 7, which inhibits M1 receptors.
Maple

# Overview
Acer (/esr/) is a genus of trees or shrubs commonly known as maple.
Maples are variously classified in a family of their own, the Aceraceae, or together with the Hippocastanaceae included in the family Sapindaceae. Modern classifications, including the Angiosperm Phylogeny Group system, favour inclusion in Sapindaceae. The type species of the genus is Acer pseudoplatanus (Sycamore maple).
There are approximately 128 species, most of which are native to Asia, with a number also appearing in Europe, northern Africa, and North America. Only one species, the poorly studied Acer laurinum, is native to the Southern Hemisphere. Fifty-four species of maples meet the International Union for Conservation of Nature criteria for being under threat of extinction in their native habitat.
The word Acer derives from a Latin word meaning "sharp" (compare "acerbic"), referring to the characteristic points on maple leaves.  It was first applied to the genus by the French botanist Joseph Pitton de Tournefort in 1700. The earliest known fossil maple is Acer alaskense, from the Latest Paleocene of Alaska.
Marsh
In geography, a marsh, or morass, is a type of wetland which is subject to frequent or continuous inundation.  Typically a marsh features grasses, rushes, reeds, typhas, sedges, and other herbaceous plants (possibly with low-growing woody plants) in a context of shallow water. A marsh is different from a swamp, which has a greater proportion of open water surface, and is generally deeper than a marsh. In North America, the term swamp is used for wetland dominated by trees rather than grasses and low herbs.
The water of a marsh can be fresh, brackish or saline. Coastal marshes may be associated with estuaries and along waterways between coastal barrier islands and the inner coast. The estuarine marsh, or tidal marsh, is often based on soils consisting of sandy bottoms or bay muds. An example is the Tantramar Marsh of eastern Canada.
Below water decomposition processes often produce marsh gas, which may through self-ignition manifest as Will o' the wisps (aka. Jack-a-lanterns or spirites).
Marshes are critically important wildlife habitats, often serving as breeding grounds for a wide variety of animal life.
Constructed wetlands featuring surface-flow design are usually in the form of a marsh.

# Images
- Marsh in Point Pelee, Ontario, Canada
Marsh in Point Pelee, Ontario, Canada
- Marsh in Long Point, Ontario, Canada
Marsh in Long Point, Ontario, Canada
Moles

# Overview
Moles are growths on the skin. They happen when cells in the skin, called melanocytes, grow in a cluster with the surrounding tissue. Moles are very common. Most people have between 10 and 40 moles. A person may develop new moles from time to time, usually until about the age of 40.
Moles are usually pink, tan or brown. They can be flat or raised. They are usually round or oval and no larger than a pencil eraser.
About one out of every ten people has at least one unusual (or atypical) mole that looks different from an ordinary mole. The medical term for these unusual moles is dysplastic nevi. They may be more likely than ordinary moles to develop into melanoma, a type of skin cancer. Because of this, you should have a healthcare professional check your moles if they look unusual, grow larger, change in color or outline, or in any other way.
Mucin

# Overview
Mucins are a family of large, heavily glycosylated proteins. Although some mucins are membrane-bound due to the presence of a hydrophobic membrane-spanning domain that favors retention in the plasma membrane, the concentration here is on those mucins that are secreted on mucosal surfaces and saliva.

# Glycosylation and aggregation
Mucin genes encode mucin monomers that are synthesized as rod-shape apomucin cores that are post-translationally modified by exceptionally abundant glycosylation.
The dense "sugar coating" of mucins gives them considerable water-holding capacity and also makes them resistant to proteolysis, which may be important in maintaining mucosal barriers.
Mucins are secreted as massive aggregates of proteins with molecular masses of roughly 1 to 10 million Da. Within these aggregates, monomers are linked to one another mostly by non-covalent interactions, although intermolecular disulfide bonds may also play a role in this process.

# Regions
Two distinctly different regions are found in mature mucins:
- The amino- and carboxy-terminal regions are very lightly glycosylated, but rich in cysteines, which are likely involved in establishing disulfide linkages within and among mucin monomers.
- A large central region formed of multiple tandem repeats of 10 to 80 residue sequences in which up to half of the amino acids are serine or threonine. This area becomes saturated with hundreds of O-linked oligosaccharides. N-linked oligosaccharides are also found on mucins, but much less abundantly.

# Genes
At least 19 human mucin genes have been distinguished by cDNA cloning--MUC1, 2, 3A, 3B, 4, 5AC, 5B, 6-9, 11-13, and 15-19.
The major secreted airway mucins are MUC5AC and MUC5B, while MUC2 is secreted mostly in the intestine but also in the airway.

# Clinical significance
Increased mucin production occurs in many adenocarcinomas, including cancer of the pancreas, lung, breast, ovary, colon, etc. Mucins are also overexpressed in lung diseases such as asthma, bronchitis, COPD or cystic fibrosis. Two membrane mucins, MUC1 and MUC4 have been extensively studied in relation to their pathological implication in the disease process. Moreover, mucins are also being investigated for their potential as diagnostic markers.
Spasm
A spasm is a sudden, involuntary contraction of a muscle, a group of muscles, or a hollow organ, or a similarly sudden contraction of an orifice.  It is sometimes accompanied by a sudden burst of pain, but is usually harmless and ceases after a few minutes. Spasmodic muscle contraction may also be due to a large number of medical conditions, however, including the dystonias.
By extension, a spasm is also a sudden and temporary burst of energy, activity, or emotion.
A subtype of spasms is colic, an episodic pain due to spasms of smooth muscle in a particular organ (e.g. the bile duct). A characteristic of colic is the sensation of having to move about, and the pain may induce nausea or vomiting if severe. Series of spasms or permanent spasms are called a spasmism.
In very severe cases, the spasm can induce muscular contractions that are more forceful than the sufferer could generate under normal circumstances. This can lead to torn tendons and ligaments.
Some argue that hysterical strength is a type of spasm induced by the brain under extreme circumstances.

# Causes

## Drug Side Effect
- Eribulin
- Ixabepilone
- Lacosamide
- Ospemifene
- Ramucirumab
- Tiagabine
N-Myc
N-myc proto-oncogene protein also known as N-Myc or basic helix-loop-helix protein 37 (bHLHe37), is a protein that in humans is encoded by the MYCN gene.

# Function
The MYCN gene is a member of the MYC family of transcription factors and encodes a protein with a basic helix-loop-helix (bHLH) domain. This protein is located in the cell nucleus and must dimerize with another bHLH protein in order to bind DNA. N-Myc is highly expressed in the fetal brain and is critical for normal brain development.
The MYCN gene has an antisense RNA, N-cym or MYCNOS, transcribed from the opposite strand which can be translated to form a protein product. N-Myc and MYCNOS are co-regulated both in normal development and in tumor cells, so it is possible that the two transcripts are functionally related. It has been shown that the antisense RNA encodes for a protein, named NCYM, that has originated de novo and is specific to human and chimpanzee. This NCYM protein inhibits GSK3b and thus prevents MYCN degradation. Transgenic mice that harbor human MYCN/NCYM pair often show neuroblastomas with distant metastasis, which are atypical for normal mice. Thus NCYM represents a rare example of a de novo gene that has acquired molecular function and plays a major role in oncogenesis.

# Clinical significance
Amplification and overexpression of N-Myc can lead to tumorigenesis. Excess N-Myc is associated with a variety of tumors, most notably neuroblastomas where patients with amplification of the N-Myc gene tend to have poor outcomes. MYCN can also be activated in neuroblastoma and other cancers through somatic mutation.

# Interactions
N-Myc has been shown to interact with MAX.
N-Myc is also stabilized by aurora A which protects it from degradation. Drugs that target this interaction are under development, and are designed to change the conformation of aurora A. Conformational change in Aurora A leads to release of N-Myc, which is then degraded in a ubiquitin-dependent manner.
NAGLU
N-acetylglucosaminidase, alpha is a protein that in humans is encoded by the NAGLU gene.

# Function
This gene encodes an enzyme that degrades heparan sulfate by hydrolysis of terminal N-acetyl-D-glucosamine residues in N-acetyl-alpha-D-glucosaminides.

# Clinical significance
Defects in this gene are the cause of mucopolysaccharidosis type IIIB (MPS-IIIB), also known as Sanfilippo syndrome B. This disease is characterized by the lysosomal accumulation and urinary excretion of heparan sulfate.
NBPF3
Neuroblastoma breakpoint family, member 3, also known as NBPF3, is a human gene of the neuroblastoma breakpoint family, which resides on chromosome 1 of the human genome.  NBPF3 is located at 1p36.12, immediately upstream of genes ALPL and RAP1GAP.

# Protein sequence
The NBPF3 gene is 633 amino acids long and contains five DUF1220 domains, which are highlighted in the image below.  DUF1220 domains are found in all other members of the neuroblastoma breakpoint family.  The protein has a very repetitive structure, since, along with the remaining members of its protein family, it likely arose form segmental duplications on chromosome 1.
The domains are located at residues 236-298, 322-385, 394-460, 469-535, and 544-610.
The protein sequence is rich in three amino acids that are polar and negatively charged at physiological pH: glutamic acid, aspartic acid and glutamine.  The isoelectric point of the protein is 4.21, the acidity of which may be attributed to the abundance of these amino acids.

# Isoforms and sequence characteristics
There are four known isoforms of the NPBF3 gene.  While isoform 1 is the dominant form of the gene, each other isoform has unique changes to the protein sequence that may affect the structure, expression or function of the gene product:
These isoforms are represented in the following schematic, along with additional sequence characteristics which include Poly-Glu compositional biases and a potential coiled coil.

# Function
The function of the neuroblastoma breakpoint family proteins, including NPBF3, is not yet understood by the scientific community.  Because of the repetitive composition of this family of genes as well as their amplification in primates, it has been suggested that the family is involved in cognitive development and the evolution of primates.
It has also been suggested that there is a connection between the neuroblastoma breakpoint family and oncogenesis.  Due to the up-regulation of NBPF genes in some tumor tissues, proteins of this family have been hypothesized to be oncogenes.  It has also been suggested that members of the neuroblastoma breakpoint family are tumor suppressor genes, due to a loss of heterozygosity in tumor tissue in the region of chromosome 1 where NBPF3 and other NBPF proteins are located.

# Homology
Orthologs of NBPF3 are found primarily in primate species, though orthologous sequences can be found in cow, horse, and dog species.  There is no mouse ortholog of NPBF3.
NPBF3 has many human paralogs because it is a member of a gene family.
Both orthologs and paralogs of NBPF3 were found using the databases BLAT. and BLAST 

# Protein interactions
NPBF3 interacts with three other proteins: C1orf19, Ankyrin-1 (ANK1) and Ewing Sarcoma Breakpoint region 1 (EWSR1).  It is not known how these proteins interact or what the product of these interactions may be.