Persius/hicric huggingface dataset:
miR-33
miR-33 is a family of microRNA precursors, which are processed by the Dicer enzyme to give mature microRNAs. miR-33 is found in several animal species, including humans. In some species there is a single member of this family which gives the mature product mir-33. In humans there are two members of this family called mir-33a and mir-33b, which are located in intronic regions within two protein-coding genes for Sterol regulatory element-binding proteins (SREBP-2 and SREBP-1) respectively.

# Function
miR-33 plays a role in lipid metabolism; it downregulates a number of ABC transporters, including ABCA1 and ABCG1, which in turn regulate cholesterol and HDL generation. Further related roles of miR-33 have been proposed in fatty acid degradation and in macrophage response to low-density lipoprotein.
It has been suggested that miR-33a and miR-33b regulates genes Involved in fatty acid metabolism and insulin signalling.
Potential binding sites for mir-33 have been identified in the cDNA of tumour suppressor p53. Further, study has shown that miR-33 is able to repress p53 expression and p53-induced apoptosis. This function is thought to be related to hematopoietic stem cell renewal.

# Applications
miR-33, along with miR-122, could be used to diagnose or treat conditions related to metabolic disorders and cardiovascular disease.
Midget
In the 19th century, midget was a medical term referring to an extremely short but normally proportioned person and was used in contrast to dwarf, which denoted disproportionate shortness. Like many other older medical terms, as it became part of popular language, it was usually used in a pejorative sense. When applied to a person who is very short, midget is now often considered offensive, an example of the euphemism treadmill.
The word "dwarf" has  generally replaced "midget" even for proportionally short people, though the term "little person" is preferred. According to the Little People of America, dwarfism is "a medical or genetic condition that usually results in an adult height of 4'10" (147 cm) or shorter, among both men and women, although in some cases a person with a dwarfing condition may be slightly taller than that."
Modern terminology now distinguishes between the two types of dwarfism using the terms proportionate dwarfism, such as primordial dwarfism, and disproportionate dwarfism, such as achondroplasia. Proportionate dwarfism is often the result of a hormonal deficiency (such as human growth hormone), and it may be treated medically.
Midgut

# Overview
The midgut is the portion of the embryo from which most of the intestines are derived. After it bends around the superior mesenteric artery, it is called the "midgut loop". It originates from the foregut at the opening of the bile duct into the duodenum and continues through the small intestine and much of the large intestine until the transition to the hindgut about two-thirds of the way through the transverse colon.

# Structures in the adult midgut
- Duodenum (3rd and 4th parts)
- Jejunum
- Ileum
- Cecum
- Appendix
- Ascending colon
- Hepatic flexure of colon.
- Transverse colon (proximal two-thirds)

# Vascular, lymphatics and innervation
Arterial supply to the midgut is from the superior mesenteric artery, an unpaired branch of the aorta. Venous drainage is to the portal venous system. Lymph from the midgut drains to prevertebral superior mesenteric nodes located at the origin of the superior mesenteric artery from the aorta. Portal drainage carries all non-lipid nutrients from digestion to the liver for processing and detoxification, while lymphatic drainage carries fatty chyle to the cisterna chyli. Autonomic innervation of the midgut is from the superior mesenteric plexus.

# Clinical notes
- Malrotation of the midgut during development can lead to volvulus.
- Pain in the midgut is referred to the umbilical region (around the belly button)
Mildew
Mildew refers to certain kinds of mold or fungus. In Old English, it meant honeydew (a substance secreted by aphids on leaves, formerly thought to distill from the air like dew), and later came to mean mildew in the modern senses.
- The term mildew is often used generically to refer to mold growth, usually with a flat growth habit. Molds can thrive on any organic matter, including clothing, leather, paper, and the ceilings, walls and floors of homes with moisture management problems. Mildew often lives on shower walls, windowsills, and other places where moisture levels are high. There are many species of molds. In unaired places, such as basements, they can produce a strong musty odor.
- What most horticulturalists and gardeners call mildew is more precisely called powdery mildew. It is caused by many different species of fungi in the order Erysiphales. Most species are specific to a narrow range of hosts, and all are obligate parasites of flowering plants. The species that affects roses is Sphaerotheca pannosa var. rosa.
- Another plant-associated type of mildew is downy mildew. Downy mildews are caused by fungus-like organisms in the family Peronosporaceae (Oomycota). They are obligate plant pathogens, and the many species are each parasitic on a narrow range of hosts. In agriculture, downy mildews are a particular problem for growers of potatoes, grapes, tobacco and cucurbits.
The English word was exported into French as mildiou and as mildiu in Spanish.
Moesin
Moesin is a protein that in humans is encoded by the MSN gene.
Moesin (for membrane-organizing extension spike protein) is a member of the ERM protein family which includes ezrin and radixin. ERM proteins appear to function as cross-linkers between plasma membranes and actin-based cytoskeletons.
Moesin is localized to filopodia and other membranous protrusions that are important for cellcell recognition and signaling and for cell movement.

# Interactions
Moesin has been shown to interact with:
- CD43
- ICAM3
- Neutrophil cytosolic factor 1,
- Neutrophil cytosolic factor 4
- VCAM-1
- EZR
Morula
A morula (Latin "morus", mulberry) is an embryo at an early stage of embryonic development, consisting of approximately 12-32 cells (called blastomeres) in a solid ball contained within the zona pellucida.

# Production
The morula is produced by embryonic cleavage, the rapid division of the zygote. After reaching the 16-cell stage, the cells of the morula differentiate. The inner blastomeres will become the inner cell mass and the blastomeres on the surface will later flatten to form the trophoblast. As this process begins, the blastomeres change their shape and tightly align themselves against each other to form a compact ball of cells.  This is called compaction and is likely mediated by cell surface adhesion glycoproteins.

# Development
In mammals the morula travels to the uterus around 3-4 days after fertilization, and at about 4 days after fertilization a fluid-filled space called the blastocoel cavity appears and the morula becomes a blastocyst.

# Additional images
- Morula, 8 cell stage
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Mutant
A mutant is an individual, organism, or new genetic character arising or resulting from an instance of mutation, which is a sudden structural change within the DNA of a gene or chromosome of an organism resulting in the creation of a new character or trait not found in the wildtype. In an organism or individual, the new character or trait may or may not be trivial, may occasionally be beneficial, but will usually result in either a genetic disorder or have no phenotypic effect whatsoever. The natural occurrence of genetic mutations is integral to the process of evolution. A more general term for mutant is sport, which includes individuals who vary from type due to mutation, as well as those who vary from type due to other reasons.
Developmental abnormalities not due to genetic change, are frequently referred to as mutants by non-experts.  The difference between a developmental abnormality and a mutation is that the former is non-hereditable as the DNA is unchanged.  Such abnormalities include extra limbs and occur when a genetically normal embryo develops abnormally.
Occasionally, a body cell in a healthy organism may acquire a mutation caused by a genetic error occurring during routine cell division. This is also known as a "somatic mutation."  Such an error may result in cancer.
Creatures with visibly obvious mutations are often regarded as objects of curiosity. Examples include rare blue lobsters. albinos of many species and animals with extra digits. A well-known mutation in fruit flies causes the flies to have legs in place of antennas. An American aquarium even displays what it calls a "double mutant" snake that is both albino and has two heads, though calling this a double mutation is a misnomer as the two-headed condition is a developmental abnormality and not a genetic mutation.
Similarly striking human mutations also occur occasionally.  People who are completely covered in a fur-like coat of hair are one example (see hypertrichosis). There are also cases of newborn babies having an extended tailbone or a sixth finger. 
Purely internal, less obvious mutations are more common; a small fraction of these cause serious medical conditions or death.  (The ratio is probably under 1.5%, as only about 1.5% of the genome encodes protein genes)

# Wild type
Wild type (sometimes written wildtype, wild-type or +) is the genetic term used in texts for the typical form of an organism, strain, gene, or characteristic as it was first observed in nature.  .  Wild type refers to the most common phenotype in the natural population, however this may, over a period of time, be replaced by a mutant form, which then becomes the new wildtype. The phenotype can be dominant or recessive.  Naturally occurring mutant phenotypes play a role in evolution.
NBEAL2
Neurobeachin-like 2 is a protein that in humans is encoded by the NBEAL2 gene.

# Function
The protein encoded by this gene contains a beige and Chediak-Higashi (BEACH) domain and multiple WD40 domains, and may play a role in megakaryocyte alpha-granule biogenesis.

# Clinical relevance
Mutation in this gene have been shown to cause gray platelet syndrome.
NBPF10
Neuroblastoma breakpoint family member 10 is a protein that in Homo sapiens is encoded by the NBPF10 gene.
The full gene is 75,313 bp, with the major isoform of mRNA being 10,697 bp long. The gene is located at 1q21.1. NBPF contains what is known as the DUF1220 repeats. The  highly conserved, repeated region is believed to be originated from MGC8902. The NBPF family has been linked to primate evolution. It is assumed to be related to the 1q21.1 deletion syndrome and 1q21.1 duplication syndrome.

# Homology
Paralogs of NBPF10 includes other NBPF family members.
Orthologs of NBPF10 are found in other primates; distant orthologs are found in bovine, equine, and canine
NBPF10 paralogs and orthologs unrooted phylogenetic tree

# Functional role
Although NBPF10's function is unknown, there is reason to believe that NBPF10 is an important biomarker for the Odontoblast Phenotype

# Gene Neighborhood
NOTCH2NL, SEC22B, HFE2, TXNIP are close neighbors of NBPF10.  All of these neighboring genes are well studied in their own right.
NBPF10's chromosomal location

# Post-translational modification
NBPF10 has extremely low threonine content which may make the protein less susceptible to post-translational modification.
NBPF16
Neuroblastoma Breakpoint Family, Member 16, also known as NBPF16, is a protein which in humans is encoded by the NBPF16 gene. The gene is 18762 bp long, with mRNA that is 3837 bp long.  The gene is located on chromosome 1q21.1.  Its sub-cellular location is predicted to be in the nucleus and cytoplasm. It contains what is known as the NBPF repeat, which is a two exon stretch of sequence that is characteristic of all 21 members of the NBPF gene family.  The repeat is considered the ancestral exons, and the NBPF family has been linked to primate evolution.

# Function
The function of NBPF16 is not fully understood.  It is a member of the NBPF family of proteins, which have been linked to possible roles in oncogenesis and tumor suppressor genes.

# Protein
The protein is composed of 670 amino acids.  The gene contains five domains of unknown function, called DUF1220.  DUF1220 domains are found in all members of the NBPF gene family, although the number differs between each member.  Repetitive structure with high intergenic and intragenic sequence conservation, both in coding and noncoding regions.  Makes it possible for homologous recombination to occur easily between different alleles.  The repetitiveness of it, and the other members of the NBPF gene family is thought to have arisen from segmental duplications on chromosome 1.

## Predicted properties
Properties of NBPF16 that were predicted using Bioinformatics tools:
- Molecular Weight: 76 kD
- Isoelectric point: 4.43
- Post-translational modification: None predicted.
- No predicted Signal Peptide or signal peptide cleavage site.
- No interacting proteins or binding partners.

## Expression
There is little to no expression data available for the gene, but most indications point to it being ubiquitously expressed throughout the body.

# Homology

## Orthologs
There exists no great orthologs outside of primates.  These orthologs were gathered from BLAT. and BLAST searches

## Paralogs
Due to there being 21 other members of the NBPF gene family, there are 21 paralogs of NBPF16.  They all show high conservation and repetitive structures.
NBPF19
Neuroblastoma breakpoint family member 19, or NBPF19, is a protein that in humans is encoded by the NBPF19 gene. This protein is included in the neuroblastoma breakpoint family of proteins.

# Gene
The NBPF19 gene is a protein-encoding gene in humans. It is composed of 80,464 bases including all introns and exons. It is located on the positive strand of chromosome 1 at locus 1q21.2.

## Expression
EST profiling of NBPF19 shows it to be ubiquitously expressed in most human tissues at unremarkable amounts. It is expressed in relatively higher amounts in the skin, lymphoid organs (lymph nodes, spleen) and the gonads (ovary, testes).

## Transcript
The mRNA transcript of NBPF19 in humans is 13,190 bases long. There are 2 predicted alternative splicing isoforms, although none have been experimentally observed.

# Protein
The protein product of the NBPF19 transcript is composed of 3,843 amino acids and weights 440.5 kD. It contains 45 DUF1220 domains of unknown function but that have been linked to evolutionary changes and generally decrease in number in species increasingly evolutionarily distant from humans.

## Structure
NBPF19 is expected to undergo many post-translational modifications, most notably phosphorylation and sumoylation. The protein is extensively phosphorylated on serine, threonine and tyrosine residues in a repetitive pattern seen in the figure to the left. There are 14 predicted repeats within the protein sequence likely to be sites of sumoylation.
The tertiary structure of NBPF19  is predicted to be roughly 50% coiled-coil and 40% alpha helical. There is no presence of a signal peptide or any transmembrane domains. NBPF19 is likely localized to the nucleus due to the presence of a nuclear localization signal near its 5' terminus.

# Homology
NBPF19 is one of 26 identified members of the neuroblastoma breakpoint family of proteins in humans. Sequence similarity among these proteins is largely limited to conservation of DUF1220 domains. The most highly-similar paralogs are listed below:
NBPF19 is not well conserved outside of humans and any notable conservation does not extend past primates and mammals. Select species possess short sequences of similarity and are listed below:
- Pan troglodytes (common chimpanzee)
- Pongo abelii (Sumatran orangutan)
- Piliocolobus tephrosceles (Ugandan red colobus)
- Bos taurus (cow)
- Felis catus (cat)
- Camelus ferus (Bactrian camel)
- Sus scrofa (wild boar)
- Equus asinus (donkey)
NDUFA2
NADH dehydrogenase  1 alpha subcomplex subunit 2 is a protein that in humans is encoded by the NDUFA2 gene. The NDUFA2 protein is a subunit of NADH dehydrogenase (ubiquinone), which is located in the mitochondrial inner membrane and is the largest of the five complexes of the electron transport chain. Mutations in the NDUFA2 gene are associated with Leigh's syndrome.

# Structure
The NDUFA2 gene is located on the long (q) arm of chromosome 5 at position 31.2 and it spans 2,422 base pairs. The NDUFA2 gene produces an 11 kDa protein composed of 99 amino acids. NDUFA2 is a subunit of the enzyme NADH dehydrogenase (ubiquinone), the largest of the respiratory complexes. The structure is L-shaped with a long, hydrophobic transmembrane domain and a hydrophilic domain for the peripheral arm that includes all the known redox centers and the NADH binding site. NDUFA2 is one of about 31 hydrophobic subunits that form the transmembrane region of Complex I. It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of Complex I. The highly conserved two-domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH:ubiquinone oxidoreductase complex at the inner mitochondrial membrane.

# Function
The human NDUFA2 gene codes for a subunit of Complex I of the respiratory chain, which transfers electrons from NADH to ubiquinone. NDUFA2 is an accessory subunit of Complex I that is believed not to be involved in catalysis but may be involved in regulating Complex I activity or its assembly via assistance in redox processes. Initially, NADH binds to Complex I and transfers two electrons to the isoalloxazine ring of the flavin mononucleotide (FMN) prosthetic arm to form FMNH2. The electrons are transferred through a series of iron-sulfur (Fe-S) clusters in the prosthetic arm and finally to coenzyme Q10 (CoQ), which is reduced to ubiquinol (CoQH2). The flow of electrons changes the redox state of the protein, resulting in a conformational change and pK shift of the ionizable side chain, which pumps four hydrogen ions out of the mitochondrial matrix.

# Clinical significance
Mutations in the NDUFA2 gene can result in Leigh's syndrome, a severe neurological disorder that typically arises in the first year of life. One such mutation interferes with normal splicing patterns and results in exon 2 being skipped. This causes a reduction in Complex I activity and disturbs its assembly. The NDUFA2 mutation is also associated with the depolarization of the mitochondria.

# Interactions
NDUFA2 has many protein interactions, including interactions with other members of the NADH dehydrogenase  1 alpha subcomplex, other subunits of Complex I as well as with redox proteins. This may be due to its potential role in Complex I assembly and assistance in redox processes.
NDUFA3
NADH dehydrogenase  1 alpha subcomplex subunit 3 is a protein that in humans is encoded by the NDUFA3 gene. The NDUFA3 protein is a subunit of NADH dehydrogenase (ubiquinone), which is located in the mitochondrial inner membrane and is the largest of the five complexes of the electron transport chain.

# Structure
The NDUFA3 gene is located on the q arm of chromosome 19 at position 13.42, and it has a total span of 4,123 base pairs. The NDUFA3 gene produces an 9.3 kDa protein composed of 84 amino acids. NDUFA3 is a subunit of the enzyme NADH dehydrogenase (ubiquinone), the largest of the respiratory complexes. The structure is L-shaped with a long, hydrophobic transmembrane domain and a hydrophilic domain for the peripheral arm that includes all the known redox centers and the NADH binding site. NDUFA3 is one of about 31 hydrophobic subunits that form the transmembrane region of Complex I. It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of Complex I. The highly conserved two-domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH:ubiquinone oxidoreductase complex at the inner mitochondrial membrane.

# Function
The human NDUFA3 gene codes for a subunit of Complex I of the respiratory chain, which transfers electrons from NADH to ubiquinone. However, NDUFA3 is an accessory subunit of the complex that is believed not to be involved in catalysis. Initially, NADH binds to Complex I and transfers two electrons to the isoalloxazine ring of the flavin mononucleotide (FMN) prosthetic arm to form FMNH2. The electrons are transferred through a series of iron-sulfur (Fe-S) clusters in the prosthetic arm and finally to coenzyme Q10 (CoQ), which is reduced to ubiquinol (CoQH2). The flow of electrons changes the redox state of the protein, resulting in a conformational change and pK shift of the ionizable side chain, which pumps four hydrogen ions out of the mitochondrial matrix.

# Interactions
NDUFA3 has been shown to interact with ubiquitin C, a polyubiquitin precursor.
NDUFA6
NADH dehydrogenase  1 alpha subcomplex subunit 6 is an enzyme that in humans is encoded by the NDUFA6 gene. The NDUFA6 protein is a subunit of NADH dehydrogenase (ubiquinone), which is located in the mitochondrial inner membrane and is the largest of the five complexes of the electron transport chain.

# Structure
The NDUFA6 gene is located on the q arm of chromosome 22 in position 13.2 and spans 5,359 base pairs. The gene produces an 18 kDa protein composed of 154 amino acids. NDUFA6 is a subunit of the enzyme NADH dehydrogenase (ubiquinone), the largest of the respiratory complexes. The structure is L-shaped with a long, hydrophobic transmembrane domain and a hydrophilic domain for the peripheral arm that includes all the known redox centers and the NADH binding site. It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of Complex I. The highly conserved two-domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH dehydrogenase (ubiquinone) complex at the inner mitochondrial membrane. NDUFA6 is one of about 31 hydrophobic subunits that form the transmembrane region of Complex I. The predicted secondary structure is primarily alpha helix, but the carboxy-terminal half of the protein has high potential to adopt a coiled-coil form. The amino-terminal part contains a putative beta sheet rich in hydrophobic amino acids that may serve as mitochondrial import signal. Related pseudogenes have also been identified on four other chromosomes.

# Function
The human NDUFA6 gene codes for a subunit of Complex I of the respiratory chain, which transfers electrons from NADH to ubiquinone. Initially, NADH binds to Complex I and transfers two electrons to the isoalloxazine ring of the flavin mononucleotide (FMN) prosthetic arm to form FMNH2. The electrons are transferred through a series of iron-sulfur (Fe-S) clusters in the prosthetic arm and finally to coenzyme Q10 (CoQ), which is reduced to ubiquinol (CoQH2). The flow of electrons changes the redox state of the protein, resulting in a conformational change and pK shift of the ionizable side chain, which pumps four hydrogen ions out of the mitochondrial matrix.