Persius/hicric huggingface dataset:
MGST3
Microsomal glutathione S-transferase 3 is an enzyme that in humans is encoded by the MGST3 gene.
The MAPEG (Membrane-Associated Proteins in Eicosanoid and Glutathione metabolism) family consists of six human proteins, several of which are involved the production of leukotrienes and prostaglandin E, important mediators of inflammation. This gene encodes an enzyme that catalyzes the conjugation of leukotriene A4 and reduced glutathione to produce leukotriene C4. This enzyme also demonstrates glutathione-dependent peroxidase activity towards lipid hydroperoxides.

# Model organisms
Model organisms have been used in the study of MGST3 function. A conditional knockout mouse line, called Mgst3tm1a(KOMP)Wtsi was generated as part of the International Knockout Mouse Consortium program  a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists  at the Wellcome Trust Sanger Institute.
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Twenty five tests were carried out on mutant mice but no significant abnormalities were observed.
MLANA
Protein melan-A also known as melanoma antigen recognized by T cells 1 or MART-1 is a protein that in humans is encoded by the MLANA o "MALENA" gene. A fragment of the protein, usually consisting of the nine amino acids 27 to 35, is bound by MHC class I complexes which present it to T cells of the immune system. These complexes can be found on the surface of melanoma cells. Decameric peptides (26-35) are being investigated as cancer vaccines.

# Discovery and nomenclature
The names MART-1 and melan-A were coined by two groups of researchers who independently sequenced the gene for this antigen in 1994.  Both names are currently in common use.  Kawakami et al. at the National Cancer Institute coined the term MART-1, which stands for "melanoma antigen recognized by T-cells."  Coulie et al. of Belgium called the gene melan-A, presumably an abbreviation for "melanocyte antigen."

# Clinical significance
MART-1/melan-A is a protein antigen that is found on the surface of melanocytes.  Antibodies against the antigen are used in the medical specialty of anatomic pathology in order to recognize cells of melanocytic differentiation, useful for the diagnosis of a melanoma.  The same name is also used to refer to the gene which codes for the antigen.
The MART-1/melan-A antigen is specific for the melanocyte lineage, found in normal skin, the retina, and melanocytes, but not in other normal tissues.  It is thus useful as a marker for melanocytic tumors (melanomas) with the caveat that it is normally found in benign nevi as well.
In many immunological studies melan-A peptides serve as a positive control for T-cell priming experiments. This is due to the fact that its high precursor frequency of about 1/1000 among cytotoxic T-cells makes it easy for antigen presenting cells to evoke peptide-specific responses.

# Structure
MART-1/melan-A is a putative 18 kDa transmembrane protein consisting of 118 amino acids. It has a single transmembrane domain.

# Regulation
Its expression is regulated by the Microphthalmia-associated transcription factor.
MMP10
Stromelysin-2 also known as matrix metalloproteinase-10 (MMP-10) or transin-2 is an enzyme that in humans is encoded by the MMP10 gene.

# Function
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene degrades proteoglycans and fibronectin. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.

# Clinical significance
MMP10 has been linked to cancer stem cell vitality and metastasis.
MMP10 is a potential prognostic biomarker for oral cancer.
MMP14
Matrix metalloproteinase-14 is an enzyme that in humans is encoded by the MMP14 gene.

# Function
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Deficits in MMP14 leads to premature aging, short lifespan, and cell senescence in mice, suggesting an important role of MMP14 in extracellular matrix remodeling during aging. Most MMP's are secreted as inactive pro-proteins which are activated when cleaved by extracellular proteinases.
However, the protein encoded by this gene is a member of the membrane-type MMP (MT-MMP) subfamily; each member of this subfamily contains a potential transmembrane domain suggesting that these proteins are tethered to the cell surface rather than secreted.
"This protein activates MMP2 protein, and this activity may be involved in tumor invasion."

# Interactions
MMP14 has been shown to interact with TIMP2.
MMP17
Matrix metalloproteinase-17 (MMP-17) also known as membrane-type matrix metalloproteinase 4 (MT-MMP 4) is an enzyme that in humans is encoded by the MMP17 gene.

# Function
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The protein encoded by this gene is considered a member of the membrane-type MMP (MT-MMP) subfamily. However, this protein is unique among the MT-MMP's in that it is a GPI-anchored protein rather than a transmembrane protein. The protein activates MMP2 by cleavage.
In melanocytic cells MMP17 gene expression may be regulated by MITF.
MMP20
Matrix metalloproteinase-20 (MMP-20) also known as enamel metalloproteinase or enamelysin is an enzyme that in humans is encoded by the MMP20 gene.

# Function
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases.
MMP-20, also known as enamelysin, appears to be the only MMP that is tooth-specific and it is expressed by cells of different developmental origin (i.e. epithelial ameloblasts and mesenchymal odontoblasts).

# Clinical significance
The human MMP-20 gene contains 10 exons and is part of a cluster of matrix metalloproteinase genes that localize to human chromosome 11q22.3. A mutation in this gene, which alters the normal splice pattern and results in premature termination of the encoded protein, has been associated with amelogenesis imperfecta. Enamel in the absence of MMP-20 is hypoplastic (thin), contains less mineral (only one-third as much total mineral as wild type), and contains more protein and water. In general, MMP-20 functions in enamel are to cleave enamel matrix proteins at specific cleavage sites.
MOCS1
Molybdenum cofactor biosynthesis protein 1 is a protein that in humans and other animals, fungi, and cellular slime molds, is encoded by the MOCS1 gene.
Both copies of this gene are defective in patients with molybdenum cofactor deficiency, type A.
Molybdenum cofactor biosynthesis is a conserved pathway leading to the biological activation of molybdenum. The protein encoded by this gene is involved in molybdenum cofactor biosynthesis. (This gene was originally thought to produce a bicistronic mRNA with the potential to produce two proteins (MOCS1A and MOCS1B) from adjacent open reading frames. However, only the first open reading frame (MOCS1A) has been found to encode a protein from the putative bicistronic mRNA.) Two of the splice variants found for this gene express proteins (MOCS1A-MOCS1B) that result from a fusion between the two open reading frames.
MOCS2
Molybdenum cofactor synthesis protein 2A and molybdenum cofactor synthesis protein 2B are a pair of proteins that in humans are encoded from the same MOCS2 gene.  These two proteins dimerize to form molybdopterin synthase.

# Function
Eukaryotic molybdoenzymes use a unique molybdenum cofactor (MoCo) consisting of a pterin, termed molybdopterin, and the catalytically active metal molybdenum. MoCo is synthesized from cyclic pyranopterin monophosphate (precursor Z) by the heterodimeric enzyme molybdopterin synthase.

# Gene
The large and small subunits of molybdopterin synthase are both encoded from the MOCS2 gene by overlapping open reading frames. The proteins were initially thought to be encoded from a bicistronic transcript. They are now thought to be encoded from monocistronic transcripts. Alternatively spliced transcripts have been found for this locus that encode the large and small subunits.
The MOCS2 gene contains 7 exons. Exons 1 to 3 encode MOCS2A (the small subunit), and exons 3 to 7 encode MOCS2B (large subunit).

## Genetic disease
Defects in both copies of MOCS2 cause the molybdenum cofactor deficiency disease in babies.

# Protein Structure
MOCS2A and MOCS2B subunits form dimers in solution. These dimers in turn dimerize to form the tetrameric molybdopterin synthase complex.
MPV17
Protein MPV17 is a protein that in humans is encoded by the MPV17 gene. It is a mitochondrial inner membrane protein, which has a so far largely unknown role in mtDNA maintenance. Protein MPV17 is expressed in human pancreas, kidney, muscle, liver, lung, placenta, brain and heart. Human MPV17 is the orthologue of the mouse kidney disease gene, Mpv17. Loss of function has been shown to cause hepatocerebral mtDNA depletion syndromes (MDS) with oxidative phosphorylation failure and mtDNA depletion both in affected individuals and in Mpv17/ mice.

# Function
This protein was first thought to be a peroxisomal protein, but in 2006, Spinazzola demonstrated that it is a mitochondrial inner membrane protein that is implicated in the formation of reactive oxygen species (ROS).
Restoration of Mpv17 expression in a Mpv17-/- mice restore mtDNA copy number, suggesting MPV17 is involved in mtDNA copy number, and in mtDNA maintenance.
MPV17 seems to be also involved in apoptosis in podocytes, and involved in ROS.

# Structure

## Gene
The human MPV17 gene is located on chromosome 2 at p21-23, comprising eight exons encoding 176 amino acids.

## Protein
MPV17 belongs to a family of integral membrane proteins consisting of four members (PXMP2, MPV17, MP-L, and FKSG24 (MPV17L2)) in mammals and two members (Sym1 and Yor292) in yeast. The amino acid sequence of MPV17 (176 amino acids) contains four cysteine residues and three putative phosphorylation sites implies that this protein may act as a redox- and ATP-sensitive channel.

# Clinical significance
Mutations in this gene have been associated with the hepatocerebral form of mitochondrial DNA depletion syndrome (MDS), a mutation in this protein leads to an mtDNA (mitochondrial DNA) copy number decrease. By 2013, MDS caused by MPV17 mutations had been reported in 32 patients with the clinical manifestations including early progressive liver failure, neurological abnormalities, hypoglycaemia and raised blood lactate. In addition, MPV17 mutations have also been associated with autosomal recessive adult-onset neuropathy and leukoencephalopathy with multiple mtDNA deletions in skeletal muscle. Thus, MPV17 mutations can lead to recessive MDS or recessive multiple mtDNA deletion disorders.

# Interactions
MPV17 has been shown to interact with Prkdc protein during Adriamycin-induced nephropathy in mice.
MRPL3
Mitochondrial ribosomal protein L3 is a protein that in humans is encoded by the MRPL3 gene.
Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes and help in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. They have an estimated 75% protein to rRNA composition compared to prokaryotic ribosomes, where this ratio is reversed. Another difference between mammalian mitoribosomes and prokaryotic ribosomes is that the latter contain a 5S rRNA. Among different species, the proteins comprising the mitoribosome differ greatly in sequence, and sometimes in biochemical properties, which prevents easy recognition by sequence homology. This gene encodes a 39S subunit protein that belongs to the L3P ribosomal protein family. A pseudogene corresponding to this gene is found on chromosome 13q. .

# Clinical relevance
Mutations in this gene have been shown to cause mitochondrial cardiomyopathy.
MRPS5
28S ribosomal protein S5, mitochondrial is a protein that in humans is encoded by the MRPS5 gene.

# Function
Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes and help in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. They have an estimated 75% protein to rRNA composition compared to prokaryotic ribosomes, where this ratio is reversed. Another difference between mammalian mitoribosomes and prokaryotic ribosomes is that the latter contain a 5S rRNA. Among different species, the proteins comprising the mitoribosome differ greatly in sequence, and sometimes in biochemical properties, which prevents easy recognition by sequence homology. This gene encodes a 28S subunit protein that belongs to the ribosomal protein S5P family. Pseudogenes corresponding to this gene are found on chromosomes 4q, 5q, and 18q.

# Model organisms
Model organisms have been used in the study of MRPS5 function. A conditional knockout mouse line called Mrps5tm1b(EUCOMM)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
MSTO1
Protein misato homolog 1 is a protein that in humans is encoded by the MSTO1 gene.
The MSTO1 gene is 5134 base pairs (located in chromosome 1) and the MSTO1 protein is 570 aminoacids in length. It is located in the outer membrane of the mitochondrion, and is involved in the regulation of mitochondrial distribution and morphology.

# Structure
The misato protein contains an N-terminal misato segment II myosin-like domain and a central tubulin domain.
MT-TD
Mitochondrially encoded tRNA aspartic acid also known as MT-TD is a transfer RNA which in humans is encoded by the mitochondrial MT-TD gene.

# Structure
The MT-TD gene is located on the p arm of the mitochondrial DNA at position 12 and it spans 67 base pairs. The structure of a tRNA molecule is a distinctive folded structure which contains three hairpin loops and resembles a three-leafed clover.

# Function
The MT-TD gene encodes for a small transfer RNA (human mitochondrial map position 7518-7585) that transfers the amino acid aspartic acid to a growing polypeptide chain at the ribosome site of protein synthesis during translation.

# Clinical significance
MT-TD mutations have been associated with complex IV deficiency of the mitochondrial respiratory chain, also known as the cytochrome c oxidase deficiency. Cytochrome c oxidase deficiency is a rare genetic condition that can affect multiple parts of the body, including skeletal muscles, the heart, the brain, or the liver. Common clinical manifestations include myopathy, hypotonia, and encephalomyopathy, lactic acidosis, and hypertrophic cardiomyopathy. A patient with a  7526A>G mutation in the MT-TD gene exhibited gradually worsening symptoms of exercise intolerance, increased creatine kinase levels, sustained exercise leading to muscle pains and general malaise. A patient with a 7543A>G mutation also exhibited symptoms of the disease.
MT-TG
Mitochondrially encoded tRNA glycine also known as MT-TG is a transfer RNA which in humans is encoded by the mitochondrial MT-TG gene.

# Structure
The MT-TG gene is located on the p arm of the mitochondrial DNA at position 12 and it spans 68 base pairs. The structure of a tRNA molecule is a distinctive folded structure which contains three hairpin loops and resembles a three-leafed clover.

# Function
MT-TG is a small 68 nucleotide transfer RNA (human mitochondrial map position 9991-10058) that transfers the amino acid glycine to a growing polypeptide chain at the ribosome site of protein synthesis during translation.

# Clinical significance

## Myoclonic epilepsy with ragged-red fibers (MERRF)
Mutations in transfer RNAs have been found to lead to marked mitochondrial energy deficiency and a hindrance of mitochondrial proliferation, and defects in oxidative phosphorylation. Such defects may result in myoclonic epilepsy with ragged-red fibers (MERRF). Myoclonic epilepsy with ragged-red fibers (MERRF) is a rare mitochondrial disorder that affects many parts of the body, particularly the muscles and nervous system. In most cases, the signs and symptoms of this disorder appear during childhood or adolescence. The features of MERRF vary widely among affected individuals, even among members of the same family. Common clinical manifestations include myoclonus, myopathy, spasticity,epilepsy, peripheral neuropathy, dementia, ataxia, atrophy and more.

## Familial hypertrophic cardiomyopathy
Mutations in the MT-TG gene has also been associated with familial hypertrophic cardiomyopathy. Familial hypertrophic cardiomyopathy is a heart condition characterized by thickening of the heart, usually in the interventricular septum. Common phenotypes include chest pain, shortness of breath, physical exertion, palpitations, lightheadedness, dizziness and fainting. A family with a transition mutation of 9997T>C in the MT-TG gene exhibited familial hypertrophic cardiomyopathy.
MT-TI
Mitochondrially encoded tRNA isoleucine also known as MT-TI is a transfer RNA which in humans is encoded by the mitochondrial MT-TI gene.

# Structure
The MT-TI gene is located on the p arm of the mitochondrial DNA at position 12 and it spans 69 base pairs. The structure of a tRNA molecule is a distinctive folded structure which contains three hairpin loops and resembles a three-leafed clover.

# Function
MT-TI is a small 69 nucleotide RNA (human mitochondrial map position 4263-4331) that transfers the amino acid isoleucine to a growing polypeptide chain at the ribosome site of protein synthesis during translation.

# Clinical significance
Mutations in MT-TI can result in multiple mitochondrial deficiencies and associated disorders.

## Myoclonic epilepsy with ragged-red fibers (MERRF)
Mutations in the MT-TI gene have been associated with myoclonic epilepsy with ragged-red fibers (MERRF). Myoclonic epilepsy with ragged-red fibers (MERRF) is a disorder that affects many parts of the body, particularly the muscles and nervous system. In most cases, the signs and symptoms of this disorder appear during childhood or adolescence. The features of MERRF vary widely among affected individuals, even among members of the same family. Common symptoms include, myoclonus, myopathy, spasticity, epilepsy, peripheral neuropathy, dementia, ataxia, atrophy, and more.

## Cardiomyopathy
Mutations in the MT-TI gene may also cause cardiomyopathy, a disorder of the heart characterized by the thickening of the heart, usually in the interventricular septum, which results in a weakened heart muscle that is unable to pump blood effectively. It is unclear why such mutations result in the symptoms of isolated cardiomyopathy. Mutations of 4300A>G, 4295A>G, 4269A>G, and 4317A>G in the MT-TI gene have been found in patients with cardiomyopathy in varying severities and onset.

## Complex IV Deficiency
MT-TI mutations have been associated with complex IV deficiency of the mitochondrial respiratory chain, also known as the cytochrome c oxidase deficiency. Cytochrome c oxidase deficiency is a rare genetic condition that can affect multiple parts of the body, including skeletal muscles, the heart, the brain, or the liver. Common clinical manifestations include myopathy, hypotonia, and encephalomyopathy, lactic acidosis, and hypertrophic cardiomyopathy. A patient with a 4269A>G mutation in MT-TI was found with the deficiency.
MT-TN
Mitochondrially encoded tRNA asparagine also known as MT-TN is a transfer RNA which in humans is encoded by the mitochondrial MT-TN gene.

# Structure
The MT-TN gene is located on the p arm of the non-nuclear mitochondrial DNA at position 12 and it spans 73 base pairs. The structure of a tRNA molecule is a distinctive folded structure which contains three hairpin loops and resembles a three-leafed clover.

# Function
MT-TN is a small 73 nucleotide RNA (human mitochondrial map position 5657-5729) that transfers the amino acid asparagine to a growing polypeptide chain at the ribosome site of protein synthesis during translation.

# Clinical significance

## Ophthalmoplegia
Mutations in MT-TN have been associated with isolated ophthalmoplegia. Ophthalmoplegia is a condition characterized by eye muscle weakness. Common symptoms of the disorder include hearing loss, loss of sensation in the limbs, ataxia, and neuropathy. Multiple mutations of 5692A>G and 5703G>A have been found in patients with ophthalmoplegia. Such mutations in MT-TN resulted in a failure in oxidative phosphorylation and protein synthesis of the mitochondria. In addition, a 5728A>G transition of MT-TN was found to result in a combined deficiency of complex I and IV, with symptoms of failure to thrive, renal failure, and mental retardation.

## Complex IV Deficiency
MT-TN mutations have been associated with complex IV deficiency of the mitochondrial respiratory chain, also known as the cytochrome c oxidase deficiency. Cytochrome c oxidase deficiency is a rare genetic condition that can affect multiple parts of the body, including skeletal muscles, the heart, the brain, or the liver. Common clinical manifestations include myopathy, hypotonia, and encephalomyopathy, lactic acidosis, and hypertrophic cardiomyopathy. 5709T>C mutations in MT-TN have been found in patients with the deficiency.