Persius/hicric huggingface dataset:
MFN2
Mitofusin-2 is a protein that in humans is encoded by the MFN2 gene. Mitofusins are GTPases embedded in the outer membrane of the mitochondria. In mammals MFN1 and MFN2 are essential for mitochondrial fusion. In addition to the mitofusins, OPA1 regulates inner mitochondrial membrane fusion, and DRP1 is responsible for mitochondrial fission.

# Function
Mitofusin-2 is a mitochondrial membrane protein that participates in mitochondrial fusion and contributes to the maintenance and operation of the mitochondrial network. Mitochondria function as a dynamic network constantly undergoing fusion and fission. The balance between fusion and fission is important in maintaining the integrity of the mitochondria and facilitates the mixing of the membranes and the exchange of DNA between mitochondria. MFN1 and MFN2 mediate outer membrane fusion while OPA1 is involved in inner membrane fusion.
Mitochondrial fusion is essential for embryonic development. knockout mice for either MFN1 or MFN2 have fusion deficits and die midgestation. MFN2 knockout mice die at embryonic day 11.5 due to a defect in the giant cell layer of the placenta.
Fusion is also important for mitochondrial transport and localization in neuronal processes. Conditional MFN2 knockout mice show degeneration in the Purkinje cells of the cerebellum, as well as improperly localized mitochondria in the dendrites. MFN2 also associates with the MIRO-Milton complex which links the mitochondria to the kinesin motor.

# Clinical significance
Mutations of the gene are implicated in Charcot-Marie-Tooth disease. Charcot-Marie-Tooth disease type 2A (CMT2A) is caused by mutations in the MFN2 gene. While the symptoms of CMT2A are variable they are characterized by a sometimes early onset, severe phenotype, and optic atrophy. Mutations in OPA1 also cause optic atrophy, which suggests a common role of mitochondrial fusion in neuronal dysfunction. The exact mechanism of how mutations in MFN2 selectively cause the degeneration of long peripheral axons is not known. There is evidence suggesting that it could be due to defects in the axonal transport of mitochondria.
The MFN2 protein may play a role in the pathophysiology of obesity. Mitochondria arrest fusion by downregulating Mfn2 in obesity and diabetes, which leads to a fragmented mitochondrial network. This fragmentation is obvious in the pancreatic beta-cells in the Islets of Langerhaans and can inhibit mitochondrial quality control mechanisms such as mitophagy and autophagy - leading to a defect in insulin secretion and eventual beta-cell failure. The expression of MFN2 in skeletal muscle is proportional to insulin sensitivity in this tissue, and its expression is reduced in high-fat diet fed mice and Zucker fatty rats.
This protein is involved in the regulation of vascular smooth muscle cell proliferation.
MFNG
Beta-1,3-N-acetylglucosaminyltransferase manic fringe is an enzyme that in humans is encoded by the MFNG gene,
a member of the fringe gene family which also includes the radical fringe (RFNG) and lunatic fringe (LFNG).
They all encode evolutionarily conserved proteins that act in the Notch receptor pathway to demarcate boundaries during embryonic development. While their genomic structure is distinct from other glycosyltransferases, fringe proteins have a fucose-specific beta1,3 N-acetylglucosaminyltransferase activity that leads to elongation of O-linked fucose residues on Notch, which alters Notch signaling.
MKL1
MKL/megakaryoblastic leukemia 1 (also termed MRTFA/myocardin related transcription factor A) is a protein that in humans is encoded by the MKL1 gene.

# Function
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The protein encoded by this gene interacts with the transcription factor serum response factor, a key regulator of smooth muscle cell differentiation. It is closely related to MKL2 and myocardin. The encoded protein can shuttle between the cytoplasm and the nucleus, and may help this way transduce signals from the cytoskeleton to the nucleus.

# Clinical significance
This gene is involved in a specific translocation event that creates a fusion of this gene and the RNA-binding motif protein-15 gene. This translocation has been associated with acute megakaryocytic leukemia.
MKS1
Meckel syndrome, type 1 also known as MKS1 is a protein that in humans is encoded by the MKS1 gene.

# Function
The MKS1 protein along with meckelin are part of the flagellar apparatus basal body proteome and are required for cilium formation.

# Clinical significance
Mutations in the MKS1 are associated with Meckel syndrome or Bardet-Biedl syndrome.

# Model organisms
Model organisms have been used in the study of MKS1 function. A conditional knockout mouse line, called Mks1tm1a(EUCOMM)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.
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 two significant abnormalities were observed. The homozygous mutant embryos identified during gestation had polydactyly, oedema and eye or craniofacial defects. None survived until weaning. The remaining tests were carried out on heterozygous mutant adult mice and no further abnormalities were observed.
MLC1
Membrane protein MLC1 is a protein that in humans is encoded by the MLC1 gene.
MLC1 (also called WKL1) is the only human gene currently associated with megalencephalic leukoencephalopathy with subcortical cysts (MLC). Evidence exists for at least one other gene for MLC, but it has not been mapped or identified.

# Function
The function of this gene product is not known; however, homology to other proteins suggests that it may be an integral membrane transport protein. Mutations in this gene have been associated with megalencephalic leukoencephalopathy with subcortical cysts, an autosomal recessive neurological disorder.
The MLC1 protein contains six putative transmembrane domains (S1S6) and a pore region (P) between S5 and S6.  Furthermore, MLC1 has highest homology with the KCNA1 shaker-related voltage-gated potassium channel (Kv1.1).  This analysis suggests that MLC1 may be a cation channel.
MLH3
DNA mismatch repair protein Mlh3 is a protein that in humans is encoded by the MLH3 gene.

# Function
This gene is a member of the MutL-homolog (MLH) family of DNA mismatch repair (MMR) genes. MLH genes are implicated in maintaining genomic integrity during DNA replication and after meiotic recombination. The protein encoded by this gene functions as a heterodimer with other family members. Somatic mutations in this gene frequently occur in tumors exhibiting microsatellite instability, and germline mutations have been linked to hereditary nonpolyposis colorectal cancer type 7 (HNPCC7). Several alternatively spliced transcript variants have been identified, but the full-length nature of only two transcript variants has been determined. Orthologs of human MLH3 have also been studied in other organisms including mouse and the budding yeast Saccharomyces cerevisiae.

# Meiosis
In addition to its role in DNA mismatch repair, MLH3 protein is also involved in meiotic crossing over.  MLH3 forms a heterodimer with MLH1 that appears to be necessary for mouse oocytes to progress through metaphase II of meiosis.
The MLH1-MLH3 heterodimers promote crossovers. Recombination during meiosis is often initiated by a DNA double-strand break (DSB) as illustrated in the accompanying diagram. During recombination, sections of DNA at the 5' ends of the break are cut away in a process called resection. In the strand invasion step that follows, an overhanging 3' end of the broken DNA molecule then "invades" the DNA of an homologous chromosome that is not broken forming a displacement loop (D-loop). After strand invasion, the further sequence of events may follow either of two main pathways leading to a crossover (CO) or a non-crossover (NCO) recombinant (see Genetic recombination.  The pathway leading to a CO involves a double Holliday junction (DHJ) intermediate. Holliday junctions need to be resolved for CO recombination to be completed.
In the budding yeast Saccharomyces cerevisiae, as in the mouse, MLH3 forms a heterodimer with MLH1.  Meiotic CO requires resolution of Holliday junctions through actions of the MLH1-MLH3 heterodimer.  The MLH1-MLH3 heterodimer is an endonuclease that makes single-strand breaks in supercoiled double-stranded DNA.  MLH1-MLH3 binds specifically to Holliday junctions and may act as part of a larger complex to process Holliday junctions during meiosis.  MLH1-MLH3 heterodimer (MutL gamma) together with Exo1 and Sgs1 (ortholog of Bloom syndrome helicase) define a joint molecule resolution pathway that produces the majority of crossovers in budding yeast and, by inference, in mammals.

# Interactions
MLH3 has been shown to interact with MSH4.
MMAB
Cob(I)yrinic acid a,c-diamide adenosyltransferase, mitochondrial is an enzyme that in humans is encoded by the MMAB gene.

# Function
This gene encodes an enzyme (cob(I)yrinic acid a,c-diamide adenosyltransferase) that catalyzes the final step in the conversion of vitamin B12 into adenosylcobalamin (AdoCbl), a vitamin B12-containing coenzyme for methylmalonyl-CoA mutase.

# Clinical significance
Mutations in the gene are the cause of vitamin B12-dependent methylmalonic aciduria linked to the cblB complementation group.
MPPP
MPPP (1-methyl-4-phenyl-4-propionoxypiperidine, Desmethylprodine) is an opioid analgesic drug. It is not used in clinical practice, but has been illegally manufactured for recreational drug use. It is an analog of meperidine (Demerol), but since it is not used in medicine, the DEA has labeled it a Schedule I drug in the United States. In fact, it is the reversed ester of meperidine and is listed as having 70% of the potency of morphine.
The drug was first illicitly synthesised by a graduate student called Barry Kidston. Kidston had apparently studied a 1947 paper by Albert Zeiring. By reversing the ester of the meperidine skeleton, a drug approaching the potency of morphine was produced. However, the intermediate tertiary alcohol is liable to dehydration in acidic conditions if the reaction temperature rises above -30C, and since Kidston did not realise this and esterified the intermediate with propanoic anhydride at room temperature, MPTP was formed as a major impurity.
1-methyl-4-phenyl-1,2,5,6-tetrahydropyridine (MPP+), a metabolite of MPTP, causes rapid onset of irreversible symptoms similar to Parkinson's Disease. MPTP is metabolized to the neurotoxin MPP+ by the enzyme MAO-B, which is expressed in neurons. This selectively kills brain tissue in the area of the brain called the substantia nigra and causes Parkinsonian symptoms.
MSH4
MutS protein homolog 4 is a protein that in humans is encoded by the MSH4 gene.

# Function
The MSH4 and MSH5 proteins form a hetero-oligomeric structure (heterodimer) in yeast and humans.  In the yeast Saccharomyces cerevisiae MSH4 and MSH5 act specifically to facilitate crossovers between homologous chromosomes during meiosis.  The MSH4/MSH5 complex binds and stabilizes double Holliday junctions and promotes their resolution into crossover products.  An MSH4 hypomorphic (partially functional) mutant of S. cerevisiae showed a 30% genome wide reduction in crossover numbers, and a large number of meioses with non exchange chromosomes. Nevertheless this mutant gave rise to spore viability patterns suggesting that segregation of non-exchange chromosomes occurred efficiently. Thus, in S. cerevisiae, proper segregation apparently does not entirely depend on crossovers between homologous pairs.
The him-14 gene of the worm Caenorhabditis elegans encodes an ortholog of MSH4.  Formation of crossovers during C. elegans meiosis requires the him-14(MSH4) gene.  Loss of him-14(MSH-4) function severely reduces crossing over, resulting in lack of chiasmata between homologs and consequent missegregation. Thus, in C. elegans, segregation apparently does depend on crossovers between homologous pairs. Him-14(MSH4) functions during the pachytene stage of meiosis, indicating that it is not needed for establishing the preceding stages of pairing and synapsis of homologous chromosomes.
In an MSH4 mutant of rice, chiasma frequency was dramatically decreased to about 10% of the wild-type frequency, although the synaptonemal complex was normally installed.  It is likely that MSH4 interacts with MSH5  to promote the majority of crossovers during rice meiosis.
In general it appears that MSH4 acts during meiosis to direct the recombinational repair of some DNA double-strand breaks towards the crossover option rather than the non-cross over option (see Homologous recombination).

# Interactions
MSH4 has been shown to interact with MLH1, MSH5 and MLH3.
MSH5
MutS protein homolog 5 is a protein that in humans is encoded by the MSH5 gene.

# Function
This gene encodes a member of the mutS family of proteins that are involved in DNA mismatch repair or meiotic recombination processes. This protein is similar to a Saccharomyces cerevisiae protein that participates in meiotic segregation fidelity and crossing-over. This protein forms heterooligomers with another member of this family, mutS homolog 4. Alternative splicing results in four transcript variants encoding three different isoforms.

# Mutations
Mice homozygous for a null Msh5 mutation (Msh5-/-) are viable but sterile.  In these mice, the prophase I stage of meiosis is defective due to the disruption of chromosome pairing.  This meiotic failure leads, in male mice, to diminution of testicular size, and in female mice, to a complete loss of ovarian structures.
A genetic investigation was performed to test women with premature ovarian failure for mutations in each of four meiotic genes.  Among 41 women with premature ovarian failure two were found to be heterozygous for a mutation in the MSH5 gene; among 34 fertile women (controls) no mutations were found in the four tested genes.
These findings in mouse and human indicate that the MSH5 protein plays an important role in meiotic recombination.
In the worm Caenorhabditis elegans, the MSH5 protein is required during meiosis both for normal spontaneous and for gamma-irradiation induced crossover recombination and chiasma formation.  Meiotic recombination is often initiated by double strand breaks. MSH5 mutants retain the competence to repair DNA double-strand breaks that are present during meiosis, but they accomplish this repair in a way that does not lead to crossovers between homologous chromosomes.  The known mechanism of non-crossover recombinational repair is called synthesis dependent strand annealing (see homologous recombination; see also Bernstein et al.).  MSH5 thus appears to be employed in directing the recombinational repair of some double-strand breaks towards the cross over option rather than the non-cross over option.

# Interactions
MSH5 has been shown to interact with MSH4.
MSI1
RNA-binding protein Musashi homolog 1 also known as Musashi-1 is a protein that in humans is encoded by the MSI1 gene.

# Function
This gene encodes a protein containing two conserved tandem RNA recognition motifs and functions as an RNA binding protein that is involved in post-transcriptional gene editing.  It is a stem cell marker that controls the balance between self-renewal and terminal differentiation.

# Clinical significance
Over expression of this gene is associated with the grade of the malignancy and proliferative activity in gliomas and melanomas.
MSI1 is highly expressed in neural progenitor cells and is required for normal development of the brain. A mutation in these gene is responsible for autosomal recessive primary microcephaly. MSI1 also interacts with the Zika virus genome and may explain why these cells are highly susceptible to Zika virus infection.
MSMB
Beta-microseminoprotein is a protein that in humans is encoded by the MSMB gene. For historical reasons, the scientific literature may also refer to this protein as Prostate secretory protein 94 (PSP94), microseminoprotein (MSP), microseminoprotein-beta (MSMB), beta-inhibitin, prostatic inhibin peptide (PIP), and inhibitin like material (ILM).

# Distribution
MSMB is one of the three major proteins secreted by the epithelial cells of the prostate and has a concentration in seminal plasma of 0.5 to 1 mg/mL Two comprehensive studies of beta-microseminoprotein in tissue have shown that it is secreted by epithelial cells in many other organs: liver, lung, breast, kidney, colon, stomach, pancreas, esophagus, duodenum, salivary glands, fallopian tube, corpus uteri, bulbourethral glands and cervix. This list corresponds closely to the sites from which all late onset cancers develop.

# Evolution and structure
MSMB is a rapidly evolving protein. Solution structures of human and porcine MSMB show remarkable similarity despite having only 51% of amino acids in common. The C-terminus domain of MSMB contains two two-stranded -sheets; these have no resemblance to other structural motifs. The rapid evolution of MSMB can be attributed to either sexual selection or innate pathogen defense; the wide distribution of MSMB in the body and the fungicidal properties of the C-terminus suggest that innate pathogen defense plays a role in driving this evolution.

# Function
Beta-microseminoprotein is a member of the immunoglobulin binding factor family. This protein has been reported to have inhibin-like properties, though this finding has been disputed. It may have a role as an autocrine paracrine factor in uterine, breast and other female reproductive tissues. Two alternatively spliced transcript variants encoding different isoforms are described for this gene. Despite having only 4 out of 11 amino acids in common, both the porcine and human fungicidal peptide on MSMB's C-terminus are potently fungicidal in the absence of calcium ions. The protein inhibits growth of cancer cells in an experimental model of prostate cancer, though this property is cell line specific.

# Clinical significance
Two large genome-wide association studies showed that decreased expression of the MSMB protein caused by the rs10993994 single nucleotide polymorphism is associated with an increased risk of developing prostate cancer (odds ratio for CT allele pair ~1.2x, and for TT allele pair ~1.6x when compared to the low risk CC allele pair).  A 2003 study proposed using a truncated form of the MSMB protein called PSP61 as a biomarker for benign prostatic hyperplasia (BPH): this study found PSP61 in the expressed prostatic secretion of 10 out of ten 10 men suffering from BPH, but did not find it in 10 out of 10 age-matched BPH-free men. This truncated form of the MSMB protein lacks the fungicidal peptide identified in 2012. The expression of MSMB is found to be decreased in prostate cancer, so it may be used as a biomarker for prostate cancer. Urinary MSMB has been found to be superior than urinary PSA at differentiating men with prostate cancer at all Gleason grades.
MSR1
Macrophage scavenger receptor 1, also known as MSR1, is a protein which in humans is encoded by the MSR1 gene.
MSR1 has also recently been designated CD204 (cluster of differentiation 204).

# Function
This gene encodes the class A macrophage scavenger receptors, which include three different types (1, 2, 3) generated by alternative splicing of this gene. These receptors or isoforms are trimeric integral membrane glycoproteins and have been implicated in many macrophage-associated physiological and pathological processes including atherosclerosis, Alzheimer's disease, and host defense. They were thought to be expressed macrophage-specific, but recently shown to be present on different dendritic cells classes, too.
The isoforms type 1 and type 2 are functional receptors and are able to mediate the endocytosis of modified low density lipoproteins (LDLs). The isoform type 3 does not internalize modified LDL (acetyl-LDL) despite having the domain shown to mediate this function in the types 1 and 2 isoforms. It has an altered intracellular processing and is trapped within the endoplasmic reticulum, making it unable to perform endocytosis. The isoform type 3 can inhibit the function of isoforms type 1 and type 2 when co-expressed, indicating a dominant negative effect and suggesting a mechanism for regulation of scavenger receptor activity in macrophages.

# Biotechnology application
Macrophage scavenger receptor has been shown to mediate adhesion of macrophages and other cell lines to tissue culture plastic.

# Interactions
MSR1 has been shown to interact with HSPA1A.
MTDH
Metadherin, also known as protein LYRIC or astrocyte elevated gene-1 protein (AEG-1) is a protein that in humans is encoded by the MTDH gene.

# Function
AEG-1 is involved in HIF-1alpha mediated angiogenesis. AEG-1 also interacts with SND1 and involved in RNA-induced silencing complex (RISC) and plays very important role in RISC and miRNA functions.
AEG-1 induces an oncogene called Late SV40 factor (LSF/TFCP2) which is involved in thymidylate synthase (TS) induction and DNA biosynthesis synthesis. Late SV40 factor (LSF/TFCP2) enhances angiogenesis by transcriptionally up-regulating matrix metalloproteinase-9 (MMP9).

# Clinical significance
AEG-1 acts as an oncogene in melanoma, malignant glioma, breast cancer and hepatocellular carcinoma. It is highly expressed in these cancers and helps in progression and development of these cancers. It is induced by c-Myc oncogene and plays very important role in anchorage independent growth of cancer cells.
Elevated expression of the metastasis gene metadherin (MTDH), which is overexpressed in more than 40% of breast cancers, is associated with poor clinical outcomes. MTDH has a dual role in promoting metastatic seeding and enhancing chemoresistance. MTDH is therefore a potential therapeutic target for enhancing chemotherapy and reducing metastasis.
LSF/TFCP2 plays multifaceted role in chemo resistance, EMT, allergic response, inflammation and Alzheimers disease.
AEG-1 controls many hallmarks of oncogenes and cancer. AEG-1/MTDH induces hepato steatosis in mouse liver. The MTDH knockdown by artificial microRNA interference functions as a potential tumor suppressor in breast cancer. Astrocyte elevated gene-1/MTDH undergoes palmitoylation in normal and abnormal physiology of the cell.The microgrooved biomaterial titanium substrata can alter the expression of AEG-1 in human primary cells.
MXD1
MAD protein is a protein that in humans is encoded by the MXD1 gene.
MAD-MAX dimerization protein belongs to a subfamily of MAX-interacting proteins. This protein competes with MYC for binding to MAX to form a sequence-specific DNA-binding complex, acts as a transcriptional repressor (while MYC appears to function as an activator) and is a candidate tumor suppressor.  The MAD-MAX protein dimer may be a reference to the popular cult classic film Mad Max (1979).

# Interactions
MXD1 has been shown to interact with Histone deacetylase 2, SMC3, MLX, SIN3A and MAX.