Persius/hicric huggingface dataset:
MBD1
Methyl-CpG-binding domain protein 1 is a protein that in humans is encoded by the MBD1 gene. The protein encoded by MBD1 binds to methylated sequences in DNA, and thereby influences transcription.  It binds to a variety of methylated sequences, and appears to mediate repression of gene expression.  It has been shown to play a role in chromatin modification through interaction with the histone H3K9 methyltransferase SETDB1. H3K9me3 is a repressive modification.

# Function
DNA methylation is the major modification of eukaryotic genomes and plays an essential role in mammalian development. Human proteins MECP2, MBD1, MBD2, MBD3, and MBD4 comprise a family of nuclear proteins related by the presence in each of a methyl-CpG binding domain (MBD). Each of these proteins, with the exception of MBD3, is capable of binding specifically to methylated DNA. MECP2, MBD1 and MBD2 can also repress transcription from methylated gene promoters.  Five transcript variants of the MBD1 are generated by alternative splicing resulting in protein isoforms that contain one MBD domain, two to three cysteine-rich (CXXC) domains, and some differences in the COOH terminus.  All five transcript variants repress transcription from methylated promoters; in addition, variants with three CXXC domains also repress unmethylated promoter activity.  MBD1 and MBD2 map very close to each other on chromosome 18q21.

# Interactions
MBD1 has been shown to interact with ATF7IP, CBX5, CHAF1A and SUV39H1.
MBD3
Methyl-CpG-binding domain protein 3 is a protein that in humans is encoded by the MBD3 gene.

# Function
DNA methylation is the major modification of eukaryotic genomes and plays an essential role in mammalian development. Human proteins MECP2, MBD1, MBD2, MBD3, and MBD4 comprise a family of nuclear proteins related by the presence in each of a methyl-CpG binding domain (MBD). However, unlike the other family members, MBD3 is not capable of binding to methylated DNA but instead binds to hydroxymethylated DNA. The predicted MBD3 protein shares 71% and 94% identity with MBD2 (isoform 1) and mouse Mbd3.  MBD3 is a subunit of the NuRD, a multisubunit complex containing nucleosome remodeling and histone deacetylase activities. MBD3 mediates the association of metastasis-associated protein 2 (MTA2) with the core histone deacetylase complex.
MBD3 also contains the coiledcoil domain common to all three MBD3 isoforms. The coiledcoil domain, but not the MBD domain, helps to maintain pluripotency of embryonic stem cells via the recruitment of polycomb repressive complex 2 to a subset of genes linked to development and organogenesis, thus establishing stable transcriptional repression.

# Interactions
MBD3 has been shown to interact with:
- AURKA,
- GATAD2B,
- HDAC1,
- MTA2, and
- MBD2.
MBDB
MBDB, or 3,4-methylenedioxy-alpha-ethyl-N-methylphenethylamine, is a lesser-known hallucinogenic phenethylamine.  It is also known as "EDEN" or "Methyl-J." It is the alpha-ethyl-N-methyl analog of MDMA (Esctasy).  It was first synthesized by David E. Nichols, a leading pharmacologist and chemist, and later tested by Alexander Shulgin and written up in his book, PiHKAL (Phenethylamines I Have Known and Loved). MBDB's dosage, according to PiHKAL, is 180-210 mg; the proper dosage relative to body mass seems unknown.  Its duration is 4-6 hours, with noticeable after-effects lasting for 1-3 hours.
MBDB causes many mild, MDMA-like effects, such as lowering of social barriers and inhibitions, a pronounced sense of empathy and compassion, and mild happiness, euphoria, and enhanced emotions are all present. However, MBDB's effects are much less profound then those of MDMA. MBDM's effects tend to produce less euphoria, less psychedelia, and have less stimulative properties than MDMA does. Many users declare that MBDB is a "watered-down" version of MDMA as MBDB loses action much more quickly, due to the milder effects, lack of a "rush," and its sedative effects. As with MDMA, users are at risk for acute dehydration if participating in strenuous physical activity and forget to drink water, as the drug may mask one's normal sense of exhaustion and thirst.

# Dangers
- DO NOT take MBDB if you are on an MAOI. MAOIs (Monoamine oxidase inhibitors) are most common in antidepressants. Ask your pharmacist/doctor if your medication contains any MAOIs. The combination is dangerous and could be lethal.*
- DO NOT Operate any machinery or anything else that can potentially harm you while under the influence of MBDB.
MCEF
MCEF or Major Cdk9-interacting elongation factor is a transcription factor related to Af4.  It is the fourth member of the Af4 family (AFF) of transcription factors, involved in numerous pathologies, including Acute Lymphoblastic Leukemia (ALL), abnormal CNS development, breast cancer and azoospermia.
Because it apparently interacts with the species-specific human co-factor (P-TEFb) for HIV-1 transcription, and because it can repress HIV-1 replication, MCEF (also known as AFF4 or AF5q31) may have future therapeutic uses.
MCEF was originally cloned and named by Mario Clemente Estable of Ryerson University, while he was a post-doctoral fellow in the laboratory of Robert G. Roeder, at the Rockefeller University.
MCL1
Induced myeloid leukemia cell differentiation protein Mcl-1 is a protein that in humans is encoded by the MCL1 gene.

# Function
The protein encoded by this gene belongs to the Bcl-2 family. Alternative splicing occurs at this locus and two transcript variants encoding distinct isoforms have been identified. The longer gene product (isoform 1) enhances cell survival by inhibiting apoptosis while the alternatively spliced shorter gene product (isoform 2) promotes apoptosis and is death-inducing.

# Clinical significance
Omacetaxine mepesuccinate (a drug approved for the treatment for chronic myelogenous leukemia (CML)) and Seliciclib  (which is under investigation as a potential multiple myeloma treatment) both act in part by inhibiting synthesis of Mcl-1.

# Interactions
MCL1 has been shown to interact with:
- BAK1,
- BCL2L11,
- BID,
- BAD,
- DAD1,
- PMAIP1,
- PCNA,
- TCTP  and
- TNKS
MCM6
DNA replication licensing factor MCM6 is a protein that in humans is encoded by the MCM6 gene. MCM6 is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of eukaryotic genome replication.

# Function
The MCM complex consisting of MCM6 (this protein) and MCM2, 4 and 7 possesses DNA helicase activity, and may act as a DNA unwinding enzyme.  The hexameric protein complex formed by the MCM proteins is a key component of the pre-replication complex (pre-RC) and may be involved in the formation of replication forks and in the recruitment of other DNA replication related proteins.  The phosphorylation of the complex by CDC2 kinase reduces the helicase activity, suggesting a role in the regulation of DNA replication. Mcm 6 has recently been shown to interact strongly Cdt1 at defined residues, by mutating these target residues Wei et al. observed lack of Cdt1 recruitment of Mcm2-7 to the pre-RC.

# Gene
The MCM6 gene, MCM6, is expressed at very high level. MCM6 contains 18 introns. There are 2 non overlapping alternative last exons. The transcripts appear to differ by truncation of the 3' end, presence or absence of 2 cassette exons, common exons with different boundaries.
MCM6 produces, by alternative splicing, 3 different transcripts, all with introns, putatively encoding 3 different protein isoforms.
MCM6 contains two of the regulatory regions for LCT, the gene encoding the protein lactase, located in two of the MCM6 introns, approximately 14 kb (-13910) and 22 kb (-22018) upstream of LCT. The (-13910) region, in particular, has been shown to function in vitro as an enhancer element capable of differentially activating transcription of LCT promoter.
Mutations in these regions are associated with lactose tolerance into adult life.

# Interactions
MCM6 has been shown to interact with:
- CDC45-related protein,
- MCM2,
- MCM4,
- MCM7,
- ORC1L,
- ORC2L,
- ORC4L,  and
- Replication protein A1.
MCM8
DNA replication licensing factor MCM8 is a protein that in humans is encoded by the MCM8 gene.
The protein encoded by this gene is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of eukaryotic genome replication. The hexameric protein complex formed by the MCM proteins is a key component of the pre-replication complex (pre_RC) and may be involved in the formation of replication forks and in the recruitment of other DNA replication related proteins. This protein contains the central domain that is conserved among the MCM proteins. This protein has been shown to co-immunoprecipitate with MCM4, 6 and 7, which suggests that it may interact with other MCM proteins and play a role in DNA replication. Alternatively spliced transcript variants encoding distinct isoforms have been described.

# DNA repair
MCM8-deficient mice are defective in gametogenesis and display genome instability due to impaired homologous recombination.  Male MCM8 (-/-) mice are sterile because spermatocytes are blocked in meiotic prophase I.  Female MCM8(-/-) mice have arrested primary follicles and frequently develop ovarian tumors.  MCM8 protein forms a complex with MCM9.
In the plant Arabidopsis thaliana, MCM8 is required for a pathway of meiotic DNA double-strand break repair.  It was proposed that MCM8 is involved with RAD51 in a backup pathway that repairs meiotic double-strand breaks without yielding crossovers when the major recombination pathway, which relies on DMC1, fails.
MCM8 forms a complex with MCM9 that is required for DNA resection by the MRN complex (MRE11-RAD50-NBS1) at double strand breaks to generate single-stranded DNA ends.  The formation of single-strand ends is an early step in homologous recombination (see Figure).   MCM8/MCM9 interacts with MRN and is required for the nuclease action and stable association of MRN with double-strand breaks.
In humans, an MCM8 mutation can give rise to premature ovarian failure, as well as chromosomal instability.
MCMI
The Millon Clinical Multiaxial Inventory-III (MCMI-III) is a psychological assessment tool intended to provide information on psychopathology, including specific disorders outlined in the DSM-IV. It is intended for adults (18 and over) with at least an 8th grade reading level. It is composed of 175 true-false questions that reportedly takes 25-30 minutes to complete. It was created by Theodore Millon, Carrie Millon, Roger Davis, and Seth Grossman.
The test is modeled on four scales
- 14 Personality Disorder Scales
- 10 Clinical Syndrome Scales
- Correction Scales (which help detect inaccurate responding)
- 42 Grossman Personality Facet Scales (based on Seth Grossman's theories of personality and psychopathology)
The test was normed on a sample of 998 male and female adults with a wide variety of clinical disorders.

# Scoring System
The major scales are divided in four ranges: normal (0-60), tendency (61-75), trait (76-85), and personality disorder (86-115).
MCPA
MCPA (2-methyl-4-chlorophenoxy-acetic acid, IUPAC (4-chloro-2-methylphenoxy)acetic acid, C9H9ClO3) is a powerful and selective phenoxy herbicide. The pure compound is brown-colored powder.

# History
Synthesis of MCPA was first reported by Synerholme and Zimmerman in 1945 and by Templeman and Foster in 1946. Templeman and Foster were searching for a compounds with similar or greater selective activity than a-napthylacetic acid in inhibiting the growth of weeds while not adversely affecting the growth of cereal grains. They synthesized MCPA from the corresponding phenol by exposing it to chloroacetic acid and dilute base in a straightforward substitution reaction.

# Chemical use
Because it is inexpensive MCPA is used in various chemical applications. Its carboxylic acid group allows the formation of conjugated complexes with metals (see below). The acid functionality makes MCPA a versatile synthetic intermediate for more complex derivatives.

# Commercial use
MCPA is used as an herbicide, generally as its salt or esterified forms. Used thus, it controls broadleaf weeds, including thistle and dock, in cereal crops and pasture. It is selective for plants with broad leaves, and this includes most deciduous trees. Clovers are tolerant at moderate application levels. It is currently classified as a restricted use pesticide. Its toxicity and biodegradation are topics of current research. Though not extremely toxic, it has recently been determined that MCPA can form complexes with metal ions and thereby increase their bioavailability, though there is also work being done to utilize this ability.

## Brand names
The following commercial products contain MCPA.
- Agritox
- Agroxone
- Chiptox
- Chwastox
- Cornox
- Methoxone
- Rhonox
- Tigrex
- Verdone Extra (UK)
- Weed-Rhap
- Weed'n'Feed
- Zero Bindii & Clover Weeder (Aus)
MDA5
MDA5 (Melanoma Differentiation-Associated protein 5) is a RIG-I-like receptor dsRNA helicase enzyme that in humans is encoded by the IFIH1 gene. MDA5 is part of the RIG-I-like receptor (RLR) family, which also includes RIG-I and LGP2, and functions as a pattern recognition receptor (recognizing dsRNA) that is a sensor for viruses. MDA5 typically recognizes dsRNA that is over 2000nts in length. For many viruses, effective MDA5-mediated antiviral responses are dependent on functionally active LGP2. The signaling cascades in MDA5 is initiated via CARD domain.

# Function
DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are implicated in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Based on their distribution patterns, some members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. This gene encodes a DEAD box protein that is upregulated in response to treatment with beta-interferon (IFNB) and a protein kinase C-activating compound, mezerein (MEZ). Irreversible reprogramming of melanomas can be achieved by treatment with both these agents; treatment with either agent alone only achieves reversible differentiation.

# Clinical significance
Mutations in IFIH1/MDA5 are associated to                 Singleton-Merten Syndrome             and to AicardiGoutieres syndrome.
Antibodies against MDA5 are associated to amyopathic dermatomyositis with rapidly progressive interstitial lung disease.
MDH1
Malate dehydrogenase, cytoplasmic also known as malate dehydrogenase 1 is an enzyme that in humans is encoded by the MDH1 gene.

# Function
Malate dehydrogenase catalyzes the reversible oxidation of malate to oxaloacetate, utilizing the NAD/NADH cofactor system in the citric acid cycle. The protein encoded by this gene is localized to the cytoplasm and may play pivotal roles in the malate-aspartate shuttle that operates in the metabolic coordination between cytosol and mitochondria and clitera. Alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.

# Regulation
The acetylation of MDH1 activates its enzymatic activity and enhance intracellular levels of NADPH, which promotes adipogenic differentiation.
Methylation on arginine 248 (R248) negatively regulates MDH1. Protein arginine methyltransferase 4 (PRMT4/CARM1) methylates and inhibits MDH1 by disrupting its dimerization. Arginine methylation of MDH1 represses mitochondria respiration and inhibits glutamine utilization. CARM1-mediated MDH1 methylation reduces cellular NADPH level and sensitizes cells to oxidative stress. Besides, MDH1 methylation suppresses cell growth and clonogenic activity. R248 of MDH1 is hypomethylated in pancreatic ductal adenocarcinoma.

# Interactive pathway map
Click on genes, proteins and metabolites below to link to respective articles. 
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MDM4
Protein Mdm4 is a protein that in humans is encoded by the MDM4 gene.

# Function
The human MDM4 gene, which plays a role in apoptosis, encodes a 490-amino acid protein containing a RING finger domain and a putative nuclear localization signal. The MDM4 putative nuclear localization signal, which all Mdm proteins contain, is located in the C-terminal region of the protein. The mRNA is expressed at a high level in thymus and at lower levels in all other tissues tested. MDM4 protein produced by in vitro translation interacts with p53 via a binding domain located in the N-terminal region of the MDM4 protein. MDM4 shows significant structural similarity to p53-binding protein MDM2

# Interactions
MDM4 has been shown to interact with E2F1, Mdm2 and P53.
MDN1
MDN1, midasin homolog (yeast) is a protein that in humans is encoded by the MDN1 gene.

# Model organisms
Model organisms have been used in the study of MDN1 function. A conditional knockout mouse line, called Mdn1tm1a(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.
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Twenty four tests were carried out on mutant mice and three significant abnormalities were observed.  No homozygous mutant embryos were identified during gestation, and therefore none survived until weaning. The remaining tests were carried out on heterozygous mutant adult mice; females had an increased susceptibility to bacterial infection.
MECR
Trans-2-enoyl-CoA reductase, mitochondrial is an enzyme that in humans is encoded by the MECR gene.

# Structure
The MECR gene is located on the 1st chromosome, with its specific location being 1p35.3. The gene contains 15 exons. MECR encodes a 21.2 kDa protein that is composed of 189 amino acids; 10 peptides have been observed through mass spectrometry data.

# Function
mtFAS is a co-factor for several mitochondrial enzymes that synthesize lipoic acid that is essential for aerobic metabolism.
A Purkinje cell specific knock out of the Mecr gene in mice leads to neurodegeneration.

# Clinical significance
Genetic mutations to MECR have been suggested to cause MEPAN Syndrome, a neurometabolic disorder in humans that involves disruptions in the pathway involved in mitochondrial fatty acid synthesis (mtFAS).  MEPAN patients were found to harbor recessive mutations in MECR, and typically present with childhood-onset dystonia, optic atrophy, and basal ganglia signal abnormalities on MRI.
MED1
Mediator of RNA polymerase II transcription subunit 1 also known as DRIP205 or Trap220 is a subunit of the Mediator complex and is a protein that in humans is encoded by the MED1 gene. MED1 functions as a nuclear receptor coactivator.

# Function
The activation of gene transcription is a multistep process that is triggered by factors that recognize transcriptional enhancer sites in DNA. These factors work with co-activators to direct transcriptional initiation by the RNA polymerase II apparatus. The mediator of RNA polymerase II transcription subunit 1 protein is a subunit of the CRSP (cofactor required for SP1 activation) complex, which, along with TFIID, is required for efficient activation by SP1. This protein is also a component of other multisubunit complexes . It also regulates p53-dependent apoptosis and it is essential for adipogenesis. This protein is known to have the ability to self-oligomerize.

# Interactions
MED1 has been shown to interact with:
- Androgen receptor,
- BRCA1,
- Calcitriol receptor,
- Cyclin-dependent kinase 8,
- Estrogen receptor alpha,
- Glucocorticoid receptor,
- Hepatocyte nuclear factor 4 alpha,
- P53,
- PPARGC1A,
- PPARG,
- TGS1,  and
- Thyroid hormone receptor alpha.

# Protein family
This entry represents subunit Med1 of the Mediator complex. The Med1 forms part of the Med9 submodule of the Srb/Med complex. It is one of three subunits essential for viability of the whole organism via its role in environmentally-directed cell-fate decisions.
MEFV
MEFV (Mediterranean fever) is a human gene that provides instructions for making a protein called pyrin (also known as marenostrin). Pyrin is produced in certain white blood cells (neutrophils, eosinophils and monocytes) that play a role in inflammation and in fighting infection. Inside these white blood cells, pyrin is found with the cytoskeleton, the structural framework that helps to define the shape, size, and movement of a cell. Pyrin's protein structure also allows it to interact with other molecules involved in fighting infection and in the inflammatory response.
Although pyrin's function is not fully understood, it likely assists in keeping the inflammation process under control. Research indicates that pyrin helps regulate inflammation by interacting with the cytoskeleton. Pyrin may direct the migration of white blood cells to sites of inflammation and stop or slow the inflammatory response when it is no longer needed.
The MEFV gene is located on the short (p) arm of chromosome 16 at position 13.3, from base pair 3,292,027 to 3,306,626.

# Related conditions
More than 80 MEFV mutations that cause familial Mediterranean fever have been identified. A few mutations delete small amounts of DNA from the MEFV gene, which can lead to an abnormally small protein. Most MEFV mutations, however, change one of the protein building blocks (amino acids) used to make pyrin. The most common mutation replaces the amino acid methionine with the amino acid valine at protein position 694 (written as Met694Val or M694V). Among people with familial Mediterranean fever, this particular mutation is also associated with an increased risk of developing amyloidosis, a complication in which abnormal protein deposits can lead to kidney failure. Some evidence suggests that another gene, called SAA1, can further modify the risk of developing amyloidosis among people with the M694V mutation.
MEFV mutations lead to reduced amounts of pyrin or a malformed pyrin protein that cannot function properly. As a result, pyrin cannot perform its presumed role in controlling inflammation, leading to an inappropriate or prolonged inflammatory response. Fever and inflammation in the abdomen, chest, joints, or skin are signs of familial Mediterranean fever.