Persius/hicric huggingface dataset:
MASTL
MASTL  is an official symbol provided by HGNC for human gene whose official name is micro tubule associated serine/threonine kinase like. This gene is 32,1 kbps long. This gene is also known as GW, GWL, THC2, MAST-L, GREATWALL. This is present in mainly mammalian cells like human, house mouse, cattle, monkey, etc. It is in the 10th chromosome of the mammalian nucleus. Recent studies have been carried on zebrafish and frogs.  This gene encodes for the protein micro tubule associated serine/threonine kinase and its sub-classes.
Micro-tubule-associated serine/threonine protein kinase is a mammalian enzyme which was first discovered in Drosophila as an essential kinase (great wall) for correct chromosome condensation and mitotic progression. The EC number for this enzyme is 2.7.11.12. This enzyme is active during mitotic division and is mainly localized in the nucleus during interphase. They get dispersed into the cytoplasm upon the degradation of nuclear envelope during mitosis. The MASTL depleted cells are delayed by RNAi in G2 phase and show a decreased condensation of the chromosomes. RNAi cells which pass through the mitosis, might not get separated into their sister chromatids in anaphase. This causes the chromatin to be trapped in the cleavage furrow and form 4N G1 cells due to cytokinesis failure. This enzyme enhances the cyclin B1-Cdk1-dependent mitotic phosphorylation events during mitosis.
This enzyme is also essential for metaphase entry by suppressing protein phosphatase 2A which will in turn leads to high level of Cdk1 substrate phosphorylation. It also provides the timely activation of APC/C during Meiosis I and Cdk1 reactivation in meiosis II.
Mutation in the gene
A missense mutation in the MASTL gene can lead to an autosomal dominant inherited thrombocytopenia. The mutation is due to the change in amino acid glutamic acid at 167 to aspartic acid. Common phenotype of a mild thrombocytopenia patient is the decrease average plate counts of 60,000 platelets per ml of blood.
Uses in the therapeutic field
MASTL enzyme is also used for therapeutic applications such as cancer progression and tumor recurrence after free cancer therapy and this enzyme can be of higher value in the therapeutic market.
MATR3
Matrin-3 is a protein that in humans is encoded by the MATR3 gene.

# Function
The protein encoded by this gene is localized in the nuclear matrix. It may play a role in transcription or may interact with other nuclear matrix proteins to form the internal fibrogranular network. Two transcript variants encoding the same protein have been identified for this gene.

# Pathology
Mutations in the Matrin 3 gene are associated with familial amyotrophic lateral sclerosis.
Wrist
In human anatomy, the wrist is the flexible and narrower connection between the forearm and the palm. The wrist is essentially a double row of small short bones, called carpals, intertwined to form a malleable hinge.
The wrist-joint (articulatio radiocarpea) is a condyloid articulation allowing three degrees of freedom.

# Structure of joint
The parts forming it are the lower end of the radius and under surface of the articular disk above; and the scaphoid, lunate, and triquetral bones below.
The articular surface of the radius and the under surface of the articular disk form together a transversely elliptical concave surface, the receiving cavity.
The superior articular surfaces of the scaphoid, lunate, and triquetrum form a smooth convex surface, the condyle, which is received into the concavity.
The bones of the wrist can be easily remembered by the mnemonic SLTPTTCH - Some Lovers Try Positions That They Can't Handle. These represent the bones in order of proximal row radial to ulnar and then distal row radial to ulnar: Scaphoid, Lunate, Triquetral, Pisiform; Trapezium, Trapezoid, Capitate, Hamate.

# Ligaments
The joint is surrounded by a capsule, strengthened by the following ligaments:
- Palmar radiocarpal ligament
- Dorsal radiocarpal ligament
- Ulnar collateral ligament (wrist)
- Radial collateral ligament (wrist)
The synovial membrane lines the deep surfaces of the ligaments above described, extending from the margin of the lower end of the radius and articular disk above to the margins of the articular surfaces of the carpal bones below. It is loose and lax, and presents numerous folds, especially behind.

# Movements
The movements permitted in this joint are flexion, extension, abduction, adduction, and circumduction. They are studied with those of the carpus, with which they are combined.
MDGA2
MDGA2 (MAM domain containing glycosylphosphatidylinositol anchor 2) is a human gene. 
It has previously been called MAMDC1.
MDGA2 is located on chromosome 14.
The gene has a homologue in rat and mouse, Mdga2,
and investigations in rats have found that the gene is expressed in the central and peripheral nervous system in a subpopulation of neurons, e.g., in the basilar pons and cerebral cortex.
There are several variants in the human gene,
and a genome-wide association study has pointed to that single-nucleotide polymorphisms in MDGA2 is associated with neuroticism. However, a more recent study has failed to replicate that finding.
MED12
Mediator of RNA polymerase II transcription, subunit 12 homolog (S. cerevisiae), also known as MED12, is a human gene found on the X chromosome.

# Clinical significance
Mutations in MED12 are responsible for at least two different forms of X-linked dominant mental retardation, Lujan-Fryns syndrome and FG syndrome, as well as instances of prostate cancer.
Mutations in MED12 are associated with uterine                 leiomyomas              and breast fibroepithelial tumors (e.g. fibroadenoma and phyllodes tumors).

# Interactions
MED12 has been shown to interact with:
- Calcitriol receptor,
- Cyclin-dependent kinase 8
- Estrogen receptor alpha,
- Gli3, G9a, PPARGC1A,
- MED26,
- SOX9, and
- Thyroid hormone receptor alpha.
MED14
Mediator of RNA polymerase II transcription subunit 14 is an enzyme that in humans is encoded by the MED14 gene.
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 protein encoded by this gene 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 e.g. thyroid hormone receptor-(TR-) associated proteins which interact with TR and facilitate TR function on DNA templates in conjunction with initiation factors and cofactors. This protein contains a bipartite nuclear localization signal. This gene is known to escape chromosome X-inactivation.

# Interactions
MED14 has been shown to interact with PPARGC1A, Estrogen receptor alpha, STAT2, Cyclin-dependent kinase 8, Glucocorticoid receptor and Hepatocyte nuclear factor 4 alpha.
MED15
Mediator of RNA polymerase II transcription subunit 15, also known as Gal11,Spt13 in yeast and  PCQAP, ARC105, or TIG-1 in humans is a protein encoded by the MED15 gene.

# Function
MED15 is a general transcriptional cofactor of the mediator complex involved in RNA polymerase II dependent transcription, originally called Gal11 and Spt13 and found in yeast as an essential factor for Gal4 dependent transactivation by T.Fukasawa and F.Winston labs. Transcription factors Gcn4, Pho4, Msn2, Ino2, members of the Gal4 family - Gal4, Oaf1, Pdr1, and viral VP16 have been reported to interact with yeast MED15.
Most of these transcription factors share the same transactivation domain, 9aaTAD, which directly interacts with KIX domain of the MED15.
Furthermore, human MED15 cooperates in mediator complex (previously known as PC2, ARC, or DRIP) with transcription factors like VP16 and  SREBP. Human SREBP regulates sterol responsive gene expression, and this regulatory action is conserved in the genetic model organism C. elegans, a roundworm (homologues MDT-15 and SBP-1). Also in C. elegans, MDT-15 is essential for the response to several stresses (fasting, heavy metal, toxin, and oxidative stress); at least in part the fasting response is conferred by interactions of MDT-15 with nuclear receptors, including NHR-49.

# Gene
The MED15 gene contains stretches of trinucleotide repeats and is located in the chromosome 22 region which is deleted in DiGeorge's syndrome. Two transcript variants encoding different isoforms have been found for this gene.
MED17
Mediator of RNA polymerase II transcription subunit 17 is an enzyme that in humans is encoded by the MED17 gene.
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 protein encoded by this gene 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 e.g. thyroid hormone receptor-(TR-) associated proteins which interact with TR and facilitate TR function on DNA templates in conjunction with initiation factors and cofactors.

# Interactions
MED17 has been shown to interact with PPARGC1A, Cyclin-dependent kinase 8 and BRCA1.
MED22
Mediator of RNA polymerase II transcription subunit 22 is an enzyme that in humans is encoded by the MED22 gene.

# Function
This gene is located in the surfeit gene cluster, a group of very tightly linked housekeeping genes that do not share sequence similarity. The gene is oriented in a head-to-head fashion with RPL7A (SURF3) and the two genes share a bidirectional promoter. The encoded proteins are localized to the cytoplasm. Two alternative transcript variants encoding different isoforms have been identified for this gene.

# Interactions
MED22 has been shown to interact with MED30.

# Model organisms
Model organisms have been used in the study of MED22 function. A conditional knockout mouse line called Med22tm1a(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
MED24
Mediator of RNA polymerase II transcription subunit 24 is an enzyme that in humans is encoded by the MED24 gene.

# Function
This gene encodes a component of the mediator complex (also known as TRAP, SMCC, DRIP, or ARC), a transcriptional coactivator complex thought to be required for the expression of almost all genes. The mediator complex is recruited by transcriptional activators or nuclear receptors to induce gene expression, possibly by interacting with RNA polymerase II and promoting the formation of a transcriptional pre-initiation complex. Multiple transcript variants encoding different isoforms have been found for this gene.

# Interactions
MED24 has been shown to interact with Estrogen receptor alpha, Cyclin-dependent kinase 8, Calcitriol receptor and BRCA1.
MED26
Mediator of RNA polymerase II transcription subunit 26 is an enzyme that in humans is encoded by the MED26 gene.
It forms part of the Mediator complex.
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 protein encoded by this gene 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 e.g. thyroid hormone receptor-(TR-) associated proteins which interact with TR and facilitate TR function on DNA templates in conjunction with initiation factors and cofactors.

# Activity
MED26 is a transcription elongation factor that increases the overall transcription rate of RNA polymerase II by reactivating transcription elongation complexes that have arrested transcription. It does this through recruiting ELL/EAF- and P-TEFb- containing complexes to promoters via a direct interaction with the N-terminal domain (NTD). The MED26 NTD also binds TFIID, and TFIID and elongation complexes interact with MED26 through overlapping binding sites.
MED26 NTD may function as a molecular switch contributing to the transition of Pol II into productive elongation.
The three structural domains of TFIIS are conserved from yeast to human. The 80 or so N-terminal residues form a protein interaction domain containing a conserved motif, which has been called the LW motif because of the invariant leucine and tryptophan residues it contains. Although the N-terminal domain is not needed for transcriptional activity, a similar sequence has been identified in other transcription factors and proteins that are predominantly nuclear localized,:
- MED26 (also known as CRSP70 and ARC70), a subunit of the Mediator complex, which is required for the activity of the enhancer-binding protein Sp1.
- Elongin A, a subunit of a transcription elongation factor previously known as SIII. It increases the rate of transcription by suppressing transient pausing of the elongation complex.
- PPP1R10, a nuclear regulatory subunit of protein phosphatase 1 that was previously known as p99, FB19 or PNUTS.
- PIBP, a small hypothetical protein that could be a phosphoinositide binding protein.
- IWS1, which is thought to function in both transcription initiation and elongation. The TFIIS N-terminal domain is a compact four-helix bundle. The hydrophobic core residues of helices 2, 3, and 4 are well conserved among TFIIS domains, although helix 1 is less conserved.

# Interactions
MED26 has been shown to interact with MED8, Cyclin-dependent kinase 8, POLR2A, MED12 and MED28. It also acts synergistically to mediate the interaction between REST (a Kruppel-type zinc finger transcription factor that binds to a 21-bp RE1 silencing element present in over 900 human genes) and Mediator.
MED27
Mediator of RNA polymerase II transcription subunit 27 is an enzyme that in humans is encoded by the MED27 gene. It forms part of the Mediator complex.
The ubiquitous expression of Med27 mRNA suggests a universal requirement for Med27 in transcriptional initiation. Loss of Crsp34/Med27 decreases amacrine cell number, but increases the number of rod photoreceptor cells.
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 protein encoded by this gene 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 e.g. thyroid hormone receptor-(TR-) associated proteins which interact with TR and facilitate TR function on DNA templates in conjunction with initiation factors and cofactors.
MED28
Mediator of RNA polymerase II transcription subunit 28 is an enzyme that in humans is encoded by the MED28 gene. It forms part of the Mediator complex.

# Function
Subunit Med28 of the Mediator may function as a scaffolding protein within Mediator by maintaining the stability of a submodule within the head module, and components of this submodule act together in a gene-regulatory programme to suppress smooth muscle cell differentiation. Thus, mammalian Mediator subunit Med28 functions as a repressor of smooth muscle-cell differentiation, which could have implications for disorders associated with abnormalities in smooth muscle cell growth and differentiation, including atherosclerosis, asthma, hypertension, and smooth muscle tumours.

# Interactions
MED28 has been shown to interact with Merlin, Grb2 and MED26.
MEF2B
Myocyte enhancer binding factor 2B (MEF2B) is a transcription factor part of the MEF2 gene family including MEF2A, MEF2C, and MEF2D. However, MEF2B is distant from the other three branches of MEF2 genes as it lacks the protein-coding Holliday junction recognition protein C-terminal (HJURP_C) region in vertebrates.

# Functions
The MEF2 gene family is expressed in muscle-specific gene activation and maintenance during development. MEF2B mRNA is present in skeletal, smooth, brain and heart muscles. MEF2B is directly involved in smooth muscle myosin heavy chain (SMHC) gene regulation. Overexpression of MEF2B will activate the SMHC promoter in smooth muscle when it is bound to the A/T-rich element of the promoter.

# Interactions
MEF2B has been shown to interact with CABIN1.

# Clinical relevance
Recurrent mutations in this gene have been associated with cases of diffuse large B-cell lymphoma. In its mutated form, MEF2B can lead to deregulation of the proto-oncogene BCL6 expression in diffuse large B-cell lymphomas (DLBCL). Mutations of MEF2B enhance its transcriptional activity due to either a disruption with its corepressor CABIN1 or causing the gene to become insensitive to inhibitory signaling events.
MEF2C
Myocyte-specific enhancer factor 2C also known as MADS box transcription enhancer factor 2, polypeptide C is a protein that in humans is encoded by the MEF2C gene. MEF2C is a transcription factor in the Mef2 family.

# Genomics
The gene is located at 5q14.3 on the minus (Crick) strand and is 200,723 bases in length. The encoded protein has 473 amino acids with a predicted molecular weight of 51.221 kiloDaltons. Three isoforms have been identified. Several post translational modifications have been identified including phosphorylation on serine-59 and serine-396, sumoylation on lysine-391, acetylation on lysine-4 and proteolytic cleavage.

# Interactions
MEF2C has been shown to interact with:
- EP300,
- HDAC4, HDAC7, HDAC9,
- MAPK7,
- SOX18
- SP1,  and
- TEAD1.

# Biological significance
This gene is involved in cardiac morphogenesis and myogenesis and vascular development. It may also be involved in neurogenesis and in the development of cortical architecture. Mice without a functional copy of the Mef2c gene die before birth and have abnormalities in the heart and vascular system. It is one of the targets of an oncomiR, MIRN21.
In humans mutations of this gene result in autosomal dominant mental retardation 20 (MRD20), characterised by severe psychomotor impairment, periodic tremor and an abnormal motor pattern with mirror movement of the upper limbs observed during infancy, hypotonia, abnormal EEG, epilepsy, absence of speech, autistic behavior, bruxism, and mild dysmorphic features, mild thinning of the corpus callosum and delay of white matter myelination in the occipital lobes
MEF2C-binding site is associated with minor allele of SNP rs630923, associated with the risk of multiple sclerosis, and responsible for reduced CXCR5 gene promoter activity in B-cells during activation, that could lead to decreased autoimmune response
MESP2
Mesoderm posterior protein 2 (MESP2), also known as class C basic helix-loop-helix protein 6 (bHLHc6), is a protein that in humans is encoded by the MESP2 gene.

# Function
This gene encodes a member of the bHLH family of transcription factors and plays a key role in defining the rostrocaudal patterning of somites via interactions with multiple Notch signaling pathways. This gene is expressed in the anterior presomitic mesoderm and is downregulated immediately after the formation of segmented somites. This gene also plays a role in the formation of epithelial somitic mesoderm and cardiac mesoderm. In zebrafish, the homolog mesp-b is critical for dermomyotome development.

# Clinical significance
Mutations in the MESP2 gene cause autosomal recessive Spondylocostal dysostosis type 2.
MEX3D
Mex-3 homolog D (C. elegans), also known as MEX3D, is a protein that in humans is encoded by the MEX3D gene.

# Function
MEX3D is an RNA binding protein that interacts with AU-rich elements of Bcl-2. Upon binding, MEX3D has a negative regulatory action on Bcl-2 expression at the posttranscriptional level.

# Structure
MEX3 proteins contain two N-terminal heterogeneous nuclear ribonucleoprotein K homology motifs ( KH domain ) and a RING domain at the C-terminus.
MFGE8
Milk fat globule-EGF factor 8 protein (Mfge8), also known as lactadherin, is a protein which in humans is encoded by the MFGE8 gene.

# Species distribution
Mfge8 is secreted protein found in vertebrates, including mammals as well as birds.

# Function
MFGE8 may function as a cell adhesion protein to connect smooth muscle to elastic fiber in arteries. An amyloid fragment of MFGE8 known as medin accumulates in the aorta with aging. MFGE8 in the vasculature of adults can induce recovery from ischemia by facilitating angiogenesis. It has been suggested that antagonizing MFGE8-induced angiogenesis could be a way of fighting cancer.
MFGE8 contains a phosphatidylserine (PS) binding domain, as well as an Arginine-Glycine-Aspartic acid motif, which enables the binding to integrins. MFGE8 binds PS, which is exposed on the surface of apoptotic cells. Opsonization of the apoptotic cells and binding to integrins on the surface of phagocytic cells, mediates the engulfment of the dead cell.
MFSD2
Major facilitator superfamily domain-containing protein 2 (MFSD2 or MFSD2A) -- also known as sodium-dependent lysophosphatidylcholine symporter 1 --  is a protein that in humans is encoded by the MFSD2A gene. MFSD2A is a membrane transport protein that is expressed in the endothelium of the bloodbrain barrier (BBB) and has an essential role in BBB formation and function. Genetic ablation of MFSD2A results in leaky BBB and increases central nervous system endothelial cell vesicular transcytosis without otherwise affecting tight junctions. MFSD2A is an atypical SLC, thus a predicted SLC transporter. It clusters phylogenetically to AMTF8.
In addition to transport of other lysophosphatidylcholines across the BBB, MSFD2A is the primary mechanism for docosahexaenoic acid (DHA, an omega-3 fatty acid) uptake and transport into the brain. It may also be responsible for uptake and transport of tunicamycin.
Complete loss of MFSD2A in human leads to a recessive lethal microcephaly syndrome consisting of enlarged lateral ventricles and underdevelopment of the cerebellum and brainstem.  This is presumably due to loss of uptake of essential polyunsaturated fatty acids by the brain endothelial cells, which utilize MFSD2A as a transporter for these fats.  Serum from patients showed elevated levels of essential polyunsaturated fatty acids, presumably due to the inability of vascular cells to uptake these lipids in the absence of protein function. Without the ability to uptake these fats into endothelial cells, there is breakdown of the blood-brain-barrier and loss of brain volume.  This was demonstrated in a zebrafish model by intracardiac injection of dye, which was found to extravasate into the brain parenchyma following  inactivating one of the paralogues of MSFD2A known as mfsd2aa.
MFSD8
Major facilitator superfamily domain containing 8 also known as MFSD8 is a protein that in humans is encoded by the MFSD8 gene. MFSD8 is an atypical SLC, thus a predicted SLC transporter. It clusters phylogenetically to the Atypical MFS Transporter family 2 (AMTF2).

# Function
MFSD8 is a ubiquitous integral membrane protein that contains a transporter domain and a major facilitator superfamily (MFS) domain. Other members of the major facilitator superfamily transport small solutes through chemiosmotic ion gradients. The substrate transported by this protein is unknown. The protein likely localizes to lysosomal membranes.

# Clinical significance
Mutations in the MFSD8 gene have been associated with neuronal ceroid lipofuscinosis.