Persius/hicric huggingface dataset:
EIF4H
Eukaryotic translation initiation factor 4H is a protein that in humans is encoded by the EIF4H gene.
This gene encodes one of the translation initiation factors, which function to stimulate the initiation of protein synthesis at the level of mRNA utilization. 
This gene is deleted in Williams syndrome, a multisystem developmental disorder caused by the deletion of contiguous genes at 7q11.23. Alternative splicing of this gene generates 2 transcript variants.
EIF4H appears analogous to drr-2 in C. elegans which regulates the mTOR pathway and affects longevity.
EIF5A
Eukaryotic translation initiation factor 5A-1 is a protein that in humans is encoded by the EIF5A gene.
It is the only known protein to contain the unusual amino acid hypusine , which is synthesized on eIF5A at a specific lysine residue from the polyamine spermidine by two catalytic steps.
EF-P is the prokaryotic homolog of eIF5A, which is also modified post-translationally in a similar but distinct way.
ELAC2
Zinc phosphodiesterase ELAC protein 2 is an enzyme that in humans is encoded by the ELAC2 gene. on chromosome 17. It is an endonuclease thought to be involved in mitochondrial tRNA maturation,

# Function
The ELAC2 gene encodes a protein that is 92 kDa in size and is localized to the mitochondrion  and the nucleus. The ELAC2 protein is a zinc phosphodiesterase, which is known to show tRNA 3'-processing endonuclease activity inside the mitochondria. Mitochondria contain their own pool of tRNAs that are involved in the protein translation of 13 subunits of the respiratory chain that are encoded by the mitochondrial genome. ELAC2 functions in the maturation of tRNA by removing a 3'-trailer (extra 3' nucleotides) from tRNA precursors, generating 3' termini of tRNAs.
The reaction leaves a 3'-hydroxy group is left at the tRNA end, and a 5'-phosphoryl group at the cleaved, trailing end. The reaction requires zinc ions as co-factors.

# Clinical significance
Variants of the ELAC2 gene are associated with prostate cancer, hereditary 2 (HPC2), a condition associated with familial cancer of the prostate. Multiple mutations including truncation and missense mutations are known to cause the disease from multiple families based on linkage analysis and positional cloning.
In addition, mutations in ELAC2 are known to cause combined oxidative phosphorylation deficiency 17 (COXPD17), a rare autosomal recessive disorder of mitochondrial functions characterized by severe hypertrophic cardiomyopathy.
ELMO1
Engulfment and cell motility protein 1 is a protein that in humans is encoded by the ELMO1 gene. ELMO1 is located on chromosome number seven in humans and is located on chromosome number thirteen in mice.

# Structure
The human engulfment and cell motility protein 1, ELMO1, is 720 residues in length.  The protein contains the following three domains:
- N-terminal Armadillo domain (residues 82-262)
- central ELMO (Engulfment and Cell Motility) domain (301-492)
- C-terminal pleckstrin homology domain (residues 527-674)
ELMO1 also has a pro-rich motif at the extreme C terminus. Secondary structure analysis has predicted that there are alpha-helical regions at both the N and C-terminus.
The structure of the pleckstrin homology domain of ELMO1 has been determine by X-ray crystallography.

# Function
The protein encoded by this gene interacts with the dedicator of cyto-kinesis 1 protein to promote phagocytosis and effect cell shape changes. Similarity to a C. elegans protein suggests that this protein may function in apoptosis and in cell migration. Alternative splicing of this gene results in multiple transcript variants encoding different isoforms.

# Interactions
ELMO1 has been shown to interact with Dock180 and HCK.  ELMO1 directly interacts with the SH3 domain of HCK.  The association between ELMO1 and HCK is dependent on polyproline interactions.
When ELMO1 is complexed with DOCK180, Rac GTPase-dependent biological processes are activated.  The pH domain of ELMO1 functions in trans to stabilize DOCK180 and make it resistant to degradation.  When ELMO1 binds to DOCK180 it relieves the steric inhibition of DOCK180 which then activates the Rac GTPase.  The pro-rich motif of the C terminus on ELMO1 is essential for the binding of ELMO1 to the SH3 domain at the N terminus of DOCK180.  The complex of ELMO1 and DOCK180 act as a regulator of Rac during development of a cell and cell migration.  Mutation of both interaction sites for DOCK180 on ELMO1 will lead to the disruption of the ELMO1-DOCK180 complex.  ELMO1 complexed with both DOCK180 and CrkII leads to maximal efficiency of phagocytosis in the cell. This complex of molecules happens upstream of Rac during phagocytosis.
ENPP3
Ectonucleotide pyrophosphatase/phosphodiesterase family member 3 is an enzyme that in humans is encoded by the ENPP3 gene.

# Function
The protein encoded by this gene belongs to a series of ectoenzymes that are involved in hydrolysis of extracellular nucleotides. These ectoenzymes possess ATPase and ATP pyrophosphatase activities and are type II transmembrane proteins. Expression of the related rat mRNA has been found in a subset of immature glial cells and in the alimentary tract. The corresponding rat protein has been detected in the pancreas, small intestine, colon, and liver. The human mRNA is expressed in glioma cells, prostate, and uterus. Expression of the human protein has been detected in uterus, basophils, and mast cells.
This protein has also been used in conjunction with CD63 as a marker for activated basophils in the Basophil Activation Test for IgE mediated allergic reactions.
EPHB3
Ephrin type-B receptor 3 is a protein that in humans is encoded by the EPHB3 gene.

# Function
Ephrin receptors and their ligands, the ephrins, mediate numerous developmental processes, particularly in the nervous system. Based on their structures and sequence relationships, ephrins are divided into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. The Eph family of receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. Ephrin receptors make up the largest subgroup of the receptor tyrosine kinase (RTK) family. The protein encoded by this gene is a receptor for ephrin-B family members.

# Interactions
EPHB3 has been shown to interact with MLLT4 and RAS p21 protein activator 1.
EPS15
Epidermal growth factor receptor substrate 15 is a protein that in humans is encoded by the EPS15 gene.

# Function
This gene encodes a protein that is part of the EGFR pathway. The protein is present at clathrin-coated pits and is involved in receptor-mediated endocytosis of EGF. Notably, this gene is rearranged with the HRX/ALL/MLL gene in acute myelogeneous leukemias. Alternate transcriptional splice variants of this gene have been observed but have not been thoroughly characterized.

# Model organisms
Model organisms have been used in the study of EPS15 function. A conditional knockout mouse line, called Eps15tm1a(KOMP)Wtsi was generated as part of the International Knockout Mouse Consortium programa high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientistsat the Wellcome Trust Sanger Institute.
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Twenty six tests were carried out on mutant mice and one significant abnormality was observed: homozygous mutant animals had a decreased mean corpuscular hemoglobin concentration.

# Interactions
EPS15 has been shown to interact with:
- CRK
- EPN1,
- HGS,
- HRB, and
- REPS2.
ERAP1
Type 1 tumor necrosis factor receptor shedding aminopeptidase regulator, also known as endoplasmic reticulum aminopeptidase 1 (ARTS-1), is a protein which in humans is encoded by the ARTS-1 gene.
Endoplasmic reticulum amino peptidase 1 is active in the endoplasmic reticulum, which is involved in protein processing and transport. This protein is an aminopeptidase, which is an enzyme that cleaves peptides at the N-terminal into smaller fragments called amino acids.

# Nomenclature
ARTS1 is also known as:
- ER aminopeptidase 1 (ERAP1) the name accepted by the Hugo Gene Nomenclature Committee
- ER aminopeptidase associated with antigen processing (ERAAP) in mice 
- Adipocyte-derived leucine aminopeptidase (ALAP)
- Puromycin-insensitive leucine aminopeptidase (PILS-AP)

# Function
ERAP1 has two major functions in the immune system:
- First, ERAP1 cleaves several proteins called cytokine receptors on the surface of cells. Cleaving these receptors reduces their ability to transmit chemical signals into the cell, which affects the process of inflammation.
- Second, ERAP1 trims peptides within the endoplasmic reticulum so that they can be loaded onto major histocompatibility complex (MHC) class I. These peptides are attached to MHC class I in the endoplasmic reticulum and exported to the cell surface, where they are displayed to the immune system. If the immune system recognizes the peptides as foreign (such as viral or bacterial peptides), it responds by triggering the infected cell to self-destruct.
ARTS-1  is a member of the M1 family of zinc metallopeptidases which acts as an aminopeptidase that degrades oligopeptides by cleavage starting at the amino terminus.  One of the functions of aminopeptidases is to degrade potentially toxic peptides in the cytosol.
ARTS-1 is a transmembrane protein that is localized to the endoplasmic reticulum.  It has been implicated in the following functions:
- Shedding of various cytokine receptors and decoy receptors
- Trimming of antigenic peptides before binding to MHC class I, affecting antigen presentation to cytotoxic T lymphocytes
- Stimulation of phagocytosis upon release by macrophages

# Clinical significance
Aminopeptidases play a role in the metabolism of several peptides that may be involved in blood pressure and the pathogenesis of essential hypertension. Mutations in the ARTS-1 have been linked to an increased risk of ankylosing spondylitis but only in HLA-B27 positive patients.
The protein encoded by this gene is an aminopeptidase involved in trimming HLA class I-binding precursors so that they can be presented on MHC class I molecules. The encoded protein acts as a monomer or as a heterodimer with ERAP2. This protein may also be involved in blood pressure regulation by inactivation of angiotensin II. Three transcript variants encoding two different isoforms have been found for this gene.
ERBB4
Receptor tyrosine-protein kinase erbB-4 is an enzyme that in humans is encoded by the ERBB4 gene. Alternatively spliced variants that encode different protein isoforms have been described; however, not all variants have been fully characterized.

# Function
Receptor tyrosine-protein kinase erbB-4 is a receptor tyrosine kinase that is a member of the epidermal growth factor receptor subfamily. ERBB4 is a single-pass type I transmembrane protein with multiple furin-like cysteine rich domains, a tyrosine kinase domain, a phosphotidylinositol-3 kinase binding site and a PDZ domain binding motif. The protein binds to and is activated by neuregulins-2 and -3, heparin-binding EGF-like growth factor and betacellulin.  Ligand binding induces a variety of cellular responses including mitogenesis and differentiation. Multiple proteolytic events allow for the release of a cytoplasmic fragment and an extracellular fragment.

# Clinical significance
Mutations in this gene have been associated with cancer. Other single-nucleotide polymorphisms and a risk haplotype have been linked to schizophrenia. Single-nucleotide polymorphisms in ERBB4 have also been found in a study of patients with familial amyotrophic lateral sclerosis type 19.

# Interactions
ERBB4 has been shown to interact with:
- DLG4
- NRG1,
- STAT5A, and
- YAP1.
ERCC5
DNA repair protein complementing XP-G cells is a protein that in humans is encoded by the ERCC5 gene.
Excision repair cross-complementing rodent repair deficiency, complementation group 5 (xeroderma pigmentosum, complementation group G) is involved in excision repair of UV-induced DNA damage. Mutations cause Cockayne syndrome, which is characterized by severe growth defects, mental retardation, and cachexia. Multiple alternatively spliced transcript variants encoding distinct isoforms have been described, but the biological validity of all variants has not been determined.
Mutations in ERCC5 cause                 arthrogryposis            .
XPG is a structure specific endonuclease that incises DNA at the 3 side of the damaged nucleotide during nucleotide excision repair.

# Syndromes
Mutational defects in the Ercc5(Xpg) gene can cause either the cancer-prone condition xeroderma pigmentosum (XP) alone, or in combination with the severe neurodevelopmental disorder Cockayne syndrome (CS) or the infantile lethal cerebro-oculo-facio-skeletal syndrome.

# Mouse model
An Ercc5(Xpg) mutant mouse model presented features of premature aging including cachexia and osteoporosis with pronounced degenerative phenotypes in both liver and brain.  These mutant mice developed a multi-system premature aging degenerative phenotype that appears to strengthen the link between DNA damage and aging. (see DNA damage theory of aging).
Dietary restriction, which extends lifespan of wild-type mice, also substantially increased the lifespan of Ercc5(Xpg) mutant mice.  Dietary restriction of the mutant mice, while delaying aging, also appeared to slow the accumulation of genome wide DNA damage and to preserve transcriptional output, thus contributing to improved cell viability.

# Interactions
ERCC5 has been shown to interact with ERCC2.
ETFDH
Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial is an enzyme that in humans is encoded by the ETFDH gene. This gene encodes a component of the electron-transfer system in mitochondria and is essential for electron transfer from a number of mitochondrial flavin-containing dehydrogenases to the main respiratory chain.

# Function
Electron-transferring-flavoprotein dehydrogenase in the inner mitochondrial membrane accepts electrons from electron-transfer flavoprotein which is located in the mitochondrial matrix and reduces ubiquinone in the mitochondrial membrane. Deficiency in electron-transferring-flavoprotein dehydrogenase have been demonstrated in some patients with type II glutaric aciduria.

# Structure
The ETFDH gene is located on the q arm of chromosome 4 in position 32.1 and has 13 exons spanning 36,613 base pairs. The protein is synthesized as a 67-kDa precursor which is targeted to mitochondria and processed in a single step to a 64-kDa mature form located in the mitochondrial membrane. This 64-kDA mature form is a monomer integrated into the mitochondrial inner membrane, containing a 4Fe-4S cluster and 1 molecule of FAD.

# Function
This enzyme, along with electron transfer flavoprotein (ETF), is required for electron transfer from more than 9 mitochondrial flavin-containing dehydrogenases to the main respiratory chains. It accepts electrons from ETF and reduces ubiquinone.

# Clinical Significance
Mutations in the ETFDH can cause glutaric aciduria 2C (GA2C), an autosomal recessively inherited disorder of fatty acid, amino acid, and choline metabolism. It is characterized by multiple acyl-CoA dehydrogenase deficiencies resulting in large excretion not only of glutaric acid, but also of lactic, ethylmalonic, butyric, isobutyric, 2-methyl-butyric, and isovaleric acids.
A c.250G>A (p.Ala84Thr) mutation, the most common mutation in the ETFDH gene, causes increased production of reactive oxygen species (ROS) and shortened neurites in cells expressing this mutant compared to wild type cells. Suberic acid, an accumulated intermediate metabolite in dehydrogenase deficiency, can significantly impair neurite outgrowth in NSC34 cells. This shortening of neurites can be restored by riboflavin, carnitine, or Coenzyme Q10 supplements.

# Interactions
The encoded protein interacts with MYH7B, LINC00174, LINC00574, Homeobox protein goosecoid-2, AIRE, OTX1, Keratin-associated protein 13-2, Keratin-associated protein 11-1, TRIM69, Zinc finger protein 581, and COX6B1.
ETHE1
Protein ETHE1, mitochondrial, also known as "ethylmalonic encephalopathy 1 protein" and "per sulfide dioxygenase", is a protein that in humans is encoded by the ETHE1 gene located on chromosome 19.

# Structure
The human ETHE1 gene consists of 7 exons and encodes for a protein that is approximately 27 kDa in size.

# Function
This gene encodes a protein that is expressed in the thyroid.
The ETHE1 protein is thought to localize primarily to the mitochondrial matrix  and functions as a sulfur dioxygenase.  Sulfur deoxygenates are proteins that function in sulfur metabolism. The ETHE1 protein is thought to catalyze the following reaction:
and requires iron and possibly glutathione as cofactors. The physiological substrate of ETHE1 is thought to be glutathione persulfide, an intermediate metabolite involved in hydrogen sulfide degradation.

# Clinical significance
Mutations in ETHE1 gene  are thought to cause ethylmalonic encephalopathy, a rare inborn error of metabolism. Patients carrying ETHE1 mutations have been found to exhibit lower activity of ETHE1 and affinity for the ETHE1 substrate. Mouse models of Ethe1 genetic ablation likewise exhibited reduced sulfide dioxygenase catabolism and cranial features of ethylmalonic encephalopathy. Decrease in sulfide dioxygenase activity results in abnormal catabolism of hydrogen sulfide, an gas-phase signaling molecule in the central nervous system, whose accumulation is thought to inhibit cytochrome c oxidase activity in the respiratory chain of the mitochondrion. However, other metabolic pathways may also be involved that could exert a modulatory effect on hydrogen sulfide toxicity.

# Interactions
ETHE1 has been shown to interact with RELA.
Enone
An enone is an unsaturated chemical compound or functional group consisting of a conjugated system of an alkene and a ketone.  The simplest enone is methyl vinyl ketone (MVK) or CH2=CHCOCH3.
As an example, an enone such as a chalcone can be synthesized in a Knoevenagel condensation. In the Meyer-Schuster rearrangement the starting compound is a propargyl alcohol.
An enone is a reactant in the Nazarov cyclization reaction and in the Rauhut-Currier reaction (dimerization).

# Related compounds
Enone is not to be confused with Ketene (R2C=C=O). An enamine is a cousin of an enone, with the carbonyl replaced by an amine group. An enal is the corresponding ,-unsaturated aldehyde
Eosin

# Overview
Eosin is a fluorescent acidic / negative compound that binds to and forms salts with basic, or eosinophilic, compounds containing positive charges (such as proteins that are basic / positive due to the presence of amino acid residues such as Arginine and Lysine) and stains them dark red or pink as a result of the actions of bromine on fluorescein. In addition to staining proteins in the cytoplasm, it can be used to stain collagen and muscle fibers for examination under the microscope.  Structures that stain readily with eosin are termed eosinophilic.

# Etymology
The name Eosin comes from Eos, the Ancient Greek word for 'dawn' and the name of the Ancient Greek goddess of the dawn.

# Variants
There are actually two very closely related compounds commonly referred to as eosin.  Most often used is Eosin Y (also known as eosin Y ws, eosin yellowish, Acid Red 87, C.I. 45380, bromoeosine, bromofluoresceic acid, D&C Red No. 22); it has a very slightly yellowish cast. The other eosin compound is eosin B (eosin bluish, Acid Red 91, C.I. 45400, Saffrosine, Eosin Scarlet, or imperial red); it has a very faint bluish cast. The two dyes are interchangeable, and the use of one or the other is a matter of preference and tradition.
Eosin Y is a tetrabromo derivative of fluorescein. Eosin B is a dibromo dinitro derivative of fluorescein.

# Use in histology
Eosin is most often used as a counterstain to hematoxylin in H&E (haematoxylin and eosin) staining.  H&E staining is one of the most commonly used techniques in histology. Tissue stained with haematoxylin and eosin shows cytoplasm stained pink-orange and nuclei stained darkly, either blue or purple. Eosin also stains red blood cells intensely red.
For staining, eosin Y is typically used in concentrations of 1 to 5 percent weight by volume, dissolved in water or ethanol. For prevention of mold growth in aqueous solutions, thymol is sometimes added. A small concentration (0.5 percent) of acetic acid usually gives a deeper red stain to the tissue.
It is listed as an IARC class 3 carcinogen.
Ezrin
Ezrin also known as cytovillin or villin-2 is a protein that in humans is encoded by the EZR gene.

# Structure
The N-terminus of ezrin contains a FERM domain which is further subdivided into three subdomains. The C-terminus contain a ERM domain.

# Function
The cytoplasmic peripheral protein encoded by this gene can be phosphorylated by protein-tyrosine kinase in microvilli and is a member of the ERM protein family. This protein serves as a linker between plasma membrane and actin cytoskeleton.  It plays a key role in cell surface structure adhesion, migration, and organization.
The N-terminal domain (also called FERM domain) binds sodium-hydrogen exchanger regulatory factor (NHERF) protein (involving long-range allostery).  This binding can happen only when ezrin is in its active state. The activation of ezrin occurs in synergism of the two factors: 1) binding of the N-terminal domain to  phosphatidylinositol(4,5)bis-phosphate (PIP2) and 2) phosphorylation of threonine T567 in  the C-terminal domain. Binding to actin filaments (via C-terminal) and to membrane proteins (via N-terminal) stabilizes the protein's conformation in its active mode. The membrane proteins like CD44 and ICAM-2 are indirect binding partners of ezrin, while EBP50 (ERM binding protein 50) can associate with ezrin directly.

# Interactions
VIL2 has been shown to interact with:
- CD43,
- FASLG,
- ICAM-1,
- ICAM2,
- ICAM3,
- Merlin,
- MSN,
- PIK3R1,
- PALLD
- S100P,
- SDC2,
- SLC9A3R1,
- SLC9A3R2,  and
- VCAM-1.
FABP2
Fatty acid-binding protein 2 (FABP2) also known as Intestinal-type fatty acid-binding protein (I-FABP) is a protein that in humans is encoded by the FABP2 gene.

# Function
The intracellular fatty acid-binding proteins (FABPs) belong to a multigene family with nearly twenty identified members. FABPs are divided into at least three distinct types, namely the hepatic-, intestinal- and cardiac-type. They form 14-15 kDa proteins and are thought to participate in the uptake, intracellular metabolism and/or transport of long-chain fatty acids. They may also be responsible in the modulation of cell growth and proliferation. Intestinal fatty acid-binding protein 2 gene contains four exons and is an abundant cytosolic protein in small intestine epithelial cells.

# Clinical significance
This gene has a polymorphism at codon 54 that identified an alanine-encoding allele and a threonine-encoding allele. Thr-54 protein is associated with increased fat oxidation and insulin resistance.
FABP5
Fatty acid-binding protein, epidermal is a protein that in humans is encoded by the FABP5 gene.

# Function
This gene encodes the fatty acid binding protein found in epidermal cells, and was first identified as being upregulated in psoriasis tissue. Fatty acid binding proteins are a family of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. It is thought that FABPs roles include fatty acid uptake, transport, and metabolism.
The phytocannabinoids (THC and CBD) inhibit endocannabinoid anandamide (AEA) uptake by targeting FABP5, and competition for FABPs may in part or wholly explain the increased circulating levels of endocannabinoids reported after consumption of cannabinoids. Results show that cannabinoids inhibit keratinocyte proliferation, and therefore support a potential role for cannabinoids in the treatment of psoriasis.

# Interactions
FABP5 has been shown to interact with S100A7.