Persius/hicric huggingface dataset:
E2F1
Transcription factor E2F1 is a protein that in humans is encoded by the E2F1 gene.

# Function
The protein encoded by this gene is a member of the E2F family of transcription factors. The E2F family plays a crucial role in the control of cell cycle and action of tumor suppressor proteins and is also a target of the transforming proteins of small DNA tumor viruses. The E2F proteins contain several evolutionarily conserved domains found in most members of the family. These domains include a DNA binding domain, a dimerization domain which determines interaction with the differentiation regulated transcription factor proteins (DP), a transactivation domain enriched in acidic amino acids, and a tumor suppressor protein association domain which is embedded within the transactivation domain.  This protein and another 2 members, E2F2 and E2F3, have an additional cyclin binding domain. This protein binds preferentially to retinoblastoma protein pRB in a cell-cycle dependent manner. It can mediate both cell proliferation and p53-dependent/independent apoptosis.

# Transcription
E2F1 promoter => E2F1  .mw-parser-output cite.citation{font-style:inherit}.mw-parser-output q{quotes:"\"""\"""'""'"}.mw-parser-output code.cs1-code{color:inherit;background:inherit;border:inherit;padding:inherit}.mw-parser-output .cs1-lock-free a{background:url("")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-limited a,.mw-parser-output .cs1-lock-registration a{background:url("")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-subscription a{background:url("")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration{color:#555}.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration span{border-bottom:1px dotted;cursor:help}.mw-parser-output .cs1-hidden-error{display:none;font-size:100%}.mw-parser-output .cs1-visible-error{display:none;font-size:100%}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-format{font-size:95%}.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-wl-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right,.mw-parser-output .cs1-kern-wl-right{padding-right:0.2em}PMID 21602887

# Interactions
E2F1 has been shown to interact with:
- ARID3A,
- CUL1,
- Cyclin A1,
- Cyclin A2,
- GTF2H1,
- MDM4,
- NCOA6,
- NDN,
- NPDC1,
- PURA,
- PHB,
- RB1,
- RBL1,
- SKP2,
- SP1,
- SP2,
- SP3,
- SP4,
- TFDP1
- TOPBP1,
- TP53BP1,  and
- UBC.
E2F4
Transcription factor E2F4 is a protein that in humans is encoded by the E2F4 gene.

# Function
Gene ID: 1874 E2F transcription factor 4, "The protein encoded by this gene is a member of the E2F family of transcription factors. The E2F family plays a crucial role in the control of cell cycle and action of tumor suppressor proteins and is also a target of the transforming proteins of small DNA tumor viruses. The E2F proteins contain several evolutionally conserved domains found in most members of the family. These domains include a DNA binding domain, a dimerization domain which determines interaction with the differentiation regulated transcription factor proteins (DP), a transactivation domain enriched in acidic amino acids, and a tumor suppressor protein association domain which is embedded within the transactivation domain. This protein binds to all three of the tumor suppressor proteins pRB, p107 and p130, but with higher affinity to the last two. It plays an important role in the suppression of proliferation-associated genes, and its gene mutation and increased expression may be associated with human cancer."

# Structure
The E2F proteins contain several evolutionally conserved domains found in most members of the family. These domains include a DNA binding domain, a dimerization domain which determines interaction with the differentiation regulated transcription factor proteins (DP), a transactivation domain enriched in acidic amino acids (Asp + Glu), and a tumor suppressor protein association domain which is embedded within the transactivation domain.

# Interactions
E2F4 has been shown to interact with Smad3.

# Clinical significance

## Colorectal cancers
"The AGC triplet repeat in the coding region of the E2F-4 gene, a member of the family, has been reported to be mutated in colorectal cancers with a microsatellite instability (MSI) phenotype. We found a wider range variation of the repeat number in DNAs from tumors, the corresponding normal mucosa, and healthy individuals. A total of 5 repeat variants, ranging from 8 to 17 AGC repeats, was detected in 6 (9.7%) of the 62 healthy individuals and 8 (8.9%) of the 90 normal DNAs of the patients. The wild-type 13 repeat was present in all of these individuals. The variation of the AGC repeat number may be a polymorphism. Further, loss of heterozygosity (LOH) at the E2F-4 locus in the tumor tissues of 2 (25%) of the 8 informative cases was detected."
EBF1
Transcription factor COE1 is a protein that in humans is encoded by the EBF1 gene. 
EBF1 stands for Early B-Cell Factor 1.
EBF1 controls the expression of key proteins required for B cell differentiation, signal transduction and function. The crucial role of this factor is shown in the regulation of expression of SLAM family co-receptors in B-cells.

# Interactions
EBF1 has been shown to interact with ZNF423 and CREB binding protein.
EBI3
Epstein-Barr virus induced gene 3, also known as interleukin-27 subunit beta or IL-27B, is a protein which in humans is encoded by the EBI3 gene.

# Function
This gene was identified by the induction of its expression in B lymphocytes by Epstein-Barr virus infection. The protein encoded by this gene is a secreted glycoprotein, which is a member of the hematopoietin receptor family related to the p40 subunit of interleukin 12 (IL-12). It plays a role in regulating cell-mediated immune responses.
EBI3 is a subunit in 2 distinct heterodimeric cytokines: interleukin-27 (IL27) and IL35. IL27 is composed of p28 (IL27) and EBI3. IL27 can trigger signaling in T cells, B cells, and myeloid cells. IL35, an inhibitory cytokine involved in regulatory T-cell function, is composed of EBI3 and the  p35 subunit of IL12.
EEA1
The gene EEA1 encodes for the 1400 amino acid protein, Early Endosome Antigen 1.
EEA1 localizes exclusively to early endosomes and has an important role in endosomal trafficking. EEA1 binds directly to the phospholipid phosphatidylinositol 3-phosphate through its C-terminal FYVE domain and forms a homodimer through a coiled coil. EEA1 acts as a tethering molecule that couples vesicle docking with SNAREs such as N-ethylmaleimide sensitive fusion protein, bringing the endosomes physically closer and ultimately resulting in the fusion and delivery of endosomal cargo.

# Function
EEA1 is a RAB5A effector protein which binds via an N-terminal zinc finger domain and is required for fusion of early and late endosomes and for sorting at the early endosome level.

# Involvement in pathogenesis
Due to the proteins importance in vesicular trafficking, a number of intracellular bacteria prevent EEA1 recruitment to the vacuole. Mycobacterium tuberculosis is known to inhibit the recruitment of EEA1 to the phagosomal membrane through CamKII. Legionella pneumophila also prevents EEA1 recruitment through a currently unknown mechanism. The related pathogen Legionella longbeachae recruits EEA1 and appears to replicate within a modified early endosome.
EEF2
Eukaryotic elongation factor 2 is a protein that in humans is encoded by the EEF2 gene.
This gene encodes a member of the GTP-binding translation elongation factor family. This protein is an essential factor for protein synthesis. It promotes the GTP-dependent translocation of the ribosome. This protein is completely inactivated by EF-2 kinase phosphorylation.
EEF2 contains a post transcriptionally modified histadine diphthamide. It is the target of diphtheria toxin (from Corynebacterium diphtheriae), and exotoxin A (from Pseudomonas aeruginosa). The inactivation of EF-2 by toxins inhibits protein production in the host, causing symptoms due to loss of function in affected cells.
EGR1
EGR-1 (Early growth response protein 1) also known as Zif268 (zinc finger protein 225) or NGFI-A (nerve growth factor-induced protein A) is a protein that in humans is encoded by the EGR1 gene.
EGR-1 is a mammalian transcription factor. It was also named Krox-24, TIS8, and ZENK. It was originally discovered in mice.

# Function
The protein encoded by this gene belongs to the EGR family of Cys2His2-type zinc finger proteins. It is a nuclear protein and functions as a transcriptional regulator. The products of target genes it activates are required for differentiation and mitogenesis. Studies suggest this is a tumor suppressor gene.
It has a distinct pattern of expression in the brain, and its induction has been shown to be associated with neuronal activity. Several studies suggest it has a role in neuronal plasticity.
EGR-1 has also been found to regulate the expression of VAMP2 (a protein important for synaptic exocytosis).

# Structure
The DNA-binding domain of EGR-1 consists of three zinc finger domains of the Cys2His2 type.
The amino acid structure of the EGR-1 zinc finger domain is given in this table, using the single letter amino acid code. The fingers 1 to 3 are indicated by f1 - f3. The numbers are in reference to the residues (amino acids) of alpha helix (there is no zero). The residues marked 'x' are not part of the zinc fingers, but rather serve to connect them all together.
Amino acid key: Alanine (Ala, A), Arginine (Arg, R), Asparagine (Asn, N), Aspartic acid (Asp, D), Cysteine (Cys, C), Glutamic acid (Glu, E), Glutamine (Gln, Q), Glycine (Gly, G), Histidine (His, H), Isoleucine (Ile, I), Leucine (Leu, L), Lysine (Lys, K), Methionine (Met, M), Phenylalanine (Phe, F), Proline (Pro, P), Serine (Ser, S), Threonine (Thr, T), Tryptophan (Trp, W), Tyrosine (Tyr, Y), Valine (Val, V)
The crystal structure of DNA bound by the zinc finger domain of EGR-1 was solved in 1991, which greatly aided early research in zinc finger DNA-binding domains.
The human EGR-1 protein contains (in its unprocessed form) 543 amino acids with a molecular weight of 57.5 kDa, and the gene is located on the chromosome 5.

# DNA binding specificity
EGR-1 binds the DNA sequence 5'-GCG TGG GCG-3' (and similar ones like 5'-GCG GGG GCG-3').
The f1 position 6 binds the 5' G (the first base count from the left); the f1 position 3 to the second base (C); f1 position -1 binds to the third position (G); f2 position 6 to the fourth base (T); and so on.

# Interactions
EGR-1 has been shown to interact with:
- CEBPB,
- CREB-binding protein,
- EP300,
- NAB1,
- P53, and
- PSMA3
EGR2
Early growth response protein 2 is a protein that in humans is encoded by the EGR2 gene.  EGR2 (also termed Krox20) is a transcription regulatory factor, containing two zinc finger DNA-binding sites, and is highly expressed in a population of migrating neural crest cells. It is later expressed in the neural crest derived cells of the cranial ganglion. The protein encoded by Krox20 contains two cys2his2-type zinc fingers. Krox20 gene expression is restricted to the early hindbrain development. It is evolutionarily conserved in vertebrates, humans, mice, chicks, and zebra fish. In addition, the amino acid sequence and most aspects of the embryonic gene pattern is conserved among vertebrates, further implicating its role in hindbrain development. When the Krox20 is deleted in mice, the protein coding ability of the Krox20 gene (including the DNA-binding domain of the zinc finger) is diminished. These mice are unable to survive after birth and exhibit major hindbrain defects. These defects include but are not limited to defects in formation of cranial sensory ganglia, partial fusion of the trigeminal nerve (V) with the facial (VII) and auditory (VII) nerves, the proximal nerve roots coming off of these ganglia were disorganized and intertwined among one another as they entered the brainstem, and there was fusion of the glossopharyngeal (IX) nerve complex.

# Function
The early growth response protein 2 is a transcription factor with three tandem C2H2-type zinc fingers.  Mutations in this gene are associated with the autosomal dominant Charcot-Marie-Tooth disease, type 1D, DejerineSottas disease, and Congenital Hypomyelinating Neuropathy. Two studies have linked EGR2 expression to proliferation of osteoprogenitors  and cell lines derived from Ewing sarcoma, which is a highly aggressive bone-associated cancer.
New research suggests that Krox20 - or the lack of it - is the reason for male baldness.
EHD1
EH domain-containing protein 1, also known as testilin or PAST homolog 1 (PAST1), is a protein that in humans is encoded by the EHD1 gene belonging to the EHD protein family.

# Function
This gene belongs to a highly conserved gene family encoding EPS15 homology (EH) domain-containing proteins. The protein-binding EH domain was first noted in EPS15, a substrate for the epidermal growth factor receptor. The EH domain has been shown to be an important motif in proteins involved in protein-protein interactions and in intracellular sorting. The protein encoded by this gene is thought to play a role in the endocytosis of IGF1 receptors.

# Interactions
EHD1 has been shown to interact with Insulin-like growth factor 1 receptor and SNAP29.
EID2
EP300 interacting inhibitor of differentiation 2, also known as EID2 is a human gene.

# Function
The protein encoded by this gene may function as an endogenous suppressor of TGF-beta signaling and  inhibits differentiation by blocking the histone acetyltransferase activity of p300, class I histone deacetylase, HDACs. The N-terminal portion of EID-2 was required for the binding to HDACs. This region was also involved in the transcriptional repression and nuclear localization, suggesting the importance of the involvement of HDACs in the EID-2 function. EID-2 inhibits TGF-beta/Smad transcriptional responses. EID-2 interacts constitutively with Smad proteins, and most strongly with Smad3. Stable expression of EID-2 in the TGF-beta1-responsive cell line inhibits endogenous Smad3-Smad4 complex formation and TGF-beta1-induced expression of p21 and p15.
EID-2 displays developmentally regulated expression with high levels in adult heart and brain. Overexpression of EID-2 inhibits muscle-specific gene expression through inhibition of MyoD-dependent transcription. This inhibitory effect on gene expression can be explained by EID-2's ability to associate with and inhibit the acetyltransferase activity of p300.
EIF1
Eukaryotic translation initiation factor 1 (eIF1) is a protein that in humans is encoded by the EIF1 gene.
eIF1 interacts with the eukaryotic small (40S) ribosomal subunit and eIF3, and is a component of the 43S preinitiation complex (PIC). eIF1 and eIF1A bind cooperatively to the 40S to stabilize an "open" conformation of the preinitiation complex (PIC) during eukaryotic translation initiation. eIF1 binds to a region near the ribosomal A-site in the 40S subunit and functions in a manner similar to the structurally related bacterial counterpart IF1.

# Structure
eIF1 is a conserved translation protein in all eukaryotic cells that is responsible for the investigation of codon-anticodon mismatches during the initiation of translation. In order to determine the structure of human eIF1, an experiment with N-terminal His tag and eIF1 are conducted via using NMR spectroscopy. Scientists have discovered a binding site by generating yeast mutation and study the neighbor conserved residues located in the same region. GST pull-down experiments has shown that eIF1 binds precisely to the p110 subunit of eIF3 as a result explaining eIF1 recruiting. 

# Function
The function of eIf1 has some hidden aspects. However, in all eukaryotic cells initiation of mRNA translation starts with scanning via ribosomal 43S preinitiation complexes starting from the 5 end of the mRNA. Next, induction via eIF1 and eIF1A are needed to disclose the conformation of the 40S subunit in order to induce DEAD-box RNA helicase eIF4A, its cofactor eIF4B, and eIF4G activity.
EIF6
Eukaryotic translation initiation factor 6 (EIF6), also known as Integrin beta 4 binding protein (ITGB4BP), is a human gene.
Hemidesmosomes are structures which link the basal lamina to the intermediate filament cytoskeleton. An important functional component of hemidesmosomes is the integrin beta-4 subunit (ITGB4), a protein containing two fibronectin type III domains. The protein encoded by this gene binds to the fibronectin type III domains of ITGB4 and may help link ITGB4 to the intermediate filament cytoskeleton. The encoded protein, which is insoluble and found both in the nucleus and in the cytoplasm, can function as a translation initiation factor and catalyzes the association of the 40S and 60S ribosomal subunits along with eIF5 bound to GTP. Multiple transcript variants encoding several different isoforms have been found for this gene.

# Overview
EIF6 plays important roles in 80S ribosome formation, cell growth and gene expression. eukaryotic ribosome is 80S ribosome, which can separate to 40S and 60S subunits. EIF6 helps to product mature 60s subunit and then EIF6 should disassociate with 60s subunit so that it can binds to 40s subunit to form ribosome. Keeping in balance of EIF6 is essential for the body: few EIF6 helps synthesis of normal ribosome, while large amount of EIF6 inhibited 60s subunits bind to 40s subunits.

# Function
EIF6 exists both in nucleolus and cytoplasm. In the eukaryotic nucleolus, a 90S pre-ribosomal complex separate to a 60S pre-ribosomal complex and a 40S pre-ribosomal complex, which are involved in synthesis of mature ribosome. EIF6 is indispensable in 60S subunit biogenesis and deletion of EIF6 has lethal effect. The partial deletion of eIF6 results in decreasing of free 60S ribosomal subunit, which means it knocks the 40S/60S subunit ratio off balance,and limiting the speed of protein synthesis. 60S pre-ribosomal complex associated with eIF6 shuttle from nucleolus to cytoplasm and then eIF6 disassociated with pre-60S so that 60S subunit can binds to 40S subunit and continues to subsequent prograss. EIF6 can act as a rate-limiting translational initiation factor, and its expression levels influence the translational rate. Few of eIF6 will small accelerate protein translation, while large of eIF6 will block translational process by inhibiting production of ribosome. The activity of eIF6 also cause glycolysis and fatty acid synthesis by mRNAs' translational controlling.

# Expression
EIF6 has different level of expression in different tissue and cell. EIF6 has high level of expression in stem cells and cycling cells, while it doesn't in postmitotic cells; high level in brain and epithelia, while low level in muscle.

# Interactions
EIF6 has been shown to interact with FHL2, ITGB4 and GNB2L1.
EIF6 plays important roles in 80S ribosome formation, cell growth and gene expression.
ELP4
Elongation protein 4 homolog (S. cerevisiae), also known as ELP4, is a protein which in humans is encoded by the ELP4 gene.

# Function
This gene encodes a component of the six subunit elongator complex, a histone acetyltransferase complex that associates directly with RNA polymerase II during transcriptional elongation. The human gene can partially complement sensitivity phenotypes of yeast ELP4 deletion mutants. Alternatively spliced variants that encode different protein isoforms have been described but the full-length nature of only one has been determined.

# Clinical significance
In a study published in February 2009, researcher linked this gene to the most common form of human epilepsy, namely Rolandic epilepsy. This is the first gene to be linked with rolandic epilepsy.

# Background
It has been found that children with Rolandic epilepsy have a mutation of gene coding for the Elongator Protein Complex 4, which is involved in transcription and tRNA modification. Furthermore, Elp4 is needed for histone acetyltransferase (HAT) activity which makes DNA more accessible for transcription.  The lack of the Elp4/5/6 led to no HAT activity.  The importance of HAT activity is the initiation of transcription as well as its assistance of RNA polymerase II in transcription elongation through chromatin and acetyl-CoA dependent pathways.  Although Rolandic epilepsy (RE), which has been observed as autosomal dominant with high penetrance, develops around age 3 and disappears by age 12 there are serious problems that need to be addressed that occur while a child has RE. One of the major problems that can arise from RE is cognitive impairment. Though the cognitive impairment seen in Rolandic Epilepsy is of unclear etiology, one contributing factor may be increased glucose uptake in cortical areas, most notably in the associative cortex. These changes in glucose uptake may somehow disrupt the learning process and prevents the child from making the associations necessary to learn new things, which is how most human learning is achieved. Other factors which may contribute to cognitive impairment include seizure frequency, abnormal electrical activity in between seizures, and medication side effects, to only name a few.
The Elongator Protein Complex (ELP) is what regulates the growth of cortical projection neurons. This means that it helps cortical neurons to exhibit dendrite branching and radial migration of neurons to form the close knit neural network of the cerebral cortex. If ELP is not working properly or is not being expressed at the correct levels (too low) then the neurons in that region in particular would not be properly situated in relation to each other for proper brain activity. The expression of ELP and the fourth sub-unit (ELP4) in particular is the cause of Rolandic epilepsy and possibly other cognitive impairment later in life if the condition is severe enough or if it is not treated effectively.
ELSI

# Overview
ELSI stands for Ethical, Legal and Social Issues. It's a term associated with the Human genome project. This project didn't only have the goal to identify all the approximately 24.000 genes in the human DNA, but also to address the ELSI that might arise from the project.
5% of the US annual Human genome project (HGP) funds is allocated to address associated ELSI of the work.

# The failure of ELSI to help the impacted groups
As Debra Harry, Executive Director of the Indigenous Peoples Council on Biocolonialism (IPCB), would explain; despite a decade of ELSI funding, the burden of genetics education has fallen on the tribes themselves to understand the motives of Human genome project and its potential impacts on their lives.
Meanwhile, the government has been busily funding projects studying indigenous groups, without any meaningful consultation with the group. (See Biopiracy)
The main criticism of ELSI is the failure to address the conditions raised by population-based research, especially with regard to unique processes for group decision-making and cultural worldviews. Genetic variation research such as HGP is group population research, but most ethical guidelines, as Harry mentions, are not euipped to address group rights. She is making such claim because those research represents a clash of culture: indigenous people's life revolves around collectivity and group decision making whereas the Western culture promotes individuality.
Harry suggests that one of the challenges of ethical research is to include respect for collective review and decision making, while also upholding the traditional model of individual rights.