Persius/hicric huggingface dataset:
Dock3
Dock3 (Dedicator of cytokinesis 3), also known as MOCA (modifier of cell adhesion) and PBP (presenilin-binding protein), is a large (~180 kDa) protein involved in intracellular signalling networks. It is a member of the DOCK-B subfamily of the DOCK family of guanine nucleotide exchange factors (GEFs) which function as activators of small G proteins. Dock3 specifically activates the small G protein Rac.

# Discovery
Dock3 was originally discovered in a screen for proteins that bind presenilin (a transmembrane protein which is mutated in early onset Alzheimer's disease). Dock3 is specifically expressed in neurones (primarily in the cerebral cortex and hippocampus).

# Structure and function
Dock3 is part of a large class of proteins (GEFs) which contribute to cellular signalling events by activating small G proteins. In their resting state G proteins are bound to Guanosine diphosphate (GDP) and their activation requires the dissociation of GDP and binding of guanosine triphosphate (GTP). GEFs activate G proteins by promoting this nucleotide exchange.
Dock3 exhibits the same domain arrangement as Dock180 (a member of the DOCK-A subfamily and the archetypal member of the DOCK family) and these proteins share a considerable (40%) degree of sequence similarity.

# Regulation of Dock3 activity
Since Dock3 shares the same domain arrangement as Dock180 it is predicted to have a similar array of binding partners, although this has yet to be demonstrated. It contains an N-terminal SH3 domain, which in Dock180 binds ELMO (a family of adaptor proteins which mediate recruitment and efficient GEF activity of Dock180), and a C-terminal proline-rich region which, in Dock180, binds the adaptor protein CRK.

# Signalling downstream of Dock3
Dock3 GEF activity is directed specifically at Rac1. Dock3 has not been shown to interact with Rac3, another Rac protein which is expressed in neuronal cells, and this may be because Rac3 is primarily located in the perinuclear region. In fact, Rac1 and Rac3 appear to have distinct and antagonistic roles in these cells. Dock3-mediated Rac1 activation promotes reorganisation of the cytoskeleton in SH-SY5Y neuroblastoma cells and primary cortical neurones as well as morphological changes in fibroblasts. It has also been shown to regulate neurite outgrowth and cell-cell adhesion in B103 and PC12 cells.

# Dock3 in neurological disorders
The first indication that Dock3 might be involved in neurological disorders came when Dock3 was shown to bind to presenilin, a transmembrane enzyme involved in the generation of beta amyloid (A), accumulation of which is an important step in the development of Alzheimer's disease. Dock3 has been shown to undergo redistribution and association with neurofibrillary tangles in brain samples from Alzheimers patients. A mutation in Dock3 was also identified in a family displaying a phenotype resembling attention-deficit hyperactivity disorder (ADHD).
Dock6
Dock6 (Dedicator of cytokinesis 6), also known as Zir1 is a large (~200 kDa) protein involved in intracellular signalling networks. It is a member of the DOCK-C subfamily of the DOCK family of guanine nucleotide exchange factors which function as activators of small G proteins.

# Discovery
Dock6 was identified as one of a family of proteins which share high sequence similarity with Dock180, the archetypal member of the DOCK family. It has a similar domain arrangement to other DOCK proteins, with a DHR1 domain known in other proteins to bind phospholipids, and a DHR2 domain containing the GEF activity.

# Function
There is currently very little information about the cellular role of this protein. However, Dock6 has been reported to exhibit dual GEF specificity towards the small G proteins Rac1 and Cdc42. It is the only DOCK family member reported to activate both of these G proteins. The same study also showed that transfection of the Dock6 DHR2 domain into N1E-115 neuroblastoma cells promoted Rac- and Cdc42-dependent neurite outgrowth, although the physiological significance of this has yet to be demonstrated.
Dock9
Dock9 (Dedicator of cytokinesis 9), also known as Zizimin1, is a large (~230 kDa) protein involved in intracellular signalling networks. It is a member of the DOCK-D subfamily of the DOCK family of guanine nucleotide exchange factors that function as activators of small G proteins. Dock9 activates the small G protein Cdc42.

# Discovery
Dock9 was discovered using an affinity proteomic approach designed to identify novel activators of the small G protein Cdc42 in fibroblasts. Subsequent northern blot analysis revealed that Dock9 is expressed primarily in the brain, heart, skeletal muscle, kidney, placenta and lung. Lower levels were detected in the colon, thymus, liver, small intestine and in leukocytes from peripheral blood.

# Structure and Function
Dock9 shares a similar structure of two core domains (known as DHR1 and DHR2), which are shared by all DOCK family members. The C-terminal DHR2 domain functions as an atypical GEF domain for small G proteins (see Dock180: structure and function) and the DHR1 domain is known, in some DOCK-A/B/C subfamily proteins, to be involved in their recruitment to the plasma membrane. Unlike DOCK-A/B/C proteins DOCK-D proteins (including Dock9) contain an N-terminal pleckstrin homology (PH) domain that mediates their recruitment to the membrane. Dock9, along with other DOCK-C/D subfamily members, can activate Cdc42 in vitro and in vivo via its DHR2 domain. However, Dock9 adopts an autoinhibitory conformation that masks the DHR2 domain in its resting state. The mechanism by which this autoinhibition is overcome is still unclear although in some other DOCK proteins, which also undergo autoinhibition, it requires an interaction with adaptor proteins such as ELMO. Dock9 has also been reported to dimerise, under resting conditions, via its DHR2 domains and this study suggests that other DOCK family proteins may also behave in the same way. Recent analysis of a chromosomal region associated with susceptibility to bipolar disorder revealed that single nucleotide polymorphisms in the DOCK9 gene contribute to the risk and severity of this condition.
Dylar
Dylar is a fictional psychoactive drug that appears in Don DeLillo's novel White Noise.
Dylar is intended to remove the fear of death.  However, the drug does not work properly and extended use sometimes results in insanity.  Extended users interpret spoken words and metaphor as actual actions and events. In an instance presented in the novel, the spoken phrase "hail of bullets" causes a Dylar-using character to panic, drop to the floor and crawl to shelter.
The drug is only produced on an experimental, highly secretive basis and comes in the form of a small white pill with an insoluble polymer coating containing only a minute hole.  During digestion water enters through the polymer coating and the active ingredients begin to dissolve, but can only leave the polymer coating through the tiny laser drilled hole, creating a highly controlled release of the chemical.  When empty, the coating collapses in on itself and passes harmlessly out through the digestive tract.
EC-No
The terms EC-No and EC# refer to the seven-digit code (sometimes called the EC number) that has been allocated by the Commission of the European Communities for commercially available chemical substances within the European Union. The European EC Number should not be confused with the Enzyme Commission EC number for enzymes.
The "EC#" designation supersedes the outmoded EINECS and ELINCS designations, and the EC# codes include those on the
so-called No-longer Polymers List, a list of substances that were on the European market between 18 September 1981 and 31 October 1993 and at the time were regarded as polymers, but are no longer regarded as such.

# Format
The EC# is made up of seven digits according to the pattern xxx-xxx-x.
EINECs numbers start with number 200-001-8.
ELINCS numbers start with 400-010-9
Numbers in the No-longer Polymers List start with 500-001-0.
The EC/EINECS/ELINCS Number may be written in a general form as:
in which R is the check digit and N represents a fundamental sequential number. The check digit is the remainder of the following sum after division by 11:
ECGF1
Thymidine phosphorylase is an enzyme that in humans is encoded by the TYMP gene.
Platelet-derived endothelial cell growth factor (ECGF1) is an angiogenic factor which promotes angiogenesis in vivo and stimulates the in vitro growth of a variety of endothelial cells. ECGF1 has a highly restricted target cell specificity acting only on endothelial cells. 
Because it limits glial cell proliferation, ECGF1 is also known as thymidine phosphorylase and as gliostatin. The ECGF1 gene contains 10 exons spanning more than 4.3 kb. Thymidine phosphorylase activity of ECGF1 in leukocytes from mitochondrial neurogastrointestinal encephalomyopathy (MNGIE) patients was less than 5 percent of controls, indicating that loss-of-function mutations in thymidine phosphorylase cause MNGIE.

# Interactive pathway map
Click on genes, proteins and metabolites below to link to respective articles.
-  The interactive pathway map can be edited at WikiPathways: "FluoropyrimidineActivity_WP1601"..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}
ECHS1
Enoyl Coenzyme A hydratase, short chain, 1, mitochondrial, also known as ECHS1, is a human gene.
The protein encoded by this gene functions in the second step of the mitochondrial fatty acid beta-oxidation pathway. It catalyzes the hydration of 2-trans-enoyl-coenzyme A (CoA) intermediates to L-3-hydroxyacyl-CoAs. The gene product is a member of the hydratase/isomerase superfamily. It localizes to the mitochondrial matrix. Transcript variants utilizing alternative transcription initiation sites have been described in the literature.

# Structure
The ECHS1 gene is approximately 11 kb in length, and is composed of eight exons, with exons I and VIII containing the 5'- and 3'-untranslated regions, respectively. There are two major transcription start sites, located 62 and 63 bp upstream of the translation codon, were mapped by primer extension analysis. The 5'-flanking region of the ECHS1 gene is GC-rich and contains several copies of the SP1 binding motive but no typical TATA or CAAT boxes are apparent. Alu repeat elements have been identified within the region -1052/-770 relative to the cap site and in intron 7. The precursor polypeptide contains 290 amino acid residues, with an N-terminal presequence of 29 residues, a  5'-untranslated sequence of 21 bp and a 3'-untranslated sequence of 391 bp.

# Function
Enoyl-CoA hydratase (ECH) catalyzes the second step in beta-oxidation pathway of fatty acid metabolism. The enzyme is involved in the formation of a -hydroxyacyl-CoA thioester. The two catalytic glutamic acid residues are believed to act in concert to activate a water molecule, while Gly-141 is proposed to be involved in substrate activation. There are two potent inhibitors of ECHS, which irreversibly inactivate the enzyme via covalent adduct formation.

# Clinical significance
Enoyl-CoA hydratase short chain has been confirmed to interact with STAT3, such that ECHS1 specifically represses STAT3 activity by inhibiting STAT3 phosphorylation. STAT3 can act as both an oncogene and a tumor suppressor. ECHS1 itself has shown to occur in many cancers, particularly in hypatocellular carcinoma (HCC) development; both exogenous and endogenous forms of ECHS1 bind to HBs and induce apoptosis as a result. This means that ECHS1 may be used in the future as a therapy for patients with HBV-related hepatitis or HCC.
ECSIT
Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial (ECSIT), also known as SITPEC, is a protein that in humans is encoded by the ECSIT gene. ECSIT is a cytosolic adaptor protein involved in inflammatory responses, embryonic development, and the assembly and stabilization of mitochondrial NADH:ubiquinone oxidoreductase (complex I).

# Structure
ECSIT is located on the p arm of chromosome 19 in position 13.2 and has 9 exons. The ECSIT gene produces a 49 kDa protein composed of 431 amino acids. ECSIT's interactions with p65/p50 NF-B proteins is dependent on lysine 372 ubiquitination. ECSIT also contains an N-terminal targeting signal that causes it to localize to mitochondria where only the 45 kDa mitochondrial ECSIT is found to interact.

# Function
ECSIT has been found to play multiple roles in cell-signaling, including those that utilize Toll-like receptors (TLRs), TGF-, and BMP. ECSIT plays a regulatory role as part of the TAK1-ECSIT-TRAF6 complex that is involved in the activation of NF-B by the TLR4 signal and through its interactions with TRIM59 to negatively regulate NF-B, IRF-3, and IRF-7-mediated signal pathways. Additionally, ECSIT appears to contribute to bactericidal activity in TLR signaling through its interaction with tumor necrosis factor receptor-associated factor 6 (TRAF6). Importantly, ubiquitination of ECSIT has shown itself to be necessary for the activation of p65/p50 NF-Bs in TLR4 signaling. Functioning as a scaffold protein, ECSIT is also essential for the association of RIG-I-like receptors (RIG-I or MDA5) to VISA. The bridging of these receptors to VISA is an important signaling event used in innate antiviral responses. Apart from inflammatory and immune responses, ECSIT, in its 45 kDa, mitochondrial form helps maintain assembly chaperone NDUFAF1's stable presence in the mitochondrion. Through this interaction, ECSIT is demonstrated to play an important role in NADH:ubiquinone oxidoreductase (complex I) assembly and stabilization. Finally, it is important to note that ECSIT is required for normal embryonic development.

# Interactions
ECSIT has 136 protein-protein interactions, with 53 of them being co-complex interactions.
EEF1D
Elongation factor 1-delta is a protein that in humans is encoded by the EEF1D gene.

# Function
This gene encodes a subunit of the elongation factor-1 complex, which is responsible for the enzymatic delivery of aminoacyl tRNAs to the ribosome. This subunit functions as guanine nucleotide exchange factor. It is reported that this subunit interacts with HIV-1 Tat, and thus it represses the translation of host-cell, but not HIV-1, mRNAs. Several alternatively spliced transcript variants have been found for this gene, however, the full length nature of only two variants has been determined.

# Interactions
EEF1D has been shown to interact with Glycyl-tRNA synthetase, EEF1G and KTN1, and is predicted to interact with TMEM63A.
EEF2K
Eukaryotic elongation factor-2 kinase (eEF-2 kinase or eEF-2K), also known as calmodulin-dependent protein kinase III (CAMKIII) and calcium/calmodulin-dependent eukaryotic elongation factor 2 kinase, is an enzyme that in humans is encoded by the EEF2K gene.

# Function
eEF-2 kinase is a highly conserved protein kinase in the calmodulin-mediated signaling pathway that links multiple up-stream signals to the regulation of protein synthesis. It phosphorylates eukaryotic elongation factor 2 (EEF2) and thus inhibits the EEF2 function.

# Activation
The activity of eEF-2K is dependent on calcium and calmodulin. Activation of eEF-2K proceeds by a sequential two-step mechanism. First, calcium-calmodulin binds with high affinity to activate the kinase domain, triggering rapid autophosphorylation of Thr-348. In the second step, autophosphorylation of Thr-348 leads to a conformational change in the kinase likely supported by the binding of phospho-Thr-348 to an allosteric phosphate binding pocket in the kinase domain. This increases the activity of eEF-2K against its substrate, elongation factor 2.
eEF-2K can gain calcium-independent activity through autophosphorylation of Ser-500. However, calmodulin must remain bound to the enzyme for its activity to be sustained.

# Clinical significance
The activity of this kinase is increased in many cancers and may be a valid target for anti-cancer treatment.
It is also suggested that eEF-2K may play a role the rapid anti-depressant effects of ketamine through its regulation of neuronal protein synthesis.

# Cancer
eEF-2K expression is often upregulated in cancer cells, including breast and pancreatic cancers and promotes cell proliferation, survival, motility/migration, invasion and tumorigenesis.
EFHC2
EF-hand domain (C-terminal) containing 2 is a protein that in humans is encoded by the EFHC2 gene.

# Gene
EFHC2 is located on the negative strand (sense strand) of the X chromosome at p11.3. EFHC2 is also one of a few, select number of genes with in vitro evidence suggesting that it escapes X inactivation. EFHC2 spans 195,796 base pairs and is neighbored by NDP, the gene encoding for Norrie disease protein. Preliminary evidence based on genome wide association studies have linked a SNP in the intron between exons 13 and 14 of EFHC2 with harm avoidance.
The mRNA transcript encoding the EFHC2 protein is 3,269 base pairs. The first ninety base pairs compose the five prime untranslated region and the last 1913 base pairs compose the three prime untranslated region.

# Protein
The EFHC2 gene encodes a 749-amino acid protein which contains three DM10 domains (InterPro: IPR006602) and three calcium-binding EF-hand motifs.
The isoelectric point of EFHC2 is estimated to be 7.13 in humans. Relative to other proteins expressed in humans, EFHC2 has fewer alanine residues and a greater number of tyrosine residues and is predicted to reside in the cytoplasm.

# Tissue distribution
EFHC2 is widely expressed in the central nervous system as well as peripheral tissues.

# Clinical significance
A related protein, EFHC1 is encoded by a gene on chromosome 6. It has been suggested that both proteins are involved in the development of epilepsy and that this gene may be associated with fear recognition in individuals with Turner syndrome.
A mutation in EFHC2 which results in a serine to a tyrosine substitution at amino acid position 430 (S430Y) has been associated with juvenile myoclonic epilepsy in a  male, German population. Additionally, a single nucleotide polymorphism in EFHC2 correlates to a reduced ability of Turner syndrome patients to recognize fear in facial expressions; however, these findings remain controversial.

# Conservation in other species
EGLN2
Egl nine homolog 2 is a protein that in humans is encoded by the EGLN2 gene. ELGN2 is a alpha-ketoglutarate-dependent hydroxylase, a superfamily of non-haem iron-containing proteins.
The hypoxia inducible factor (HIF) is a transcriptional complex which is involved in oxygen homeostasis. At normal oxygen levels, the alpha subunit of HIF is targeted for degradation by prolyl hydroxylation. 
This gene encodes an enzyme responsible for this posttranslational modification. Multiple alternatively spliced variants, encoding the same protein, have been identified.
EHMT1
Euchromatic histone-lysine N-methyltransferase 1, also known as G9a-like protein (GLP), is a protein that in humans is encoded by the EHMT1 gene.

# Function
The protein encoded by this gene is a histone methyltransferase that is part of the E2F6 complex, which represses transcription. The encoded protein methylates the Lys-9 position of histone H3, which tags it for transcriptional repression. This protein may be involved in the silencing of MYC- and E2F-responsive genes and therefore could play a role in the G0/G1 cell cycle transition.

# Clinical significance
Defects in this gene are a cause of chromosome 9q subtelomeric deletion syndrome (9q-syndrome).
EHMT2
Euchromatic histone-lysine N-methyltransferase 2 (EHMT2), also known as G9a, is a histone methyltransferase enzyme that in humans is encoded by the EHMT2 gene. G9a catalyzes the mono- and di-methylated states of histone H3 at lysine residue 9 (i.e., H3K9me1 and H3K9me2) and lysine residue 27 (H3K27me1 and HeK27me2).

# Function
A cluster of genes, BAT1-BAT5, has been localized in the vicinity of the genes for TNF alpha and TNF beta. This gene is found near this cluster; it was mapped near the gene for C2 within a 120-kb region that included a HSP70 gene pair. These genes are all within the human major histocompatibility complex class III region. This gene was thought to be two different genes, NG36 and G9a, adjacent to each other but a recent publication shows that there is only a single gene. The protein encoded by this gene is thought to be involved in intracellular protein-protein interaction. There are three alternatively spliced transcript variants of this gene but only two are fully described.
G9a and G9a-like protein, another histone-lysine N-methyltransferase, catalyze the synthesis of H3K9me2, which is a repressive mark. G9a is an important control mechanism for epigenetic regulation within the nucleus accumbens (NAcc); reduced G9a expression in the NAcc plays a central role in mediating the development of an addiction.  G9a opposes increases in FosB expression via H3K9me2 and is suppressed by FosB. G9a exerts opposite effects to that of FosB on drug-related behavior (e.g., self-administration) and synaptic remodeling (e.g., dendritic arborization  the development of additional tree-like dendritic branches and spines) in the nucleus accumbens, and therefore opposes FosB's function as well as increases in its expression. G9a and FosB share many of the same gene targets.

# Interactions
EHMT2 has been shown to interact with KIAA0515 and the prostate tissue associated homeodomain protein NKX3.1.
eIF-2
eIF-2 (Eukaryotic Initiation Factor 2) is a heterotrimer of subunits alpha, beta, and gamma. eIF-2 mediates the binding of methionyl-tRNAimet to the ribosome in a GTP-dependent manner.
eIF-2 is released from the ribosome bound to GDP as an inactive binary complex.
To participate in another round of translation initiation, this GDP must be exchanged for GTP.
Under steady-state conditions of translation, eIF-2 must be recycled in order to participate in another round of translation initiation.

# eIF-2B
Conversion of the inactive eIF-2-GDP to the active eIF-2-GTP form is catalyzed by a guanine nucleotide exchange factor, eIF-2B.
Phosphorylation of the alpha subunit of eIF-2 inhibits translation initiation by impairing the eIF-2B-catalyzed guanine nucleotide exchange reaction.
EIF3K
Eukaryotic translation initiation factor 3 subunit K (eIF3k) is a protein that in humans is encoded by the EIF3K gene.

# Function
The ~800 kDa eukaryotic initiation factor 3 (eIF3) is the largest eIF and contains at least 12 subunits, including eIF3k/EIF2S12. eIF3 plays an essential role in translation by binding directly to the 40S ribosomal subunit and promoting formation of the 43S preinitiation complex.

# Interactions
eIF3k has been shown to interact with Cyclin D3 and eIF3a.