Persius/hicric huggingface dataset:
Kepone

# Overview
Kepone, also known as chlordecone, is a carcinogenic insecticide related to mirex, used between 1966 and 1975 in the USA for ant and roach baits. It was produced by Allied Signal Company in Hopewell, Virginia and produced nationwide pollution controversy due to improper handling and dumping of the substance into the James River. Its use was banned in 1975.
Chemically, kepone is a chlorinated polycyclic ketone insecticide and fungicide with the chemical formula Template:Carbon10Template:Hydrogen2Template:Chlorine10Template:Oxygen. The dry powder is readily absorbed through the skin and respiratory tract. Some unprotected production workers exposed to Kepone powder suffered tremors, jerky eye movements, memory loss, headaches, slurred speech, unsteadiness, lack of coordination, lost of weight, rash, enlarged liver, decreased libido, sterility, chest pain, anrthralgia, and the increased risk of developing cancer. Kepone persisted in the environment, with a half-life of about 30 years.
In July 2005, a Richmond Magazine article chronicled the ill health effects on Allied Signal employees and described how Dan Rather and CBS's 60 Minutes brought nationwide attention to the problem.
Due to the pollution scare, many businesses and restaurants along the river suffered, and then-Governor Mills Godwin Jr. shut down the James River to fishing from Richmond to the Chesapeake Bay.

# Trivia
The Dead Kennedys recorded a song named Kepone Factory, deliberately referring to the Minamata disease, for their 1981 album 
In God We Trust, Inc..  The song was written in 1978 and was performed live despite not appearing on any recording until 1981.
Kepone (band) was also an American indie rock band based out of Richmond, Virginia. Formed in 1991 ) the band's name is derived from the Kepone crisis that occurred in the Richmond area in the 1970's. Originally formed as a sideproject of Michael Bishop, ex-bassist of GWAR.
Kilohm
The ohm (symbol: ) is the SI unit of electrical impedance or, in the direct current case, electrical resistance, named after Georg Ohm.

# Definition
The ohm is the electric resistance between two points of a conductor when a constant potential difference of 1 volt, applied to these points, produces in the conductor a current of 1 ampere, the conductor not being the seat of any electromotive force.

# Conversions
- A measurement in ohms is the reciprocal of a measurement in siemens, the SI unit of electrical conductance. Note that 'siemens' is both singular and plural.  The non-SI unit, the mho (ohm written backwards), is equivalent to siemens but is mostly obsolete and rarely used.
- Ohms to watts: The power dissipated by a resistor may be calculated using resistance and voltage. The formula is a combination of Ohm's law and Joule's law:

# References and notes
-  BIPM SI Brochure: Appendix 1, p. 144
Kir2.1
The Kir2.1 inward-rectifier potassium ion channel is encoded by the KCNJ2 gene.

# Clinical significance
A defect in this gene is associated with Andersen-Tawil syndrome.
A mutation in the KCNJ2 gene  has also been shown to cause short QT syndrome.

# In research
In neurogenetics, Kir2.1 is used in Drosophila research to inhibit neurons, as overexpression of this channel will hyperpolarize cells.
In optogenetics, a trafficking sequence from Kir2.1 has been added to halorhodopsin to improve its membrane localization. The resulting protein eNpHR3.0 is used in optogenetic research to inhibit neurons with light.
Expression of Kir2.1 gene in human HEK293 cells induce a transient outward current, creating a steady membrane potential close to the reversal potential of potassium.

# Interactions
Kir2.1 has been shown to interact with:
- DLG4,
- Interleukin 16, and
- TRAK2
Kir2.6
The Kir2.6 also known as inward rectifier potassium channel 18 is a protein that in humans is encoded by the KCNJ18 gene. Kir2.6 is an inward-rectifier potassium ion channel.

# Function
Inwardly rectifying potassium channels, such as Kir2.6, maintain resting membrane potential in excitable cells and aid in repolarization of cells following depolarization. Kir2.6 is primarily expressed in skeletal muscle and is transcriptionally regulated by thyroid hormone.

# Clinical signifiance
Mutations in this gene have been linked to thyrotoxic periodic paralysis.
Kir6.2
Kir6.2 is a major subunit of the ATP-sensitive K+ channel, an inward-rectifier potassium ion channel. The gene encoding the channel is called KCNJ11 and mutations in this gene are associated with congenital hyperinsulinism.

# Structure
It is an integral membrane protein. The protein, which has a greater tendency to allow potassium to flow into a cell rather than out of a cell, is controlled by G-proteins and is found associated with the sulfonylurea receptor (SUR) to constitute the ATP-sensitive K+ channel.

# Pathology
Mutations in this gene are a cause of familial persistent hyperinsulinemic hypoglycemia of infancy (PHHI), an autosomal recessive disorder characterized by unregulated insulin secretion. Defects in this gene may also contribute to autosomal dominant non-insulin-dependent diabetes mellitus type II (NIDDM).
Kykeon
Kykeon (Gr. , from , "to stir, to mix") was an Ancient Greek drink made mainly of water, barley and herbs. It was used at the climax of the Eleusinian Mysteries to break a sacred fast, but it was also a favourite drink of Greek peasants.
Kykeon is mentioned in Homeric texts: the Iliad describes it as consisting of barley, water, herbs, and ground goat cheese (XV, 638641). In the Odyssey, Circe adds some honey and pours her magic potion in it (X, 234). In the The Homeric Hymn to Demeter, the goddess refuses red wine but accepts kykeon made from water, barley and pennyroyal.
It was supposed to have digestive properties. Hermes recommends it in Aristophanes' Peace (v. 712) to the hero who ate too much dry fruit and nuts. Aristocrats shunned it as a peasant drink. Theophrastus depicts in his Characters (IV, 23) a peasant whose thyme breath inconveniences his neighbours at the Ecclesia.
In an attempt to solve the mystery of how so many people over the span of two millennia could have consistently experienced revelatory states during the culminating ceremony of the Eleusinian Mysteries, it has been posited that the barley used in the Eleusinian kykeon was parasitized by ergot, and that the psychoactive properties of that fungus triggered the intense experiences alluded to by the participants at Eleusis.
Various modern attempts to duplicate the kykeon using ergot have yielded inconclusive results.
For more on the possibilities of the Kykeon's psychoactive properties, see entheogenic theories of the mysteries.

# Bibliography
- French Armand Delatte, Le Cyceon, breuvage rituel des mysteres d'Eleusis, Belles Lettres, Paris, 1955
L2HGDH
L-2-hydroxyglutarate dehydrogenase, mitochondrial is an enzyme that in humans is encoded by the L2HGDH gene, also known as C14orf160,  on chromosome 14.

# Function
This gene encodes L-2-hydroxyglutarate dehydrogenase, a flavin adenine dinucleotide (FAD)-dependent enzyme that oxidizes L-2-hydroxyglutarate to alpha-ketoglutarate in a variety of mammalian tissues. Mutations in this gene cause L-2-hydroxyglutaric aciduria, a rare autosomal recessive neurometabolic disorder resulting in moderate to severe mental retardation.
L2HGDH codes for a protein that is 50 kDa in size. The L2HGDH protein contains a mitochondrial-targeting transit peptide and is localized to the mitochondrial inner membrane inside mitochondria inside the cell. The L2HGDH protein catalyzes the following reaction,  and  requires flavin adenine dinucleotide (FAD) as a co-factor:
(S)-2-hydroxyglutarate + acceptor = 2-oxoglutarate + reduced acceptor.
L-2-hydroxyglutarate is produced by promiscuous action of malate dehydrogenase on 2-oxoglutarate; the L2HGDH protein is thus an example of a metabolite repair enzyme because it reconverts the useless damage product L-2-hydroxyglutarate back to 2-oxoglutarate.

# Clinical significance
Mutations in the L2HGDH gene cause L-2-hydroxyglutaric aciduria, a rare autosomal recessive neurometabolic disorder. Individuals with L2HGDH mutations present toxic accumulation of high concentration of L-2-hydroxyglutaric acid in the plasma and cerebrospinal fluid. At least 70 disease-causing variants in the L2HGDH gene have been discovered in patients. Patients with L-2-hydroxyglutaric aciduria are associated with moderate to severe mental retardation, psychomotor retardation, cerebellar ataxia, macrocephaly, or epilepsy.
L2HGDH has a role in mediating differentiation in T-cells via its activity on S-2HG

# Molecular interactions
KLK10
LACTB2
Lactamase, beta 2 is a protein that in humans is encoded by the LACTB2 gene.

# Structure
LACTB2 is located on the 8th chromosome, with its specific location being 8q13.3. The gene contains 7 exons.
The LACTB2 protein has a metallo -lactamase (MBL) fold, with two zinc ions in the active site.

# Function
The metallo beta-lactamases were first identified in bacteria; they give some strains antibiotic resistance by degrading beta-lactam antibiotics (such as penicillins). However, the protein family includes many members that are ribonucleases (RNases), deoxyribonucleases (DNases) and other metabolic enzymes  MBL ribonucleases are responsible for RNA processing, generating the 3' end of tRNA,(RNase Z ) eukaryotic mRNA (CPSF-73) and  snRNA molecules  LACTB2 is a mitochondrial endoribonuclease which may have a role in degrading mitochondrial mRNAs.

# Clinical significance
A tumor-specific LACTB2-NCOA2 fusion originating from intra-chromosomal rearrangement of chromosome 8 has been identified at both DNA and RNA levels. Unlike conventional oncogenic chimeric proteins, the fusion product lacks functional domain from respective genes, indicative of an amorphic rearrangement. This chimeric LACTB2-NCOA2 transcript was detected in 6 out of 99 (6.1%) colorectal cancer (CRC) cases, where NCOA2 was significantly downregulated. Enforced expression of wild-type NCOA2 but not the LACTB2-NCOA2 fusion protein impaired the pro-tumorigenic phenotypes of CRC cells, whereas knockdown of endogenous NCOA2 in normal colonocytes had opposite effects. Mechanistically, NCOA2 inhibited Wnt/-catenin signaling through simultaneously upregulating inhibitors and downregulating stimulators of Wnt/-catenin pathway. NCOA2 is a novel negative growth regulatory gene repressing the Wnt/-catenin pathway in CRC, where recurrent fusion with LACTB2 contributes to its disruption.
LANCL2
LanC-like protein 2 is a protein that in humans is encoded by the LANCL2 gene. It is a protein broadly expressed in the plasma a nuclear membranes of immune, epithelial and muscle cells and a potential therapeutic target for chronic inflammatory, metabolic and immune-mediated diseases such as Crohns disease and diabetes.

# Function
The natural ligand of LANCL2, abscisic acid (ABA), has been identified as a new endogenous mammalian hormone implicated in glycemic control. The mammalian ABA receptor has been identified as LANCL2 on the basis of (1) modeling predictions, (2) direct and specific ABA binding to the purified recombinant protein, and (3) abrogation of the functional effects of ABA by silencing of LANCL2 expression in ABA-sensitive cells.
Selective binding between LANCL2 and ABA or other ligands such as the benzimidazole NSC61610 and piperazine BT-11, lead to elevation of intracellular cAMP, activation of PKA and suppression of inflammation in macrophages. In hepatocytes, LANCL2 regulates cell survival by phosphorylation of Akt through its interaction with the Akt kinase mTORC2. Active mTORC2 causes translocation of GLUT4 to the plasma membrane and stimulates glucose uptake. LANCL2 expression in immune cells, adipose tissue, skeletal muscle and pancreas, and the potential to manipulate LANCL2 signaling and GLUT4 translocation with ABA make this G protein-coupled receptor a novel therapeutic target for glycemic control. In humans, ABA release was detected with increasing glycemia, although this mechanism failed in people suffering from type 2 and gestational diabetes. Also, plasma ABA concentrations increase after oral glucose load (OGTT) in healthy subjects. ABA stimulates glucose-dependent insulin release from human and rodent pancreatic -cells. At a low dose (micrograms/Kg body weight) oral ABA significantly reduces both glycemia and insulinemia in rats and in humans undergoing an OGTT  indicating that ABA reduces the amount of insulin required to control hyperglycemia. This insulin-sparing effect suggests that LANCL2 can be used as a therapeutic target for the treatment of inflammatory and metabolic diseases such as metabolic syndrome, prediabetes and diabetes.
Novel LANCL2 ligands such as BT-11 significantly decrease disease activity in the Dextran Sodium Sulfate (DSS)-induced model of acute colitis and the IL-10-/- mice and CD4+ T cell transfer-induced chronic colitis models. BT-11 treatment decreased leukocytic infiltration, mucosal thickening and epithelial erosion in the colon, decreased Th1 and Th17 CD4+ T cells and TNF while increasing regulatory T cells, LANCL2 and IL-10 expression.
LILRB4
Leukocyte immunoglobulin-like receptor subfamily B member 4 is a protein that in humans is encoded by the LILRB4 gene.
This gene is a member of the leukocyte immunoglobulin-like receptor (LIR) family, which is found in a gene cluster at chromosomal region 19q13.4. The encoded protein belongs to the subfamily B class of LIR receptors which contain two or four extracellular immunoglobulin domains, a transmembrane domain, and two to four cytoplasmic immunoreceptor tyrosine-based inhibitory motifs (ITIMs). The receptor is expressed on immune cells where it binds to MHC class I molecules on antigen-presenting cells and transduces a negative signal that inhibits stimulation of an immune response. The receptor can also function in antigen capture and presentation. It is thought to control inflammatory responses and cytotoxicity to help focus the immune response and limit autoreactivity. Multiple transcript variants encoding different isoforms have been found for this gene.

# Interactions
LILRB4 has been shown to interact with PTPN6 and INPP5D (SHIP-1).
LRPPRC
Leucine-rich PPR motif-containing protein, mitochondrial is a protein that in humans is encoded by the LRPPRC gene. Transcripts ranging in size from 4.8 to 7.0 kb which result from alternative polyadenylation have been reported for this gene.

# Function
This gene encodes a protein that is leucine-rich and is thought to play a role in regulating the interaction of the cytoskeleton with a variety of cellular processes.

# Clinical significance
An integrative genomics strategy led to the discovery that mutations in LRPPRC cause the French-Canadian variant of Leigh syndrome.  Furthermore, mutation in the LRPPRC gene causes lowered expression of MT-CO1 (cytochrome c oxidase I) and MT-CO3.
LRRC23
Leucine-rich repeat-containing protein 23 is a protein that in humans is encoded by the LRRC23 gene.

# Function
The function of LRRC23 is unknown. It is a member of the leucine-rich repeat family of proteins, which are known for participating in protein-protein interactions. Experimental evidence suggests that LRRC23 interacts with the CD28 protein in a pathway related to the immune system and development of regulatory T cells that control spontaneous autoimmune disease.

# Protein sequence
LRRC23 spans 343 residues containing two varieties of internally repeating sequence. Detected and aligned by RADAR, the most abundant repeat is the leucine-rich repeat, repeating 9 times in bases 89-287. The other repeated sequence occurs twice in bases 3-36. The RADAR program output, below, summarizes the composition and location of all the repeats and aligns them for comparison against each other.
File:LRRC23 RADAR Internal Repeats.png
The human genome produces three known variants of LRRC23. The largest splice variant, variant 3, contains 8 exons. Variants 1 and 2 use alternative first exons, and variant 2 excludes the seventh exon, giving it a total of seven exons making up the mRNA.

# Protein structure
Although the actual structure of LRRC23 is unknown, comparison to the crystal structures of various similar proteins such as 2OMW A (e-value 1.00e-17) reveals a structure typical of other leucine-rich repeat proteins. Alternating beta sheets and coils create a spiraled peptide chain forming an arch shape with beta-sheets occupying the concave surface.
The aligned structure of 2OMW_A with LRRC23 spans acids 72-272 of the LRRC23 protein. Conserved asparagines are highlighted in yellow, showing the regularity of spacing and repeat structure within. This model was generated using Cn3D software provided by NCBI.
File:CBlast 72-272 asparagines.png
LRRC24
Leucine rich repeat containing 24 is a protein that, in humans, is encoded by the LRRC24 gene. The protein is represented by the official symbol LRRC24, and is alternatively known as LRRC14OS. The function of LRRC24 is currently unknown. It is a member of the leucine-rich repeat (LRR) superfamily of proteins.

# Gene
In humans, LRRC24 is located on Chromosome 8 (8q24.3). The gene spans approximately 4.66 kb on the opposite strand. LRRC24 is composed of five exons, and only a single gene isoform has been identified.

# Protein

## General features
LRRC24 is a transmembrane protein of unknown function. Human LRRC24 consists of 513 amino acids including a 23 amino acid signal peptide. The mature form of the protein has a molecular weight of 52.9 kDa. The isoelectric point of the mature human protein is 7.98 The protein is largely composed of alpha helices.

## Domains
LRRC24 is a single-pass transmembrane protein. The protein consists of six leucine-rich repeats and an immunoglobulin-like domain.

## Localization
LRRC24 is a secreted protein as is evidenced by the presence of a signal peptide. The structure of the protein suggests that it localizes to the cell membrane.

# Homology
LRRC24 is conserved in Euteleostomi with the exception of Aves. Also, based on sequence homology analysis, distant orthologs of LRRC24 are also conserved in invertebrates of phyla Mollusca and Arthropoda. No human paralogs of LRRC24 have been identified.

# Expression
Microarray and in situ hybridization experiments suggest LRRC24 is primarily expressed within the brain. Expression is observed to be especially high within the midbrain, neocortex, and tissues of the limbic system, including the hypothalamus and hippocampal formation.

# Interactions
Protein-protein interactions of LRRC24 implicate the protein with cell signaling, cell migration, and axon guidance. ROBO2 was found to interact with LRRC24. ROBO2 is a member of the Roundabout gene family, which are well known to play a significant role in nervous system development. Also, LRRC24 was found to interact with LRRTM4, a protein believed to be involved in synaptogenesis, as well as the maintenance of the nervous system in vertebrates.
LRRC24 has also been found to interact with IGFBP7, a known regulator of insulin-like growth factors (IGFs). IGFBP7 is also involved in the stimulation of cell adhesion.

# Clinical significance
To date, no study has specifically implicated LRRC24 or the LRRC24 gene with any case of clinical significance.
LRRC40
Leucine rich repeat containing 40 (LRRC40) is a protein that in humans is encoded by the LRRC40 gene.

# Species distribution
LRRC40 is conserved throughout all of its orthologs. The entire protein is highly conserved in mammals, while conservation is high within the leucine rich repeats in the rest of the orthologs. Orthologs were found all the way back to the scarlet sea anemone and homologs were found in bacteria and Archaea using BLAST. The following table gives information on the homologs of LRRC40.

# Gene
LRRC40 is located on the negative DNA strand (see Sense (molecular biology)) of chromosome 1 from 70,611,483- 70,671,223. The gene produces a 2958 base pair mRNA. There are 15 predicted exons in the human gene  with four other splice patterns predicted on GeneCards by the Alternative Splice Database.

## Gene neighborhood
LRRC40 is neighbored downstream by LRRC7 (70,225,888 - 70,587,570) on the positive DNA strand and upstream by SRSF11 (70,687,320-70,716,488) on the positive DNA strand.

## Gene expression
LRRC40 is expressed between the 50th and 100th percentile in almost every tissue in the body.

# Protein
While the exact function of the LRRC40 protein is not yet understood, it is believed to participate in protein-protein interactions because it is a member of the leucine rich repeat family of proteins which are known to participate in protein-protein interactions.

## Properties
LRRC40 is a 602 amino acid protein with a molecular weight of 68.254 kDa and an isoelectric point of 6.04. LRRC40 is expected to localize to the nucleus  and has no transmembrane domains to anchor it to the nuclear membrane. LRRC40 has many predicted phosphorylation sites. Of the 19 predicted phosphoserine sites, only two are conserved within the orthologs. These two sites are S38 and S391.

## Protein structure
The secondary structure of the protein has a pattern within the leucine repeat regions. Each leucine repeat has a -sheet and -helix. The image to the right shows the particular horseshoe-like structure of a protein with many leucine rich repeats. Depending on the area where the LRRs are located, other proteins can bind within the curve of the horseshoe or attach to the outside of the protein.

# Protein interactions
According to Genecards, LRRC40 has 756 possible protein interactions. These interactions are based on results in the Molecular Interaction database which provided two possible protein interactions. The two proteins are described in the table below.
LRRC50
Leucine-rich repeat-containing protein 50 is a protein that in humans is encoded by the LRRC50 gene.

# Function
Leucine-rich repeat-containing protein 50 is cilium-specific and is required for the stability of the ciliary architecture. It is involved in the regulation of microtubule-based cilia and actin-based brush border microvilli.

# Clinical significance
Mutations in the LRRC50 gene are associated with primary ciliary dyskinesia.
LRRC8A
Leucine-rich repeat-containing protein 8A is a protein that in humans is encoded by the LRRC8A gene. Researchers have found out that this protein, along with the other LRRC8 proteins LRRC8B, LRRC8C, LRRC8D, and LRRC8E, is a subunit of the heteromer protein volume-regulated anion channel (VRAC). (VRACs) are crucial to the regulation of cell size by transporting chloride ions and various organic osmolytes, such as taurine or glutamate, across the plasma membrane, and that is not the only function these channels have been linked to.
While LRRC8A is one of many proteins that can be part of VRAC, it is the most important subunit for the channels ability to function.  However, while we know it is necessary for VRAC function, other studies have found that it is not sufficient for the full range of usual VRAC activity. This is where the other LRRC8 proteins come in, as the different composition of these subunits affects the range of specificity for VRACs.
In addition to its role in VRACs, the LRRC8 protein family is also associated with agammaglobulinemia-5.