Persius/hicric huggingface dataset:
JARID1A
Jumonji, AT rich interactive domain 1A, also known as JARID1A, is a human gene.
The protein encoded by this gene is a ubiquitously expressed nuclear protein. It binds directly, with several other proteins, to retinoblastoma protein which regulates cell proliferation. It was formally known as Retinoblastoma Binding Protein 2 (RBP2). This protein also interacts with rhombotin-2 which functions distinctly in erythropoiesis and in T-cell leukemogenesis. Rhombotin-2 is thought to either directly affect the activity of the encoded protein or may indirectly modulate the functions of the retinoblastoma protein by binding to this protein. Alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.
This protein was found to be an H3K4 histone demethylase that binds to c-Myc.  It was recently renamed to Lysine Demethylase 5A (KDM5A).
JARID1B
Lysine-specific demethylase 5B also known as histone demethylase JARID1B is a demethylase enzyme that in humans is encoded by the KDM5B gene. JARID1B belongs to the alpha-ketoglutarate-dependent hydroxylase superfamily.

# Function
Jarid1B (also known as KDM5B or PLU1) is in the family of JHDM genes. These are responsible for demethylation of tri- and di-methylated lysines in the 4 position of histone 3 (H3K4me3 and H3K4me2). Jarid1B is a multidomain enzyme that is part of the subfamily KDM5. The whole Jarid1 family is a protein family that possesses H3K4 histone demethylase activity.
Jarid1B has been implicated in the development of prostate, breast, and skin cancer and also has been associated with melanoma maintenance. Knockout mice (Jarid1b/) produced are viable in neonatal life. These mice do exhibit the phenotype of premature mortality, decreased fertility in female mice, reduction in body weight and impairment in mammary gland development. It also acted to decrease serum estrogen levels and caused reduced mammary epithelial cell proliferation in the early stages of puberty. These Jarid1b/ mice seem to be greatly affected in many regulators of the development of mammy development such as FOXA1 and estrogen receptor . However, others have shown that a Jarid1B knockout embryos usually have neonatal lethality due to the failure of their respiratory system. Knockout embryos have also been seen to have several different neural defects including: disorganized cranial nerves, increased incidences of exencephaly, and defects in eye development.

# Interactions
JARID1B has been shown to interact with FOXG1 and PAX9.
JWH-051
JWH-051 is an analgesic drug which is a cannabinoid agonist. Its chemical structure is closely related to that of the potent cannabinoid agonist HU-210, with the only difference being the removal of the hydroxyl group at position 1 of the aromatic ring.
JWH-051 retains high affinity for the CB1 receptor, but is a much stronger agonist for CB2, with a Ki value of 0.03nM at CB2 vs 1.20nM at CB1. It was one of the first CB2-selective ligands developed, although its selectivity for CB2 is modest compared to newer compounds such as HU-308.
It has similar effects to other cannabinoid agonists such as sedation and analgesia, but with a relatively strong antiinflammatory effect due to its strong activity at CB2.
J chain
A J chain is a protein component of the antibodies IgM and IgA.  It is a 137 residue polypeptide, encoded by the IGJ gene.

# Structure
The J Chain's molecular weight is approximately 15 kDa.  It exhibits a standard immunoglobulin folding structure of two -pleated sheets of four ribbons folded against one another.  It has 8 cystine residues.  Two of these residues link the  chains of IgA or the  chains of IgM via disulfide bridges, effectively serving as the "glue" between two Fc regions of the antibody.
The J-chain shows a large degree of homology between avian and human species, suggesting that it serves an important function.

# Function
The J Chain is required for IgM or IgA to be secreted into mucosa. As part of a polymeric immunoglobulin (pIg), the J-chain is essential for binding of pIg to the pIgR, which forms the secretory component upon excretion of the secretory pIg by epithelial cells. This binding facilitates transport of the J-chain positive pIg molecules from the basal to the apical sides of epithelial cells.
Because IgM and IgA are the only two types of antibody that polymerize, initial hypotheses stated that J chain was required for polymerization.  However, it was subsequently found that IgM is able to polymerize in the absence of J chain as both a pentamer and a hexamer, however, both of these exist to lesser numbers in organisms lacking J chains.  In such cases, there are also fewer IgA dimers.
The J-chain also plays a role in the activation of complement. J-chain negative IgM hexamers are 15-20 times more effective at activating complement than J-chain positive IgM pentamers. A consequence of this lack of complement activation is it allows J-chain positive pIgM to bind antigens without causing excessive damage to epithelial membranes through complement activation.
Jejunum

# Overview
In anatomy of the digestive system, the jejunum is the central of the three divisions of the small intestine and lies between the duodenum and the ileum.  The change from the duodenum to the jejunum is usually defined as the ligament of Treitz.
In adult humans, the small intestine is usually between 5.5-6m long, 2.5m of which is the jejunum.
The pH in the jejunum is usually between 7 and 8 (neutral or slightly alkaline).
The jejunum and the ileum are suspended by mesentery which gives the bowel great mobility within the abdomen. It also contains muscles to help move the food along.

# Internal structure
The inner surface of the jejunum, its mucous membrane, is covered in projections called villi, which increase the surface area of tissue available to absorb nutrients from the gut contents. The villi in the jejunum are much longer than in the duodenum or ileum.
The jejunum contains very few Brunner's glands (found in the duodenum) or Peyer's patches (found in the ileum). Instead, it has many large circular folds in its submucosa called plicae circulares which increase the surface area for nutrient absorption.

# Etymology
Jejunum is derived from the adjective jejune, which means "fasting" or "hungry" in Early Modern English.
It was so called because this portion of the intestine was found "empty" following death 

# Additional images
- Duodenojejunal fossa.
- Transmission electron microscope (TEM) of Human Jejunum
- TEM of Mouse Jejunum x14000
KIR2DL4
Killer cell immunoglobulin-like receptor 2DL4 is a protein that in humans is encoded by the KIR2DL4 gene.

# Function
Killer cell immunoglobulin-like receptors (KIRs) are transmembrane glycoproteins expressed by natural killer cells and subsets of CD8+ T cells. The KIR genes are polymorphic and highly homologous and they are found in a cluster on chromosome 19q13.4 within the 1 Mb leukocyte receptor complex (LRC). The gene content of the KIR gene cluster varies among haplotypes, although several "framework" genes are found in all haplotypes (KIR3DL3, KIR3DP1, KIR3DL4, KIR3DL2). The KIR proteins are classified by the number of extracellular immunoglobulin domains (2D or 3D) and by whether they have a long (L) or short (S) cytoplasmic domain. KIR proteins with the long cytoplasmic domain transduce inhibitory signals upon ligand binding via an immune tyrosine-based inhibitory motif (ITIM), while KIR proteins with the short cytoplasmic domain lack the ITIM motif and instead associate with the TYRO protein tyrosine kinase binding protein to transduce activating signals. The ligands for several KIR proteins are subsets of HLA class I molecules; thus, KIR proteins are thought to play an important role in regulation of the immune response. This gene is one of the "framework" loci that is present on all haplotypes. Alternative splicing results in multiple transcript variants.
The only so far reported ligand of KIR2DL4 is the non-classical HLA class 1 gene HLA-G, leading to the inhibition of the cytolytic NK cell function.
KIRREL3
Kin of IRRE-like protein 3 (KIRREL3) also known as kin of irregular chiasm-like protein 3 or NEPH2 is a protein that in humans is encoded by the KIRREL3 gene.
NEPH2 is a member of the NEPH protein family of transmembrane proteins, which includes NEPH1 (KIRREL) and NEPH3 (KIRREL2). The NEPH proteins can interact with nephrin and CASK.

# Function
NEPH2 has been implicated in synapse formation. Disruption of KIRREL3 gene function had been associated with abnormal brain function.
NEPH1 and NEPH2 are involved in the blood filtration function of the kidney and are located in the slit diaphragm.
KREMEN1
Kremen protein 1 is a protein that in humans is encoded by the KREMEN1 gene. Kremen1 is conserved in chordates including amphioxus and most vertebrate species. The protein is a type I transmembrane receptor of ligands Dickkopf1, Dickkopf2, Dickkopf3, Dickkopf4, EpCAM and Rspondin1.

# Function
This gene encodes a high-affinity dickkopf homolog 1 (DKK1) transmembrane receptor that functionally cooperates with DKK1 to block wingless (WNT)/beta-catenin signaling. The encoded protein is a component of a membrane complex that modulates canonical WNT signaling through lipoprotein receptor-related protein 6 (LRP6). It contains extracellular kringle, WSC, and CUB domains. Alternatively spliced transcript variants encoding distinct isoforms have been observed for this gene.
Kremen1 also has a function in the induction of cell death by apoptosis. This proapototic activity is conditional and depends on the absence of ligand Dickkopf1. These observations led to the classification of this protein as a Dependence Receptor.
A mouse knock out of Kremen1 and its paralog Kremen2 is viable and fertile.
Kalirin
Kalirin, also known as Huntingtin-associated protein-interacting protein (HAPIP), protein duo (DUO), or serine/threonine-protein kinase with Dbl- and pleckstrin homology domain, is a protein that in humans is encoded by the KALRN gene. Kalirin was first identified in 1997 as a protein interacting with huntingtin-associated protein 1. Is also known to play an important role in nerve growth and axonal development.
Kalirin is a member of the Dbl family of proteins and is a Rho guanine nucleotide exchange factor.
It is named after the multiple-handed Hindu goddess Kali for its ability to interact with numerous other proteins. Kalirin's other name, DUO, comes from the fact that it is 98% identical to rat DUO protein and 80.6% identical to a human protein named TRIO. Unlike TRIO, which is expressed in numerous tissues, Kalirin isoforms are mainly found in the brain.

# Clinical significance
Several isoforms of Kalirin are produced through alternative splicing. One of the isoforms, Kalirin-7, was found to be necessary for the remodeling of synapses in mature cortical neurons and is thought to be important in the development of schizophrenia, as demonstrated by adolescent development of schizophrenia-like symptoms in kalirin knockout mice. Alzheimer's disease may also be linked to kalirin-7.
Kikayon
Kikayon () is the Hebrew name of a plant mentioned in the Biblical Book of Jonah.

# Origins
The first use of the term kikayon is in the biblical book of Jonah, Chapter 4:

# Classification
The word kikayon is only referenced in the book of Jonah and there is some question as to what kind of plant it is.  Some hypotheses include a gourd and a castor oil plant.

# Entheogenic interpretation
The description may indicate an entheogenic mushroom such as fly agaric (Amanita muscaria). Mushrooms grow and wither very rapidly ("in a night"), were uncultivated in ancient times ("not labored over") due to the invisibility of mushroom spores to the naked eye, and in some cultures the Amanita muscaria mushroom is associated withand named after an umbrella or parasol because of its shape  ("a shadow over his head"). Paradoxically, the red cap of Amanita muscaria was also associated with the sun due to its round shape and color. When the mushroom cap is dried its color changes from red to gold, like the sun rising in the sky. The "rising sun" mushroom cap beating on Jonah's head and causing him to become faint describes the effects of fly agaric intoxication. In ancient times worms, maggots, serpents and dragons all fitted into one category  (the Old English "wyrm" could mean any of these creatures), symbolizing chthonic forces, to which the Amanita muscaria mushroom also belonged. The Sanskrit mushroom names ahichattra(ka) and sarpacchattra(ka) mean "snake parasol".
Nitrone
A nitrone is the N-oxide of an imine and a functional group in organic chemistry. The general structure is R1R2C=NR3+O-.
A nitrone is 1,3-dipole in 1,3-dipolar cycloadditions. It reacts with alkenes to an isoxazolidine:
One example of this reaction type is the reaction of various Baylis-Hillman adducts with C-Phenyl-N-methylnitrone forming an isoxazolidine in which R1 is phenyl, R2 is hydrogen and R3 is a methyl group .
Nitrones react with terminal alkynes and a copper salt to beta-lactam. This reaction is also called the The Kinugasa reaction  for example in this reaction: :
The first step in this reaction is a dipolar cycloaddition of the nitrone with the in situ generated copper(I) acetylide to a 5-membered ring structure which rearranges in the second step.
Patella

# Overview
The patella or kneecap is a thick, triangular bone which articulates with the femur and covers and protects the front of the knee joint. It is the largest sesamoid bone in the human body. It is attached to the tendon of the quadriceps femoris muscle, which contracts to straighten the leg. The vastus intermedialis muscle is attached to the base of patella. The vastus lateralis and vastus medialis are attached to lateral and medial borders of patella respectively.
The patella is stabilised by the insertion of vastus medialis and the prominence of the anterior femoral condyles, which prevent lateral dislocation during flexion. The retinacular fibres of the patella also stabilise it during exercise.
The primary functional role of the patella is knee extension. The patella increases the leverage that the tendon can exert on the femur by increasing the angle at which it acts.
The patella ossifies between the ages 2-6 years. In some people it may be absent congenitally or hypoplastic. In 2% of the population there is a bipartite patella, which is usually asymptomatic.
Regarding non-human animals, the patella is fully developed only in placental mammals; marsupials have only rudimentary, non-ossified patellae.
LAPTM4B
Lysosomal-associated transmembrane protein 4B is a protein that in humans is encoded by the LAPTM4B gene.
LAPTM4B protein contains a lysosome localization motif and localizes on late endosomes and lysosomes.

# Clinical significance
Increased expression of LAPTM4B has been found in breast, liver, lung, ovarian, uterine, gastric cancers. Elevated LAPTM4B level contributes to chemotherapy resistance in breast cancer. It was found that overexpression of LAPTM4B causes anthracyclines (doxorubicin, daunorubicin, and epirubicin) resistance by retaining drug in the cytoplasm and decreasing nuclear localization of drug and drug induced DNA damage.
In 2011, the same group reported that LAPTM4B also promotes autophagy, a cell survival mechanism mediated by lysosomes. LAPTM4B promotes autophagy and renders tumor cells resistant to metabolic and genotoxic stress and results in more rapid tumor growth.
Based on these findings, LAPTM4B can be utilized to be a therapeutic target to prevent chemotherapy resistance or a marker to identify the patients who will not benefit from anthracyclines.
LGALS13
Placental protein 13 (PP13) is a protein that in humans is encoded by the LGALS13 gene.

# Structure and function

# Function
It is composed of two identical subunits which are held together by disulfide bonds. The monomer of this protein has structural similarity to several members of the beta-galactoside-binding S-type lectin family, but it could not bind beta-galactoside. This is because the ligand binding site is lack of key residue for binding beta-galactoside. It is a galectin-like protein. The ligand of this protein is still unknown.

# Clinical significance
PP13 levels that are low in the first trimester of pregnancy confers a higher risk for developing pre-eclampsia later in pregnancy.
LRRC16A
Leucine rich repeat containing 16A is a protein that in humans is encoded by the LRRC16A gene. The gene is also known as LRRC16, CARMIL, CARMIL1 or CARMIL1a.

# Model organisms
Model organisms have been used in the study of LRRC16A function. A conditional knockout mouse line, called Lrrc16atm1a(KOMP)Wtsi was generated as part of the International Knockout Mouse Consortium program  a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists  at the Wellcome Trust Sanger Institute.
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Twenty two tests were carried out on mutant mice but no significant abnormalities were observed.
LYPLAL1
Lysophospholipase-like 1 is a protein in humans that is encoded by the LYPLAL1 gene.
 The protein is a /-hydrolase of uncharacterized metabolic function. Genome-wide association studies in humans have linked the gene to fat distribution and waist-to-hip ratio. The protein's enzymatic function is unclear. LYPLAL1 was reported to act as a triglyceride lipase in adipose tissue and another study suggested that the protein may play a role in the depalmitoylation of calcium-activated potassium channels. However, LYPLAL1 does not depalmitoylate the oncogene Ras and a structural and enzymatic study concluded that LYPLAL1 is generally unable to act as a lipase and is instead an esterase that prefers short-chain substrates, such as acetyl groups.

# Relationship to acyl-protein thioesterases
Sequence conservation and structural homology suggest a close relationship of LYPLAL1 proteins to acyl-protein thioesterases, and, therefore, it has been suggested that LYPLAL1 might be the third human acyl-protein thioesterase. However, the major structural difference between both protein families has been established in the hydrophobic substrate binding tunnel, which has been identified in human acyl-protein thioesterases 1 and 2, as well as in Zea mays acyl-protein thioesterase 2. In LYPLAL1, this tunnel is closed due to a different loop conformation, changing the enzyme's substrate specificity to short acyl chains.

# Model organisms
Model organisms have been used in the study of LYPLAL1 function. A conditional knockout mouse line called Lyplal1tm1a(KOMP)Wtsi was generated at the Wellcome Trust Sanger Institute. Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Additional screens performed:  - In-depth immunological phenotyping
Lacteal

# Overview
A lacteal is a lymphatic capillary that absorbs dietary fats in the villi of the small intestine.
The combination of fat and lymph in the lacteals is milky in appearance and called chyle. Individual lacteals merge to form larger lymphatic vessels that transport the fats to the thoracic duct which empties into the left subclavian vein.
At this point, the fats are in the bloodstream. They can be converted to lipoproteins (HDL, LDL or VLDL) in the liver or be transported to tissues throughout the body and stored in adipose cells as triglycerides.
Laetoli
Laetoli is a site in Tanzania, dated to the Plio-Pleistocene and famous for its hominid footprints, preserved in volcanic ash (Site G). The site of the Laetoli footprints is located 45 km south of Olduvai gorge. Professor Terry Harrison, a physical anthropologist at New York University, has continued research at the site since the late 1990s.

# Date
The footprint-bearing layers are Pliocene in age, dated by the K/Ar method to 3.7 million years ago (m.y.a.).

# The footprints
A line of hominid fossil footprints, discovered in 1978 by Mary Leakey, Richard Hay, Tim White and their team, is preserved in powdery volcanic ash from an eruption of the 20 km distant Sadiman Volcano. Soft rain cemented the ash-layer (15 cm thick) to tuff without destroying the prints. In time, they were covered by other ash deposits. The hominid prints were produced by three individuals, one walking in the footprints of the other, making the original tracks difficult to discover. As the tracks lead in the same direction, they might have been produced by a group -- but there is nothing else to support the common reconstruction of a nuclear family visiting the waterhole together.
The footprints demonstrate that the hominids walked upright habitually, as there are no knuckle-impressions. The feet do not have the mobile big toe of apes; instead, they have an arch (the bending of the sole of the foot) typical of modern humans. The hominids seem to have moved in a leisurely stroll.

# Other animals
Other prints show the presence of twenty other animal species, among them hyenas, wild cats (Machairodont), baboons, wild boar, giraffes, gazelles, rhinos, several kinds of antelope, hipparion, buffalo, elephants (of the extinct Deinotherium genus), hare and birds. Traces of raindrops can be seen as well. Few prints are superimposed, which indicates that they were rapidly covered up again. Most of these animals are represented by skeletal remains in the area as well.

# Human remains
The German anthropologist Ludwig Kohl-Larsen was the first to go to Laetoli to look for fossil remains. In 1934 he found the jaw of Australopithecus afarensis.
The remains of 13 hominids have been found, mainly mandibles and teeth. They show affinities to the female skeleton Lucy from Hadar, Ethiopia. Most scholars classify them as Australopithecus afarensis, but some stress the greater similarity to Homo and prefer to speak of Homo sp. indet.
A rather complete skull found at Ngaloba in 1976 has been dated to ca. 120,000 to 100,000 years ago. It is very modern anatomically, with a cranial capacity of ca. 1200 cm3, but the forehead is still very low.

# Artifacts
No artifacts have been found in the vicinity.

# Further reading
- Mary D. Leakey and J. M. Harris (eds), Laetoli:  a Pliocene site in Northern Tanzania (Oxford, Clarendon Press 1987). ISBN 0-19-854441-3.
- Richard L. Hay and Mary D. Leakey, "Fossil footprints  of Laetoli." Scientific American, February 1982, 50-57.