Persius/hicric huggingface dataset:
ID1
DNA-binding protein inhibitor ID-1 is a protein that in humans is encoded by the ID1 gene.

# Function
The protein encoded by this gene is a helix-loop-helix (HLH)  protein that can form heterodimers with members of the basic HLH family of transcription factors. The encoded protein has no DNA binding activity and therefore can inhibit the DNA binding and transcriptional activation ability of basic HLH proteins with which it interacts. This protein may play a role in cell growth, senescence, and differentiation. Two transcript variants encoding different isoforms have been found for this gene.

# Interactions
ID1 has been shown to interact weakly with MyoD but very tightly with ubiquitously expressed E proteins. E proteins heterodimerize with tissue restricted bHLH proteins such as Myod, NeuroD, etc. to form active transcription complexes so by sequestering E proteins, Id proteins can inhibit tissue restricted gene expression in multiple cell lineages using the same biochemical mechanism. Other interacting partners include CASK.

# Clinical significance
ID1 can be used to mark endothelial progenitor cells which are critical to tumor growth and angiogenesis. Targeting ID1 results in decreased tumor growth.
ID2
DNA-binding protein inhibitor ID-2 is a protein that in humans is encoded by the ID2 gene.

# Function
The protein encoded by this gene belongs to the inhibitor of DNA binding (ID) family, members of which are transcriptional regulators that contain a helix-loop-helix (HLH) domain but not a basic domain. Members of the ID family inhibit the functions of basic helix-loop-helix transcription factors in a dominant-negative manner by suppressing their heterodimerization partners through the HLH domains. This protein may play a role in negatively regulating cell differentiation. A pseudogene has been identified for this gene.
A research published by "Nature" in 01/2016, authored by Italian researchers Antonio Iavarone and Anna Lasorella, from Columbia University, states that ID2 protein has a relevant role in the development and resistance to therapies of glioblastoma, the most aggressive of brain cancers.

# Interactions
ID2 has been shown to interact with MyoD and NEDD9.
Leg
A leg is the part of an animal's body that supports the rest of the animal above the ground betwean the ankle and the hip and is used for locomotion. The end of the leg furthest from the animal's body is often either modified or attached to another structure that is modified to disperse the animal's weight on the ground (see foot).
In bipedal vertebrate animals, the two lower limbs are usually referred to as the 'legs' and the two upper limbs as the 'arms' or 'wings' as the case may be.
Legs typically come in even-numbered quantities. Many taxonomic groups are characterized by the number of legs its members possess.
- Uniped: 1
- Biped: 2
- Tripedal: 3
- Quadruped: 4
- Quinped: 5
- Arthropoda: 4, 6, 8, 12, or 14
Some arthropods have more than a dozen legs; a few species possess over 100. Despite what their names might suggest,
Centipedes typically have fewer than one hundred legs
Millipedes have fewer than one thousand legs.
- Some arthropods have more than a dozen legs; a few species possess over 100. Despite what their names might suggest,
Centipedes typically have fewer than one hundred legs
Millipedes have fewer than one thousand legs.
- Centipedes typically have fewer than one hundred legs
- Millipedes have fewer than one thousand legs.

# Evolution
The leg has evolved several times, most significantly among arthropods (crustaceans, insects, arachnids, et cetera) and vertebrates. In both cases, they are thought to have first evolved for locomotion underwater, then have been exploited for movement over land ever less desperate conditions as the generations passed.

# The human leg
The bones of the human leg are:
- Tibia, or shin bones
- Fibula, or calf bones
MCC
What are you looking for?
- MCC (gene), a tumor suppressor gene involved in colorectal tumor pathogenesis
- Merkel cell carcinoma, a rare and aggressive cancer of the skin
- Morbus cordis coronarius, the Latin name for coronary artery disease
MCL
What are you looking for?
- Johnie McL disease, a synonym for Hurler's syndrome
- Mantle cell lymphoma, a subtype of B-cell lymphoma
- Mast cell leukemia, an aggressive subtype of acute myeloid leukemia
- Medial collateral ligament, one of many ligaments of the knee
- Midclavicular line
- Mucocutaneous leishmaniasis, an infection caused by Leishmania spp. parasites
- Multiple cutaneous leiomyoma, a subtype of leiomyoma (smooth muscle tumor)
- Myeloid cell leukemia sequence 1 (MCL-1) gene, a member of the BCL-2 family, that encodes the "induced myeloid leukemia cell differentiation" (mcl-1) protein that is targeted by pharmacologic agents such as Omacetaxine, Mepesuccinate, and Seliciclib
Pus
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# Overview
Pus is a whitish-yellow or yellow substance produced during inflammatory responses of the body that can be found in regions of pyogenic bacterial infections. An accumulation of pus in an enclosed tissue space is known as an abscess. A visible collection of pus within or beneath the epidermis, on the other hand, is known as a pustule or pimple. Pus is produced from the dead and living white blood cells which travel into the intercellular spaces around the affected cells.
Something that creates pus is called suppurative, pyogenic, or purulent. If it creates mucus as well as pus, it is called mucopurulent.
Pus consists of a thin, protein-rich fluid, known as liquor puris, and dead neutrophils (white blood cells), which are part of the body's innate immune response.  Neutrophils are produced in the bone marrow and released into the blood. When the need to fight infection arises, they move to the site of infection by a process known as chemotaxis, usually triggered by cytokine release from macrophages that sense invading organisms.  At the site of infection they engulf and kill bacteria.  Eventually, the neutrophils die, and these dead cells are then phagocytosed by macrophages, which break them down further.  Pus, therefore, is the viscous material composed of these dead neutrophils.
Neutrophils are the most abundant type of leukocyte in human blood, composing anywhere between 40% to 75% of leukocytes.
When seen in a wound or dry skin, pus indicates the area is infected and should be cleaned with antiseptic.
Despite normally being of a whitish-yellow hue, changes in the color of pus can be observed under certain circumstances. Blue pus is found in certain infections of Pseudomonas aeruginosa as a result of the pyocyanin bacterial pigment it produces; amoebic abscesses of the liver, meanwhile, produce brownish pus. Pus might have a reddish tint to it after mixing with blood. Pus also can have an odour.
NaK
NaK (often pronounced as such, rhyming with "sack") is an alloy of sodium (Na) and potassium (K), and particularly one that is liquid at room temperatures. It is a commercially available material in various grades. NaK is highly reactive with air or water, and must be handled with special precautions. Quantities as small as one gram can be a fire or explosion risk.

# Physical properties
Alloys with between about 40% and 90% potassium by weight are liquid at room temperature. The mixture with the lowest melting point (the eutectic mix), consisting of 78% potassium and 22% sodium, is liquid from 12.6 to 785 C, and has a density of 866 kg/m3 at 21C and 855 kg/m3 at 100C.

# Usage

## As coolant
One notable use is as the coolant in experimental fast neutron nuclear reactors. Unlike commercial plants, these are frequently shut down and defuelled. Use of lead or pure sodium, the other materials used in practical reactors, would require continual heating to maintain the coolant as a liquid. Use of NaK overcomes this. NaK is used in many other heat transfer applications for similar reasons.
The Soviet RORSAT radar satellites were powered by a NaK-cooled reactor. Apart from the wide liquid temperature range, NaK has a very low vapor pressure, important in the vacuum of space. Some of the coolant has leaked and these NaK droplets constitute a significant space debris hazard.

## In catalysis
NaK is also used as a catalyst for many reactions, including precursors of ibuprofen.

## As desiccant
Both sodium and potassium are used as desiccants in drying solvents prior to distillation. However, without heating, the solid metal is only able to react at the surface. Formation of crusts of oxide also helps to reduce the reactivity. As a liquid metal alloy at room temperature, the use of NaK as a desiccant helps to avoid these problems.
p73
p73 is a protein related to the p53 tumor protein. Because of its structural resemblance to p53, it has also been considered a tumor suppressor. It is involved in cell cycle regulation, and induction of apoptosis. Like p53, p73 is characterized by the presence of different isoforms of the protein. This is explained by splice variants, and an alternative promoter in the DNA sequence.
p73, also known as tumor protein 73 (TP73), protein was the first identified homologue of the tumor suppressor gene, p53. Like p53, p73 has several variants. It is expressed as distinct forms differing at either at the C- or the N-terminus. Currently, six different C-terminus splicing variants have been found in normal cells. The p73 gene encodes a protein with a significant sequence homology and a functional similarity with the tumor suppressor p53. The over-expression of p73 in cultured cells promotes a growth arrest and/or apoptosis similarly to p53.
The p73 gene has been mapped to a chromosome region (1p36. 2-3) a locus commonly deleted in various tumor entities and human cancers. Similar to p53 the protein product of p73 induces cell cycle arrest or apoptosis, hence its classification as a tumor suppressor. However unlike its counterpart, p73 is infrequently mutated in cancers. Perhaps, even more shocking is the fact that p73  deficient mice do not show a tumorigenic phenotype. A deficiency of p53 almost certainly leads to unchecked cell proliferation and is noted in 60% of cancers.
Analyses of many tumors typically found in humans including breast and ovarian cancer show a high expression of p73 when compared to normal tissues in corresponding areas. Adenoviruses that cause cellular transformations have also been found to result in increased p73 expression. Furthermore, recent finding are suggesting that over-expression of transcription factors involved in cell cycle regulation and synthesis of DNA in mammalian cells (e.g.: E2F-1) induces the expression of p73. Many researchers believe that these results imply that p73 may not be a tumor suppressor but rather an oncoprotein. Some suggest that the TP73 locus encodes both a tumor suppressor (TAp73) and a putative oncogene (Np73). This is a strong theory and causes much confusion, as it is unknown which of the two p73 variants is over-expressed and ultimately plays a role in tumorigenesis.
Genes of the p53 family are known to be complex. The viral oncoproteins (e.g. Adenovirus E1B) that efficiently inhibit p53 function are unable to inactivate p73, and those that seem to inhibit p73 have no effect on p53.
Debate persists about the exact function of p73. Recently it has been reported that p73 is enriched in the nervous system and that the p73-deficient mice, which do not exhibit an increased susceptibility to spontaneous tumorigenesis, have neurological and immunological defects. These results have been expanded and it has also been shown that p73 is present in early stages of neurological development and neuronal apoptosis by blocking the proapoptotic function of p53. This strongly implicates p73 as playing a large role in cellular differentiation.
PGY
PGY, short for post-graduate year, refers to a North American numerical scheme denoting the progress of post-medical school graduation medical residents in their residency program. It is used to stratify responsibility in most training programs and to determine salary.
The length of residency depends mostly on the field a medical school graduate chooses to take. Specialties such as family medicine and internal medicine often require only three years, whereas surgery usually requires a minimum of five. Subspecialization (vascular or orthopedic spine surgery as a branch of surgery, for example) in any field will add time to post-graduate training.
For more information on specific medical residency programs, see the  American Medical Association's Fellowship and Residency Electronic Interactive Database.
Pharmacy residencies, which are becoming more popular, also use the PGY nomenclature. Here, PGY-1 is the usual general pharmacy practice residency, and PGY-2 can be completed, often as an option, for pharmacy specialties such as critical care, cardiology, oncology, etc.
In some teaching institutions, trainees are required to indicate level of training on all signatures (John Doe, M.D., PGY-1 or R-1).
Paw
A paw is the soft foot of a mammal, generally a quadruped, that has claws or nails. A hard foot is called a hoof. Paws are used to pad feet for walking and reduce friction.

# Common characteristics
The paw is characterised by thick, pigmented, keratinised, hairless epidermis covering subcutaneous, collagenous, adipose tissue which make up the pads. These pads act as a cushion for the load-bearing limbs of the animal. The paw consists of the large, heart-shaped metacarpal pad (forelimb) or metatarsal pad (rear limb), and generally four load bearing digital pads, although there can be five or six toes in the case of bears and the Giant Panda. A carpal pad is also found on the forelimb which is used for additional traction when stopping or descending a slope in digitigrade species. Additional dew claws can also be present.
The paw also includes a horny, beak shaped claw on each digit. Though usually hairless, certain animals do have fur on the soles of their paws.  An example being the Red Panda, whose furry soles help insulate them in their snowy habitat.

# Animals with paws
- Members of the Canidae family, such as dogs and foxes
- Felines, such as cats and tigers, some of these animals may have toe tufts
- Bears and Raccoons
- Weasels and other mustelids
- Rodents
- A dog's paw resting on a hard concrete surface.
A dog's paw resting on a hard concrete surface.
- A tiger's paw, showing pads.
A tiger's paw, showing pads.
- A cat's paw, showing pads.
A cat's paw, showing pads.
QKI
Quaking homolog, KH domain RNA binding (mouse), also known as QKI, is a protein which in humans is encoded by the QKI gene.
QKI belongs to a family of RNA-binding proteins called STAR proteins for Signal Transduction and Activation of RNA. They have an HNRNPK homology (KH) domain embedded in a 200-amino acid region called the GSG domain. Other members of this family include SAM68 (KHDRBS1) and SF1 . Two more new members are KHDRBS3 and KHDRBS2.
The QKI gene is implicated as being important in schizophrenia, and QKI controls translation of many oligodendrocyte-related genes.
RP9
Retinitis pigmentosa 9 (autosomal dominant), also known as RP9 or PAP-1, is a protein which in humans is encoded by the RP9 gene.

# Function
The removal of introns from nuclear pre-mRNAs occurs on a complex called a spliceosome, which is made up of 4 small nuclear ribonucleoprotein (snRNP) particles and an undefined number of transiently associated splicing factors. The exact role of PAP-1 in splicing is not fully understood, but it is thought that PAP-1 localizes in nuclear speckles containing the splicing factor SC35 and interacts directly with another splicing factor, U2AF35.

# Clinical significance
Mutations in PAP1 underlie autosomal dominant retinitis pigmentosa mapped to the RP9 gene locus.

# Interactions
RP9 has been shown to interact with U2 small nuclear RNA auxiliary factor 1.
RRH
Peropsin, a visual pigment-like receptor, is a protein that in humans is encoded by the RRH gene.
Peropsin is an opsin and so belongs to the guanine nucleotide-binding protein (G protein)-coupled receptors. Peropsin genes have seven-exons as neuropsin and RGR-opsin genes.

# Phylogeny
The peropsins are one of the four subgroups of the Go/RGR opsins, also known as RGR/Go or Group 4 opsins. Go/RGR opsins are one of the four major groups of type-II opsins, also known as metazoan or animal opsins. The Go/RGR opsins consist of four groups: The Go-opsins, the RGR-opsins, the peropsins, and the neuropsins. Animal opsins belong to four classes: C-opsins (ciliary), R-opsins (rhabdomeric), Cnidops (cnidarian), and Go/RGR-opsins. Three of these subclades occur only in Bilateria (all but Cnidops). However, the bilaterian clades constitute a parphyletic taxon without the Cnidops.
RUQ

# Overview
RUQ refers to the right-upper quadrant of the human abdomen. The term allows a doctor to localise pain and tenderness, scars, lumps and other items of interest. The RUQ extends from the median plane to the right of the patient, and from the umbilical plane to the right ribcage.
The RUQ may be painful and/or tender in such conditions as hepatitis, cholecystitis, and peptic ulcer.
The term is not used in comparative anatomy, since most other animals do not stand erect. The equivalent term for animals is 'right anterior quadrant'.
SK3
SK3 (small conductance calcium-activated potassium channel 3) also known as KCa2.3 is a protein that in humans is encoded by the KCNN3 gene.
SK3 is a small-conductance calcium-activated potassium channel partly responsible for the calcium-dependent after hyperpolarisation current (IAHP). It belongs to a family of channels known as small-conductance potassium channels, which consists of three members  SK1, SK2 and SK3 (encoded by the KCNN1, 2 and 3 genes respectively), which share a 60-70% sequence identity. These channels have acquired a number of alternative names, however a NC-IUPHAR has recently achieved consensus on the best names, KCa2.1 (SK1), KCa2.2 (SK2) and KCa2.3 (SK3). Small conductance channels are responsible for the medium and possibly the slow components of the IAHP.

# Structure
KCa2.3 contains 6 transmembrane domains, a pore-forming region, and intracellular N- and C- termini and is readily blocked by apamin. The gene for KCa2.3, KCNN3, is located on chromosome 1q21.

# Expression
KCa2.3 is found in the central nervous system (CNS), muscle, liver, pituitary, prostate, kidney, pancreas and vascular endothelium tissues. KCa2.3 is most abundant in regions of the brain, but has also been found to be expressed in significant levels in many other peripheral tissues, particularly those rich in smooth muscle, including the rectum, corpus cavernosum, colon, small intestine and myometrium.
The expression level of KCNN3 is dependent on hormonal regulation, particularly by the sex hormone estrogen. Estrogen not only enhances transcription of the KCNN3 gene, but also affects the activity of KCa2.3 channels on the cell membrane. In GABAergic preoptic area neurons, estrogen enhanced the ability of 1 adrenergic receptors to inhibit KCa2.3 activity, increasing cell excitability. Links between hormonal regulation of sex organ function and KCa2.3 expression have been established. The expression of KCa2.3 in the corpus cavernosum in patients undergoing estrogen treatment as part of gender reassignment surgery was found to be increased up to 5-fold. The influence of estrogen on KCa2.3 has also been established in the hypothalamus, uterine and skeletal muscle.

# Physiology
KCa2.3 channels play a major role in human physiology, particularly in smooth muscle relaxation. The expression level of KCa2.3 channels in the endothelium influences arterial tone by setting arterial smooth muscle membrane potential. The sustained activity of KCa2.3 channels induces a sustained hyperpolarisation of the endothelial cell membrane potential, which is then carried to nearby smooth muscle through gap junctions. Blocking the KCa2.3 channel or suppressing KCa2.3 expression causes a greatly increased tone in resistance arteries, producing an increase in peripheral resistance and blood pressure.

# Pathology
Mutations in KCa2.3 are suspected to be a possible underlying cause for several neurological disorders, including schizophrenia, bipolar disorder, Alzheimer's disease, anorexia nervosa and ataxia as well as myotonic muscular dystrophy.
SRY

# Overview
SRY (Sex-determining Region Y) is a sex-determining gene on the Y chromosome in humans and other primates.
The SRY gene encodes the testis determining factor, which is also referred to as the SRY protein.
This intronless gene encodes a transcription factor that is a member of the high mobility group (HMG)-box family of DNA-binding proteins. This protein is the testis-determining factor (TDF), which initiates male sex determination. Mutations in this gene give rise to XY females with gonadal dysgenesis (Swyer syndrome); translocation of part of the Y chromosome containing this gene to the X chromosome causes XX male syndrome.

# Impact upon anatomical sex
Since its discovery, the importance of the SRY gene in sex determination has been extensively documented:
- Humans with one Y chromosome and multiple X chromosomes (XXY, XXXY etc.) are usually males.
- Individuals with a male phenotype and an XX (female) genotype have been observed; these males have the SRY gene in one or both X chromosomes, moved there by chromosomal translocation. (However, these males are infertile.)
- Similarly, there are females with an XXY or XY genotype.  These females have no SRY gene in their Y chromosome, or the SRY gene exists but is defective (mutated).

# SRY and the Olympics
One of the most controversial uses of this discovery was as a means for gender verification at the Olympic Games, under a system implemented by the International Olympic Committee in 1992. Athletes with a SRY gene were not permitted to participate as females, although all athletes in whom this was "detected" at the 1996 Summer Olympics were ruled false positives and were not disqualified. In the late 1990s, a number of relevant professional societies in United States called for elimination of gender verification, including the American Medical Association, the American Academy of Pediatrics, the American College of Physicians, the American College of Obstetricians and Gynecologists, the Endocrine Society and the American Society of Human Genetics, stating that the method used was uncertain and ineffective. The screening was eliminated as of the 2000 Summer Olympics.

# SRY-related diseases and defects
Individuals with XY genotype and functional SRY gene can have a female phenotype, where the underlying cause is androgen insensitivity syndrome (AIS).
SRY has been linked to the fact that men are more likely than women to develop dopamine-related diseases such as schizophrenia and Parkinson's disease.  SRY makes a protein that controls concentrations of dopamine, the neurotransmitter that carries signals from the brain that control movement and coordination.