Persius/hicric huggingface dataset:
ASIC2
Acid-sensing ion channel 2 (ASIC2) also known as amiloride-sensitive cation channel 1, neuronal (ACCN1) or brain sodium channel 1 (BNaC1) is a protein that in humans is encoded by the ASIC2 gene.  The ASIC2 gene is one of the five paralogous genes that encode proteins that form trimeric acid-sensing ion channels (ASICs) in mammals. The cDNA of this gene was first cloned in 1996. The ASIC genes have splicing variants that encode different proteins that are called isoforms.
These genes are mainly expressed in the central and peripheral nervous system.
ASICs can form both homotrimeric (meaning composed of three identical subunits) and heterotrimeric channels.

# Structure and function
This gene encodes a member of the ASIC/ENaC superfamily of proteins. The members of this family are amiloride-sensitive sodium channels that contain intracellular N and C termini, 2 hydrophobic transmembrane (TM) regions, and a large extracellular loop, which has many cysteine residues with conserved spacing. The TM regions are generally symbolized as TM1 (clone to N-terminus) and TM2 (close to C-terminus).
The pore of the channel through which ions selectively flow from the extracellular side into the cytoplasm is formed by the three TM2 regions of the trimer.
ASIC3
Acid-sensing ion channel 3 (ASIC3) also known as amiloride-sensitive cation channel 3 (ACCN3) or testis sodium channel 1 (TNaC1) is a protein that in humans is encoded by the ASIC3 gene. The ASIC3 gene is one of the five paralogous genes that encode proteins that form trimeric acid-sensing ion channels (ASICs) in mammals. The cDNA of this gene was first cloned in 1998. The ASIC genes have splicing variants that encode different proteins that are called isoforms.
These genes are mainly expressed in the central and peripheral nervous system.
ASICs can form both homotrimeric (meaning composed of three identical subunits) and heterotrimeric channels.

# Structure and function
This gene encodes a member of the ASIC/ENaC superfamily of proteins. The members of this family are amiloride-sensitive sodium channels that contain intracellular N and C termini, 2 hydrophobic transmembrane (TM) regions, and a large extracellular loop, which has many cysteine residues with conserved spacing. The TM regions are generally symbolized as TM1 (clone to N-terminus) and TM2 (close to C-terminus).
The pore of the channel through which ions selectively flow from the extracellular side into the cytoplasm is formed by the three TM2 regions of the trimer.

# Interactions
ASIC3 has been shown to interact with LIN7B, GOPC and MAGI1.
ASIC4
Acid-sensing ion channel 4 (ASIC4) also known as amiloride-sensitive cation channel 4 (ACCN4) is a protein that in humans is encoded by the ASIC4 gene. The ASIC4 gene is one of the five paralogous genes that encode proteins that form trimeric acid-sensing ion channels (ASICs) in mammals. The cDNA of this gene was first cloned in 2000. The ASIC genes have splicing variants that encode different proteins that are called isoforms.
These genes are mainly expressed in the central and peripheral nervous system.
ASICs can form both homotrimeric (meaning composed of three identical subunits) and heterotrimeric channels.

# Structure and function
This gene encodes a member of the ASIC/ENaC superfamily of proteins. The members of this family are amiloride-sensitive sodium channels that contain intracellular N and C termini, 2 hydrophobic transmembrane (TM) regions, and a large extracellular loop, which has many cysteine residues with conserved spacing. The TM regions are generally symbolized as TM1 (clone to N-terminus) and TM2 (close to C-terminus).
The pore of the channel through which ions selectively flow from the extracellular side into the cytoplasm is formed by the three TM2 regions of the trimer.
ASK-1
Apoptosis signal-regulating kinase 1, ASK-1, is part of the mitogen-activated protein kinase (MAPK) cascade. In humans it is also known as "mitogen-activated protein kinase kinase kinase 5", abbreviated as "MAP3K5".
Mitogen-activated protein kinase (MAPK) signaling cascades include MAPK or extracellular signal-regulated kinase (ERK), MAPK kinase (MKK or MEK), and MAPK kinase kinase (MAPKKK or MEKK). MAPKK kinase/MEKK phosphorylates and activates its downstream protein kinase, MAPK kinase/MEK, which in turn activates MAPK. The kinases of these signaling cascades are highly conserved, and homologs exist in yeast, Drosophila, and mammalian cells. Phosphorylation of ASK-1 protein can lead to apoptosis or other cellular responses depending on the cell type. Northern blot analysis shows that ASK-1 transcript is abundantly expressed in human heart and pancreas. The ASK-1 (MAPKKK5) protein phosphorylates and activates MKK4 (aliases SERK1, MAPKK4) in vitro, and activates c-Jun N-terminal kinase (JNK)/stress-activated protein kinase (SAPK) during transient expression in COS and 293 cells; ASK-1 does not activate MAPK/ERK.
ASK-1 found in the inactive form, bound to reduced thioredoxin.  When oxidized by a reactive oxygen species, Trx dissociates from ASK-1. The ASK-1, which is found as a homo-oligodimer, autophosphorylates and becomes an active MAP kinase kinase kinase.
ASK-1 contains 1,374 amino acids with all 11 kinase subdomains. It is located on chromosome 6 at locus 6q22.33.
ASXL1
Putative Polycomb group protein ASXL1 is a protein that in humans is encoded by the ASXL1 gene.
In Drosophila, the Additional sex combs (Asx) gene encodes a chromatin-binding protein required for normal determination of segment identity in the developing embryo. The protein is a member of the Polycomb group of proteins, which are necessary for the maintenance of stable repression of homeotic and other loci. The protein is thought to disrupt chromatin in localized areas, enhancing transcription of certain genes while repressing the transcription of other genes. Although the function of the protein encoded by this gene is not known, it does show some sequence similarity to the protein encoded by the Drosophila Asx gene.

# Model organisms
Model organisms have been used in the study of ASXL1 function. A conditional knockout mouse line, called Asxl1tm1a(EUCOMM)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.
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Twenty five tests were carried out on mutant mice and four significant abnormalities were observed. Few homozygous mutant embryos were identified during gestation and those that were alive had craniofacial and eye defects, none survived until weaning. The remaining tests were carried out on heterozygous mutant adult mice; decreased vertebrae number and increased bone strength was observed in these animals.
ATG12
Autophagy-related protein 12 is a protein that in humans is encoded by the ATG12 gene.
Autophagy is a process of bulk protein degradation in which cytoplasmic components, including organelles, are enclosed in double-membrane structures called autophagosomes and delivered to lysosomes or vacuoles for degradation. ATG12 is the human homolog of a yeast protein involved in autophagy (Mizushima et al., 1998).
Autophagy requires the covalent attachment of the protein Atg12 to ATG5 through a ubiquitin-like conjugation system. The Atg12-Atg5 conjugate then promotes the conjugation of ATG8 to the lipid phosphatidylethanolamine.
Atg12 was found to be involved in apoptosis. This protein promotes apoptosis through an interaction with anti-apoptotic members of the Bcl-2 family.
ATG4B
Cysteine protease ATG4B is an enzyme that in humans is encoded by the ATG4B gene.

# Function
Autophagy is the process by which endogenous proteins and damaged organelles are destroyed intracellularly. Autophagy is postulated to be essential for cell homeostasis and cell remodeling during differentiation, metamorphosis, non-apoptotic cell death, and aging. Reduced levels of autophagy have been described in some malignant tumors, and a role for autophagy in controlling the unregulated cell growth linked to cancer has been proposed. This gene encodes a member of the autophagin protein family. The encoded protein is also designated as a member of the C-54 family of cysteine proteases. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.
One main function of Atg4 is to cleave the pre-protein of Atg8, leading to the non-lipidated soluble (-I) form which can be processed further by Atg3, Atg7, Atg5-12 into the lipidated form (-II) anchored to the autophagic membrane.

# Interactions
ATG4B has been shown to interact with GABARAPL2.
ATG4D
The human ATG4D gene encodes the protein Autophagy related 4D, cysteine peptidase.

# Function
Autophagy is the process by which endogenous proteins and damaged organelles are destroyed intracellularly. Autophagy is postulated to be essential for cell homeostasis and cell remodeling during differentiation, metamorphosis, non-apoptotic cell death, and aging. Reduced levels of autophagy have been described in some malignant tumors, and a role for autophagy in controlling the unregulated cell growth linked to cancer has been proposed.
This gene belongs to the autophagy-related protein 4 (Atg4) family of C54 endopeptidases. Members of this family encode proteins that play a role in the biogenesis of autophagosomes, which sequester the cytosol and organelles for degradation by lysosomes. Alternative splicing results in multiple transcript variants. .
ATP5H
The human gene ATP5PD encodes subunit d of the peripheral stalk part of the enzyme mitochondrial ATP synthase.
Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. It is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, F0, which comprises the proton channel. The F1 complex consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled in a ratio of 3 alpha, 3 beta, and a single representative of the other 3. The Fo seems to have nine subunits (a, b, c, d, e, f, g, F6 and 8). This gene encodes the d subunit of the Fo complex. 
Alternatively spliced transcript variants encoding different isoforms have been identified for this gene. In addition, three pseudogenes are located on chromosomes 9, 12 and 15.
ATP5I
ATP synthase subunit e, mitochondrial is an enzyme that in humans is encoded by the ATP5ME gene.
Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. It is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, which comprises the proton channel. The F1 complex consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled in a ratio of 3 alpha, 3 beta, and a single representative of the other 3. The Fo seems to have nine subunits (a, b, c, d, e, f, g, F6 and 8). This gene encodes the e subunit of the Fo complex.
In yeast, the FO complex E subunit appears to play an important role in supporting F-ATPase dimerisation. This subunit is anchored to the inner mitochondrial membrane via its N-terminal region, which is involved in stabilising subunits G and K of the FO complex. The C-terminal region of subunit E is hydrophilic, protruding into the intermembrane space where it can also help stabilise the F-ATPase dimer complex.
ATP5J
ATP synthase-coupling factor 6, mitochondrial is an enzyme that in humans is encoded by the ATP5PF gene.

# Function
Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. It is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, F0, which comprises the proton channel. The F1 complex consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled in a ratio of 3 alpha, 3 beta, and a single representative of the other 3. The Fo seems to have nine subunits (a, b, c, d, e, f, g, F6 and 8). This gene encodes the F6 subunit of the F0 complex, required for F1 and Fo interactions. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene.
The F6 subunit is part of the peripheral stalk that links the F1 and FO complexes together, and which acts as a stator to prevent certain subunits from rotating with the central rotary element. The peripheral stalk differs in subunit composition between mitochondrial, chloroplast and bacterial F-ATPases. In mitochondria, the peripheral stalk is composed of one copy each of subunits OSCP (oligomycin sensitivity conferral protein), F6, B and D. There is no homologue of subunit F6 in bacterial or chloroplast F-ATPase, whose peripheral stalks are composed of one copy of the delta subunit (homologous to OSCP), and two copies of subunit B in bacteria, or one copy each of subunits B and B' in chloroplasts and photosynthetic bacteria.
ATP5L
ATP synthase subunit g, mitochondrial is an enzyme that in humans is encoded by the ATP5MG gene.
Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. It is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, which comprises the proton channel. The F1 complex consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled in a ratio of 3 alpha, 3 beta, and a single representative of the other 3. The Fo seems to have nine subunits (a, b, c, d, e, f, g, F6 and 8). This gene encodes the g subunit of the F0 complex.
The function of subunit G is currently unknown. There is no counterpart in chloroplast or bacterial F-ATPases identified so far.
AXIN1
Axin-1 is a protein that in humans is encoded by the AXIN1 gene.

# Function
This gene encodes a cytoplasmic protein which contains a regulation of G-protein signaling (RGS) domain and a dishevelled and axin (DIX) domain. The encoded protein interacts with adenomatosis polyposis coli, catenin (cadherin-associated protein) beta 1, glycogen synthase kinase 3 beta, protein phosphatase 2, and itself. This protein functions as a negative regulator of the wingless-type MMTV integration site family, member 1 (WNT) signaling pathway and can induce apoptosis. The crystal structure of a portion of this protein, alone and in a complex with other proteins, has been resolved. Mutations in this gene have been associated with hepatocellular carcinoma, hepatoblastomas, ovarian endometriod adenocarcinomas, and medulloblastomas. Two transcript variants encoding distinct isoforms have been identified for this gene.

# Structure
The full-length human protein comprises 862 amino acids with a (predicted) molecular mass of 96 kDa. The N-terminal RGS domain, a GSK3 kinase interacting peptide of Axin1 and homologs of the C-terminal DIX domains have been solved at atomic resolution. Large WNT-downregulating central regions have been characterized as intrinsically disordered by biophysical experiments and bioinformatic analysis. Biophysical destabilization of the folded RGS domain induces formation of nanoaggregates that expose and locally concentrate intrinsically disordered regions, which in turn misregulate Wnt signalling. Many other large IDPs are affected by missense mutations, such as BRCA1, Adenomatous polyposis coli(APC), CREB-binding protein/(CBP) and might be affected in similar ways by missense mutations of their folded domains.

# Interactions
AXIN1 has been shown to interact with:
- APC,
- CTNNB1,
- CSNK1E,
- CSNK1A1,
- DVL1,
- GSK3B,
- LRP5,
- MAP3K1,
- PPP2R5A, and
- TSC2.
AXIN2
Axin-2 also known as axin-like protein (Axil) or axis inhibition protein 2 (AXIN2) or conductin is a protein that in humans is encoded by the AXIN2 gene.

# Function
The Axin-related protein, Axin2, presumably plays an important role in the regulation of the stability of beta-catenin in the Wnt signaling pathway, like its rodent homologs, mouse conductin/rat axil. In mouse, conductin organizes a multiprotein complex of APC (adenomatous polyposis of the colon), beta-catenin, glycogen synthase kinase 3-beta, and conductin, which leads to the degradation of beta-catenin.

# Clinical significance
The deregulation of beta-catenin is an important event in the genesis of a number of malignancies. The AXIN2 gene has been mapped to 17q23-q24, a region that shows frequent loss of heterozygosity in breast cancer, neuroblastoma, and other tumors. Mutations in this gene have been associated with colorectal cancer with defective mismatch repair.
The most critical events of teeth, lip and palate formation occur almost concurrently. Hypodontia, defined as the congenital lack of one or more permanent teeth, is the most common dental abnormality found in humans and affects approximately 20% of the population worldwide. AXIS inhibition protein 2 (AXIN2) gene polymorphic variants may be associated with both hypodontia and oligodontia (characterized by the lack of six or more permanent teeth). Mutations of this gene have been found in individuals with colorectal carcinomas and liver tumors.
An AXIN2 mutation (1966C>T) detected in a Finnish family was associated with both tooth agenesis and colon neoplasia. In essence, the mutation seems to disrupt tooth development early in life and later contributes to the emergence of polyps and eventually colon cancer, an observation that suggests that the lack of permanent teeth may be an indicator of colon cancer susceptibility. Dentists may at the very least need to remain aware of the possible association, to be able to detect such cases of tooth agenesis and forward the patient to more complete genetic diagnostic examinations. This is a simple example of how molecular genetic discoveries today interact with traditional disciplines (Longtin, 2004).

# Interactions
AXIN2 has been shown to interact with  GSK3B.
Abuse

# Background
Abuse refers to the use or treatment of something (a person, item, substance, concept, or vocabulary) that is seen as harmful.

# Types of Abuse
Several types of abuse include:
- Spiritual abuse: abusive or aberrational practices identified in the behavior and teachings of some churches, spiritual and religious organizations and groups.
- Sexual abuse: The improper use of another person for sexual purposes, generally without their consent or under physical or psychological pressure (also, child sexual abuse, whether abused by parents, those in loco parentis or strangers).
- Physical abuse: Where one person inflicts physical violence or pain on another.
- Verbal abuse: When a person uses profanity, demeaning talk, or threatening statements.
- Emotional abuse or psychological abuse: coercion, humiliation, intimidation, relational aggression, parental alienation or covert incest:  Where one person uses emotional or psychological coercion to compel another to do something they do not want, or is not in their best interests; or when one person manipulates another's emotional or psychological state for their own ends (see battered person syndrome),  or commits psychological aggression using ostensibly non-violent methods to inflict mental or emotional violence or pain on another.
- Drug abuse: the misuse of drugs, alcohol or other substances, usually a form of addiction. Law enforcement officials, among others, often define drug abuse as "any" use of illegal drugs, whether or not use is actually harmful to the user or to anyone else.
- Child abuse: Abuse, usually physical, emotional or sexual, directed at a child.
- Spousal abuse (or domestic violence): Abuse, usually physical, or psychological abuse, directed at one's domestic partner.
- Elder abuse: Abuse, most often physical or in the form of psychological threats, directed at the elderly, especially in nursing homes and similar institutions.
- Human rights abuse: Violation of human rights.
- Animal abuse: Abuse or cruelty directed at animals.
- Legal abuse: Vexatious litigation or malicious prosecution to retaliate, coerce, or emotionally/financially harm a person.
- Internet abuse includes a wide range of inappropriate online behavior, such as unsolicited promotional email, intrusion attempts, and phishing.
ca:Abus
de:Missbrauch
it:Abuso
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hu:Visszaeles
scn:Abbusu
simple:Abuse
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Acron
Acron, son of Xenon, was an eminent Greek physician born at Agrigentum.  His exact date is not known; but, as he is mentioned as being contemporary with Empedocles, who died about the beginning of the Peloponnesian war, he must have lived in the fifth century BC.  From Sicily he went to Athens, and there opened a philosophical school (Template:Polytonic).
It is said that he was in that city during the great plague (430 BC), and that large fires for the purpose of purifying the air were kindled in the streets by his direction, which proved of great service to several of the sick.  It should however be borne in mind that there is no mention of this in Thucydides, and, if it is true that Empedocles or Simonides (who died in 467 BC) wrote the epitaph on Acron, it may be doubted whether he was in Athens at all during the plague.
On his return to his native country, the physician asked the senate for a spot of ground where he might build a family tomb. The request was refused at the suggestion of Empedocles, who conceived that such a grant for such a purpose would interfere with the principle of equality he was anxious to establish at Agrigentum.  As the sarcastic epitaph on Acron is probably the most complete jeu de mots on record, and therefore defies all translation, it will be given in Greek to preserve the paronomasia of the original:
The second line was sometimes read thus:
Some persons attributed the whole epigram to Simonides.
Pliny considers him as the first of the Empirics.  But this has been considered an error on the part of the Roman naturalist; for the sect alluded to did not arise until the third century BC, roughly 200 years after the time of Acron.  Some scholars consider that the sect of the Empirici, in order to boast of a greater antiquity than the Dogmatics (founded by Thessalus, the son, and Polybus, the son-in-law, of Hippocrates, about 400 BC), merely claimed Acron as their founder.
None of Acron's works are now extant, though he wrote several in the Doric dialect on medical and physical subjects, of which the titles are preserved by the Suda and Eudocia.
Agada
Agada is one of the eight branches into which medical pseudoscience is divided by the Hindus. Agada treats of the best antidotes to Poisons, or toxicology.
Agada Tantra is defined as a section of toxicology; practitioners claim to be able to deal with food poisoning, snakebites, dog bites, insect bites etc. The school of toxicology was founded and run by Kashyapa, also known as Vriddhakashyapa, another contemporary of Atreya Punarvasu. He lived in Taksashila, Pakistan. His text was called the Kashyapa Samhita. This, however, is a different book than the Kashyapa Samhita of pediatrics. This text is not available now but the references of this text are found mentioned in different commentaries. Some other texts written by Alambayana, Ushana, Saunaka, and Latyayana were known to exist. However except for references to them, the original texts are no longer available.
The traditional practice of toxicology is still practiced by different families of Vishavaidyas (poison doctors) who claim to be specialists in toxicology. In fact, their knowledge is quite limited (especially compared to the knowledge attributed to earlier ayurvedic physicians) but villages still use these practices to attempt to deal with poisonous bites. In ancient times, it was the job of Vishavaidyas to protect members of the royal families from being poisoned, as well to poison enemies of the kings.