Persius/hicric huggingface dataset:
ACVR1
Activin A receptor, type I (ACVR1) is a protein which in humans is encoded by the ACVR1 gene; also known as ALK-2 (activin receptor-like kinase-2).  ACVR1 has been linked to the 2q23-24 region of the genome. This protein is important in the bone morphogenic protein (BMP) pathway which is responsible for the development and repair of the skeletal system. While knock-out models with this gene are in progress, the ACVR1 gene has been connected to Fibrodysplasia Ossificans Progressiva, a disease characterized by the formation of heterotopic bone throughout the body.

# Function
Activins are dimeric growth and differentiation factors which belong to the transforming growth factor-beta (TGF beta) superfamily of structurally related signaling proteins. Activins signal through a heteromeric complex of receptor serine kinases which include at least two type I ( I and IB) and two type II (II and IIB) receptors. These receptors are all transmembrane proteins, composed of a ligand-binding extracellular domain with cysteine-rich region, a transmembrane domain, and a cytoplasmic domain with predicted serine/threonine specificity. Type I receptors are essential for signaling; and type II receptors are required for binding ligands and for expression of type I receptors. Type I and II receptors form a stable complex after ligand binding, resulting in phosphorylation of type I receptors by type II receptors. This gene encodes activin A type I receptor which signals a particular transcriptional response in concert with activin type II receptors.

# Signaling
ACVR1 transduces signals of BMPs. BMPs bind either ACVR2A/ACVR2B or a BMPR2 and then form a complex with ACVR1. These go on to recruit the R-SMADs SMAD1, SMAD2, SMAD3 or SMAD6.

# Clinical significance
A mutation in the gene ACVR1 (= ALK2) is responsible for the fibrodysplasia ossificans progressiva. ACVR1 encodes activin receptor type-1, a BMP type-1 receptor. The mutation causes the ACVR1 protein to have the amino acid histidine substituted for the amino acid arginine at position 206. This causes the protein ALK2 to change in the critical glycine-serine activation domain of the protein which will cause the protein to bind its inhibitory ligand (FKBP12) less tightly, and activate its SMAD pathway specific proteins more effectively than usual. The result is the BMP pathway will trigger when it should not, and bone will form in soft tissues throughout the body. This causes endothelial cells to transform to mesenchymal stem cells and then to bone.
Mutations in the ACVR1 gene have also been linked to cancer, especially diffuse intrinsic pontine glioma (DIPG).
AD-36
AD-36 is one of 51 types of adenoviruses known to infect humans. It was first shown to be associated with obesity in chickens by Dr. Nikhil Dhurandhar.
There has been a positive correlation between body fat and the presence of AD-36 antibodies in the blood. Previous research showed that chicken or mice injected with similar types of viruses show a statistically significant weight gain.
A 2.5 fold increase in fat storage was not uncommon, among the test subjects. There is, however, a distinctive signature of the viral weight gain, in addition to the obvious anti-bodies that can now be tested for, the weight gain is unusual in that lipids, triglycerides, and cholesterol are markedly absent, or at least very low, in the blood of the victim. This is distinct from normal obesity, where these chemicals are usually found in the blood in abundance, as a natural tendency in the cause and effect chain. Currently, no one knows where these chemicals are going, but the current hypothesis is that they are being stored within cells, instead of excreted via the blood stream.
It was noted the following in the experiment:
AD-36 has been found to increase adiposity in chickens among other non-human subjects. This is not to be mistaken for the sole, or even leading, cause of obesity if any cause at all. It is fact that this causes and increase in fat but not for any known amount of time, and certainly not for many years. 
Recent testing has been completed on several other human adenoviruses including AD-37 and AD-2. AD-37 showed similar correlations with the increase in fat tissue as it inducted human stem cells into fat cells. However, AD-37 had the reverse effect on cholesterol (increasing it) from that of AD-36. The most important discovery of these experiments (AD-36 in 2004 and AD-37 in 2007) was notes that AD-2 actually lowered the body fat in the test subjects. It is important to understand that the virus is not the only cause of obesity and that further research is needed in order to even prove that it causes any kind of long term obesity.
PSEN2
Lua error in Module:Redirect at line 65: could not parse redirect on page "AD4".
Presenilin-2 is a protein that in humans is encoded by the PSEN2 gene.

# Function
Alzheimer's disease (AD) patients with an inherited form of the disease carry mutations in the presenilin proteins (PSEN1; PSEN2) or the amyloid precursor protein (APP).  These disease-linked mutations result in increased production of the longer form of amyloid-beta (main component of amyloid deposits found in AD brains).  Presenilins are postulated to regulate APP processing through their effects on gamma-secretase, an enzyme that cleaves APP.  Also, it is thought that the presenilins are involved in the cleavage of the Notch receptor, such that they either directly regulate gamma-secretase activity or themselves are protease enzymes.  Two alternative transcripts of PSEN2 have been identified.
In melanocytic cells PSEN2 gene expression may be regulated by MITF.

# Interactions
PSEN2 has been shown to interact with:
- BCL2-like 1,
- CAPN1,
- CIB1,
- Calsenilin,
- FHL2,
- FLNB,
- KCNIP4,
- Nicastrin,  and
- UBQLN1.
ADCK3
Lua error in Module:About-distinguish at line 61: attempt to index field 'wikibase' (a nil value).
aarF domain containing kinase 3 is a protein that in humans is encoded by the ADCK3 gene.
This gene encodes a mitochondrial protein similar to yeast ABC1, which functions in an electron-transferring membrane protein complex in the respiratory chain. It is not related to the family of ABC transporter proteins. Expression of this gene is induced by the tumor suppressor p53 and in response to DNA damage, and inhibiting its expression partially suppresses p53-induced apoptosis. Alternatively spliced transcript variants have been found; however, their full-length nature has not been determined.
ADCY1
Adenylyl cyclase type 1 is an enzyme that in humans is encoded by the ADCY1 gene.
This gene encodes a form of adenylyl cyclase expressed in brain. A similar protein in mice is involved in pattern formation of the brain.

# Function
ADCY1 is a calmodulin-sensitive adenylyl cyclase. In terms of function, It may be involved in regulatory processes in the central
nervous system; specifically, it may play a role in memory acquisition and learning. It is inhibited by the G protein beta and gamma subunit complex.
ADCY3
Adenylyl cyclase type 3 is an enzyme that in humans is encoded by the ADCY3 gene.

# Function
This gene encodes adenylyl cyclase 3, which is a membrane-associated enzyme and catalyzes the formation of the secondary messenger cyclic adenosine monophosphate (cAMP).
The ADCY3 subtype likely mediates odorant detection (possibly) via modulation of intracellular cAMP concentration.
ADH1B
Alcohol dehydrogenase 1B is an enzyme that in humans is encoded by the ADH1B gene.
The protein encoded by this gene is a member of the alcohol dehydrogenase family. Members of this enzyme family metabolize a wide variety of substrates, including ethanol (beverage alcohol), retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. The encoded protein, known as ADH1B or beta-ADH, can form homodimers and heterodimers with ADH1A and ADH1C subunits, exhibits high activity for ethanol oxidation and plays a major role in ethanol catabolism (oxidizing ethanol into acetaldehyde). The acetaldehyde is further metabolized to acetate by aldehyde dehydrogenase genes.  Three genes encoding the closely related alpha, beta and gamma subunits are tandemly organized in a genomic segment as a gene cluster.
The human gene is located on chromosome 4 in 4q22.
Previously ADH1B was called ADH2. There are more genes in the family of alcohol dehydrogenase. These genes are now referred to as ADH1A, ADH1C, and ADH4, ADH5, ADH6 and ADH7.

# Variants
A single nucleotide polymorphism (SNP) in ADH1B is rs1229984, that changes arginine to histidine at residue 47 of the mature protein; standard nomenclature now includes the initiating methionine, so the position is officially 48.
The 'typical' variant of this has been referred to as ADH2(1) or ADH2*1 while the 'atypical' has been referred to as, e.g., ADH2(2), ADH2*2, ADH1B*48His.
This SNP is associated with the risk for alcohol dependence, alcohol use disorders and alcohol consumption, with the atypical genotype having reduced risk of alcoholism.
Another SNP is rs2066702 . originally called position 369. This SNP is at high frequencies in populations from Africa, and also reduces risk for alcohol dependence.

# Role in pathology
A marked decrease of ADH1B mRNA was detected in corneal fibroblasts taken from persons suffering from keratoconus.
AEBP2
Adipocyte Enhancer-Binding Protein is a zinc finger protein that in humans is encoded by the evolutionarily well-conserved gene AEBP2. It was initially identified due to its binding capability to the promoter of the adipocyte P2 gene, and was therefore named Adipocyte Enhancer Binding Protein 2. AEBP2 is a potential targeting protein for the mammalian Polycomb Repression Complex 2 (PRC2).

# Function
AEBP2 is a DNA-binding transcriptional repressor. It may interact with and stimulate the activity of the PRC2 complex.
AEBP2 may regulate the migration and development of the neural crest cells through the PRC2-mediated epigenetic mechanism and is most likely a targeting protein for the mammalian PRC2 complex.

# Clinical significance
Diseases associated with AEBP2 include Waardenburg's syndrome, and Hirschsprung's disease.
AGG01
AGG01 is the tentative name of a new Penicillin-class antibiotic, recently  discovered in the breast milk of the Tammar Wallaby, reportedly one hundred times more powerful than penicillin.
This compound was found to be effective against MRSA, E. coli, Streptococci, Salmonella, Bacillus subtilis, Pseudomonas spp., Proteus vulgaris, and Staphylococcus aureus.
AGG01 has not yet been classified as a Beta-lactam antibiotic.
AGG01 is a cationic peptide, which is a polycationic protein which is rich in positive residues of the amino acidss arginine and lysine, and which folds into an amphipathic structure (one which has both hydrophobic and hydrophilic areas). These features mean that it can interact with the anionic lipids in the bacterial membrane, such as phosphatidylglycerol. It inserts itself into the membrane, by competing with cross-linking proteins between each membrane layer, and then sets up trans-membrane protein channels which induce ion transport out of the cell. This causes huge leakage via osmosis through these 'pores and the general consensus is that the loss of these essential molecules is the mechanism by which bacteria are killed. The bacterial membrane has a different structure from the mammalian plasma membrane, so the protein can only kill pathogenic cells and not human ones.
AIFM1
Apoptosis-inducing factor 1, mitochondrial is a protein that in humans is encoded by the AIFM1 gene on the X chromosome. This protein localizes to the mitochondria, as well as the nucleus, where it carries out nuclear fragmentation as part of caspase-independent apoptosis.

# Structure
AIFM1 is expressed as a 613-residue precursor protein that containing a mitochondrial targeting sequence (MTS) at its N-terminal and two nuclear leading sequences (NLS). Once imported into the mitochondria, the first 54 residues of the N-terminal are cleaved to produce the mature protein, which inserts into the inner mitochondrial membrane. The mature protein incorporates the FAD cofactor and folds into three structural domains: the FAD-binding domain, the NAD-binding domain, and the C-terminal. While the C-terminal is responsible for the proapoptotic activity of AIFM1, the FAD-binding and NAD-binding domains share the classical Rossmann topology with other flavoproteins and the NAD(P)H dependent reductase activity.
Three alternative transcripts encoding different isoforms have been identified for this gene. Two alternatively spliced mRNA isoforms correspond to the inclusion/exclusion of the C-terminal and the reductase domains. A pseudogene that is thought to be related to this gene has been identified on chromosome 10.

# Function
This gene encodes a flavoprotein essential for nuclear disassembly in apoptotic cells that is found in the mitochondrial intermembrane space in healthy cells. Induction of apoptosis results in the cleavage of this protein at residue 102 by calpains and/or cathepsins into a soluble and proapoptogenic form that translocates to the nucleus, where it effects chromosome condensation and fragmentation. In addition, this gene product induces mitochondria to release the apoptogenic proteins cytochrome c and caspase-9. AIFM1 also contributes reductase activity in redox metabolism.

# Clinical significance
Mutations in the AIFM1 gene are correlated with Charcot-Marie-Tooth disease (Cowchock syndrome). At a cellular level, AIFM1 mutations result in deficiencies in oxidative phosphorylation, leading to severe mitochondrial encephalomyopathy. Clinical manifestations of this mutation are characterized by muscular atrophy, neuropathy, ataxia, psychomotor regression, hearing loss and seizures.

# Interactions
AIFM1 has been shown to interact with HSPA1A.

# Evolution
Phylogenetic analysis indicates that the divergence of the AIFM1 and other human AIFs (AIFM2a and AIFM3)  sequences occurred before the divergence of eukaryotes.This conclusion is supported by domain architecture of these proteins. Both eukaryotic and eubacterial AIFM1 proteins contain additional domain AIF_C.
AKAP4
A-kinase anchor protein 4 is a scaffold protein that in humans is encoded by the AKAP4 gene. It involves in the intracellular signalling of protein kinase -A. AKAP4 is called as cancer /testis antigen (CTA), it belongs to a class of tumour linked antigens categories by high expression in germ cells and cancer than normal tissues. AKAP4 is not normally expressed in mRNA and protein level in MM cell line.

# Function
The A-kinase anchor proteins (AKAPs) are a group of structurally diverse proteins, which have the common function of binding to the regulatory subunit of protein kinase A (PKA) and confining the holoenzyme to discrete locations within the cell. This gene encodes a member of the AKAP family. The encoded protein is localized to the sperm flagellum and may be involved in the regulation of sperm motility. Alternative splicing of this gene results in two transcript variants encoding different isoforms.
AKAP 4 protein belongs to the family of scaffold proteins and is involved in controlled mechanism of flagellar function. In mice, AKAP4 is required for sperm development and male mice that lack AKAP4 are infertiel The fibrous sheath was not formed, flagellum become short and often some proteins associated with the fibrous sheath in this case they were very few or absent. Surprisingly, another component of flagellum was developed as normal. In the conclusion, they state that AKAP4 plays a pivotal role in the fibrous sheath and effect on the motility of sperm, in the absence of AKAP4 these activities affected due to a failure of signal transduction and glycolytic enzymes because they were not able to attach with the fibrous sheath.

# Clinical significance
AKAP4 is a potential biomarker for early diagnosis and immunotherapy of colon cancer. AKAP4 may be implicated as a biomarker and immunotherapeutic target for cervical cancer. AKAP4 is also a circulating biomarker for non-small cell lung cancer. To detect the early stage breast cancer and diagnosis, AKAP4 is used as serum. Investigation was undertaken about AKAP4 with various clinical parameters which could be use as early detector biomarker to treat cancer by developing a tissue or serum.
AKAP4 is associated with diseases such as multiple myeloma, lung cancer, breast cancer and prostate cancer.
AKAP4 is over expressed in multiple myeloma (MM)

# Interactions
AKAP4 has been shown to interact with:
- AKAP3, and
- PRKAR1A.
AKAP6
A-kinase anchor protein 6 is an enzyme that in humans is encoded by the AKAP6 gene.
The A-kinase anchor proteins (AKAPs) are a group of structurally diverse proteins, which have the common function of binding to the regulatory subunit of protein kinase A (PKA) and confining the holoenzyme to discrete locations within the cell. This gene encodes a member of the AKAP family. The encoded protein is highly expressed in various brain regions and cardiac and skeletal muscle. It is specifically localized to the sarcoplasmic reticulum and nuclear membrane, and is involved in anchoring PKA to the nuclear membrane or sarcoplasmic reticulum.

# Interactions
AKAP6 has been shown to interact with Ryanodine receptor 2 and PDE4D3.
AKAP9
A-kinase anchor protein 9 is a protein that in humans is encoded by the AKAP9 gene. AKAP9 is also known as Centrosome- and Golgi-localized protein kinase N-associated protein (CG-NAP) or AKAP350 or AKAP450 

# Function
The A-kinase anchor proteins (AKAPs) are a group of structurally diverse proteins which have the common function of binding to the regulatory subunit of protein kinase A (PKA) and confining the holoenzyme to discrete locations within the cell. This gene encodes a member of the AKAP family. Alternate splicing of this gene results in many isoforms that localize to the centrosome and the Golgi apparatus, and interact with numerous signaling proteins from multiple signal transduction pathways. These signaling proteins include type II protein kinase A, serine/threonine kinase protein kinase N, protein phosphatase 1, protein phosphatase 2a, protein kinase C-epsilon and phosphodiesterase 4D3.

# Model organisms
Model organisms have been used in the study of AKAP9 function. A conditional knockout mouse line, called Akap9tm1a(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.
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Twenty six tests were carried out on mutant mice and eight significant abnormalities were observed. Fewer than expected homozygous mutant mice survived until weaning. The remaining tests were carried out on both homozygous and heterozygous mutant adult mice. Animals of both sex displayed decreased body fat and body weight, hematopoietic abnormalities and an atypical plasma chemistry panel. Female homozygotes also displayed abnormal tooth morphology while males heterozygous animals displayed an abnormal pelvic girdle bone morphology.

# Interactions
AKAP9 has been shown to interact with:
- CALM2,
- CALM1,
- FNBP1,
- KvLQT1
- PRKAR2A,
- PKN1,  and
- TRIP10.
AKTIP
AKT-interacting protein is a protein that in humans is encoded by the AKTIP gene.
The mouse homolog of this gene produces fused toes and thymic hyperplasia in heterozygous mutant animals while homozygous mutants die in early development. This gene may play a role in apoptosis as these morphological abnormalities are caused by altered patterns of programmed cell death. The protein encoded by this gene is similar to the ubiquitin ligase domain of other ubiquitin-conjugating enzymes but lacks the conserved cysteine residue that enables those enzymes to conjugate ubiquitin to the target protein. This protein interacts directly with serine/threonine kinase protein kinase B (PKB)/Akt and modulates PKB activity by enhancing the phosphorylation of PKB's regulatory sites. Alternative splicing results in two transcript variants encoding the same protein.

# Interactions
AKTIP has been shown to interact with AKT1.

# Molecular genetics
The association between the AKTIP gene variants in a sample of 273 bipolar patients using 3 single-nucleotide polymorphisms has been investigated. No association between suicidal behavior and AKTIP variants nor any interaction between AKTIP and AKT1 polymorphisms was observed.
ALARA
See also: radiation protection

# Overview
ALARA is an acronym for an important principle in radiation protection and stands for "As Low As Reasonably Achievable". The aim is to minimize the risk of radioactive exposure or amount of dose while keeping in mind that some exposure may be acceptable in order to further the task at hand.
This compromise is well illustrated in radiology. The application of radiation can aid the patient by providing doctors with a medical diagnosis, but the exposure should be reasonably low enough to keep the statistical probability of cancers or sarcomas (stochastic effects) below an acceptable level, and to eliminate deterministic effects (eg. skin reddening or cataracts). An acceptable level of incidence of stochastic effects is considered to be equal for a worker to the risk in another work generally considered to be safe.
This policy is based on the principle that any amount of radiation exposure, no matter how small, can increase the chance of negative biological effects such as cancer, though perhaps by a negligible amount.  It is also based on the principle that the probability of the occurrence of negative effects of radiation exposure increases with cumulative lifetime dose. These ideas are combined to form the linear no-threshold model. At the same time, radiology and other practices that involve use of radiations bring benefits to population, so reducing radiation exposure can reduce the efficacy of a medical practice. The economic cost, for example of adding a barrier against radiation, must also be considered when applying the ALARA principle.
There are four major ways to reduce radiation exposure to workers or to population:
- Shielding. Use proper barriers to block or reduce ionizing radiation.
- Time. Spend less time in radiation fields.
- Distance. Increase distance between radioactive sources and workers or population.
- Amount. Reduce the quantity of radioactive material for a practice.
ALAS2
Delta-aminolevulinate synthase 2 also known as ALAS2 is a protein that in humans is encoded by the ALAS2 gene. ALAS2 is an aminolevulinic acid synthase.
The product of this gene specifies an erythroid-specific mitochondrially located enzyme. The encoded protein catalyzes the first step in the heme biosynthetic pathway. Defects in this gene cause X-linked pyridoxine-responsive sideroblastic anemia. Alternatively spliced transcript variants encoding different isoforms have been identified.
Its gene contains an IRE in its 5'-UTR region on which an IRP binds if the iron level is too low, thus inhibiting its translation.
ALCAM
CD166 antigen is a 100-105 kD typeI transmembrane glycoprotein that is a member of the immunoglobulin superfamily of proteins. In humans it is encoded by the ALCAM gene. It is also called CD166 (cluster of differentiation 166), MEMD, SC-1/DM-GRASP/BEN in the chicken, and KG-CAM in the rat.
Some literature sources have also cited it as the CD6 ligand (CD6L). It is expressed on activated T cells, activated monocytes, epithelial cells, fibroblasts, neurons, melanoma cells, and also in sweat and sebaceous glands. CD166 protein expression is reported to be upregulated in a cell line deriving from a metastasizing melanoma. CD166 plays an important role in mediating adhesion interactions between thymic epithelial cells and CD6+ cells during intrathymic T cell development.
Recently, CD166 has also been used as a potential cancer stem cell marker.