Persius/hicric huggingface dataset:
2C-T-17
2C-T-17 or 2,5-dimethoxy-4-(-isobutylthio)phenethylamine is a psychedelic phenethylamine of the 2C family.  It was presumably first synthesized by Alexander Shulgin and reported in his book PIHKAL.

# Chemistry
2C-T-17 is the 2 carbon homologue of Aleph-17, which has never been synthesized.  The full chemical name is 2-ethanamine.  The drug has structural properties similar to drugs in the 2C-T series, with the most closely related compounds being 2C-T-7 and 2C-T-8.

# General Information
The dosage range of 2C-T-17 is typically 60-100 mg and its duration is approximately 10-15 hours according to Shulgin.  2C-T-17 has highly psychedelic effects on thinking, but produces few to no visuals.

# Pharmacology
The mechanism that produces 2C-T-17s hallucinogenic and entheogenic effects has not been specifically established, however it is most likely to result from action as a 5-HT2A serotonin receptor agonist in the brain, a mechanism of action shared by all of the hallucinogenic tryptamines and phenethylamines for which the mechanism of action is known.

# Dangers
The toxicity of 2C-T-17 is not well documented.  2C-T-17 is much less potent than 2C-T-7, but it may be expected that at very high doses it would display similar toxicity to that of other phenethylamines of the 2C-T family. Other phenethylamine derivatives substituted with an alkylthio group at the 4 position such as 2C-T-7 and 4-MTA are known to act as selective monoamine oxidase A inhibitors, a side effect which can lead to lethal serotonin syndrome when they are combined with stimulant drugs. Most confirmed fatalities involving 2C-T drugs involve their combination with other hard drugs such as alcohol, ecstasy or cocaine.

# Legality
2C-T-17 is not illegal, but possession and sales of 2C-T-17 could be prosecuted under the Federal Analog Act because of its structural similarities to 2C-T-7.

# Reference
-  Template:CitePiHKAL

# Categorization
7SK RNA
In molecular biology 7SK is an abundant small nuclear RNA found in metazoans.   It plays a role in regulating transcription by controlling the positive transcription elongation factor P-TEFb. 7SK is found in a small nuclear ribonucleoprotein complex (snRNP) with a number of other proteins that regulate the stability and function of the complex.

# Structure
An early study indicated that 7SK in cells is associated with a number of proteins and probing of the secondary structure suggested a model for base pairing between different regions of the RNA. A breakthrough in the function of the 7SK snRNP came with the finding that the positive transcription elongation factor P-TEFb was a component of the complex. 7SK associates with and inhibits the cyclin dependent kinase activity of P-TEFb through the action of the RNA binding proteins HEXIM1 or HEXIM2. The gamma phosphate at the 5' end of 7SK is methylated by the methylphosphate capping enzyme MEPCE which is a constitutive component of the 7SK snRNP.   A La related protein LARP7 is also found associated with 7SK, presumably in part through its interaction with the 3' end of the RNA.    Reduction of either MEPCE or LARP7 by siRNA mediated knockdown leads to destabilization of 7SK in vivo.  A subset of 7SK snRNPs lack P-TEFb and HEXIM, but contains hnRNPs instead.

# Function
The major function of the 7SK snRNP is control of the P-TEFb, a factor that regulates the elongation phase of transcription.   The kinase activity of P-TEFb is inhibited when the factor is in the 7SK snRNP.  P-TEFb can be released from the 7SK snRNP by either the HIV transactivator Tat or the bromodomain containing protein BRD4.  This release leads to a conformational change in 7SK RNA and the ejection of HEXIM.   hnRNPs stabilize the complex lacking P-TEFb and HEXIM.  After P-TEFb functions on specific genes it is re-sequestered in the 7SK snRNP by an unknown mechanism.  The 7SK snRNP has been characterized in both human and Drosophila. 
Detailed review.
ADAMTS1
A disintegrin and metalloproteinase with thrombospondin motifs 1 is an enzyme that in humans is encoded by the ADAMTS1 gene.

# Function
This gene encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motif) protein family. Members of the family share several distinct protein modules, including a propeptide region, a metalloproteinase domain, a disintegrin-like domain, and a thrombospondin type 1 (TS) motif. Individual members of this family differ in the number of C-terminal TS motifs, and some have unique C-terminal domains. The protein encoded by this gene contains two disintegrin loops and three C-terminal TS motifs and has anti-angiogenic activity. The expression of this gene may be associated with various inflammatory processes as well as development of cancer cachexia. This gene is likely to be necessary for normal growth, fertility, and organ morphology and function.

# Interactions
ADAMTS1 has been shown to interact with Vascular endothelial growth factor A.
ADAMTS2
A disintegrin and metalloproteinase with thrombospondin motifs 2 (ADAM-TS2) also known as procollagen I N-proteinase (PC I-NP) is an enzyme that in humans is encoded by the ADAMTS2 gene.

# Gene
The ADAMTS2 gene is located on the long (q) arm of chromosome 5 at the end (terminus) of the arm, from base pair 178,473,473 to base pair 178,704,934.

# Function
ADAMTS2 is responsible for processing several types of procollagen proteins. Procollagens are the precursors of collagens, the proteins that add strength and support to many body tissues. Specifically, this enzyme clips a short chain of amino acids off one end of the procollagen. This clipping step is necessary for collagen molecules to function normally and assemble into fibrils outside cells.

# Clinical significance
Ehlers-Danlos syndrome, dermatosparaxis type is caused by mutations in the ADAMTS2 gene. Several mutations in the ADAMTS2 gene have been identified in people with this syndrome. These mutations greatly reduce the production of the enzyme made by the ADAMTS2 gene. Procollagen cannot be processed correctly without this enzyme. As a result, collagen fibrils are not assembled properly; they appear ribbon-like and disorganized under the microscope. Cross-links, or chemical interactions, between collagen fibrils are also affected. These defects weaken connective tissue (the tissue that binds and supports the body's muscles, ligaments, organs, and skin), which causes the signs and symptoms of the disorder.
ADAMTS3
A disintegrin and metalloproteinase with thrombospondin motifs 3 is an enzyme that in humans is encoded by the ADAMTS3 gene. The protein encoded by this gene is the major procollagen II N-propeptidase.

# Structure
This gene encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) protein family. Members of the family share several distinct protein modules, including a propeptide region, a metalloproteinase domain, a disintegrin-like domain, and a thrombospondin type 1 (TS) motif. Individual members of this family differ in the number of C-terminal TS motifs, and some have unique C-terminal domains. The protein encoded by this gene is the major procollagen II N-propeptidase.

# Function
Because of the high similarity to ADAMTS2, the major substrate of ADAMTS3 had been erroneously assumed to be procollagen II. However, ADAMTS3 appears largely irrelevant for collagen maturation but instead is required for the activation of the lymphangiogenic growth factor VEGF-C. Hence, ADAMTS3 is essential for the development and growth of lymphatic vessels. The proteolytic processing of VEGF-C by ADAMTS3 is regulated by the CCBE1 protein.

# Clinical significance
A deficiency of this protein may be responsible for dermatosparaxis, a genetic defect of connective tissues.
Some hereditary forms of lymphedema are caused by mutations in ADAMTS3.
ADAMTS4
A disintegrin and metalloproteinase with thrombospondin motifs 4 is an enzyme that in humans is encoded by the ADAMTS4 gene.
This gene encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) protein family. Members of the family share several distinct protein modules, including a propeptide region, a metalloproteinase domain, a disintegrin-like domain, and a thrombospondin type 1 (TS) motif. Individual members of this family differ in the number of C-terminal TS motifs, and some have unique C-terminal domains. The enzyme encoded by this gene lacks a C-terminal TS motif. It can degrade aggrecan, a major proteoglycan of cartilage, brevican, a brain-specific extracellular matrix protein, neurocan and versican. The cleavage of aggrecan and brevican suggests key roles of this enzyme in arthritic disease and in the central nervous system, potentially, in the progression of glioma.

# Structure
ADAMTS4 is the shortest known ADAMTS, lacking the C-terminal domain and is the only non-glycosylated ADAMTS. It also only has one thrombospondin type 1 motif (TSR), whereas all the other ADAMTS have two or more TSRs. The TSR is important for binding of the enzyme to the extracellular matrix and hence its substrate specificity. Adjacent to the C-terminal TSR is a disintegrin-like domain, a cysteine-rich region
that stacks against the active-site of the enzyme when in its final folded tertiary structure.

# Function
ADAMTS4 is capable of cleaving all the large chondroitin sulfate hyaluronan-binding proteoglycans (CSPGs), including aggrecan, brevican, neurocan and versican. Like ADAMTS5, it can be effectively inhibited by tissue inhibitor of metalloproteinase-3 (TIMP3) and this inhibition can be enhanced in the presence of aggrecan. In addition to TIMP3, it can also be inhibited by calcium pentosan polysulfate.
ADAMTS4 is expressed in ovary, spinal cord, adrenal cortex, ciliary ganglion, trigeminal ganglion, brain, retina, pancreas (islets), fetal lung, breast myoepithelial cells, tendon and cartilage.

# Clinical Significance
ADAMTS4 (and ADAMTS5) are the major proteinases responsible for the degradation of proteoglycans in articular cartilage in osteoarthritis. Which of these aggrecanases is more important in cartilage degradation appears to be species-specific, with ADAMTS4 more important in human disease (but ADAMTS5 more important in mouse models of osteoarthritis).

# Alternative names
- Aggrecanase-1 (initial name reflecting its ability to cleave aggrecan)
ADAMTS5
A disintegrin and metalloproteinase with thrombospondin motifs 5 also known as ADAMTS5 is an enzyme that in humans is encoded by the ADAMTS5 gene.

# Function
ADAMTS5 is a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) protein family. Members of the family share several distinct protein modules, including a propeptide region, a metalloproteinase domain, a disintegrin-like domain, and a thrombospondin type 1 (TS) motif. Individual members of this family differ in the number of C-terminal TS motifs, and some have unique C-terminal domains. The enzyme encoded by this gene contains two C-terminal TS motifs and functions as aggrecanase to cleave aggrecan, a major proteoglycan of cartilage. ADAMTS5 may also have a role in the pathogenesis of human osteoarthritis.

# Animal studies
Genetically modified mice in which the catalytic domain of ADAMTS5 was deleted are resistant to cartilage destruction in an experimental model of osteoarthritis. ADAMTS5 is the major aggrecanase in mouse cartilage in a mouse model of inflammatory arthritis.
ADAMTS8
A disintegrin and metalloproteinase with thrombospondin motifs 8 is an enzyme that in humans is encoded by the ADAMTS8 gene.

# Function
This gene encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) protein family. Members of the family share several distinct protein modules, including a propeptide region, a metalloproteinase domain, a disintegrin-like domain, and a thrombospondin type 1 (TS) motif. Individual members of this family differ in the number of C-terminal TS motifs, and some have unique C-terminal domains. The enzyme encoded by this gene contains two C-terminal TS motifs, and disrupts angiogenesis in vivo.

# Clinical significance
A number of disorders have been mapped in the vicinity of this gene, most notably lung neoplasms.
ALDH1A1
Aldehyde dehydrogenase 1 family, member A1, also known as ALDH1A1 or retinaldehyde dehydrogenase 1 (RALDH1), is an enzyme that in humans is encoded by the ALDH1A1 gene.

# Function
"The protein encoded by this gene belongs to the aldehyde dehydrogenase family. Aldehyde dehydrogenase is the next enzyme after alcohol dehydrogenase in the major pathway of alcohol metabolism. There are two major aldehyde dehydrogenase isozymes in the liver, cytosolic and mitochondrial, which are encoded by distinct genes, and can be distinguished by their electrophoretic mobility, kinetic properties, and subcellular localization. This gene encodes the cytosolic isozyme. Studies in mice show that through its role in retinol metabolism, this gene may also be involved in the regulation of the metabolic responses to high-fat diet."
ALDH1A1 also belongs to the group of corneal crystallins that help maintain the transparency of the cornea.

# Transcriptions
"The promoter region of the gene contains an ATA box and a CCAAT box, which are located 32 and 74 bp upstream, respectively, from the transcription initiation site."
ALDH1B1
Aldehyde dehydrogenase X, mitochondrial is an enzyme that in humans is encoded by the ALDH1B1 gene.

# Function
This protein belongs to the aldehyde dehydrogenases family of proteins. Aldehyde dehydrogenase is the second enzyme of the major oxidative pathway of alcohol metabolism. This gene does not contain introns in the coding sequence. The variation of this locus may affect the development of alcohol-related problems.

# Model organisms
Model organisms have been used in the study of ALDH1B1 function. A conditional knockout mouse line called Aldh1b1tm2a(EUCOMM)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 - in-depth bone and cartilage phenotyping
ALDH3B1
Aldehyde dehydrogenase 3 family, member B1 also known as ALDH3B1 is an enzyme that in humans is encoded by the ALDH3B1 gene.

# Function
The aldehyde dehydrogenases are a family of isozymes that may play a major role in the detoxification of aldehydes generated by alcohol metabolism and lipid peroxidation. This particular gene spans about 20 kb of genomic DNA and is composed of 9 coding exons. The gene encodes a single transcript of 2.8 kb that is highly expressed in kidney and lung. The functional significance of this gene and the cellular localization of its product are presently unknown. Two transcript variants encoding different isoforms have been found for this gene.

# Model organisms
Model organisms have been used in the study of ALDH3B1 function. A conditional knockout mouse line called Aldh3b1tm1b(EUCOMM)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 - in-depth bone and cartilage phenotyping
ANGPTL3
Angiopoietin-like 3, also known as ANGPTL3, is a protein that in humans is encoded by the ANGPTL3 gene.

# Function
The protein encoded by this gene is a member of the angiopoietin-like family of secreted factors. It is expressed predominantly in the liver, and has the characteristic structure of angiopoietins, consisting of a signal peptide, N-terminal coiled-coil domain, and the C-terminal fibrinogen (FBN)-like domain. The FBN-like domain in angiopoietin-like 3 protein was shown to bind alpha-5/beta-3 integrins, and this binding induced endothelial cell adhesion and migration. This protein may also play a role in the regulation of angiogenesis.
Angptl3 also acts as dual inhibitor of lipoprotein lipase (LPL) and endothelial lipase (EL), thereby increasing plasma triglyceride, LDL cholesterol and HDL cholesterol in mice and humans.
ANGPTL3 inhibits endothelial lipase hydrolysis of HDL-phospholipid (PL), thereby increasing HDL-PL levels. Circulating PL-rich HDL particles have high cholesterol efflux abilities.
Angptl3 plays a major role in promoting uptake of circulating triglycerides into white adipose tissue in the fed state, likely through activation by Angptl8, a feeding-induced hepatokine, to inhibit postprandial LPL activity in cardiac and skeletal muscles, as suggested by the ANGPTL3-4-8 model.

# Clinical significance
In human, ANGPTL3 is a determinant factor of HDL level and positively correlates with plasma HDL cholesterol.
In humans with genetic loss-of-function variants in one copy of ANGPTL3, the serum LDL-C levels are reduced. In those with loss-of-function variants in both copies of ANGPTL3, low LDL-C, low HDL-C, and low triglycerides are seen ("familial combined hypolipidemia").
ANKRD15
KN motif and ankyrin repeat domain-containing protein 1 is a protein that in humans is encoded by the KANK1 gene.
This gene encodes a protein containing four ankyrin repeat domains in its C-terminus. The suggested role for this protein is in tumorigenesis of renal cell carcinoma. 
Two alternatively spliced transcript variants encoding different isoforms have been identified.
ANKRD26
Ankyrin repeat domain-containing protein 26 is a protein that in humans is encoded by the ANKRD26 gene. This protein has a function that is not currently understood.
Ankyrin repeat domain-containing protein 26 is a protein that in humans is encoded by the ANKRD26 gene.

# Gene
ANKRD26 is found on chromosome 10, at 10q21. It has 6816 base pairs in the reference sequence mRNA transcript.

## Neighborhood
LOC100289548 (PUTAETIVE UNCHARACTERIZED PROTEIN C10ORF52-LIKE) is located directly to the left (3') of ANKRD26, and is a protein coding gene located at 10p12.1.  It has an unknown function. On the other side of LOC100289548  is NCRNA00202 non-protein coding RNA 202.   On the 5' end of ANKRD26, YME1L1 can be found at 10q14.1. The protein encoded by the YME1-like 1 is an ortholog of yeast mitochondrial AAAmetalloprotease.  This gene is thought to play a role in mitochondrial protein metabolism.   On the positive strand of human chromosome ten, located next to the 5' end of ANKRD26 is MASTL, microtubule associated serine/threonine kinase-like. This particular gene encodes the microtubule associated serine/threonine kinase.1 Mutations within these gene have been expected to be associated with thrombocytopenia-2.

# Protein 
Ankyrin repeat domain-containing protein 26 has three conserved domains: ANK, SbcC, and DUF3496. ANK conserved domain is located from amino acid 74-199. Ankyrin repeats are found to mediate protein-protein interactions, and also contains two antiparallel helices, as well as a beta-hairpin. SbcC conserved domain can be found from amino acid 743-1333, and is domain associated with ATPase involved in DNA repair. There is also a domain of unknown function from amino acid 1538-1649.

# Expression
In humans ANKRD26 was seen to be most highly expressed in the ear, lymph, esophagus, parathyroid, and placenta, as well as, most commonly seen in esophageal tumors and lymphoma, as well as seen in the blastocyst, fetus, juvenile, and adult developmental stages. In humans this is associated at all stages of life with lymphoma cancer as well as esophageal tumors. The association with expression in tissues and disease states doesn't show enough difference to link one another.
APOBEC4
C->U-editing enzyme APOBEC-4, also known as Apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 4, is a protein that in humans is encoded by the APOBEC4 gene. It is primarily expressed in testis and found in mammals, chicken, but not fishes.

# Function
This gene encodes a member of the AID / APOBEC family of polynucleotide (deoxy)cytidine deaminases, which convert cytidine to uridine. Other AID/APOBEC family members are involved in mRNA editing, somatic hypermutation and recombination of immunoglobulin genes, and innate immunity to retroviral infection.
A recent study on APOBEC4 (A4) revealed an interesting finding that A4 enhanced the replication of HIV-1 through boosting promoter activity, it also increased the expression of other relevant promoter mediated enhanced protein expression. Biochemical analysis of A4 showed the lack of cytidine deaminase activity on single stranded DNA and it binds DNA rather weak.
ARFGAP1
ADP-ribosylation factor GTPase-activating protein 1 is an enzyme that in humans is encoded by the ARFGAP1 gene.  Two transcript variants encoding different isoforms have been found for this gene.

# Function
The protein encoded by this gene is a GTPase-activating protein (GAP) which associates with the Golgi apparatus and which interacts with ADP-ribosylation factor 1 (ARF1). The encoded protein promotes hydrolysis of ARF1-bound GTP and is required for the dissociation of coat proteins from Golgi-derived membranes and vesicles. Dissociation of the coat proteins is required for the fusion of these vesicles with target compartments. The activity of this protein is stimulated by phosphoinositides and inhibited by phosphatidylcholine.
The protein has two amphipathic lipid packing sensor motifs (ALPS), that let the protein sense the curvature of the membrane (<30 nm) or lipid packing defects, and in this way evaluate if the vesicle is mature and ready for coat disassembly.

# Interactions
ARFGAP1 has been shown to interact with KDELR1 and LRRK2.
ARFGEF1
Brefeldin A-inhibited guanine nucleotide-exchange protein 1 is a protein that in humans is encoded by the ARFGEF1 gene.

# Function
ADP-ribosylation factors (ARFs) play an important role in intracellular vesicular trafficking. The protein encoded by this gene is involved in the activation of ARFs by accelerating replacement of bound GDP with GTP. It contains a Sec7 domain, which may be responsible for the guanine-nucleotide exchange activity and also the brefeldin A inhibition.

# Interactions
ARFGEF1 has been shown to interact with FKBP2, ARFGEF2 and PRKAR1A.
ARFGEF2
Brefeldin A-inhibited guanine nucleotide-exchange protein 2 is a protein that in humans is encoded by the ARFGEF2 gene.

# Function
ADP-ribosylation factors (ARFs) play an important role in intracellular vesicular trafficking. The protein encoded by this gene is involved in the activation of ARFs by accelerating replacement of bound GDP with GTP and is involved in Golgi transport. It contains a Sec7 domain, which may be responsible for its guanine-nucleotide exchange activity and also brefeldin A inhibition.

# Interactions
ARFGEF2 has been shown to interact with ARFGEF1, PRKAR1A and PRKAR2A.
ARHGAP5
Rho GTPase-activating protein 5 is an enzyme that in humans is encoded by the ARHGAP5 gene.

# Function
Rho GTPase activating protein 5 negatively regulates RHO GTPases, a family that may mediate cytoskeleton changes by stimulating the hydrolysis of bound GTP. Two transcript variants encoding different isoforms have been found for this gene.

# Interactions
ARHGAP5 has been shown to interact with Rnd1, Rnd2, Rnd3 and RHOA.