Persius/hicric huggingface dataset:
UGT1A1
This gene encodes a UDP-glucuronosyltransferase, an enzyme of the glucuronidation pathway that transforms small lipophilic molecules, such as steroids, bilirubin, hormones, and drugs, into water-soluble, excretable metabolites. This gene is part of a complex locus that encodes several UDP-glucuronosyltransferases. The locus includes thirteen unique alternate first exons followed by four common exons. Four of the alternate first exons are considered pseudogenes. Each of the remaining nine 5' exons may be spliced to the four common exons, resulting in nine proteins with different N-termini and identical C-termini. Each first exon encodes the substrate binding site, and is regulated by its own promoter. The preferred substrate of this enzyme is bilirubin, although it also has moderate activity with simple phenols, flavones, and C18 steroids. Mutations in this gene result in Crigler-Najjar syndromes types I and II and in Gilbert syndrome.
UGT1A1 is a gene associated with Crigler-Najjar syndrome, and a common splice variant is associated with serious side effects to the common chemotherapeutic drug irinotecan.  The primary function of the gene's protein product is uridine diphospate glycosyltrasnferase 1 and is involved in the conversion of lipophilic molocules to water soluble substances suitable for excretion via substrate glycosylation.
Lack of expression of UGT1A1 in the neonatal liver is the major cause of jaundice in newborns. This jaundice is generally caused by massive breakdown of fetal blood cells which produces bilirubin which cannot be cleared if UGT1A1 is expressed at low levels or is absent. This type of jaundice can remedied by UV light exposure.
It transports bilirubin and phenol.
UGT1A6
UDP-glucuronosyltransferase 1-6 is an enzyme that in humans is encoded by the UGT1A6 gene.

# Function
UDP-glucuronosyltransferase 1-6 is a UDP-glucuronosyltransferase, an enzyme of the glucuronidation pathway that transforms small lipophilic molecules, such as steroids, bilirubin, hormones, and drugs, into water-soluble, excretable metabolites.
This gene is part of a complex locus that encodes several UDP-glucuronosyltransferases. The locus includes thirteen unique alternate first exons followed by four common exons. Four of the alternate first exons are considered pseudogenes. Each of the remaining nine 5' exons may be spliced to the four common exons, resulting in nine proteins with different N-termini and identical C-termini. Each first exon encodes the substrate binding site, and is regulated by its own promoter. The enzyme encoded by this gene is active on phenolic and planar compounds. Alternative splicing in the unique 5' end of this gene results in two transcript variants.
UDP-glucuronosyltransferase is also responsible for the inactivation of popular analgesic drugs, such as aspirin and acetaminophen, by glucuronidation. The loss of a functional UGT1A6 gene in certain hypercarnivores, and particularly cats, renders the animals extremely sensitive to the adverse effects of these analgesics.
UGT1A9
UDP-glucuronosyltransferase 1-9 is an enzyme that in humans is encoded by the UGT1A9 gene.

# Function
This gene encodes a UDP-glucuronosyltransferase, an enzyme of the glucuronidation pathway that transforms small lipophilic molecules, such as steroids, bilirubin, hormones, and drugs, into water-soluble, excretable metabolites. This gene is part of a complex locus that encodes several UDP-glucuronosyltransferases. The locus includes thirteen unique alternate first exons followed by four common exons. Four of the alternate first exons are considered pseudogenes. Each of the remaining nine 5 exons may be spliced to the four common exons, resulting in nine proteins with different N-termini and identical C-termini. Each first exon encodes the substrate binding site, and is regulated by its own promoter.  The enzyme encoded by this gene is active on phenols.

# Interactive pathway map
Click on genes, proteins and metabolites below to link to respective articles. 
-  The interactive pathway map can be edited at WikiPathways: "IrinotecanPathway_WP46359"..mw-parser-output cite.citation{font-style:inherit}.mw-parser-output q{quotes:"\"""\"""'""'"}.mw-parser-output code.cs1-code{color:inherit;background:inherit;border:inherit;padding:inherit}.mw-parser-output .cs1-lock-free a{background:url("")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-limited a,.mw-parser-output .cs1-lock-registration a{background:url("")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-subscription a{background:url("")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration{color:#555}.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration span{border-bottom:1px dotted;cursor:help}.mw-parser-output .cs1-hidden-error{display:none;font-size:100%}.mw-parser-output .cs1-visible-error{display:none;font-size:100%}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-format{font-size:95%}.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-wl-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right,.mw-parser-output .cs1-kern-wl-right{padding-right:0.2em}
UGT2B4
UDP glucuronosyltransferase 2 family, polypeptide B4, also known as UGT2B4, is an enzyme that in humans is encoded by the UGT2B4 gene.

# Function
UGT2B4 is mainly involved in the glucuronidation of hyodeoxycholic acid, a bile acid, and catechol-estrogens, such as 17-epiestriol and 4-hydroxy-estrone.
The expression of the UGT2B4 enzyme is upregulated by the farnesoid X receptor (FXR), a nuclear receptor which is activated by bile acids.  These same bile acids are substrates for the UGT2B4 enzyme.  Hence upregulation of UGT2B4 by activated FXR provides a mechanism for the detection, conjugation and subsequent elimination of toxic bile acids.
UNC13A
Unc-13 homolog A (C. elegans) is a protein that in humans is encoded by the UNC13A gene.

# Function
This gene encodes a member of the UNC13 family. UNC13A plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. It is involved in neurotransmitter release by acting in synaptic vesicle priming prior to vesicle fusion and participates in the activity-dependent refilling of readily releasable vesicle pool. In Drosophila melanogaster, the protein has been shown to define the vesicle release site by regulating the coupling distance between synaptic vesicles and calcium channels in cooperation with another isoform, UNC13B. It is particularly important in most glutamatergic-mediated synapses but not GABA-mediated synapses. It plays a role in dendrite formation by melanocytes and in secretory granule priming in insulin secretion.

# Protein structure
Several conserved domains have been found in UNC13A. These conserved domains include three C2 domains. One C2 domain is centrally located, another is at the carboxyl end, and there is a third. In addition, there is one C1 domain, as well as Munc13 homology domains 1 (MHD1) and 2 (MHD2).

# Subcellular location
UNC13A is localized to the active zone of presynaptic density. It is translocated to the plasma membrane in response to phorbol ester binding.

# Interaction
UNC13A has been shown to interact with:
- STX1A,
- STX1B1,
- DOC2A,
- BSN,
- RIMS1,
- RIMS2,
- ERC2, and
- RAB3A.

# Clinical significance
Single nucleotide polymorphisms in this gene may be associated with sporadic amyotrophic lateral sclerosis. This single nucleotide polymorphism has been discovered on chromosome 19. This variation of the single nucleotide involving UNC13A has also been implicated in frontotemporal dementia (FTD). Pathology involving TDP-43 is a result of the single nucleotide polymorphisms in both ALS and FTD. This gene has also been associated with Alzheimer's Disease (AD).
UNC13D
Protein unc-13 homolog D, also known as munc13-4, is a protein that in humans is encoded by the UNC13D gene.

# Function
Munc13-4 is a member of the UNC13 family, containing similar domain structure as other family members but lacking an N-terminal phorbol ester-binding C1 domain present in other Munc13 proteins. The protein appears to play a role in vesicle maturation during exocytosis and is involved in regulation of cytolytic granules secretion.
Munc13-4 is an essential protein in the intracellular trafficking and exocytosis of lytic granules. It is targeted to CD63 positive secretory lysosomes. The C-terminal C2 domain of the protein is involved in this process.

# Clinical significance
Mutations in the UNC13D gene are associated with hemophagocytic lymphohistiocytosis type 3.
UNC93A
Unc-93 homolog A (C. elegans) is a protein that in humans is encoded by the UNC93A gene.
Unc93A is a major facilitator superfamily (MFS), and a putative solute carrier in humans. It belongs to the atypical SLCs that was recently listed. It is therefore presumed that UNC93A is a transporter protein.
UNC93A is closely related to Unc93B1 and MFSD11.
UNC93A is affected by amino acid deprivation in cell cortex cultures and starvation in in vivo samples.
It is expressed in neurons, with staining close to the plasma membrane.
Read also  for functional studies in C.elegans.
UQCR11
UQCR11 (ubiquinol-cytochrome c reductase, complex III sub-unit XI) is a protein that in humans is encoded by the UQCR11 gene. UQCR11 is the smallest known component of Complex III in the mitochondrial respiratory chain.

# Structure
The UQCR11 gene, located on the p arm of chromosome 19 in position 13.3, is made up of 3 exons and is 8,329 base pairs in length. The UQCR11 protein weighs 6.6 kDa and is composed of 56 amino acids. This gene encodes the smallest known component of the ubiquinol-cytochrome c reductase complex, which is also known as Complex III and is part of the mitochondrial respiratory chain. In vertebrates, Complex III contains 11 sub-units: 3 respiratory sub-units, 2 core proteins and 6 low-molecular weight proteins. Proteobacterial complexes may contain as few as three sub-units.

# Function
The UQCR11 protein may function as a binding factor for the iron-sulfur protein in Complex III, which is ubiquitous in human cells. Complex III catalyzes the chemical reaction
Thus, the two substrates of Complex III are dihydroquinone (QH2) and ferri- (Fe3+) cytochrome c, whereas its 3 products are quinone (Q), ferro- (Fe2+) cytochrome c, and H+. This complex belongs to the family of oxidoreductases, specifically those acting on diphenols and related substances as donor with a cytochrome as acceptor.  This enzyme participates in oxidative phosphorylation.  It has four cofactors: cytochrome c1, cytochrome b-562, cytochrome b-566 and a 2-Iron ferredoxin of the Rieske type.
UQCRC2
Cytochrome b-c1 complex subunit 2, mitochondrial (UQCRC2), also known as QCR2, UQCR2, or MC3DN5 is a protein that in humans is encoded by the UQCRC2 gene. The product of UQCRC2 is a subunit of the respiratory chain protein Ubiquinol Cytochrome c Reductase (UQCR, Complex III or Cytochrome bc1 complex), which consists of the products of one mitochondrially encoded gene, MTCYTB (mitochondrial cytochrome b) and ten nuclear genes: UQCRC1, UQCRC2, Cytochrome c1, UQCRFS1 (Rieske protein), UQCRB, "11kDa protein", UQCRH (cyt c1 Hinge protein), Rieske Protein presequence, "cyt. c1 associated protein", and "Rieske-associated protein." Defects in UQCRC2 are associated with mitochondrial complex III deficiency, nuclear, type 5.

# Structure
UQCRC2 is located on the p arm of chromosome 16 in position 12.2 and has 14 exons. The UQCRC2 gene produces a 48.4 kDa protein composed of 453 amino acids. UQCRC2 belongs to the peptidase M16 family and UQCRC2/QCR2 subfamily. UQCRC2 has a transit peptide domain. Ubiquinol Cytochrome c Reductase (b-c1 complex) contains 11 subunits: 3 respiratory subunits (cytochrome b, cytochrome c1 and Rieske/UQCRFS1), 2 core proteins (UQCRC1/QCR1 and UQCRC2/QCR2) and 6 low-molecular weight proteins (UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8, UQCR10/QCR9, UQCR11/QCR10 and a cleavage product of Rieske/UQCRFS1). UQCRC2 is part of the hydrophobic core of the b-c1 complex and is necessary for the stabilization of Ubiquinol Cytochrome c Reductase.

# Function
The protein encoded by this gene is located in the mitochondrion, where it is part of the ubiquinol-cytochrome c reductase complex (also known as complex III). This complex constitutes a part of the mitochondrial respiratory chain. The core protein UQCRC2 is required for the assembly and stabilization of the complex.

# Clinical Significance
Variants of UQCRC2 have been associated with mitochondrial complex III deficiency, nuclear, type 5. Mitochondrial complex III deficiency nuclear type 5 is a disorder of the mitochondrial respiratory chain resulting in a highly variable phenotype depending on which tissues are affected. Clinical features include mitochondrial encephalopathy, psychomotor retardation, ataxia, severe failure to thrive, liver dysfunction, renal tubulopathy, muscle weakness, exercise intolerance, lactic acidosis and hypoglycemia. Homozygous mutations resulting in a change from Arginine to Tryptophan at position 183 have been associated with mitochondrial complex III deficiency due to UQCRC2 dysfunction. Autosomal recessive inheritance has been proposed as a transmission pattern.

# Interactions
UQCRC2 has 98 protein-protein interactions with 90 of them being co-complex interactions. CAC1A, QCR1, UQCRC1, CACNA1A, STOM, a8k1f4, HLA-B, ARF6, and Mapk3 have been found to interact with UQCRC2.
Upjohn
The Upjohn Company was a pharmaceutical manufacturing firm founded in 1886 in Kalamazoo, Michigan by Dr. William E. Upjohn, an 1875 graduate of the University of Michigan medical school.  The company was originally formed to make friable pills, which were specifically designed to be easily digested.
In 1995, Upjohn merged with Pharmacia AB, to form Pharmacia & Upjohn.  Today, through a series of mergers, the remainder of Upjohn is owned by Pfizer.

# Chemistry
In chemical research, the company is best known for the development of the Upjohn dihydroxylation by V. VanRheenen, R. C. Kelly and D. Y. Cha in 1976.
Upjohn research is best known for the process that made possible large scale production of cortisone. The oxygen atom at the 11 position in this steroid is an absolute requirement for biological activity. There are however no known natural sources for starting materials that contain that feature. The only method for preparing this drug prior to 1952 was a lengthy synthesis starting from cholic acid isolated from bile. In 1952 two Upjohn biochemists, Dury Peterson and Herb Murray announced that they were able to introduce this crucial oxygen atom by fermentation of the steroid progesterone with the mold Aspergillus nigercans Over the next several years a group of chemists headed by John Hogg developed a process for preparing cortisone from the soybean steroid stigmasterol. The microbiological oxygenation is a key step in this process.
Upjohn is also well known for manufacturing Xanax.
Uranyl
The uranyl ion is the dipositive cation 2+, which forms salts with acids. In this ion, uranium is in its +6 oxidation state. The other common oxidation state of uranium is uranium(IV), called uranous. The uranyl ion is the most common species encountered in the aqueous chemistry of uranium.  Solid uranyl compounds are often colored red, yellow, orange or green. Like all uranium compounds, uranyl compounds are toxic. The toxicity of soluble uranyl salts is higher due to their faster incorporation into tissues.

# Examples
Examples of uranyl compounds include:
- Uranium trioxide, UO3
- Uranyl acetate, UO2(C2H3O2)2
- Uranyl ammonium carbonate, UO2CO32(NH4)2CO3
- Uranyl carbonate, UO2CO3
- Uranyl chloride, UO2Cl2
- Uranyl hydroxide, UO2(OH)2 or (UO2)2(OH)2 also in aqueous
- Uranyl nitrate, UO2(NO3)2
- Uranyl sulfate, UO2SO4
- Uranyl zinc acetate, ZnUO2(CH3COO)4

# Minerals
Such minerals occur in oxidised portions of uranium ore deposits. Common uranyl minerals include tyuyamunite (Ca(UO2)2V2O88H2O), autunite (Ca(UO2)2(PO4)28-12H2O), torbernite (Cu(UO2)2 (PO4)8-12H2O) and uranophane (H3O)2Ca (UO2)2(SiO4)3H2O) (Hutchinson and Blackwell, 1984).
Uranyl minerals, which contain uranium(VI) can help show the genesis of uranium deposits and the water-rock interactions that occur in uranium-rich mineral seams.

# Chemistry
Uranium chemistry has traditionally revolved around the aqueous chemistry of the uranyl ion, and related molecular species. One important use of this chemistry is for preparation of uranium dioxide ceramic pellets that are used as the fuel in light water nuclear reactors. Often the fuel materials start to break down chemically before the uranium is completely spent, and this too is an active area of investigation, as many of the corrosion products are of the uranyl group.

# Structure
The geometry of the uranyl ion has been the subject of much debate.  The close approach of two oxygen atoms to uranium, with each linear O-U-O bond from 1.7 to 1.9 A, prevents the close approach of a third or more.  d-p and f-p bonding have been suggested to explain the short U-O bonds.

# Health and environmental issues
Uranyl nitrate is an oxidizing and highly toxic compound and should not be ingested; it causes severe renal insufficiency and acute tubular necrosis and is a lymphocyte mitogen.
Target organs include the kidneys, liver, lungs and brain. 
Uranyl ion accumulation in tissues including gonocytes produces congenital disorders, and in white blood cells causes immune system damage. Uranyl compounds are also neurotoxins.

# Combustion of uranium
Aerial oxidation of any uranium compound eventually results in the formation of a uranyl compound. Uranyl ion contamination has been found on and around depleted uranium targets.
Ureter
Steven C. Campbell, M.D., Ph.D.

# Overview
In human anatomy, the ureters are the ducts that carry urine from the kidneys to the urinary bladder, passing anterior to the psoas major. The ureters are muscular tubes that can propel urine along by the motions of peristalsis. In the adult, the ureters are usually 25-30cm long.
In humans, the ureters enter the bladder through the back, running within the wall of the bladder for a few centimetres. There are no valves in the ureters, backflow being prevented by pressure from the filling of the bladder, as well as the tone of the muscle in the bladder wall.
In the female, the ureters pass through the mesometrium on the way to the urinary bladder.

# Histology
The ureter has a diameter of about 3 millimeters, and the lumen is star-shaped. Like the bladder, it is lined with transitional epithelium, and contains layers of smooth muscle.
The epithelial cells of the ureter are stratified (in many layers), are normally round in shape but become squamous (flat) when stretched. The lamina propria is thick and elastic (as it is important that it is impermeable).
There are two spiral layers of smooth muscle in the ureter wall, an inner loose spiral, and an outer tight spiral. The inner loose spiral is sometimes described as longitudinal, and the outer as circular, (this is the opposite to the situation in the gastrointestinal tract).  The distal third of the ureter contains another layer of outer longitudinal muscle.
The adventitia of the ureter, like elsewhere is composed of fibrous connective tissue, that binds it to adjacent tissues.

# Diseases and disorders
Medical problems that can affect the ureter include:
- Cancer of the ureter
- Passage of kidney stones
- Ureterocele
- Megaureter
- Vesico-ureteric reflux
- Anatomical abnormalities, such as duplexing and ectopia
VEGFR1
Vascular endothelial growth factor receptor 1 is a protein that in humans is encoded by the FLT1 gene.

# Function
Oncogene FLT belongs to the src gene family and is related to oncogene ROS (MIM 165020). Like other members of this family, it shows tyrosine protein kinase activity that is important for the control of cell proliferation and differentiation. The sequence structure of the FLT gene resembles that of the FMS gene (MIM 164770); hence, Yoshida et al. (1987) proposed the name FLT as an acronym for FMS-like tyrosine kinase.
The ablation of VEGFR1 by chemical and genetic means has also recently been found to augment the conversion of white adipose tissue to brown adipose tissue as well as increase brown adipose angiogenesis in mice.
Functional genetic variation in FLT1 (rs9582036) has been found to affect non-small cell lung cancer survival.

# Interactions
FLT1 has been shown to interact with PLCG1 and vascular endothelial growth factor B (VEGF-B).
VPS13A
Vacuolar protein sorting-associated protein 13A is a protein that in humans is encoded by the VPS13A gene.

# Function
The protein encoded by this gene may control steps in the cycling of proteins through the trans-Golgi network to endosomes, lysosomes and the plasma membrane. Mutations in this gene cause the autosomal recessive disorder, chorea acanthocytosis. Alternative splicing of this gene results in multiple transcript variants.

# Model organisms
Model organisms have been used in the study of VPS13A function. A conditional knockout mouse line called Vps13atm1b(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