Persius/hicric huggingface dataset:
USF2
Upstream stimulatory factor 2 is a protein that in humans is encoded by the USF2 gene.

# Function
This gene encodes a member of the basic helix-loop-helix leucine zipper family, and can function as a cellular transcription factor. The encoded protein can activate transcription through Pyridine-rich initiator (Inr) elements and E-box motifs. Two transcript variants encoding distinct isoforms have been identified for this gene.

# Interactions
USF2 has been shown to interact with USF1 (human gene), PPRC1 and BRCA1.

# Regulation
The USF2 gene is repressed by the microRNA miR-10a.
UTF1
Undifferentiated embryonic cell transcription factor 1 is a protein in humans that is encoded by the UTF1 gene.
 UTF1, first reported in 1998, is expressed in pluripotent cells including embryonic stem cells and embryonic carcinoma cells. Its expression is rapidly reduced upon differentiation. UTF1 protein is localized to the cell nucleus, where it functions to regulate the pluripotent chromatin state and buffer mRNA levels by promoting degradation of mRNA.
Aberrant expression of UTF1 has also been reported in cervical cancer cells, where the UTF1 gene promoter loses methylation and becomes abnormally expressed compared to normal cervical cells.
Ulna

# Overview
The ulna (elbow bone) is a long bone, prismatic in form, placed at the medial side of the forearm, parallel with the radius.

# Articulations
The ulna articulates with:
- the humerus, at the right side elbow as a hinge joint.
- the radius, near the elbow as a pivot joint, this allows the radius to cross over the ulna in pronation.
- the distal radius, where it fits into the ulna notch.
- the radius along its length via the interosseous membrane that forms a syndesmoses joint.

# Proximal and distal aspects
The ulna is broader proximally, and narrower distally.
Proximally, the ulna has a bony process, the olecranon process, a hook-like structure that fits into the olecranon fossa of the humerus. This prevents hyperextension and forms a hinge joint with the trochlea of the humerus.
There is also a radial notch for the head of the radius, and the ulnar tuberosity to which muscles can attach.
Distally (near the hand), there is a styloid process.

# Structure
The long, narrow medullary cavity is enclosed in a strong wall of compact tissue which is thickest along the interosseous border and dorsal surface.
At the extremities the compact layer thins.
The compact layer is continued onto the back of the olecranon as a plate of close spongy bone with lamell parallel.
From the inner surface of this plate and the compact layer below it trabecul arch forward toward the olecranon and coronoid and cross other trabecul, passing backward over the medullary cavity from the upper part of the shaft below the coronoid.
Below the coronoid process there is a small area of compact bone from which trabecul curve upward to end obliquely to the surface of the semilunar notch which is coated with a thin layer of compact bone.
The trabecul at the lower end have a more longitudinal direction.
VAPB
Vesicle-associated membrane protein-associated protein B/C is a protein that in humans is encoded by the VAPB gene.  The VAPB gene is found on the 20th human chromosome. Together with VAPA, it forms the VAP protein family.

# Function
The protein encoded by this gene is a type IV membrane protein found in plasma and intracellular vesicle membranes. The encoded protein is found as a homodimer and as a heterodimer with VAPA. This protein also can interact with VAMP1 and VAMP2 and may be involved in vesicle trafficking.
Like VAPA, VAPB binds to proteins that contain a FFAT motif. Considerable interest in VAPB has arisen because mutations in this protein are associated with rare, familial forms of Motor Neurone Disease (also called Amyotrophic Lateral Sclerosis and Lou Gehrig's disease).
VAT1
Synaptic vesicle membrane protein VAT-1 homolog is a protein that in humans is encoded by the VAT1 gene.
Synaptic vesicles are responsible for regulating the storage and release of neurotransmitters in the nerve terminal. The protein encoded by this gene is an abundant integral membrane protein of cholinergic synaptic vesicles and is thought to be involved in vesicular transport. It belongs to the quinone oxidoreductase subfamily of zinc-containing alcohol dehydrogenase proteins.
In melanocytic cells VAT1 gene expression may be regulated by MITF.
VAX1
Ventral anterior homeobox 1 is a protein that in humans is encoded by the VAX1 gene.

# Function
This gene appears to influence the development in humans of the forebrain. It is also present in mice and xenopus frogs, which suggests a long evolutionary history, and in those organisms its expression is confined to the forebrain, optic and olfactory areas.
VAX1 gene is a transcription factor that has a homeodomain located in the 100-159 amino acid position and an Alarich region located in 216-253 amino acid position of the gene. Expression studies in mice show that it is expressed in the palate, coloboma in the visual system, and the basal telencephalon, optic stalk, and visual eye fields where it is expressed along with the Shh and Bmp4 genes.

# Clinical significance
Mice with homozygous VAX1 mutations have been reported to display craniofacial malformations including cleft palate.
Genome Wide Association Studies (GWAS) reported significant associations between non-syndromic clefts and SNPs in the VAX1 gene. Replication studies have confirmed these associations in different population groups
VWA2
von Willebrand factor A domain-containing protein 2, also known as A domain-containing protein similar to matrilin and collagen (AMACO) is a protein that in humans is encoded by the VWA2 gene.
AMACO is a member of the von Willebrand factor A-like (VWA) domain containing protein superfamily and consists of three VWA-like domains, two EGF-like domains, a cysteine-rich domain and a unique C-terminal domain.
AMACO is an extracellular matrix protein and mostly deposited adjacent to basement membranes.
AMACO binds directly to FRAS1 which is part of the Fraser complex important for epithelial-connective tissue interaction, the exact biological role of AMACO, however,  is still unknown. In 2005 AMACO was found markedly induced in colon cancers ; indicating that it might be a good candidate as a biomarker for this type of cancer.
WBP2
WW domain-binding protein 2 is a protein that in humans is encoded by the WBP2 gene.
The globular WW domain is composed of 38 to 40 semiconserved amino acids shared by proteins of diverse functions including structural, regulatory, and signaling proteins. The domain is involved in mediating protein-protein interactions through the binding of polyproline ligands. This gene encodes a WW domain binding protein, which binds to the WW domain of Yes kinase-associated protein by its PY motifs. The function of this protein has not been determined.

# Model organisms
Model organisms have been used in the study of WBP2 function. A conditional knockout mouse line, called Wbp2tm1a(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 three tests were carried out on mutant mice and two significant abnormalities were observed. Homozygous mutant animals displayed an abnormal brainstem auditory evoked potential, while females also had decreased circulating amylase levels.
WDR3
WD repeat-containing protein 3 is a protein that in humans is encoded by the WDR3 gene.
This gene encodes a nuclear protein containing 10 WD repeats. WD repeats are approximately 30- to 40-amino acid domains containing several conserved residues, which usually include a trp-asp at the C-terminal end. Proteins belonging to the WD repeat family are involved in a variety of cellular processes, including cell cycle progression, signal transduction, apoptosis, and gene regulation.

# Model organisms
Model organisms have been used in the study of WDR3 function. A conditional knockout mouse line, called Wdr3tm1a(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 four tests were carried out on mutant mice and two significant abnormalities were observed. No homozygous mutant embryos were identified during gestation, and therefore none survived until weaning. The remaining tests were carried out on heterozygous mutant adult mice; no additional significant abnormalities were observed in these animals.
WDR5
WD repeat-containing protein 5 is a protein that in humans is encoded by the WDR5 gene.
This gene encodes a member of the WD repeat protein family. WD repeats are minimally conserved regions of approximately 40 amino acids typically bracketed by gly-his and trp-asp (GH-WD), which may facilitate formation of heterotrimeric or multiprotein complexes. Members of this family are involved in a variety of cellular processes, including cell cycle progression, signal transduction, apoptosis, and gene regulation. This protein contains 7 WD repeats. Alternatively spliced transcript variants encoding the same protein have been identified.

# Interactions
WDR5 has been shown to interact with Host cell factor C1 and MLL. It also interacts with the long non-coding RNA HOTTIP.
WDR5 is a key determinant for MYC recruitment to chromatin
WFS1
Wolframin is a protein that in humans is encoded by the WFS1 gene.

# Function
Wolframin is a transmembrane protein. Wolframin appears to function as a cation-selective ion channel.

# Clinical significance
Mutations in this gene are associated with an autosomal recessive syndrome characterized by insulin-dependent diabetes mellitus and bilateral progressive optic atrophy, usually presenting in childhood or early adult life. Diverse neurologic symptoms, including a predisposition to psychiatric illness, may also be associated with this disorder. A large number and variety of mutations in this gene, particularly in exon 8, can be associated with this syndrome. Mutations in this gene can also cause autosomal dominant deafness 6 (DFNA6), also known as DFNA14 or DFNA38.
Mutations in this gene have also been associated with congenital cataracts.
WNK4
Serine/threonine-protein kinase WNK4 also known as WNK lysine deficient protein kinase 4 or WNK4, is an enzyme that in humans is encoded by the WNK4 gene.. Missense mutations cause a genetic form of pseudohypoaldosteronism type 2, also called Gordon syndrome.

# Function
The WNK4 gene encodes a serine-threonine kinase expressed in distal nephron. Its primary role in renal physiology is as a molecular switch between the angiotensin IIaldosterone mediated volume retention and the aldosterone mediated potassium wasting. This is achieved by regulating the sodium-chloride symporter (NCC), that is uniquely expressed in the distal nephron and is sensitive to thiazide type diuretics.
Under basal conditions (low circulating Ang II and low Aldosterone), WNK4 will inhibit NCC function. It has been proposed that in the event of hyperkalemia and an increased secretion of aldosterone (which will upregulate both ENac and ROMK), this inhibition of NCC, will allow an increase in the arrival of sodium to the distal nephron (rich in ENaC and ROMK) which will allow the exchange of sodium for potassium ions, thereby reducing plasma potassium levels, without increasing sodium chloride retention (which is always accompanied by volume expansion). Furthermore, it has been proposed that in the presence of AngII the WNK4 mediated NCC inhibition will be suppressed thereby increasing sodium-chloride reabsorption in the distal convoluted tubule. This along with the concomitant increase in passive water reabsortion due to the increased salt load in the distal convluted tubule cells will ultimately increase circulating volume.
WNT6
Wingless-type MMTV integration site family, member 6, also known as WNT6, is a human gene.
The WNT gene family consists of structurally related genes that encode secreted signaling proteins. These proteins have been implicated in oncogenesis and in several developmental processes, including regulation of cell fate and patterning during embryogenesis. This gene is a member of the WNT gene family, which are involved in the Wnt signaling pathway. It is overexpressed in cervical cancer cell line and strongly coexpressed with another family member, WNT10A, in colorectal cancer cell line. The gene overexpression may play key roles in carcinogenesis. This gene and the WNT10A gene are clustered in the chromosome 2q35 region. The protein encoded by this gene is 97% identical to the mouse Wnt6 protein at the amino acid level.
Role in Development
Wnt6 plays a role in the formation and maturation of different embryonic structures, namely the fetal heart, ventral body wall, and somite derived structures. Wnt6, through the canonical Wnt signaling pathway, inhibits the induction of cardiogenic mesoderm. For this reason, Wnt6 inhibitors like Cerberus must be present to allow the cells to be induced. Knockout models show that without Wnt6 the fetus develops an enlarged heart, while upregulating Wnt6 results in the heart being underdeveloped. Several Wnts, including Wnt6, have shown to be involved in the formation of the ventral body wall and when inhibited result in birth defects such as failure of the wall to close, hypoplasia of the musculature, and other defects.  Following the formation of the somites from the Paraxial Mesoderm, the outermost cells of the somites undergo a mesenchymal to epithelial transition. Wnt6 is expressed by the overlying ectoderm and promotes the production of Paraxis, which facilitates the transition. While many structures will still form if Wnt6 is knocked out, the structures (ribs, vertebra, and muscles) are fused and not organized properly. On the other hand, if Wnt6 is upregulated, muscle in the limbs and surrounding areas are decreased as the mesenchymal progenitor cells that migrate and become the muscle are locked in the somite as epithelial cells.
WWC1
Protein KIBRA also known as kidney and brain expressed protein (KIBRA) or WW domain-containing protein 1 (WWC1) is a protein that in humans is encoded by the WWC1 gene.

# Research on human memory
A single nucleotide polymorphism  (rs17070145)  in the gene has been associated with human memory performance in one 2006 study. While no significant support for KIBRA's association with memory was found in a 2008 study with 584 subjects, the original 2006 study was replicated in a smaller sample of an elderly population in 2008.  A subsequent study in 2009 in two large UK samples indicated that KIBRA is specifically associated with forgetting of non-semantic material.
Studies have also begun to investigate the role of KIBRA in Alzheimer's disease.

# Interactions
KIBRA has at least 10 interaction partners, including synaptopodin, PKC and  Dendrin, most of which modify synaptic plasticity.
For instance, Dendrin is  a post-synaptic protein with expression regulated by sleep deprivation.
KIBRA has been shown to interact with Protein kinase M.
WWOX
WW domain-containing oxidoreductase is an enzyme that in humans is encoded by the WWOX gene.

# Function
WW domain-containing proteins are found in all eukaryotes and play an important role in the regulation of a wide variety of cellular functions such as protein degradation, transcription, and RNA splicing. This gene encodes a protein which contains 2 WW domains and a short-chain dehydrogenase/reductase domain (SRD). The highest normal expression of this gene is detected in hormonally regulated tissues such as testis, ovary, and prostate. This expression pattern and the presence of an SRD domain suggest a role for this gene in steroid metabolism. The encoded protein is more than 90% identical to the mouse protein, which is an essential mediator of tumor necrosis factor-alpha-induced apoptosis, suggesting a similar, important role in apoptosis for the human protein. In addition, there is evidence that this gene behaves as a suppressor of tumor growth. Alternative splicing of this gene generates transcript variants that encode different isoforms.
WWOX is also known as human accelerated region 6.  It may, therefore, have played a key role in differentiating humans from apes.

# Interactions
WWOX has been shown to interact with P53 and ACK1.
WWP2
NEDD4-like E3 ubiquitin-protein ligase WWP2 also known as atrophin-1-interacting protein 2 (AIP2) or WW domain-containing protein 2 (WWP2) is an enzyme that in humans is encoded by the WWP2 gene.

# Function
This gene encodes a member of the NEDD4-like protein family. The family of proteins is known to possess ubiquitin-protein ligase activity. The encoded protein contains 4 tandem WW domains. The WW domain is a protein motif consisting of 35 to 40 amino acids and is characterized by 4 conserved aromatic residues. The WW domain may mediate specific proteinprotein interactions. Three alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.

# Interactions
WWP2 has been shown to interact with SCNN1B and ATN1.

# Clinical significance
Full-length WWP2 (WWP2-FL), together with N-terminal, (WWP2-N); C-terminal (WWP2-C) isoforms bind to SMAD proteins.  WWP2-FL interacts with SMAD2, SMAD3 and SMAD7 in the TGF- pathway. The WWP2-N isoform interacts with SMAD2 and SMAD3, whereas WWP2-C interacts only with SMAD7. Disruption of interactions between WWP2 and SMAD7 can stabilize SMAD7 protein levels and prevent TGF- induced Epithelial-mesenchymal transition. Hence inhibiting WWP2 may in turn lead to the disabling of an inhibitor that normally controls cell growth and tumorogenesis. In tissue cultures lacking the inhibitor SMAD7, cancer cells spread rapidly, so that silencing WWP2 prevented the spread.
XCR1
The "C" sub-family of chemokine receptors contains only one member: XCR1, the receptor for XCL1 and XCL2 (or lymphotactin-1 and -2).
XCR1 is also known as GPR5.

# Function
The protein encoded by this gene is a chemokine receptor belonging to the G protein-coupled receptor superfamily. The family members are characterized by the presence of 7 transmembrane domains and numerous conserved amino acids. This receptor is most closely related to RBS11 and the MIP1-alpha/RANTES receptor. It transduces a signal by increasing the intracellular calcium ions level. The viral macrophage inflammatory protein-II is an antagonist of this receptor and blocks signaling. Two alternatively spliced transcript variants encoding the same protein have been found for this gene.
Cross-presenting dendritic cells (DCs) in the spleen develop into XCR1+ DCs in the small intestine, T cell zones of Peyers patches, and T cell zones and sinuses of mesenteric lymph nodes. XCR1+ DCs specialize in cross-presentations of orally applied antigens. The integrin SIRP is also a differentiating factor for the XCR1+ DCs. The development transcription factor Batf3 helps develop the differences between XCR1+ DCs and CD103+ CD11b- DCs.
XCL1 contributes to chemotaxis only in CD8+ murine cells, but not other DC types, B cells, T cells, or NK cells. Only some of these CD8+ murine cells expressed XCR1 receptors. NK cells release XCL1 along with IFN- and some other chemokines upon encountering certain bacteria such as Listeria or MCMV. XCR1+ and CD8+cells work together to cross-present antigen and communicate CD8+ activation. Cross presentation of XCR1+ CD8+ and XCR1+ CD8- cells was strongest, as is expected since they have XCR1 receptors. CD4+ and CD8+ may become outdated terms, since the activity of the cell appears to be primarily dependent upon the expression of XCR1, which will make a population far more similar than the expression of CD4 or CD8.
XCR1+ cells are dependent on the growth factor Ftl3 ligand and are nonexistent in Batf3- deficient mice. Also, XCR1+ DCs are related to CD103+CD11b- DCs.
XCL1 is expressed by medullary thymic epithelial T cells (mTECs) while XCR1 is expressed by thymic dendritic cells (tDCs). This communication helps with the destruction of cells that are not self-tolerant. When mice lose the ability to express XCL1, they are deficient in accumulation of tDCs and producing naturally occurring regulatory T cells (nT reg cells). The displaying of XCL1 by mTECs, tDC chemotaxis, and nT reg cell production are all decreased in mice that lack Aire, demonstrating it as a important regulator of XCL1 production.
Naive CD8+ T cells are prepared when tumors form by cross-presentation via XCR1+ DCs and as a result will require a lower threshold to respond to antigen. Memory CD8+ T lymphocytes (mCTLs) are activated first after infection and then are signaled by CXCR3, IL-12, and CXCL9 by other XCR1+ DCs. In order to make a powerful secondary infection response, cytokine and chemokine signaling between XCR1+ DCs and NK cells must occur.
XPO1
Exportin 1 (XPO1), also known as chromosomal maintenance 1 (CRM1), is an eukaryotic protein that mediates the nuclear export of proteins,  rRNA, snRNA, and some mRNA.

# History
XPO1 (CRM1) originally was identified in the fission yeast Schizosaccharomyces pombe in a genetic screen, and investigators determined that it was involved in control of the chromosome structure

# Function
Exportin 1 mediates leucine-rich nuclear export signal (NES)-dependent protein transport. Exportin 1 specifically mediates the nuclear export of Rev and U snRNAs. It is involved in the control of several cellular processes by controlling the localization of cyclin B, MAPK, and MAPKAP kinase 2. This protein also regulates NFAT and AP-1.

# Interactions
XPO1 has been shown to interact with:
- APC,
- CDKN1B,
- CIITA,
- NMD3,
- Nucleoporin 62,
- RANBP1,
- RANBP3,
- Ran,
- SMARCB1,  and
- p53.