Persius/hicric huggingface dataset:
Vomer
The vomer (from Latin vomer, -eris, "ploughshare") is one of the unpaired facial bones of the skull.  It is located in the midsagittal line, and touches the sphenoid, the ethmoid, the left and right palatine bones, and the left and right maxillary bones.

# Vomeronasal organ
The vomeronasal organ, also called Jacobson's organ, is a chemoreceptor organ named for its closeness to the vomer and nasal bones, and is particularly developed in animals such as cats (who adopt a characteristic pose called  the Flehmen reaction or flehming when making use of it), and is thought to have to do with the perception of certain pheromones.

# Anatomical details
The vomer is situated in the median plane, but its anterior portion is frequently bent to one or other side.
It is thin, somewhat quadrilateral in shape, and forms the hinder and lower part of the nasal septum; it has two surfaces and four borders.
The surfaces are marked by small furrows for blood vessels, and on each is the nasopalatine groove, which runs obliquely downward and forward, and lodges the nasopalatine nerve and vessels.
The superior border, the thickest, presents a deep furrow, bounded on either side by a horizontal projecting ala of bone; the furrow receives the rostrum of the sphenoid, while the margins of the al articulate with the vaginal processes of the medial pterygoid plates of the sphenoid behind, and with the sphenoidal processes of the palatine bones in front.
The inferior border articulates with the crest formed by the maxill and palatine bones.
The anterior border is the longest and slopes downward and forward. Its upper half is fused with the perpendicular plate of the ethmoid; its lower half is grooved for the inferior margin of the septal cartilage of the nose.
The posterior border is free, concave, and separates the choanae. It is thick and bifid above, thin below.

# Articulations
The vomer articulates with six bones:
- two of the cranium, the sphenoid and ethmoid.
- four of the face, the two maxillae; and the two palatine bones.
It also articulates with the septal cartilage of the nose.

# Trivia
By alternately thrusting with the tongue against the roof of the mouth and pressing with one of the fingers between the two eyebrows, one can articulate the vomer bone. This process, repeated for about 20 seconds, will cause the sinuses to discharge, thus rapidly clearing a stuffy head without the use of drugs.

# Additional images
- Median wall of left nasal cavity showing vomer in situ.
- The vomer.
- Base of skull. Inferior surface.
- The skull from the front.
- Sagittal section of skull.
WASF1
Wiskott-Aldrich syndrome protein family member 1, also known as WASP-family verprolin homologous protein 1 (WAVE1), is a protein that in humans is encoded by the WASF1 gene.

# Function
The protein encoded by this gene, a member of the Wiskott-Aldrich syndrome protein (WASP) family, plays a critical role downstream of Rac, a Rho-family small GTPase, through its involvement in the WAVE regulatory complex in regulating the actin cytoskeleton required for membrane ruffling. It has been shown to associate with an actin nucleation core Arp2/3 complex while enhancing actin polymerization in vitro.

# Clinical significance
Wiskott-Aldrich syndrome is a disease of the immune system, likely due to defects in regulation of actin cytoskeleton.

# Interactions
WASF1 has been shown to interact with BAIAP2 and Profilin 1.
WBP11

# Alternative names
- WW domain binding protein 11 (WBP11)
- Npw38-binding protein (NpwBP)
- Splicing factor that Interacts with PQBP-1 and PP1 (SIPP1)
- SH3 domain binding Protein, 70 kDa (SNP70)

# Function
Studies suggest that Wbp11 plays a role in DNA/ RNA transcriptional or post-transcriptional events related to cell division.  Wbp11 is found in the nucleus but not the nucleoli of cells in interphase.  However it is distributed throughout the cytoplasm in dividing cells.  Immunoelectron-microscopy experiments suggest that relocation from a peri-nuclear to a cytoplasmic distribution, coinciding with the onset of mitosis in cell division. Other studies have shown that Wbp11 is a component of the spliceosome.  Also, that Wbp11 fragments block pre-mRNA splicing catalysis.

# Protein interactions
Wbp11 is a polypeptide known to interact with other WW domain of proteins such as the nuclear protein Npw38 via two proline-rich regions. It associates with Npw38 (hence the name NpwBP) in the nuclei and with Poly(rG) and G-rich ssDNA. The 70kDa protein has also been found to interact with SH3 (Src homology domain 3) domains. The C-terminal proline-rich sequences of SNP70/NpwBP/Wbp11, which binds to the WW domain of Npw38 also fits with both classic type I and type II SH3 binding sequences, hence the name (SNP70).
Wbp11 was found to bind strongly to the tandem SH3 domains of p47phox and to the N-terminal SH3 domain of p47phox, and more weakly to the SH3 domains from c-src and p85. p47phox.
Furthermore, it has been shown to interact with PP1(protein phosphotase 1), hence the name SIPP1. It has an inhibitory effect to PP1, with its inhibitory potency increasing upon phosphorylation with protein kinase CK1. The binding of Wbp11 with PP1 involves a RVXF (Arg-Val-Xaa-Phe) motif, which functions as a PP1- binding sequence in most interactors of PP1.
A number of other interactions have been indicated such as:
- Vimentin 
- Growth factor receptor-bound protein 2 (GRB2) 
- Genome polyprotein 
- Tyrosine-protein kinase Fyn 
- Pre-mRNA-processing factor 39 (PRP39) 
- TNF receptor-associated factor 4 (TRAF4) 
- Calcineurin B homologous protein 3 (TESC) 
- Probable ATP-dependent RNA helicase DDX17 
- CD2 antigen cytoplasmic tail-binding protein 2 (CD2BP2) 
- Poly(rC)-binding protein 1 (PCBP1)
WDR45
WD repeat domain phosphoinositide-interacting protein 4 (WIPI-4) is a protein that in humans is encoded by the WDR45 gene. Mutations in this gene cause a distinct form of Neurodegeneration with brain iron accumulation (NBIA).

# Function
WIPI-4 is 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 gene WDR45 has a pseudogene at chromosome 4q31.3. Multiple alternatively spliced transcript variants encoding distinct isoforms have been found for this gene, but the biological validity and full-length nature of some variants have not been determined.

# Role in Disease
De novo loss of function mutations in WDR45 were identified by exome sequencing in 20 patients with NBIA. The mutations cause an X-linked dominant form of NBIA now called Beta-propeller protein-associated neurodegeneration (BPAN).
WDR47
WD repeat domain 47 is a protein that in humans is encoded by the WDR47 gene.

# Model organisms
Model organisms have been used in the study of WDR47 function. A conditional knockout mouse line, called Wdr47tm1a(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-six tests were carried out on mutant mice and three significant abnormalities were observed. Homozygous mutant animals had an absence of corpus callosum and increased circulating alkaline phosphatase levels. Male homozygous mice also had abnormal indirect calorimetry measures.
WDR62
WD repeat-containing protein 62 is a protein that in humans is encoded by the WDR62 gene.

# Clinical relevance
Mutations in the WDR62 gene cause of a wide spectrum of severe cerebral cortical malformations including microcephaly, pachygyria with cortical thickening, hypoplasia of the corpus callosum, polymicrogyria as well as microlissencephaly.
In 2018 Xu et al  showed that WDR62 stability and neurogenesis is regulated by  MEKK3 in coordination with FBW7 (F-box and WD repeat domain-containing protein 7).
WFDC2
WAP four-disulfide core domain protein 2 - also known as Human Epididymis Protein 4 (HE4) - is a protein that in humans is encoded by the WFDC2 gene.
HE4 is a tumor marker of ovarian cancer, with 80% sensitivity at a cut-off of 150 pmol/L.

# Function
This gene encodes a protein that is a member of the WFDC domain family. The WFDC domain, or WAP Signature motif, contains eight cysteines forming four disulfide bonds at the core of the protein, and functions as a protease inhibitor in many family members. This gene is expressed in pulmonary epithelial cells, and was also found to be expressed in some ovarian cancers. The encoded protein is a small secretory protein, which may be involved in sperm maturation.
WIPF1
WAS/WASL-interacting protein family member 1 (WIP) is a protein that in humans is encoded by the WIPF1 gene.

# Function
This gene encodes a protein that plays an important role in the organization of the actin cytoskeleton. Overexpression of WIP in mammalian cells has been shown to increase actin polymerization. The encoded protein binds to a region of Wiskott-Aldrich syndrome protein that is frequently mutated in Wiskott-Aldrich syndrome, an X-linked recessive disorder. Impairment of the interaction between these two proteins may contribute to the disease. Two transcript variants encoding the same protein have been identified for this gene. In patients lacking the WIPF1 gene WASp protein levels are depleted and WAS symptoms present.

# Interactions
WIPF1 has been shown to interact with Wiskott-Aldrich syndrome protein, Cortactin, NCK1, and ITSN1. While Wiskott-Aldrich syndrome protein is expressed only in haematopoetic cells, WIPF1 is expressed ubiquitously. Majority of the mutations causing Wiskott Aldrich Syndrome are located in the WH1 domain of WASp. These mutations affect WASp-WIPF1 binding. WIPF1 yeast homologue verprolin Vrp1 binds class 1 myosin and enhances class 1 myosin dependent actin nucleation.
WIPF1 has an N-terminal profilin binding domain, two actin binding WH2 domains, a central polyproline stretch, and a C-terminal WASP Binding Domain.
WIPI2
WD repeat domain phosphoinositide-interacting protein 2 is a protein that in humans is encoded by the WIPI2 gene.

# Function
WD40 repeat proteins are key components of many essential biologic functions. They regulate the assembly of multiprotein complexes by presenting a beta-propeller platform for simultaneous and reversible protein-protein interactions. Members of the WIPI subfamily of WD40 repeat proteins, such as WIPI2, have a 7-bladed propeller structure and contain a conserved motif for interaction with phospholipids.
WIPI2 is the mammalian homolog of Atg18, not Atg21, along with the closely related protein, WIPI1. WIPI2 mRNA is readily detectable in several commonly used laboratory cell lines (HEK293A, HeLa, A431) and several cancer cell lines, while WIPI1 expression is limited to cancer cells.
The Atg proteins regulate autophagy, which is a lysosomal degradation pathway required for maintaining cell health, surviving periods of nutrient deprivation and also plays a role in cancer, neurodegeneration and immune responses to a diverse range of pathogens. WIPI2 is recruited early to the forming autophagosome, along with DFCP-1, ULK-1 and Atg16, where it positively regulates the lipidation of Atg8 (LC3). This is not true for WIPI1.
WNT16
Protein Wnt-16 is a protein that in humans is encoded by the WNT16 gene. It has been proposed that stimulation of WNT16 expression in nearby normal cells is responsible for the development of chemotherapy-resistance in cancer cells.

# Function
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. It contains two transcript variants diverging at the 5' termini. These two variants are proposed to be the products of separate promoters and not to be splice variants from a single promoter. They are differentially expressed in normal tissues, one of which (variant 2) is expressed at significant levels only in the pancreas, whereas another one (variant 1) is expressed more ubiquitously with highest levels in adult kidney, placenta, brain, heart, and spleen.
WNT16B expression is regulated by nuclear factor of  light polypeptide gene enhancer in B cells 1 (NF-B) after DNA damage, as can occur to normal cells during radiation or chemotherapy. Subsequently WNT16B signals in a paracrine manner to activate the Wnt expression program in tumor cells. The expression of WNT16B in the tumor microenvironment attenuates the effects of cytotoxic chemotherapy in vivo, promoting tumor cell survival and disease progression. This implies a mechanism by which cycles of genotoxic therapy might enhance subsequent treatment resistance in the tumor microenvironment.

# Model organisms
Model organisms have been used in the study of WNT16 function. A conditional knockout mouse line called Wnt16tm2b(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
WWTR1
WW domain-containing transcription regulator protein 1 is a protein that in humans is encoded by the WWTR1 gene.

# Function
WWTR1 It is a transcriptional coactivator which acts as a downstream regulatory target in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein MST1/MST2, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/LATS2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. WWTR1 enhances PAX8 and NKX2-1/TTF1-dependent gene activation. Regulates the nuclear accumulation of SMADs and has a key role in coupling them to the transcriptional machinery such as the mediator complex.
Using the human SHSY5Y cell line as a model of neuronal differentiation, human FAT1 was shown to regulate the nucleocytoplasmic relocation of WWTR1/TAZ and enhanced transcription of the Hippo target gene CTGF. The same study also showed FAT1 was able to regulate TGF-beta signalling
WebMD
WebMD is a medical and wellness information service, primarily known for its public internet site, which provides health information, a symptom checklist, pharmacy information, a place to store personal medical information, and an online community with over 140 moderated expert-led and peer-to-peer message boards.  The site is reported to receive over 40 million hits each month  and is the leading health portal in the nation according to comScore Media Metrix.
WebMD also offers services to physicians and private clients.  For example, they publish WebMD the Magazine, a patient-directed publication distributed bimonthly to 85 percent of physician waiting rooms.. Medscape is a professional portal for physicians with 30 medical specialty areas and over 30 physician discussion boards.
WebMD owns several other medically-related internet sites including WebMD Health, Medscape, MedicineNet, eMedicine, eMedicine Health, RxList and theheart.org.
The organization is financed by third-party contributions and sponsorships.
XRCC2
DNA repair protein XRCC2 is a protein that in humans is encoded by the XRCC2 gene.

# Function
This gene encodes a member of the RecA/Rad51-related protein family that participates in homologous recombination to maintain chromosome stability and repair DNA damage. This gene is involved in the repair of DNA double-strand breaks by homologous recombination and it functionally complements Chinese hamster irs1, a repair-deficient mutant that exhibits hypersensitivity to a number of different DNA-damaging agents.
The XRCC2 protein is one of five human paralogs of RAD51, including RAD51B (RAD51L1), RAD51C (RAD51L2), RAD51D (RAD51L3), XRCC2 and XRCC3.  They each share about 25% amino acid sequence identity with RAD51 and each other.
The RAD51 paralogs are all required for efficient DNA double-strand break repair by homologous recombination and depletion of any paralog results in significant decreases in homologous recombination frequency.
XRCC2 forms a four-part complex with three related paralogs: BCDX2 (RAD51B-RAD51C-RAD51D-XRCC2) while two paralogs form a second complex CX3 (RAD51C-XRCC3). These two complexes act at two different stages of homologous recombinational DNA repair.  The BCDX2 complex is responsible for RAD51 recruitment or stabilization at damage sites.  The BCDX2 complex appears to act by facilitating the assembly or stability of the RAD51 nucleoprotein filament.
The CX3 complex acts downstream of RAD51 recruitment to damage sites.  The CX3 complex was shown to associate with Holliday junction resolvase activity, probably in a role of stabilizing gene conversion tracts.

# Interactions
XRCC2 has been shown to interact with RAD51L3, Bloom syndrome protein and RAD51C.

# Epigenetic deficiency in cancer
There are two known epigenetic causes of XRCC2 deficiency that appear to increase cancer risk.  These are methylation  of the XRCC2 promoter and epigenetic repression of XRCC2 by over-expression of EZH2 protein.
The XRCC2 gene was found to be hypermethylated in the promoter region in 52 of 54 cases of cervical cancer.  Promoter hypermethylation reduces gene expression, and thus would reduce the tumor suppressing homologous recombinational repair otherwise supported by XRCC2.
Increased expression of EZH2 leads to epigenetic repression of RAD51 paralogs, including XRCC2, and thus reduces homologous recombinational repair.  This reduction was proposed to be a cause of breast cancer.  EZH2 is the catalytic subunit of Polycomb Repressor Complex 2 (PRC2) which catalyzes methylation of histone H3 at lysine 27 (H3K27me) and mediates gene silencing of target genes via local chromatin reorganization.  EZH2 protein is up-regulated in numerous cancers.  EZH2 mRNA is up-regulated, on average, 7.5-fold in breast cancer, and between 40% to 75% of breast cancers have over-expressed EZH2 protein.
XYLT2
Xylosyltransferase 2 is an enzyme that in humans is encoded by the XYLT2 gene.

# Function
The protein encoded by this gene is an isoform of xylosyltransferase, which belongs to a family of glycosyltransferases. This enzyme transfers xylose from UDP-xylose to specific serine residues of the core protein and initiates the biosynthesis of glycosaminoglycan chains in proteoglycans including chondroitin sulfate, heparan sulfate, heparin and dermatan sulfate.

# Clinical significance
The enzyme activity, which is increased in scleroderma patients, is a diagnostic marker for the determination of sclerotic activity in systemic sclerosis.
Mutations in this gene have been shown to be the cause of the spondylo-ocular syndrome. It has also been implicated as  cofactor in pseudoxanthoma elasticum.
Xenin
Xenin is a peptide hormone produced by a subpopulation of chromogranin A-positive endocrine cells in the mucous membrane of the duodenum. The peptide has been found in humans, dogs, pigs, rats, and rabbits.
In humans, xenin circulates in the blood plasma. There is a relationship between peaks of xenin concentration in the plasma and the third phase of the Migrating Motor Complex. For example, infusion of synthetic xenin in fasting volunteers will cause phase III activity. After a meal (the 'postprandial state'), infusion of xenin increases both frequency and the percentage of aborally propagated contractions. In higher concentrations xenin stimulates exocrine pancreatic secretion and inhibits the gastrin-stimulated secretion of acid in dogs. Xenin is also produced in neuroendocrine tumors of the duodenal mucosa.
In vitro, xenin interacts with the neurotensin receptor 1.

# Structure and sequence
Xenin is a 25-amino acid polypeptide. The amino acid sequence of xenin is identical to the N-terminal end of cytoplasmic coatomer subunit alpha, from which xenin can be cleaved by aspartic proteases. Xenin is structurally related to the amphibian peptide xenopsin and to the neuropeptide neurotensin.

# Proxenin
Proxenin is the precursor to xenin. It is a 35-amino acid polypeptide. Like xenin, its amino acid sequence  exactly matches the N-terminus of coatomer subunit alpha.

# As a drug target
Xenin promotes beta-cell survival and xenin has been evaluated in animal models of obesity and diabetes where it has demonstrated an antidiabetic potential. In humans, co-administration of xenin-25 and gastric inhibitory polypeptide (GIP) reduces postprandial glycemia by delaying gastric emptying.
YIPF1
Protein YIPF1 is a protein that in humans is encoded by the YIPF1 gene.

# Model organisms
Model organisms have been used in the study of YIPF1 function. A conditional knockout mouse line, called Yipf1tm1a(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  at the Wellcome Trust Sanger Institute.
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Twenty three tests were carried out on mutant mice, however no significant abnormalities were observed.
YWHAG
14-3-3 protein gamma is a protein that in humans is encoded by the YWHAG gene.
This gene product belongs to the 14-3-3 protein family which mediate signal transduction by binding to phosphoserine-containing proteins. This highly conserved protein family is found in both plants and mammals, and this protein is 100% identical to the rat ortholog. It is induced by growth factors in human vascular smooth muscle cells, and is also highly expressed in skeletal and heart muscles, suggesting an important role for this protein in muscle tissue. It has been shown to interact with RAF1 and protein kinase C, proteins involved in various signal transduction pathways.

# Interactions
YWHAG has been shown to interact with C-Raf, EPB41L3, KIF1C and Stratifin.