Persius/hicric huggingface dataset:
PRRX1
Paired related homeobox 1 is a protein that in humans is encoded by the PRRX1 gene.

# Function
The DNA-associated protein encoded by this gene is a member of the paired family of homeobox proteins localized to the nucleus. The protein functions as a transcription coactivator, enhancing the DNA-binding activity of serum response factor, a protein required for the induction of genes by growth and differentiation factors. The protein regulates muscle creatine kinase, indicating a role in the establishment of diverse mesodermal muscle types. Alternative splicing yields two isoforms that differ in abundance and expression patterns.

# Role in mesenchymal stem cell differentiation
Prrx1 expression is restricted to the mesoderm during embryonic development, and both Prrx1 and Prrx2 are expressed in mesenchymal tissues in adult mice. Mice that lack both Prrx1 and Prrx2 have profound defects in mesenchymal cell differentiation in the craniofacial region. Several  recent studies demonstrate that PRRX1 can regulate differentiation of mesenchymal precursors. For example, PRRX1 inhibits adipogenesis by activating transforming growth factor-beta (TGF-beta) signaling, and also acts downstream of tumor necrosis factor-alpha to inhibit osteoblast differentiation.
PRSS8
Prostasin is a protein that in humans is encoded by the PRSS8 gene.
This gene encodes a trypsinogen, which is a member of the trypsin family of serine proteases. This enzyme is highly expressed in prostate epithelia and is one of several proteolytic enzymes found in seminal fluid. The proprotein is cleaved to produce a light chain and a heavy chain which are associated by a disulfide bond. It is active on peptide linkages involving the carboxyl group of lysine or arginine.
The protein is implicated in epithelial sodium channel regulation and may help regulate a variety of tissue functions that involve a sodium channel.
PSAT1
Phosphoserine aminotransferase (PSA) also known as phosphohydroxythreonine aminotransferase (PSAT) is an enzyme that in humans is encoded by the PSAT1 gene.
The protein encoded by this gene is likely a phosphoserine aminotransferase, based on similarity to proteins in mouse, rabbit, and Drosophila. Alternative splicing of this gene results in two transcript variants encoding different isoforms.

# Clinical significance
Homozygous or compound heterozygous mutations in PSAT1 cause Neu-Laxova syndrome and phosphoserine aminotransferase deficiency.

# Model organisms
Model organisms have been used in the study of PSAT1 function. A conditional knockout mouse line, called Psat1tm1a(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.
PSIP1
PC4 and SFRS1 interacting protein 1, also known as lens epithelium-derived growth factor (LEDGF/p75), dense fine speckles 70kD protein (DFS 70) or transcriptional coactivator p75/p52, is a protein that in humans is encoded by the PSIP1 gene.

# Function
PSIP1 has not been clearly linked to a specific cellular mechanism.  The term LEDGF/p75 (Lens epithelium-derived growth factor) has entered common usage based on the initial characterization of PSIP1, however this is a misnomer, as the protein is present in most tissues and has no direct role in the development of lens epithelium. LEDGF/p75, a transcription coactivator, gained prominence as a host factor that assists HIV integration and is probably the only integrase interactor whose knock-down severely affects the HIV integration levels. The interaction between HIV integrase and human LEDGF/p75 is a promising target for anti-HIV drug discovery. LEDGF/p75 recruits MLL complexes to HOX genes to regulate their expression. LEDGF/p52 is shown to recruit splicing factors to H3K36 trimethylated chromatin to modulate alternative splicing, also regulates HOTTIP lncRNA, which is shown to regulate HOX genes in cis.

# Structure
LEDGF/p75 is a 60kDa, 530-amino-acid-long protein.  The N-terminal portion of the protein consists of a PWWP domain, a nuclear localization sequence, and two copies of the AT-hook DNA binding motif.  The C-terminal portion of LEDGF/p75 contains a structure termed the integrase-binding domain, which interacts with lentiviral integrase proteins as well as numerous cellular proteins.  The N-terminal portion interacts strongly with chromatin, making LEDGF/p75 a constitutively nuclear protein.  An isoform of the protein, LEDGF/p52, is produced by alternative splicing.  LEDGF/p52 shares the N-terminal 325 amino acids of LEDGF/p75 but lacks the integrase-binding domain.

# Interactions
PSIP1 has been shown to interact with the proteins ASF/SF2, JPO2, Cdc7-Dbf4, and POGZ as well as the menin/MLL protein complex.
PTBP1
Polypyrimidine tract-binding protein 1 is a protein that in humans is encoded by the PTBP1 gene.
This gene belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA-binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport. While all of the hnRNPs are present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. The protein encoded by this gene has four repeats of quasi-RNA recognition motif (RRM) domains that bind RNAs. This protein binds to the intronic polypyrimidine tracts that requires pre-mRNA splicing and acts via the protein degradation ubiquitin-proteasome pathway. It may also promote the binding of U2 snRNP to pre-mRNAs. This protein is localized in the nucleoplasm and it is also detected in the perinucleolar structure. Alternatively spliced transcript variants encoding different isoforms have been described.

# PTBP1 In Mammals
In brains of mammals, transcripts from the PTBP1 gene are missing one exon (exon 9) that is included in the brains of other vertebrates, as a result of alternative splicing. This contributes to the evolutionary difference between the nervous system of mammals and other vertebrates.

# Interactions
PTBP1 has been shown to interact with HNRPK, PCBP2, SFPQ and HNRNPL.
This gene is targeted by the microRNA miR-124. During neuronal differentiation, miR-124 reduces PTBP1 levels, leading to the accumulation of correctly spliced PTBP2 mRNA and a dramatic increase in PTBP2 protein.
PTCH1
Protein patched homolog 1 is a protein that is the member of the patched family and in humans is encoded by the PTCH1 gene.

# Function
PTCH1 is a member of the patched gene family and is the receptor for sonic hedgehog, a secreted molecule implicated in the formation of embryonic structures and in tumorigenesis. This gene functions as a tumor suppressor. The PTCH1 gene product, is a transmembrane protein that suppresses the release of another protein called smoothened, and when sonic hedgehog binds PTCH1, smoothened is released and signals cell proliferation.

# Clinical significance
Mutations of this gene have been associated with nevoid basal cell carcinoma syndrome (AKA Gorlin's Syndrome), esophageal squamous cell carcinoma, trichoepitheliomas, transitional cell carcinomas of the bladder, as well as holoprosencephaly. Alternative splicing results in multiple transcript variants encoding different isoforms. Additional splice variants have been described, but their full length sequences and biological validity cannot be determined currently.
Mutations in PTCH1 cause Gorlin syndrome and mutations have also been found in holoprosencephaly patients. Some of these patients present cleft lip and palate among  the holoprosencephaly features, and missense variants in PTCH1 were also found in a sequencing screening of nonsyndromic cleft lip and palate patients. In addition association between SNPs in or near PTCH1 have been found to be associated with nonsyndromic cleft lip and palate. Mutations in PTCH1 are also associated with medulloblastoma.
PTCH2
Patched 2 is a protein that in humans is encoded by the PTCH2 gene.

# Function
This gene encodes a transmembrane receptor of the patched gene family. The encoded protein may function as a tumor suppressor in the hedgehog signaling pathway.

# Clinical significance
Alterations in this gene have been associated with nevoid basal cell carcinoma syndrome, basal cell carcinoma, medulloblastoma, and susceptibility to congenital macrostomia.
PTK2B
Protein tyrosine kinase 2 beta is an enzyme that in humans is encoded by the PTK2B gene.

# Function
This gene encodes a cytoplasmic protein tyrosine kinase that is involved in calcium-induced regulation of ion channels and activation of the map kinase signaling pathway. The encoded protein may represent an important signaling intermediate between neuropeptide-activated receptors or neurotransmitters that increase calcium flux and the downstream signals that regulate neuronal activity.
The encoded protein undergoes rapid tyrosine phosphorylation and activation in response to increases in the intracellular calcium concentration 
, nicotinic acetylcholine receptor activation, membrane depolarization, or protein kinase C activation. In addition, SOCE-induced Pyk2 activation mediates disassembly of endothelial adherens junctions, via tyrosine (Y1981-residue) phosphorylation of VE-PTP.
This protein has been shown to bind a CRK-associated substrate, a nephrocystin, a GTPase regulator associated with FAK, and the SH2 domain of GRB2.
The encoded protein is a member of the FAK subfamily of protein tyrosine kinases but lacks significant sequence similarity to kinases from other subfamilies. Four transcript variants encoding two different isoforms have been found for this gene.

# Interactions
PTK2B has been shown to interact with:
- BCAR1,
- Cbl gene,
- DDEF2,
- DLG3,
- DLG4,
- Ewing sarcoma breakpoint region 1,
- FYN,
- GRIN2A,
- Gelsolin,
- NPHP1,
- PITPNM1,
- PTPN11,
- PTPN6,
- Paxillin,
- RAS p21 protein activator 1,
- RB1CC1,
- SORBS2,
- Src,  and
- TGFB1I1,
- VE-PTP
PTPN5
Protein tyrosine phosphatase non-receptor type 5 is an enzyme that in humans is encoded by the PTPN5 gene.
Protein tyrosine phosphatase (PTP), non-receptor type 5, also known as STEP (STriatal-Enriched protein tyrosine Phosphatase), was the first brain-specific PTP discovered. The human STEP locus maps to chromosome 11p15.2-p15.1 and the murine STEP gene to chromosome 7B3-B5. The single STEP gene is alternatively spliced to produce several isoforms, the best characterized of which are the cytosolic STEP46 protein and the membrane-associated STEP61 protein.

# Substrates
Seven known targets of STEP have been identified as of 2015, including ERK1/2, p38, Fyn, Pyk2, PTP, and the glutamate receptor subunits GluN2B and GluA2. STEP dephosphorylation of the kinases (ERK1/2, p38, Fyn, and Pyk2) occurs at a regulatory tyrosine within the kinase activation loop and leads to their inactivation. Dephosphorylation of a regulatory tyrosine on PTP prevents the translocation of PTP from the cytosol to lipid rafts, where it normally activates Fyn. STEP thereby directly inactivates Fyn and also prevents the translocation of PTP to compartments where it activates Fyn. STEP dephosphorylation of GluN2B and GluA2 leads to the internalization of NMDARs (GluN1/GluN2B) and AMPARs (GluA1/GluA2). Thus, one function of STEP is to oppose synaptic strengthening by inactivating kinases and internalizing receptors that are critical for the development of synaptic strengthening.

# Clinical significance
STEP levels are disrupted in several diseases. Alzheimers disease (AD) was the first illness to be associated with elevated STEP expression both in human cortex and in several mouse models of AD. STEP is also increased in fragile X syndrome, schizophrenia, and Parkinsons disease. In AD and FXS mouse models, genetic reduction of STEP expression reverses many of the cognitive and behavioral deficits.
Other laboratories have now shown that STEP activity is also reduced in several additional disorders. Thus, STEP levels or activity is decreased in Huntingtons disease, cerebral ischemia, alcohol abuse, and stress disorders. The emergent model suggests that an optimal level of STEP is required at synaptic sites, and that both high and low levels disrupt synaptic function.

# Inhibition
Several STEP inhibitors have now been discovered. GlaxoSmithKline chose STEP as a new project for their Discovery Partnerships with Academia (DPAc) in 2014. This is a relatively new program in drug discovery and brings together the academic world with the drug discovery expertise of GSK to discover new inhibitors of validated targets.
- TC-2153
PTPN6
Tyrosine-protein phosphatase non-receptor type 6, also known as Src homology region 2 domain-containing phosphatase-1 (SHP-1), is an enzyme that in humans is encoded by the PTPN6 gene.

# Function
The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. N-terminal part of this PTP contains two tandem Src homolog (SH2) domains, which act as protein phospho-tyrosine binding domains, and mediate the interaction of this PTP with its substrates. This PTP is expressed primarily in hematopoietic cells, and functions as an important regulator of multiple signaling pathways in hematopoietic cells. This PTP has been shown to interact with, and dephosphorylate a wide spectrum of phospho-proteins involved in hematopoietic cell signaling, (e.g., the LYN-CD22-SHP-1 pathway). Multiple alternatively spliced variants of this gene, which encode distinct isoforms, have been reported.

# Expression
SHP-1 gene has two promoters: P-1, active in epithelial cells, and P-2, active in hemopoietic cells. In addition the expression of SHP-1 is low in epithelial cells and high in hemopoetic cells. SHP-1 level in epithelial cells increases and in hematopoetic cells decreases in cancer.

# Interactions
PTPN6 has been shown to interact with:
- BCR gene,
- CD117,
- CD22,
- CD31,
- CTNND1,
- EGFR,
- EPOR,
- FCRL3,
- Grb2,
- HOXA10,
- JAK2,
- LAIR1,
- LILRB2,
- LILRB4,
- Lck,
- LCP2,
- PRKCD,
- PTK2B,
- ROS1,
- SIRPA,
- SYK,  and
- TYK2.
PTPRB
Receptor-type tyrosine-protein phosphatase beta or VE-PTP is an enzyme specifically expressed in endothelial cells  that in humans is encoded by the PTPRB gene.

# Function
VE-PTP is a member of the classical protein tyrosine phosphatase (PTP) family. The deletion of the gene in mouse models was shown to be embryonically lethal, thus indicating that it is important for vasculogenesis and blood vessel development.  In addition, it was shown to participate in adherens junctions complex and regulate vascular permeability. Recently, Soni et al. have shown that tyrosine phosphorylation of VE-PTP via Pyk2 kinase downstream of STIM1-induced calcium entry mediates disassembly of the endothelial adherens junctions.

# Interactions
VE-PTP contains an extracellular domain composed of multiple fibronectin type_III repeats, a single transmembrane segment and one intracytoplasmic catalytic domain, thus belongs to R3 receptor subtype PTPs. 
The extracellular region was shown to interact with the angiopoietin receptor Tie-2 and with the adhesion protein VE-cadherin.
VE-PTP was also found to interact with Grb2 and plakoglobin through its cytoplasmatic domain.
PTPRD
Receptor-type tyrosine-protein phosphatase delta is an enzyme that in humans is encoded by the PTPRD gene.

# Function
The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP contains an extracellular region, a single transmembrane segment and two tandem intracytoplasmic catalytic domains, thus represents a receptor-type PTP. The extracellular region of this protein is composed of three Ig-like and eight fibronectin type III-like domains. Studies of the similar genes in chick and fly suggest the role of this PTP is in promoting neurite growth, and regulating neurons axon guidance. Multiple tissue specific alternatively spliced transcript variants of this gene have been reported.

# Clinical significance
Mutations in the PTPRD gene are associated with autism, obsessivecompulsive disorder, and breast cancer.

# Interactions
PTPRD has been shown to interact with PTPRS and liprin-alpha-1.
PTPRS
Receptor-type tyrosine-protein phosphatase S, also known as R-PTP-S, R-PTP-sigma, or PTP, is an enzyme that in humans is encoded by the PTPRS gene.

# Function
The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP contains an extracellular region, a single transmembrane segment and two tandem intracytoplasmic catalytic domains, and thus represents a receptor-type PTP. The extracellular region of this protein is composed of multiple Ig-like and fibronectin type III-like domains. Studies of the similar gene in mice suggested that this PTP may be involved in cell-cell interaction, primary axonogenesis, and axon guidance during embryogenesis. This PTP has been also implicated in the molecular control of adult nerve repair. Four alternatively spliced transcript variants, which encode distinct proteins, have been reported.

# Clinical significance
A PTPRS protein mimetic may improve muscular and bladder control in rats with spinal cord injuries.

# Interactions
PTPRS has been shown to interact with:
- chondroitin sulphate proteoglycans,
- PTPRD, glial-derived  and
- liprin-alpha-1.
PTTG1
Securin is a protein that in humans is encoded by the PTTG1 gene.

# Function
The encoded protein is a homolog of yeast securin proteins, which prevent separins from promoting sister chromatid separation. It is an anaphase-promoting complex (APC) substrate that associates with a separin until activation of the APC. The gene product has transforming activity in vitro and tumorigenic activity in vivo, and the gene is highly expressed in various tumors. The gene product contains 2 PXXP motifs, which are required for its transforming and tumorigenic activities, as well as for its stimulation of basic fibroblast growth factor expression. It also contains a destruction box (D box) that is required for its degradation by the APC. The acidic C-terminal region of the encoded protein can act as a transactivation domain. The gene product is mainly a cytosolic protein, although it partially localizes in the nucleus.

# Interactions
PTTG1 has been shown to interact with:
- DNAJA1,
- Ku70
- P53,
- PTTG1IP,  and
- RPS10.

# Regulation
During Mitosis CDK1 phosphorylate PTTG1 at Ser-165.PTTG1 is down-regulated in melanoma cells in response to the cyclin-dependent kinase inhibitor PHA-848125.
PUS7L
Pseudouridylate synthase 7 homolog-like protein is an enzyme that in humans is encoded by the PUS7L gene.

# Model organisms
Model organisms have been used in the study of PUS7L function. A conditional knockout mouse line, called Pus7ltm2a(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 three tests were carried out on homozygous mutant mice and one significant abnormality was observed: an increased susceptibility to bacterial infection.
PYCR2
Pyrroline-5-carboxylate reductase family, member 2 is a protein that in humans is encoded by the PYCR2 gene.

# Function
This gene belongs to the pyrroline-5-carboxylate reductase family. The encoded mitochondrial protein catalyzes the conversion of pyrroline-5-carboxylate to proline, which is the last step in proline biosynthesis. Loss of PYCR2 does not lead to a gross defect in mitochondrial protein synthesis, but loss of function of PYCR2 leads to increased apoptosis under oxidative stress.

# Clinical significance
Mutations in the PYCR2 gene have been identified as the cause of a unique syndrome characterized by postnatal microcephaly, hypomyelination, and reduced cerebral white-matter volume. Hypomyelination and the absence of wrinkly skin makes this condition distinct from that caused by previously reported mutations in the gene encoding PYCR2s isozyme, PYCR1, suggesting a unique and indispensable role for PYCR2 in the human CNS during development. This is substantiated by the fact that PYCR2 mRNA is moderately expressed in the developing human brain, and in much higher forms than either of the other two isoforms. Although PYCR2 is an enzyme for proline biosynthesis, systemic deprivation of proline does not appear to be the pathogenetic mechanism of this condition, given that plasma amino acid analysis in two affected individuals did not show low proline levels. Furthermore, mitochondrial protein synthesis was not affected in PYCR2-deficient cells. Therefore, deficiency of proline, as a building block of proteins, might not be the major pathophysiology. However, proline has been reported as a non-enzymatic antioxidant that suppresses apoptosis, and therefore local proline biosynthesis in neurons might be important for neuronal protection against oxidative stress.
The PYCR family also has been correlated with melanoma cells. PYCR2 as well as PYCR are abundant in melanoma cells but not detected in melanocytes.
Plunc
Palate, lung, and nasal epithelium clone protein  (PLUNC) is a gene encoding a secretory protein.  It is also called Secretory protein in upper respiratory tracts (SPURT). In humans, it is encoded by the BPIFA1 gene, previously called PLUNC.

# Function
This gene is the human homolog of murine plunc, and like the mouse gene, is specifically expressed in the airways and nasopharyngeal regions. Plunc inhibits the epithelial sodium channel (ENaC), and also has anti-microbial functions.  As such, plunc is believed to play a role in innate immune defense in the airways. PLUNC's ability to regulate ENaC is pH-sensitive and fails in acidic cystic fibrosis airways.  Thus, defective PLUNC1 function is thought to contribute to the development of lung pathology in cystic fibrosis patients.
It may also serve as a potential molecular marker for detection of micrometastasis in non-small-cell lung cancer.