Persius/hicric huggingface dataset:
OR2T11
Olfactory receptor 2T11 is a protein that in humans is encoded by the OR2T11 gene.
Olfactory receptors interact with odorant molecules in the nose, to initiate a neuronal response that triggers the perception of a smell. The olfactory receptor proteins are members of a large family of G-protein-coupled receptors (GPCR) arising from single coding-exon genes. Olfactory receptors share a 7-transmembrane domain structure with many neurotransmitter and hormone receptors and are responsible for the recognition and G protein-mediated transduction of odorant signals. The olfactory receptor gene family is the largest in the genome. The nomenclature assigned to the olfactory receptor genes and proteins for this organism is independent of other organisms.

# Ligands
- tert-Butylthiol (the response is enhanced by the presence of ionic copper)
- Ethanethiol (the response is enhanced by the presence of ionic copper)
- 2-Propenethiol (allyl mercaptan) (the response is enhanced by the presence of ionic copper)
- Thietane (the response is enhanced by the presence of ionic copper)
OSBPL3
Oxysterol-binding protein-related protein 3 is a protein that in humans is encoded by the OSBPL3 gene.

# Function
This gene encodes a member of the oxysterol-binding protein (OSBP) family, a group of intracellular lipid receptors. Most members contain an N-terminal pleckstrin homology domain and a highly conserved C-terminal OSBP-like sterol-binding domain. Several transcript variants encoding different isoforms have been identified.

# Model organisms
Model organisms have been used in the study of OSBPL3 function. A conditional knockout mouse line called Osbpl3tm1a(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
OSBPL9
Oxysterol binding protein-like 9 is a protein that in humans is encoded by the OSBPL9 gene.
This gene encodes a member of the oxysterol-binding protein (OSBP) family, a group of intracellular lipid receptors. Most members contain an N-terminal pleckstrin homology domain and a highly conserved C-terminal OSBP-like sterol-binding domain, although some members contain only the sterol-binding domain. This family member functions as a cholesterol transfer protein that regulates Golgi structure and function. Multiple transcript variants, most of which encode distinct isoforms, have been identified. Related pseudogenes have been identified on chromosomes 3, 11 and 12.

# Model organisms
Model organisms have been used in the study of OSBPL9 function. A conditional knockout mouse line, called Osbpl9tm1a(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  at the Wellcome Trust Sanger Institute.
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Twenty four tests were carried out on homozygous mutant adult mice, however no significant abnormalities were observed.
OTUD6B
OTU domain containing 6B is a protein that in humans is encoded by the OTUD6B gene.
OTUD6B is a functional deubiquitinating enzyme, a class of protease that specifically cleaves ubiquitin linkages, negating the action of ubiquitin ligases. OTUD6B, also known as DUBA5, belongs to a DUB subfamily characterized by an ovarian tumor domain (OTU). OTUD6B function may be connected to growth and proliferation. This hypothesis is supported by a recent study indicating that OTUD6B knock out mice, obtained through exon 4 deletion, are subviable and smaller in size.  In humans, OTUD6B mutations have been connected to an intellectual disability syndrome associated with dysmorphic features.
Previous studies on model organisms (see below) cannot be verified by this editor.
Model organisms have been used in the study of OTUD6B function. A conditional knockout mouse line, called Otud6btm1a(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 five tests were carried out on homozygous mutant adult mice, however no significant abnormalities were observed.
Occult

# Overview
The word occult comes from the Latin word occultus (clandestine, hidden, secret), referring to  "knowledge of the hidden".  In the medical sense it is used to refer to a structure or process that is hidden, e.g. an "occult bleed" may be one detected indirectly by the presence of otherwise unexplained anaemia.
-  Crabb, G. (1927). English synonyms explained, in alphabetical order, with copious illustrations and examples drawn from the best writers. New York: Thomas Y. Crowell Co.
-  Harvard Medical School Family Health Guide. Harvard Medical School 2005. 1272 pages ISBN 0684863731
Ostium

# Overview
An ostium is a small opening or orifice, as in a body organ or passage.

# Anatomy
- Ostium of Fallopian tube.
- Ostium primum or foramen ovale (ostium secundum) of the developing heart.
- Ostium maxillare of the Maxillary Sinus
- Ostium of uterus
- Ostium vaginae (vaginal orifice)
- Coronary ostium (Opening of coronary arteries at root of aorta, superior to aortic valve)

# Ostial Disease
Ostial disease refer to diseases involving the ostium of a body organ, passage or vessel.  In particular, ostial stenosis is a narrowing in a ostium. It can refer to:
- Coronary ostial stenosis
- Renal ostial stenosis
Oxamyl

# Overview
Oxamyl is a chemical used as a pesticide that comes in two forms: granulated and liquid. The granulated form has been banned in the United States.

# Structure and uses
Oxamyl is a carbamate pesticide.  According to the WHO Food and Agriculture Organization, "Oxamyl is a colourless crystalline solid with a melting point of 100-102 C changing to a dimorphic form with a melting point of 108-110 C. It has a slightly sulfurous odour. Oxamyl is non-corrosive. It has a specific gravity of 0.97 (25/4)."
According to the United Nations Environment Programme, "This product is efficient in controlling most nematode species in addition to a large number of sucking and chewing insects such as aphids and thrips." Oxamyl is extremely toxic to humans whether ingested, inhaled, or contact with the skin. Its overuse can also lead to residue accumulation in food, though its chemical composition--once coming into contact with the soil--rapidly degrades. Signs of Oxamyl poisoning include: Malaise, muscle weakness, dizziness, sweating, Headache, salivation, nausea, vomiting, abdominal pain, Miosis with blurred vision, incoordination, muscle twitching and slurred speech--though symptoms can worsen with severe poisoning. According to the Food and Agriculture Organization, "Contact with the skin, inhalation of dust or spray, or swallowing may be fatal."
Because of its toxicity, its use is restricted in the EU/UK with maximum residue limits for apples and oranges being 0.01 mg/kg and this amount is only allowed because this is the limit of detection.
PABPC1
Polyadenylate-binding protein 1 is a protein that in humans is encoded by the PABPC1 gene. The protein PABP1 binds mRNA and facilitates a variety of functions such as transport out of the nucleus, degradation, translation, and stability. There are two separate PABP1 proteins, one which is located in the nucleus (PABPN1) and the other which is found in the cytoplasm (PABPC1). The location of PABP1 affects the role of that protein and its function with RNA.

# Function
The poly(A)-binding protein (PAB or PABP), which is found complexed to the 3' poly(A) tail of eukaryotic mRNA, is required for poly(A) shortening and translation initiation. In humans, the PABPs comprise a small nuclear isoform and a conserved gene family that displays at least 3 functional proteins: PABP1 (PABPC1), inducible PABP (iPABP, or PABPC4; MIM 603407), and PABP3 (PABPC3; MIM 604680). In addition, there are at least 4 pseudogenes, PABPCP1 to PABPCP4.
PABPC1 is usually diffused within the cytoplasm and concentrated at sites of high mRNA concentration such as stress granules, processing bodies, and locations of high translational activity. PABPC1 is also associated with nonsense-mediated mRNA decay (NMD). PABPC1 binds to the poly(A) tail and interact with eIF4G, which stabilizes the circularization of mRNAs. This structure is required for the prevention of mRNA degradation via NMD.
In the nucleus PABP1 binds to the poly(A) tails of pre-mRNAs to facilitate stability, export, transport, and degradation. PABP1 binding is also required for nuclear-mediated degradation. PABPC1 contains four RNA-recognition motifs (RRMs). The first two, RRM1 and RRM2, bind both -importin and the poly(A) tail of processed mRNA. This feature prevents mRNA from going back into the nucleus.

# Interactions
PABPC1 has been shown to interact with:
- ANAPC5,
- CNOT7,
- EIF4G3,
- EIF4G1,
- GSPT2,
- PAIP1,  and
- PAIP2.
PABPC4
Polyadenylate-binding protein 4 (PABPC4) is a protein that in humans is encoded by the PABPC4 gene.

# Function
Poly(A)-binding proteins (PABPs) bind to the poly(A) tail present at the 3-prime ends of most eukaryotic mRNAs. PABPC4 or IPABP (inducible PABP) was isolated as an activation-induced T-cell mRNA encoding a protein. Activation of T cells increased PABPC4 mRNA levels in T cells approximately 5-fold. PABPC4 contains 4 RNA-binding domains and proline-rich C terminus. PABPC4 is localized primarily to the cytoplasm. It is suggested that PABPC4 might be necessary for regulation of stability of labile mRNA species in activated T cells. PABPC4 was also identified as an antigen, APP1 (activated-platelet protein-1), expressed on thrombin-activated rabbit platelets. PABPC4 may also be involved in the regulation of protein translation in platelets and megakaryocytes or may participate in the binding or stabilization of polyadenylates in platelet dense granules.

# Model organisms
Model organisms have been used in the study of PABPC4 function. A conditional knockout mouse line, called Pabpc4tm1a(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 tests were carried out on mutant mice and one significant abnormality was observed: female homozygous mutants displayed impaired glucose tolerance.

# Interactions
PABPC4 has been shown to interact with PHLDA1.
PARD6A
Partitioning defective 6 homolog alpha is a protein that in humans is encoded by the PARD6A gene.

# Function
This gene is a member of the PAR6 family and encodes a protein with a PSD95/Discs-large/ZO1 (PDZ) domain and a semi-Cdc42/Rac interactive binding (CRIB) domain. This cell membrane protein is involved in asymmetrical cell division and cell polarization processes as a member of a multi-protein complex. The protein also has a role in the epithelial-to-mesenchymal transition (EMT) that characterizes the invasive phenotype associated with metastatic carcinomas. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.
A recent study shows that Par6 associates with PKC- but not with PKC-zeta in melanoma. Oncogenic PKC-iota can promote melanoma cell invasion by up-regulating PKC-/Par6 pathway during EMT. PKC- inhibition or knockdown resulted an increase E-cadherin and RhoA levels while decreasing total Vimentin, phophorylated Vimentin (S39) and Par6 in metastatic melanoma cells. These results suggested that PKC- is involved in signaling pathways which upregulate EMT in melanoma.

# Interactions
PARD6A has been shown to interact with:
- CDC42,
- ECT2
- Protein kinase M, and
- RAC1.
- Protein kinase C-.
PCDH15
Protocadherin-15 is a protein that in humans is encoded by the PCDH15 gene.

# Function
This gene is a member of the cadherin superfamily. Family members encode integral membrane proteins that mediate calcium-dependent cell-cell adhesion. The protein product of this gene consists of a signal peptide, 11 extracellular calcium-binding domains, a transmembrane domain and a unique cytoplasmic domain. It plays an essential role in maintenance of normal retinal and cochlear function. It is thought to interact with CDH23 to form tip-link filaments.

# Clinical significance
Mutations in this gene have been associated with hearing loss, which is consistent with its location at the Usher syndrome type 1F (USH1F) critical region on chromosome 10. Variation within it has also been found to be associated with normal differences in human facial appearance.
PCDHA9
Protocadherin alpha-9 is a protein that in humans is encoded by the PCDHA9 gene.
This gene is a member of the protocadherin alpha gene cluster, one of three related gene clusters tandemly linked on chromosome 5 that demonstrate an unusual genomic organization similar to that of B-cell and T-cell receptor gene clusters. The alpha gene cluster is composed of 15 cadherin superfamily genes related to the mouse CNR genes and consists of 13 highly similar and 2 more distantly related coding sequences.
The tandem array of 15 N-terminal exons, or variable exons, are followed by downstream C-terminal exons, or constant exons, which are shared by all genes in the cluster. The large, uninterrupted N-terminal exons each encode six cadherin ectodomains while the C-terminal exons encode the cytoplasmic domain. These neural cadherin-like cell adhesion proteins are integral plasma membrane proteins that most likely play a critical role in the establishment and function of specific cell-cell connections in the brain. Alternative splicing has been observed and additional variants have been suggested but their full-length nature has yet to be determined.
PDCD10
Programmed cell death protein 10 is a protein that in humans is encoded by the PDCD10 gene.

# Function
This gene encodes a protein, originally identified in a premyeloid cell line, with similarity to proteins that participate in apoptosis. Three alternative transcripts encoding the same protein, differing only in their 5' UTRs, have been identified for this gene.

# Gene
Loss of function mutations in PDCD10 result in the onset of Cerebral Cavernous Malformations (CCM) illness.  Therefore, this gene is also called CCM3.  Cerebral cavernous malformations (CCMs) are vascular malformations in the brain and spinal cord made of dilated capillary vessels.

# Interactions
CCM3 encodes a protein called Programmed Cell Death 10 (PDCD10).  The function of this protein has only recently begun to be understood.  PDCD10 has roles in vascular development and VEGF signaling1, apoptosis and functions as part of a larger signaling complex that includes germinal center kinase III,.  Specifically, PDCD10 has been shown to interact with RP6-213H19.1, STK25, STRN, STRN3, MOBKL3, CTTNBP2NL, STK24 and FAM40A.

# Model organisms
Model organisms have been used in the study of PDCD10 function. A conditional knockout mouse line, called Pdcd10tm1a(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 five 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.
PDE10A
cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A is an enzyme that in humans is encoded by the PDE10A gene.
Various cellular responses are regulated by the second messengers cAMP and cGMP. Phosphodiesterases, such as PDE10A, eliminate cAMP- and cGMP-mediated intracellular signaling by hydrolyzing the cyclic nucleotide to the corresponding nucleoside 5-prime monophosphate.

# Inhibitors
- Compound 96: IC50 = 700 pM, high selectivity against all other members of the PDE family
- Papaverine
- PF-2545920
- TAK-063: IC50 = 300 pM
- AMG 579

# Research
Preliminary evidence indicates a possible link between PDE10A expression and obesity in mice and humans.
PDLIM3
Actin-associated LIM protein (ALP), also known as PDZ and LIM domain protein 3 is a protein that in humans is encoded by the PDLIM3 gene. ALP is highly expressed in cardiac and skeletal muscle, where it localizes to Z-discs and intercalated discs. ALP functions to enhance the crosslinking of actin by alpha actinin-2 and also appears to be essential for right ventricular chamber formation and contractile function.

# Structure
ALP exists primarily as two alternatively spliced variants; a 39.2 kDa (364 amino acids) protein in skeletal muscle and a 34.3 kDa (316 amino acids) protein in cardiac muscle and smooth muscle. ALP has a N-terminal PDZ domain and a C-terminal LIM domain. In addition, the ALP subfamily contains a specific 34 amino acid domain named the ALP-like motif, containing protein kinase C consensus sequences. The PDZ domain of ALP binds to alpha actinin-2, specifically to its spectrin-like repeats. The PDZ domain is a motif composed of 80-120 amino acids with conserved four residue GLGF sequences that typically interact with C-termini of cytoskeletal proteins. The region of heterogeneity in the two isoforms is between the PDZ domain and LIM domain. ALP is localized to chromosome 4q35. It has been shown that deletion of muscleblind-like 1 in mice can alter the splicing pattern of PDLIM3.

# Function
Studies have shown that ALP is present at the first stage of myofibrilogenesis where it is bound to alpha actinin-2, and this association remains intact in mature myofibrils where ALP is localized to Z-discs and intercalated discs. Alpha actinin-2 is however not required for targeting ALP to Z-lines. Studies in ALP knockout mice have shown that ALP facilitates the cross-linking of actin filaments by alpha actinin-2, and absence of ALP induces abnormal right ventricular chamber formation, dysplasia and cardiomyopathy. Further studies using right ventricular epicardial systolic strain and geometric remodeling analysis in these animals unveiled that absence of ALP diminishes right ventricular contractile function and alters the pattern of cardiac hypertrophic remodeling. Two studies using integrative genomic approaches to investigate genetic modifiers of collagen deposition or intrinsic aerobic running capacity (ARC) have mapped PDLIM3 to respective quantitative trait loci, suggesting that ALP may be involved in molecular networks related to these cardiac phenomena.

# Clinical significance
Chromosome 4 pericentric inversion has been observed in 10 patients, with associated cardiac defects linked to terminal 4q35.1 deletions, which may affect PDLIM3.

# Interactions
ALP interacts with:
- alpha actinin-2
- beta-catenin
PET100
PET100 homolog is a protein that in humans is encoded by the PET100 gene. Mitochondrial complex IV, or cytochrome c oxidase, is a large transmembrane protein complex that is part of the respiratory electron transport chain of mitochondria. The small protein encoded by the PET100 gene plays a role in the biogenesis of mitochondrial complex IV. This protein localizes to the inner mitochondrial membrane and is exposed to the intermembrane space. Mutations in this gene are associated with mitochondrial complex IV deficiency. This gene has a pseudogene on chromosome 3. Alternative splicing results in multiple transcript variants.

# Structure
The PET100 gene is located on the p arm of chromosome 19 in position 13.2 and spans 1,839 base pairs. The gene produces a 9.1 kDa protein composed of 73 amino acids. The encoded protein localizes to the inner mitochondrial membrane and is exposed to the intermembrane space. This protein's N-terminus is essential for mitochondrial localization. It assembles into a 300 kDA complex which is dependent on the mitochondrial membrane potential, accumulating over time.

# Function
The protein encoded by PET100 is involved in Complex IV biogenesis as a COX chaperone; it is required for interaction between MR-1S, PET117, and Complex IV.

# Clinical significance
In 8 patients of Lebanese origin living in Australia, a c.3G>C mutation in the PET100 gene caused Complex IV deficiency and Leigh syndrome. Symptoms included delayed psychomotor development, seizures, hypotonia, brain abnormalities, and elevated blood and cerebrospinal fluid lactate levels. In another patient of Pakistani origin, a homozygous c.142C>T mutation resulted in Complex IV deficiency with intrauterine growth retardation, metabolic and lactic acidosis, hypoglycemia, coagulopathy, elevated serum creatine kinase levels, seizures, and intraventricular cysts.

# Interactions
The encoded protein interacts with MR-1S and COX7A2.
This protein is required for MR-1S, PET117, and Complex IV to interact.
PET117
PET117 homolog is a protein that in humans is encoded by the PET117 gene. Localized to mitochondria, this protein is a chaperone protein  involved in the assembly of mitochondrial Complex IV, or Cytochrome C Oxidase. Mutations in this gene can cause Complex IV deficiency with symptoms including medulla oblongata lesions and lactic acidosis.

# Structure
The PET117 gene is located on the p arm of chromosome 20 in position 11.23 and spans 5,314 base pairs. The gene produces a 9.2 kDa protein composed of 81 amino acids. PET117 localizes to mitochondria.

# Function
The protein encoded by PET117 is a chaperone protein involved in Complex IV biogenesis, interacting with MR-1S and possibly other Complex IV structural subunits. The presence of PET100 is required for this interaction.

# Clinical Significance
The only reported mutation in the PET117 gene was a homozygous nonsense mutation (c. 172 C>T) in two sister patients. Both were diagnosed with Complex IV deficiency and had lesions in their medulla oblongata, along with lactic acidosis. Symptoms in the older sister included abnormal motor development, regression in speech and motor skills after age ten, bradykinesia, hypokinesia, and pyramidal signs with positive Babinski response. The younger sister had protein losing enteropathy (PLE), recurrent respiratory infections, neutropenia, hypogammaglobulinemia, delayed motor and general development, and exercise intolerance.

# Interactions
PET117 interacts with MR-1S and possibly other Complex IV structural subunits. This interaction is dependent on the presence of PET100.
PFKFB4
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 4 also known as PFKFB4 is an enzyme which in humans is encoded by the PFKFB4 gene.

# Function
The bifunctional 6-phosphofructo-2-kinase (EC 2.7.1.105)/fructose-2,6-bisphosphatase (EC 3.1.3.46) (PFKFB) regulates the steady-state concentration of fructose 2,6-bisphosphate, an activator of a key regulatory enzyme of glycolysis, phosphofructokinase.
In 2012 research by scientists at Cancer Research UKs London Research Institute show that an enzyme called PFKFB4 is essential for balancing these two processes  making sure the cells energy needs are met without allowing free radicals to build up and trigger cell death.
Study leader Dr. Almut Schulze, said: Our study suggests that PFKFB4 acts to fine-tune the process by which cells convert glucose into energy. Blocking this enzyme in prostate cancer cells grown in the lab stalled growth and triggered a catastrophic build-up of free-radicals, suggesting that it could be a suitable drug target. Importantly, this route to energy production is common to many different types of cancer, suggesting that drugs to target it could potentially be used to treat a variety of cancers.