Persius/hicric huggingface dataset:
GNG2
Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 is a protein that in humans is encoded by the GNG2 gene.
Heterotrimeric G proteins play vital roles in cellular responses to external signals. The specificity of a G protein-receptor interaction is primarily mediated by the gamma subunit.

# Interactive pathway map
Click on genes, proteins and metabolites below to link to respective articles.
-  The interactive pathway map can be edited at WikiPathways: "NicotineDopaminergic_WP1602"..mw-parser-output cite.citation{font-style:inherit}.mw-parser-output q{quotes:"\"""\"""'""'"}.mw-parser-output code.cs1-code{color:inherit;background:inherit;border:inherit;padding:inherit}.mw-parser-output .cs1-lock-free a{background:url("")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-limited a,.mw-parser-output .cs1-lock-registration a{background:url("")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-subscription a{background:url("")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration{color:#555}.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration span{border-bottom:1px dotted;cursor:help}.mw-parser-output .cs1-hidden-error{display:none;font-size:100%}.mw-parser-output .cs1-visible-error{display:none;font-size:100%}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-format{font-size:95%}.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-wl-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right,.mw-parser-output .cs1-kern-wl-right{padding-right:0.2em}
GNLY
Granulysin, also known as GNLY, is a protein which in humans is encoded by the GNLY gene.

# Function
Granulysin is a protein present in cytotoxic granules of cytotoxic T cells and natural killer cells. Granulysin is a member of the saposin-like protein (SAPLIP) family and is released from cytotoxic T cells upon antigen stimulation. Granulysin has antimicrobial activity against M. tuberculosis and other organisms. Granulysin is alternatively spliced, resulting in the NKG5 and 519 transcripts.
Granulysin is a cytolytic and proinflammatory molecule first identified by a screen for genes expressed late (35 days) after activation of human peripheral blood mononuclear cells. Granulysin is present in cytolytic granules of cytotoxic T lymphocytes (CTL) and natural killer (NK) cells.  Granulysin is made as a 15 kD molecule, and a portion of it is cleaved at both the amino and carboxy termini into a 9 kD form. The 9 kD form is released by receptor-mediated granule exocytosis while the 15 kD form is constitutively secreted.  Recombinant 9 kD granulysin is broadly cytolytic against tumors and microbes, including gram positive and gram negative bacteria, fungi/yeast and parasites. 9kD granulysin is also a chemoattractant for T lymphocytes, monocytes, and other inflammatory cells and activates the expression of a number of cytokines, including RANTES, MCP-1, MCP-3, MIP-1, IL-10, IL-1, IL-6 and IFN.  Mice do not have a granulysin homolog, but  transgenic mice expressing human granulysin have been engineered. Granulysin has been implicated in a myriad of diseases including infection, cancer, transplantation, autoimmunity, skin and reproductive maladies.
GOPC
Golgi-associated PDZ and coiled-coil motif-containing protein is a protein that in humans is encoded by the GOPC gene.
PIST is a PDZ domain-containing Golgi protein. PDZ domains contain approximately 90 amino acids and bind the extreme C terminus of proteins in a sequence-specific manner.

# Interactions
GOPC has been shown to interact with GRID2, BECN1, RHOQ,ACCN3, Cystic fibrosis transmembrane conductance regulator and CSPG5.
GOT1
Aspartate aminotransferase, cytoplasmic is an enzyme that in humans is encoded by the GOT1 gene.
Glutamic-oxaloacetic transaminase is a pyridoxal phosphate-dependent enzyme which exists in cytoplasmic and mitochondrial forms, GOT1 and GOT2, respectively.  GOT plays a role in amino acid metabolism and the urea and tricarboxylic acid cycles. The two enzymes are homodimeric and show close homology.

# Interactive pathway map
Click on genes, proteins and metabolites below to link to respective articles. 
-  The interactive pathway map can be edited at WikiPathways: "GlycolysisGluconeogenesis_WP534"..mw-parser-output cite.citation{font-style:inherit}.mw-parser-output q{quotes:"\"""\"""'""'"}.mw-parser-output code.cs1-code{color:inherit;background:inherit;border:inherit;padding:inherit}.mw-parser-output .cs1-lock-free a{background:url("")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-limited a,.mw-parser-output .cs1-lock-registration a{background:url("")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-subscription a{background:url("")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration{color:#555}.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration span{border-bottom:1px dotted;cursor:help}.mw-parser-output .cs1-hidden-error{display:none;font-size:100%}.mw-parser-output .cs1-visible-error{display:none;font-size:100%}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-format{font-size:95%}.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-wl-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right,.mw-parser-output .cs1-kern-wl-right{padding-right:0.2em}
GPVI
Glycoprotein VI (platelet) also known as GPVI is a glycoprotein receptor for collagen which is expressed in platelets.  In humans, glycoprotein VI is encoded by the GPVI gene.
GPVI was first cloned in 2000 by several groups including that of Martine Jandrot-Perrus from INSERM.

# Function
Glycoprotein VI (GP6) is a 58-kD platelet membrane glycoprotein that plays a crucial role in the collagen-induced activation and aggregation of platelets. Upon injury to the vessel wall and subsequent damage to the endothelial lining, exposure of the subendothelial matrix to blood flow results in deposition of platelets. Collagen fibers are the most thrombogenic macromolecular components of the extracellular matrix, with collagen types I, III, and VI being the major forms found in blood vessels. Platelet interaction with collagen occurs as a 2-step procedure: (1) the initial adhesion to collagen is followed by (2) an activation step leading to platelet secretion, recruitment of additional platelets, and aggregation. In physiologic conditions, the resulting platelet plug is the initial hemostatic event limiting blood loss. However, exposure of collagen after rupture of atherosclerotic plaques is a major stimulus of thrombus formation associated with myocardial infarction or stroke.
Complete or partial deficiency of GPVI in humans is a rare condition presenting as a mild bleeding disorder.

# Interactions
GPVI has been shown to interact with LYN.
GRAP
GRB2-related adapter protein is a protein that in humans is encoded by the GRAP gene.
This gene encodes a member of the GRB2/Sem5 (C. elegans homolog)/Drk (Drosophila homolog) family. This member functions as a cytoplasmic signaling protein which contains an SH2 domain flanked by two SH3 domains. The SH2 domain interacts with ligand-activated receptors for stem cell factor and erythropoietin, and facilitates the formation of a stable complex with the BCR-ABL oncoprotein. This protein also associates with the Ras guanine nucleotide exchange factor SOS1 (son of sevenless homolog 1) through its N-terminal SH3 domain.

# Interactions
GRAP has been shown to interact with Linker of activated T cells.
GRB2
Growth factor receptor-bound protein 2 also known as Grb2 is an adaptor protein involved in signal transduction/cell communication.  In humans, the GRB2 protein is encoded by the GRB2 gene.
The protein encoded by this gene binds receptors such as the epidermal growth factor receptor and contains one SH2 domain and two SH3 domains. Its two SH3 domains direct complex formation with proline-rich regions of other proteins, and its SH2 domain binds tyrosine phosphorylated sequences. This gene is similar to the sem-5 gene of Caenorhabditis elegans, which is involved in the signal transduction pathway. Two alternatively spliced transcript variants encoding different isoforms have been found for this gene.

# Function and expression
Grb2 is widely expressed and is essential for multiple cellular functions. Inhibition of Grb2 function impairs developmental processes in various organisms and blocks transformation and proliferation of various cell types. It is thus not surprising that targeted gene disruption of Grb2 in mice is lethal at an early embryonic stage. Grb2 is best known for its ability to link the epidermal growth factor receptor tyrosine kinase to the activation of Ras and its downstream kinases, ERK1,2.  Grb2 is composed of an SH2 domain flanked on each side by an SH3 domain. Grb2 has two closely related proteins with similar domain organizations, Gads and Grap.  Gads and Grap are expressed specifically in hematopoietic cells and function in the coordination of tyrosine kinase mediated signal transduction.

# Domains
The SH2 domain of Grb2 binds to phosphorylated tyrosine-containing peptides on receptors or scaffold proteins with a preference for pY-X-N-X, where X is generally a hydrophobic residue such as valine (see ).
The N-terminal SH3 domain binds to proline-rich peptides and can bind to the Ras-guanine exchange factor SOS.
The C-terminal SH3 domain binds to peptides conforming to a P-X-I/L/V/-D/N-R-X-X-K-P motif that allows it to specifically bind to proteins such as Gab-1.

# Interactions
Grb2 has been shown to interact with:
- ADAM15,
- Abl gene,
- Arachidonate 5-lipoxygenase,
- B-cell linker,
- BCAR1,
- BCR gene,
- Beta-2 adrenergic receptor,
- C-Met,
- CBLB,
- CD117,
- CD22,
- CD28,
- CDKN1B,
- CRK,
- Cbl gene,
- Colony stimulating factor 1 receptor,
- DCTN1,
- DNM1,
- Dock180,
- Dystroglycan,
- EPH receptor A2,
- ETV6,
- Epidermal growth factor receptor,
- Erythropoietin receptor,
- FRS2,
- Fas ligand,
- GAB1,
- GAB2,
- Glycoprotein 130,
- Granulocyte colony-stimulating factor receptor,
- HER2/neu,
- HNRNPC,
- Huntingtin,
- INPP5D,
- IRS1,
- ITK,
- Janus kinase 1,
- Janus kinase 2,
- KHDRBS1,
- Linker of activated T cells,
- Lymphocyte cytosolic protein 2,
- MAP2,
- MAP3K1
- MAP4K1,
- MED28,
- MST1R,
- MUC1,
- Mitogen-activated protein kinase 9,
- NCKIPSD,
- NEU3,
- PDGFRB,
- PIK3R1,
- PLCG1,
- PRKAR1A,
- PTK2,
- PTPN11,
- PTPN12,
- PTPN1,
- PTPN6,
- PTPRA,
- RAPGEF1,
- RET proto-oncogene,
- SH2B1,
- SH3KBP1,
- SHC1,
- SOS1,
- Src,
- Syk,
- TNK2,
- TrkA,
- VAV1,
- VAV2,
- VAV3,  and
- Wiskott-Aldrich syndrome protein.
GRB7
Growth factor receptor-bound protein 7, also known as GRB7, is a protein that in humans is encoded by the GRB7 gene.

# Function
The product of this gene belongs to a small family of adaptor proteins that are known to interact with a number of receptor tyrosine kinases and signaling molecules. This gene encodes a growth factor receptor-binding protein that interacts with epidermal growth factor receptor (EGFR) and ephrin receptors. The protein plays a role in the integrin signaling pathway and cell migration by binding with focal adhesion kinase (FAK). Alternative splicing results in multiple transcript variants encoding different isoforms, although the full-length natures of only two of the variants have been determined to date.

# Clinical significance
GRB7 is an SH2-domain adaptor protein that binds to receptor tyrosine kinases and provides the intra-cellular direct link to the Ras proto-oncogene.
Human GRB7 is located on the long arm of chromosome 17, next to the ERBB2 (alias HER2/neu) proto-oncogene.
These two genes are commonly co-amplified (present in excess copies) in breast cancers.
GRB7 thought to be involved in migration, is well known to be over-expressed in testicular germ cell tumors, esophageal cancers, and gastric cancers.

# Interactions
GRB7 has been shown to interact with:
- EPH receptor B1,
- Insulin receptor,
- PTK2,
- RET proto-oncogene,  and
- Rnd1

# Model organisms
Model organisms have been used in the study of GRB7 function. A conditional knockout mouse line called Grb7tm1b(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
Gli3
Gli3 is a known transcriptional repressor but may also have a positive transcriptional function.  Gli3 represses dHand and Germlin which are involved in developing digits  There is evidence that Shh-controlled processing (e.g cleavage) regulates transcriptional activity of Gli3 similarly to that of CI.  Gli3 mutant mice have many abnormalities including CNS and lung defects and limb polydactyly. There is evidence that the autosomal dominant disorder Greig cephalopolysyndactyly syndrome (GCPS) that affects limb and craniofacial development in humans is caused by a translocations within the GLI3 gene.
The independent overexpression Gli1 and Gli2 in mice models to lead to formation of basal cell carcinoma (BCC).  Gli1 knockout is shown to lead to similar embryonic malformations as Gli1 overexpressions but not the formation of BCC's.  Overexpression of Gli3 in transgenic mice and frogs does not lead to the development of BCC-like tumors and is not thought to play a role in tumor BCC formation.
Gli1 and Gli2 overexpression leads to BCC formation in mouse models and a one step model for tumour formation has been suggested in both cases.  This also indicates that Gli1 and/or Gli2 overexpression is vital in BCC formation.  Co-overexpression of Gli1 with Gli2 and Gli2 with Gli3 leads to transgenic mice malformations and death respectively but not the formation of BCC.  This suggests that over expression of more that one Gli protein is not necessary for BCC formation.
Gurn
A gurn is a distorted facial expression, and a verb to describe the action. A typical gurn might involve projecting the lower jaw as far forward and up as possible, and covering the upper lip with the lower lip.
The English Dialect Dictionary, compiled by Joseph Wright, defines the word gurn as 'to snarl as a dog; to look savage; to distort the countenance', while the Oxford English Dictionary suggests the derivation may originally be Scottish, related to 'grin'.  In Northern Ireland the verb 'gurn' means, 'to cry', hence crying in Northern Ireland is often called gurnin.
The term is also used to describe the facial expressions of people under the influence of the drug ecstasy and other stimulants. Sufferers often complain of 'hamster cheeks' and 'Forsyth chin'. The following day is especially uncomfortable - chewing becomes difficult and even speaking is a chore.

# Gurning contests
Gurning contests are a rural English tradition and were once common at travelling sideshow]s, fairs and freak shows. They are still held regularly in some villages, and the contestants traditionally frame their faces through a horse collar - known as 'gurnin' through a braffin'. The World Gurning Championship is held annually in Egremont, Cumbria as one part of the Egremont Crab Fair.  Those with the greatest gurn capabilities are often those with no teeth, as this provides greater room to move the jaw further up. In some cases the elderly or otherwise toothless can be capable of spectacular gurns covering the entire nose.
In Australia the most common form of gurning is the "duck face", with many areas holding local annual competitions for this form of facial expression. The "duck face" has been brought into mainstream culture by such people as TV's Kath and Kim, and is characterised by pursed lips and raised eyebrows.

# Notes
-   Guide to Traditional Customs of Britain/Brian Shuel/National Trust/1985/ISBN 0-86350-051-X
H1N2
H1N2 is a subtype of the species  Influenza A virus (sometimes called bird flu virus). It is currently endemic in both human and pig populations.
H1N1, H1N2, and H3N2 are the only known Influenza A  virus subtypes currently circulating among humans.
The new A(H1N2) strain appears to have resulted from the reassortment of the genes of the currently circulating influenza A(H1N1) and A(H3N2) subtypes.  The hemagglutinin protein of the A(H1N2) virus is similar to that of the currently circulating A(H1N1) viruses and the neuraminidase protein is similar to that of the current A(H3N2) viruses.
It is unknown where the A(H1N2) virus originated, but on February 6 2002, the World Health Organization (WHO) in Geneva and the Public Health Laboratory Service (PHLS) in the United Kingdom reported the identification influenza A(H1N2) virus from humans in England, Israel, and Egypt. In addition to the virus isolates reported by WHO and PHLS, the Centers for Disease Control and Prevention has identified influenza A(H1N2) virus from patient specimens collected during the 2001-2002 and 2002-2003 seasons. Influenza A(H1N2) viruses have circulated transiently in the past. Between December 1988 and March 1989, 19 influenza A(H1N2) virus isolates were identified in 6 cities in China, but the virus did not spread further.
The H1N2 virus is not very different from the currently circulating influenza viruses. The H1 protein of the H1N2 virus is like the H1 protein of the currently circulating H1N1 viruses and the N2 protein is similar to the N2 protein in the currently circulating H3N2 viruses. The difference is that we don't commonly see the H1 and N2 proteins on the same virus.
The A(H1N2) virus is not causing a more severe illness than other influenza viruses, and no unusual increases in influenza activity have been associated with the A(H1N2) virus. Because both the hemagglutinin and neuraminidase protein on the A(H1N2) virus closely matches the hemagglutinin and neuraminidase proteins of viruses included in the current influenza vaccine, the vaccine should provide good protection against influenza A(H1N2) virus as well as protection against the currently circulating A(H1N1), A(H3N2), and B viruses.

# Sources
- Questions and Answers About Influenza A(H1N2) Viruses This is the source of most of this article.
- Phylogenetic analysis of H1N2 isolates of influenza A virus from pigs in the United States
- CDC
H3N8
H3N8 is a subtype of the species  Influenza A virus (sometimes called bird flu virus). H3N8 is now endemic in birds, horses and dogs.
H3N8 is suspected of causing a human pandemic in either 1889 or 1900. Sources differ; some say the 1889 pandemic was caused H2N2. The experts also differ on exactly how sure we can be that either were involved.
It was the subtype that was responsible for over one-forth of the flu infections in wild ducks in a 1997 study.
H5N2
H5N2 is a subtype of the species Influenzavirus A (avian influenza virus or bird flu virus).
A highly pathogenic strain of H5N2 caused flu outbreaks with significant spread to numerous farms, resulting in great economic losses in 1983 in Pennsylvania, USA in chickens and turkeys, in 1994 in Mexico in chickens and a minor outbreak in 1997 in Italy in chickens. 
It was reported on  November 12, 2005 that "One of 2 birds found infected with bird flu in Kuwait has the H5N1 strain of the virus, authorities said. The infected bird was a migrating flamingo found on a Kuwait beach. The other was an imported falcon found to have the milder H5N2 variant."
In China, inactivated H5N2 has been used as a vaccine for H5N1. 
Japan's Health Ministry said May 11, 2006 that 93 poultry farm workers near Tokyo may have been exposed to H5N2 (which was not previously known to infect humans) in 2005. "Preliminary tests on the workers were positive for H5N2 antibodies, indicating they were previously exposed, Takimoto said. While exposure carries with it the possibility of infection and illness, he said none had tested positive for the virus itself or had developed flu symptoms.  About 5.7 million birds have been destroyed in Ibaraki following the H5N2 outbreaks."
In 2006, an H5N2 outbreak on a single farm in South Africa resulted in the destruction of all its sixty ostriches. The strain was similar to the one that caused outbreaks in South Africa 2004/2005. 
In 2007, a low-pathogenic strain of H5N2 was found in samples collected from 25,000 turkeys in Pendleton County, West Virginia in a routine testing prior to their slaughter. The birds showed no sign of illness or mortality. Measures were taken to prevent the virus from mutating and spreading.
In late 2007 (December 21), an H5N2 outbreak was found in the Dominican Republic, in a Suburb of Higuey City, on the eastern side of the island. 15 roosters and 2 hens where eliminated even though they had no visible sign of infection. 

# Sources
-   WHO
-    article Kuwait: Avian influenza H5N1 confirmed case in flamingo November 12, 2005
-  people.com.cn
-    article Japan workers may have been exposed to flu published May 12, 2006
-   Mail&Guardian South African online news article Outbreak of avian flu in W Cape not H5N1 published 03 July 2006
-   Regional News Service article Bird Flu Found in Pendleton County published April 3, 2007
-    Listin Diario Article"Detectan virus gripe aviar en Higuey y Santo Domingo" In Spanish
nl:H5N2
H5N8
H5N8 is a subtype of the species  Influenza A virus (sometimes called bird flu virus).
A highly pathogenic strain of it called A/turkey/Ireland/1378/83 caused a minor flu outbreak in 1983 in Ireland in turkeys.

# Sources
-  "Avian influenza A(H5N1)- update 31: Situation (poultry) in Asia: need for a long-term response, comparison with previous outbreaks". Epidemic and Pandemic Alert and Response. World Health Organization. 2004-03-02. Retrieved 2007-11-04..mw-parser-output cite.citation{font-style:inherit}.mw-parser-output q{quotes:"\"""\"""'""'"}.mw-parser-output code.cs1-code{color:inherit;background:inherit;border:inherit;padding:inherit}.mw-parser-output .cs1-lock-free a{background:url("")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-limited a,.mw-parser-output .cs1-lock-registration a{background:url("")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-subscription a{background:url("")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration{color:#555}.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration span{border-bottom:1px dotted;cursor:help}.mw-parser-output .cs1-hidden-error{display:none;font-size:100%}.mw-parser-output .cs1-visible-error{display:none;font-size:100%}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-format{font-size:95%}.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-wl-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right,.mw-parser-output .cs1-kern-wl-right{padding-right:0.2em}
-  Scientific Committee on Animal Health and Animal Welfare (2006-06-27). "The Definition of Avian Influenza : The use of Vaccination against Avian Influenza" (pdf). European Commission, Health & Consumer Protection Directorate-General. Retrieved 2007-11-04.

# Further reading
- Walker JA, Kawaoka Y (1993). "Importance of conserved amino acids at the cleavage site of the haemagglutinin of a virulent avian influenza A virus". J. Gen. Virol. 74 ( Pt 2): 3114. PMID 8429306. |access-date= requires |url= (help)