Persius/hicric huggingface dataset:
GPR88
Probable G-protein coupled receptor 88 is a protein that in humans is encoded by the GPR88 gene.
- Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (12): 1714. doi:10.1016/0378-1119(94)90802-8. PMID 8125298..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}
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K,  et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (12): 14956. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- Mizushima K, Miyamoto Y, Tsukahara F,  et al. (2001). "A novel G-protein-coupled receptor gene expressed in striatum". Genomics. 69 (3): 31421. doi:10.1006/geno.2000.6340. PMID 11056049.
- Strausberg RL, Feingold EA, Grouse LH,  et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Van Waes V, Tseng K, Steiner H (2011). "GPR88 - a putative signaling molecule predominantly expressed in the striatum: Cellular localization and developmental regulation". Basal Ganglia. 1 (2): 8389. doi:10.1016/j.baga.2011.04.001. PMC 3144573. PMID 21804954.
GPR97
G-protein coupled receptor 97 also known as adhesion G protein-coupled receptor G3 (ADGRG3) is a protein that in humans is encoded by the ADGRG3 gene. GPR97 is a member of the adhesion GPCR family.
Adhesion GPCRs are characterized by an extended extracellular region often possessing N-terminal protein modules that is linked to a TM7 region via a domain known as the GPCR-Autoproteolysis INducing (GAIN) domain.
GPR97 is expressed in human granulocytes and endothelial cells of the vasculature as well as in mouse granulocytes, monocytes, macrophages, and dendritic cells.

# Signaling
The inositol phosphate (IP3) accumulation, aequorin, and 35S isotope binding assays in overexpressing HEK293 cells have demonstrated coupling of GPR97 to Go protein triggering cyclic adenosine monophosphate (cAMP). GPR97 actives cAMP response element-binding protein (CREB), NF-B, and small GTPases to regulate cellular functions.

# Function
Systemic steroid exposure is a therapy to treat a variety of medical conditions and is associated with epigenetic processes such as DNA methylation that may reflect pharmacological responses and/or side effects. GPR97 was found to be differently methylated at CpG sites in the genome of blood cells from patient under systemic steroid treatment. GPR97 is transcribed in immune cells. Gene-deficient mice revealed that Gpr97 is crucial for maintaining B-cell population via constitutive CREB and NF-B activities. Human lymphatic endothelial cells (LECs) abundantly express GPR97. Silencing GPR97 in human LECs indicated that GPR97 modulates cytoskeletal rearrangement, cell adhesion and migration through regulating the small GTPase RhoA and cdc42. In vertebrates, GPR97 has an indispensable role in the bone morphogenetic proteins (BMP) signaling pathway in bone formation. A microarray meta-analysis revealed that mouse Gpr97 is a direct transcriptional target of BMP signaling in long bone development.
GPR98
G protein-coupled receptor 98, also known as GPR98 or VLGR1, is a protein that in humans is encoded by the GPR98 gene. Several alternatively spliced transcripts have been described.
The adhesion GPCR Very Large GPCR receptor 1 (Vlg1R1) is the largest GPCR known, with a size of 6300 amino acids and consisting of 90 exons.   There are 8 splice variants of VlgR1, named VlgR1a-1e and Mass1.1-1.3.  The N-terminus consists of 5800 amino acids containing 35 Calx-beta domains, one pentraxin domain, and one epilepsy associated repeat.  Mutations of VlgR1 have been shown to result in Usher's syndrome.  Knockouts of Vlgr1 in mice have been shown to phenocopy Usher's syndrome and lead to audiogenic seizures.

# Function
This gene encodes a member of the adhesion-GPCR family of receptors. The protein binds calcium and is expressed in the central nervous system. It is also known as very large G-protein coupled receptor 1 because it is 6300 residues long. It contains a C-terminal 7-transmembrane receptor domain, whereas the large N-terminal segment (5900 residues) includes 35 calcium binding Calx-beta domains, and 6 EAR domains.

# Evolution
The Sea Urchin genome has a homolog of VLGR1 in it.

# Clinical significance
Mutations in this gene are associated with Usher syndrome 2 and familial febrile seizures.
GPSM2
G-protein-signaling modulator 2, also called LGN for its 10 Leucine-Glycine-Asparagine repeats, is a protein that in humans is encoded by the GPSM2 gene.

# Function
Heterotrimeric G proteins transduce extracellular signals received by cell surface receptors into integrated cellular responses. GPSM2 belongs to a group of proteins that modulate activation of G proteins (Blumer et al., 2002).

# Interactions
GPSM2 has been shown to interact with nuclear mitotic apparatus protein 1 and GNAI2.
GRACE

# Overview
GRACE (the Global Registry of Acute Coronary Events) is a large, prospective, multinational observational study of patients hospitalized with ACS. The aim of GRACE is to improve the quality of care for patients with ACS by describing differences in, and relationships between, patient characteristics, treatment practices, and in-hospital and postdischarge outcomes at hospitals around the world. 

# Methods
A total of 73 hospitals with on-site angiographic facility in 14 countries in North America, South America, Europe, Australia, and New Zealand were collaborated in GRACE and enrolled 24,189 patients.
Clusters were chosen on the basis of local demographic characteristics and hospital facilities to ensure a representative sample of patients with ACS from each country. Patients are identified by use of either active or passive surveillance approaches.
A standardized core case report form is completed for all patients. Information on patient demographics, medical history, acute symptoms, clinical characteristics, electrocardiographic findings, treatment approaches, and in-hospital outcomes is collected.
Patients are followed up at 6 months after hospital discharge to identify recurrent coronary events, use of various medications, and mortality.

# Conclusions
The information collected from the GRACE project provides important and extensive insights into patient demographic and clinical characteristics, current practice patterns, and outcomes for patients with ACS from a number of countries throughout the world. Given the pressures of practicing evidence-based medicine, the results of GRACE should provide a multinational perspective into these important outcomes and identify practice variations that will allow new opportunities to improve patient care.
GRB10
Growth factor receptor-bound protein 10 also known as insulin receptor-binding protein Grb-IR is a protein that in humans is encoded by the GRB10 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 insulin receptors and insulin-like growth-factor receptors (e.g., IGF1R and IGF2R). Overexpression of some isoforms of the encoded protein inhibits tyrosine kinase activity and results in growth suppression. This gene is imprinted in a highly isoform- and tissue-specific manner. Alternatively spliced transcript variants encoding different isoforms have been identified.

# Animal studies
Mice whose paternally inherited Grb10 gene is inactivated are more aggressive while those whose maternally inherited allele is inactivated exhibit foetal overgrowth and are significantly bigger than wild-type litter-mates.

# Interactions
GRB10 has been shown to interact with
- Abl gene,
- BCR gene,
- C-Raf,
- c-Kit,
- Insulin receptor,
- Insulin-like growth factor 1 receptor,
- MAP2K1, and
- RET proto-oncogene.
GRB14
Growth factor receptor-bound protein 14 is a protein that in humans is encoded by the GRB14 gene.
The product of this gene belongs to a small family of adapter 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 insulin receptors and insulin-like growth-factor receptors. This protein likely has an inhibitory effect on receptor tyrosine kinase signaling and, in particular, on insulin receptor signaling. This gene may play a role in signaling pathways that regulate growth and metabolism. Transcript variants have been reported for this gene, but their full-length natures have not been determined to date.

# Interactions
GRB14 has been shown to interact with Epidermal growth factor receptor, Fibroblast growth factor receptor 1 and TNKS2.
GRIA1
Glutamate receptor 1 is a protein that in humans is encoded by the GRIA1 gene.

# Function
Glutamate receptors are the predominant excitatory neurotransmitter receptors in the mammalian brain and are activated in a variety of normal neurophysiologic processes. These receptors are heteromeric protein complexes with multiple subunits, each possessing transmembrane regions, and all arranged to form a ligand-gated ion channel. The classification of glutamate receptors is based on their activation by different pharmacologic agonists. The GRIA1 belongs to a family of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA) receptors. Each of the members (GRIA1-4) include flip and flop isoforms generated by alternative RNA splicing. The receptor subunits encoded by each isoform vary in their signal transduction properties. The isoform presented here is the flop isoform. In situ hybridization experiments showed that human GRIA1 mRNA is present in granule and pyramidal cells in the hippocampal formation.
GRIA1 (GluR1) is centrally involved in synaptic plasticity.  Expression of the GluR1 gene is significantly reduced in the human frontal cortex with increasing age.

# Interactions
GRIA1 has been shown to interact with:
- DLG1
- EPB41L2, and
- GRID2.
GRID1
Glutamate receptor delta-1 subunit also known as GluD1 or GluR1 is a protein that in humans is encoded by the GRID1 gene.

# Function
This gene encodes a subunit of glutamate receptor ligand-gated ion channel. These channels mediate most of the fast excitatory synaptic transmission in the central nervous system and play key roles in synaptic plasticity.

# Clinical significance
Several genetic epidemiology studies have shown a strong association between several variants of the GRID1 gene and increased risk of developing schizophrenia.
GRID2
Glutamate receptor, ionotropic, delta 2, also known as GluD2, GluR2, or 2, is a protein that in humans is encoded by the GRID2 gene. This protein together with GluD1 belongs to the delta receptor subtype of ionotropic glutamate receptors. They possess 1424% sequence homology with AMPA, kainate, and NMDA subunits, but, despite their name, do not actually bind glutamate or various other glutamate agonists.
delta iGluRs have long been considered orphan receptors as their endogenous ligand was unknown. They are now believed to bind glycine and D-serine but these do not result in channel opening.

# Function
GluD2-containing receptors are selectively/predominantly expressed in Purkinje cells in the cerebellum where they play a key role in synaptogenesis, synaptic plasticity, and motor coordination.
GluD2 induces synaptogenesis through interaction of its N-terminal domain with Cbln1, which in turn interacts with presynaptic neurexins, forming a bridge across cerebellar synapses.
The main functions of GluD2 in synaptic plasticity are carried out by its intracellular C-terminus. This is regulated by D-serine, which binds to the ligand-binding domain and results in changes in the structure of GluD2 without opening the channel. These changes may signal up to the N-terminal domain or down to the C-terminal domain to alter protein-protein interactions.

# Pathology
A heterozygous deletion in GRID2 in humans causes a complicated spastic paraplegia with ataxia, frontotemporal dementia, and lower motor neuron involvement whereas a homozygous biallelic deletion leads to a syndrome of cerebellar ataxia with marked developmental delay, pyramidal tract involvement and tonic upgaze, that can be classified as an ataxia with oculomotor apraxia (AOA) and has been named spinocerebellar ataxia, autosomal recessive type 18 (SCAR18).
A gain of channel function, resulting from a point mutation in mouse GRID2, is associated with the phenotype named 'lurcher', which in the heterozygous state leads to ataxia and motor coordination deficits resulting from selective, cell-autonomous apoptosis of cerebellar Purkinje cells during postnatal development.  Mice homozygous for this mutation die shortly after birth from massive loss of mid- and hindbrain neurons during late embryogenesis.

# Ligands
9-Aminoacridine, 9-tetrahydroaminoacridine, N1-dansyl-spermine, N1-dansyl-spermidine, and pentamidine have been shown to act as antagonists of 2-containing receptors.

# Interactions
GRID2 has been shown to interact with GOPC, GRIK2, PTPN4 and GRIA1. A possible correlation between GRID2 and the pre-B lymphocyte protein 3 (VPREB3) has been suggested, due to the apparent importance of B-lymphocytes in the origins of cerebellar Purkinje neurons in humans. Morphological studies conducted in GRID2-knockout mice suggest that GRID2 may be present in lymphocytes as well as in the adrenal cortex, however further studies must be conducted to confirm these claims.
GRIK4
GRIK4 (glutamate receptor, ionotropic, kainate 4) is a kainate receptor subtype belonging to the family of ligand-gated ion channels which is encoded by the GRIK4 gene.

# Function
This gene encodes a protein that belongs to the glutamate-gated ionic channel family. Glutamate functions as the major excitatory neurotransmitter in the central nervous system through activation of ligand-gated ion channels and G protein-coupled membrane receptors. The protein encoded by this gene forms functional heteromeric kainate-preferring ionic channels with the subunits encoded by related gene family members.

# Clinical significance
A single nucleotide polymorphism (rs1954787) in the GRIK4 gene has shown a treatment-response-association with antidepressant treatment.
Variation in GRIK4 have been associated with both increased and decreased risk of bipolar disorder. A possible mechanism for this observation is that the sequence variation influences secondary structures in the 3' UTR.
Interfering with GRIK4/KA1 function with a specific anti-KA1 antibody protects against kainate-induced neuronal cell death.
A test of that gene can be made in order to know if a depressed patient will respond to the SSRI citalopram.

# Evolutionary significance
The GRIK4 gene displayed significantly higher rates of evolution in primates than in rodents and especially in the lineage leading from primates to humans.  Furthermore, the GRIK4 gene is implicated in the development of the nervous system.  Hence evolution of the GRIK4 gene is thought to have played a role in the dramatic increases in size and complexity of the brain that occurred during evolutionary history leading to humans.
GSK3A
Glycogen synthase kinase-3 alpha is an enzyme that in humans is encoded by the GSK3A gene.
Glycogen synthase kinase 3-alpha EC 2.7.1.37 is a multifunctional protein serine kinase, homologous to Drosophila 'shaggy' (zeste-white3) and implicated in the control of several regulatory proteins including glycogen synthase and various transcription factors (e.g., JUN). It also plays a role in the WNT and phosphoinositide 3-kinase (especially PIK3CG) signaling pathways.

# Model organisms
Model organisms have been used in the study of GSK3A function. A conditional knockout mouse line, called Gsk3atm1a(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 one tests were carried out on mutant mice but no significant abnormalities were observed.
GSK3B
Glycogen synthase kinase 3 beta, also known as GSK3B, is an enzyme that in humans is encoded by the GSK3B gene.  In mice, the enzyme is encoded by the GSK-3 gene. Abnormal regulation and expression of GSK3 is associated with an increased susceptibility towards bipolar disorder.

# Function
Glycogen synthase kinase-3 (GSK-3) is a proline-directed serine-threonine kinase that was initially identified as a phosphorylating and an inactivating agent of glycogen synthase. Two isoforms, alpha (GSK3A) and beta, show a high degree of amino acid homology.  GSK3B is involved in energy metabolism, neuronal cell development, and body pattern formation. It might be a new therapeutic target for ischemic stroke.

# Loss of function mutations
Homozygous disruption of the GSK-3 locus in mice results in embryonic lethality during mid-gestation.  This lethality phenotype could be rescued by inhibition of tumor necrosis factor.

# Signaling pathways
Pharmacological inhibition of ERK1/2 restores GSK3 activity and protein synthesis levels in a model of tuberous sclerosis.

# Interactions
GSK3B has been shown to interact with:
- KIAA1211L
- AKAP11,
- AXIN1,
- AXIN2,
- AR,
- CTNNB1,
- DNM1L,
- MACF1
- MUC1,
- SMAD3
- NOTCH1,
- NOTCH2,
- P53,
- PRKAR2A,
- SGK3,  and
- TSC2.
GSTA4
Glutathione S-transferase A4, also known as GSTA4, is an enzyme which in humans is encoded by the GSTA4 gene.

# Function
Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. These enzymes are involved in cellular defense against toxic, carcinogenic, and pharmacologically active electrophilic compounds. At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta. This gene encodes a glutathione S-transferase belonging to the alpha class. The alpha class genes, which are located in a cluster on chromosome 6, are highly related and encode enzymes with glutathione peroxidase activity that function in the detoxification of lipid peroxidation products.
GSTA4 shows very high activity with reactive carbonyl compounds such as alk-2-enals. GSTA4 is highly effective in catalyzing the conjugate addition of reduced glutathione to 4-hydroxynonenal, an important product of peroxidative degradation of arachidonic acid and a commonly used biomarker for oxidative damage in tissue.

# Clinical significance
Reactive electrophiles produced by oxidative metabolism have been linked to a number of degenerative diseases including Parkinson's disease, Alzheimer's disease, cataract formation, and atherosclerosis hence reduced expression of the GSTA4 enzyme may have pathophysiological consequences. The expression of this gene is decreased drastically among burn and trauma victims.
GSTM4
Glutathione S-transferase Mu 4 is an enzyme that in humans is encoded by the GSTM4 gene.
Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta. This gene encodes a glutathione S-transferase that belongs to the mu class. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are organized in a gene cluster on chromosome 1p13.3 and are known to be highly polymorphic. These genetic variations can change an individual's susceptibility to carcinogens and toxins as well as affect the toxicity and efficacy of certain drugs. Diversification of these genes has occurred in regions encoding substrate-binding domains, as well as in tissue expression patterns, to accommodate an increasing number of foreign compounds. Multiple transcript variants, each encoding a distinct protein isoform, have been identified.
In the August 2009 issue of Oncogene journal, researchers at Huntsman Cancer Institute (HCI) at the University of Utah demonstrated that expression levels of GSTM4 could predict response to chemotherapy in patients with Ewing's Sarcoma.  The study found that patients who did not respond to chemotherapy had high levels of GSTM4.
GSTP1
Glutathione S-transferase P is an enzyme that in humans is encoded by the GSTP1 gene.

# Function
Glutathione S-transferases (GSTs) are a family of enzymes that play an important role in detoxification by catalyzing the conjugation of many hydrophobic and electrophilic compounds with reduced glutathione.  Based on their biochemical, immunologic, and structural properties, the soluble GSTs are categorized into four main classes: alpha, mu, pi, and theta.  The glutathione S-transferase pi gene (GSTP1) is a polymorphic gene encoding active, functionally different GSTP1 variant proteins that are thought to function in xenobiotic metabolism and play a role in susceptibility to cancer, and other diseases.

# Interactions
GSTP1 has been shown to interact with Fanconi anemia, complementation group C and MAPK8.
GST-Pi is expressed in many human tissues, particularly in the biliary tree and renal distal convoluted tubules.It the most common gene alteration in ca prostate  (hyper methylation)

# Possible drug target
Triple-negative breast cancer cells rely on glutathione-S-transferase Pi1, and inhibitors are being studied.  Piperlongumine has been found to silence the gene.