Persius/hicric huggingface dataset:
H7N2
H7N2 is a subtype of the species  Influenza A virus (sometimes called bird flu virus).

# Outbreaks of H7N2
One person Virginia, US in 2002 and one person in New York, US, in 2003 were found to have serologic evidence of infection from H7N2; both fully recovered.
In February 2004, an outbreak of low pathogenic avian influena (LPAI) A (H7N2) was reported on 2 chicken farms in Delaware and in four live bird markets in New Jersey supplied by the same farms. In March 2004, surveillance samples from a flock of chickens in Maryland tested positive for LPAI H7N2. It is likely that this was the same strain. 
A CDC study following the 2002 outbreaks of H7N2 in  commercial poultry farms in western Virginia concluded:
On 24 May 2007, an outbreak of H7N2 was confirmed at a poultry farm near Corwen, in Wales from tests on chickens that died from H7N2. The owners of the Conwy farm bought 15 Rhode Island Red chickens two weeks prior but all died from H7N2. The 32 other poultry at the site were slaughtered. A one kilometer exclusion zone was put in force around the property in which birds and bird products cannot be moved and bird gathering can only take place under licence. Nine people who were associated with the infected or dead  poultry and reported flu-like symptoms were tested. Four tested positive for evidence of infection from H7N2 and were successfully treated for mild flu. In early June it was discovered that the virus had spread to a poultry farm 70 miles (113 km) away near St. Helens in north-west England. All the poultry at the farm were slaughtered and a 1 km exclusion zone imposed.

# Sources
-  CDC
-  flu research
-   BBC physorg
-   Scotsman News article Mild bird flu virus spreads to north-west England June 8, 2007
- CDC avian flu information

# Further reading
- Research Update on H7n2 Avian Influenza Virus in Turkeys and Chickens
- Epidemiology of an H7N2 Avian Influenza Outbreak in Broilers in Pennsylvania in November 2001- January 2002
- Avian influenza H7N2 in Wales and the Northwest of England
- North Wales bird flu outbreak ends
H7N3
H7N3 is a subtype of the species  Influenza A virus (sometimes called bird flu virus).
In North America, the presence of H7N3 was confirmed at several poultry farms in British Columbia in February 2004.  As of April 2004, 18 farms had been quarantined to halt the spread of the virus.  Two cases of humans infected with it have been confirmed in that region. Symptoms included conjunctivitis and mild influenza-like illness. Both fully recovered.
"The H7N3 strain was first detected in turkeys in Britain in 1963 and made one of its last known appearances in poultry in Canada in April and May 2004, according to the WHO and World Organisation for Animal Health. An outbreak of the less virulent H5N2 strain of bird flu in Taiwan in 2004 led to the culling of hundreds of thousands of fowl." 
"Taiwan found a highly pathogenic strain of avian flu, H7N3, in droppings left by a migratory bird and is carrying out tests to see whether the virus has spread to nearby poultry farms, the agriculture department said 14 November 2005." 
For the first time since 1979, H7N3 was found in the UK in April 2006. It infected birds and one poultry worker (whose only symptom was conjunctivitis) in a Norfolk, England Witford Lodge Farm. "Antiviral Tamiflu was administered to poultry workers on the farm as a precautionary measure.  35,000 chickens will be culled in the infected farm and a 1 kilometre exclusion zone has been placed."
In September 27, 2007 another outbreak of H7N3 was detected in a poultry operation in Saskatchewan, Canada. The Canadian Food Inspection Agency has requested the euthanization of the flock, and the disinfection of all building, materials and equipment in contact with the birds or their droppings.

# Sources
-  Washington.edu
-  Washington.edu
-   Medical News Today article Norfolk Poultry Worker Contracts H7N3 Bird Flu Strain, UK published April 28, 2006
- CDC detailed analysis
- CDC - Novel Avian Influenza H7N3 Strain Outbreak, British Columbia

# Further reading
- Comparative Pathobiology of Low and High Pathogenicity H7N3 Chilean Avian Influenza Viruses in Chickens
de:Influenzavirus A/H7N3
HARS
Histidyl-tRNA synthetase  (HARS) also known as histidine-tRNA ligase, is an enzyme which in humans is encoded by the HARS gene.

# Function
Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene is a cytoplasmic enzyme which belongs to the class II family of aminoacyl tRNA synthetases. The enzyme is responsible for the synthesis of histidyl-transfer RNA, which is essential for the incorporation of histidine into proteins. The gene is located in a head-to-head orientation with HARSL on chromosome five, where the homologous genes share a bidirectional promoter.

# Clinical significance
The gene product is a frequent target of autoantibodies in the human autoimmune disease polymyositis/dermatomyositis.

# Interactions
HARS has been shown to interact with EEF1B2 and EEF1G.
HAS1
Hyaluronan synthase 1 is an enzyme that in humans is encoded by the HAS1 gene.

# Structure
Hyaluronan or hyaluronic acid (HA) is a high molecular weight unbranched polysaccharide synthesized by a wide variety of organisms from bacteria to mammals, and is a constituent of the extracellular matrix.  It consists of alternating glucuronic acid and N-acetylglucosamine residues that are linked by beta-1-3 and beta-1-4 glycosidic bonds.  HA is synthesized by membrane-bound synthase at the inner surface of the plasma membrane, and the chains are extruded via ABC-transporter into the extracellular space.

# Function
It serves a variety of functions, including space filling, lubrication of joints, and provision of a matrix through which cells can migrate.  HA is actively produced during wound healing and tissue repair to provide a framework for ingrowth of blood vessels and fibroblasts.  Changes in the serum concentration of HA are associated with inflammatory and degenerative arthropathies such as rheumatoid arthritis.  In addition, the interaction of HA with the leukocyte receptor CD44 is important in tissue-specific homing by leukocytes, and overexpression of HA receptors has been correlated with tumor metastasis.  HAS1 is a member of the newly identified vertebrate gene family encoding putative hyaluronan synthases, and its amino acid sequence shows significant homology to the hasA gene product of Streptococcus pyogenes, a glycosaminoglycan synthetase (DG42) from Xenopus laevis, and a recently described murine hyaluronan synthase.
HATS

# Objective
To assess the effects of lipid-lowering drugs and/or antioxidant vitamins on progression or regression of coronary heart disease as measured by quantitative angiography in patients with low high density lipoprotein (HDL) cholesterol.

# Methods
HDL-Atherosclerosis Treatment Study (HATS) was a randomized, 2 x 2 factorial study wherein 160 patients, both men and women with low HDL cholesterol, with at least one 50% stenotic coronary lesion or three 30% stenotic coronary lesions were enrolled.  All the patients were randomized into four groups which were simvastatin (10-20g/day) plus niacin (2-4g/day), antioxidant vitamins (vitamins E, C, A and selenium), simvastatin-niacin plus antioxidants; or placebos. The primary end points were arteriographic evidence of a change in coronary stenosis and the occurrence of a first cardiovascular event (death, myocardial infarction, stroke, or revascularization). Coronary angiograms were done at baseline and at three years to assess the change.

# Results
- In the simvastatin-niacin group mean LDL-C was reduced by 42% and mean HDL-C was increased by 26% while levels of LDL-C and HDL-C in the antioxidants and placebo groups remained unaltered.
- The rate of progression of coronary stenoses was lower in the simvastatin-niacin group compared to the other groups.
- Patients receiving simvastatin and niacin sustained lower cardiovascular events.
- Antioxidant vitamins alone had no benefit on progression or on clinical events.

# Conclusion
Addition of a drug that increases HDL-C levels to a statin proves to have additional protection over just statin alone.
HAX1
HCLS1-associated protein X-1 is a protein that in humans is encoded by the HAX1 gene.
The protein encoded by this gene is known to associate with HS1, a substrate of Src family tyrosine kinases. It also interacts with the product of PKD2 gene, mutations in which are associated with autosomal-dominant polycystic kidney disease, and with F-actin-binding protein, cortactin. It was earlier thought that this gene product is mainly localized in the mitochondria, however, recent studies indicate it to be localized in the cell body. Two transcript variants encoding different isoforms have been found for this gene.
In 2015, localization of the protein to P-bodies was demonstrated.

# Severe congenital neutropenia
Homozygous mutations in HAX1 are associated with autosomal recessive severe congenital neutropenia, also known as Kostmann syndrome.

# Interactions
HAX1 has been shown to interact with IL1A.  The protein has also been shown to interact with the 3' untranslated regions of vimentin and DNA polymerase B transcripts.
HBA1
Hemoglobin, alpha 1, also known as HBA1, is a human gene encoding the hemoglobin protein.
"The human alpha globin gene cluster located on chromosome 16 spans about 30 kb and includes seven loci: 5'- zeta - pseudozeta - mu - pseudoalpha-1 - alpha-2 - alpha-1 - theta - 3'. The alpha-2 (HBA2) and alpha-1 (HBA1) coding sequences are identical. These genes differ slightly over the 5' untranslated regions and the introns, but they differ significantly over the 3' untranslated regions. Two alpha chains plus two beta chains constitute HbA, which in normal adult life comprises about 97% of the total hemoglobin; alpha chains combine with delta chains to constitute HbA-2, which with HbF (fetal hemoglobin) makes up the remaining 3% of adult hemoglobin. Alpha thalassemias result from deletions of each of the alpha genes as well as deletions of both HBA2 and HBA1; some nondeletion alpha thalassemias have also been reported."

# Gene

## Transcriptions
"The 3' flanking area contained the highly conserved hexanucleotide sequence A-A-T-A-A-A found in eukaryotic messages between the terminator codon and the polyadenylylation site (44)."
HCN1
Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1 is a protein that in humans is encoded by the HCN1 gene.

# Function
Hyperpolarization-activated cation channels of the HCN gene family, such as HCN1, contribute to spontaneous rhythmic activity in both heart and brain.

# Tissue distribution
HCN1 channel expression is found in the sinoatrial node, the neocortex, hippocampus, cerebellar cortex, dorsal root ganglion, trigeminal ganglion and brainstem.

# Interactions
HCN1 has been shown to interact with HCN2.

# Epilepsy
De novo mutations in HCN1 cause                 epilepsy            .
HEXB
Beta-hexosaminidase subunit beta is an enzyme that in humans is encoded by the HEXB gene.
Hexosaminidase B is the beta subunit of the lysosomal enzyme beta-hexosaminidase that, together with the cofactor GM2 activator protein, catalyzes the degradation of the ganglioside GM2, and other molecules containing terminal N-acetyl hexosamines.  Beta-hexosaminidase is composed of two subunits, alpha and beta, which are encoded by separate genes.  Both beta-hexosaminidase alpha and beta subunits are members of family 20 of glycosyl hydrolases.  Mutations in the alpha or beta subunit genes lead to an accumulation of GM2 ganglioside in neurons and neurodegenerative disorders termed the GM2 gangliosidoses.  Beta subunit gene mutations lead to Sandhoff disease (GM2-gangliosidosis type II).

# Structure

## Gene
The HEXB gene lies on the chromosome location of 5q13.3 and consists of 15 exons, spanning 35-40Kb.

## Protein
HEXB consists of 556 amino acid residues and weighs 63111Da.

# Function
HEXB is one of the two subunits forming -hexosaminidase which functions as a glycosyl hydrolase that remove -linked nonreducing-terminal GalNAc or GlcNAc residues in the lysosome. Inability of HEXB will lead to-hexosaminidase defect and result in a group of recessive disorders called GM2 gangliosidoses, characterized by the accumulation of GM2 ganglioside.

# Clinical significance
Genetic defects in HEXB can result in the accumulation of GM2 ganglioside in neural tissues and two of three lysosomal storage diseases collectively known as GM2 gangliosidosis, of which Sandhoff disease (defects in the  subunit) is the best studied one. Patients present with neurosomatic manifestations. Therapeutic effects of Hex subunit gene transduction have been examined on Sandhoff disease model mice. Intracerebroventricular administration of the modified -hexosaminidase B to Sandhoff mode mice restored the -hexosaminidase activity in the brains, and reduced the GM2 ganglioside storage in the parenchyma.

# Interactions
HEXB has been found to interact with HEXA and ganglioside.
HEY2
Hairy/enhancer-of-split related with YRPW motif protein 2 (HEY2) also known as cardiovascular helix-loop-helix factor 1 (CHF1) is a protein that in humans is encoded by the HEY2 gene.

# Function
CHF1 is a member of the hairy and enhancer of split-related (HESR) family of basic helix-loop-helix (bHLH)-type transcription factors. The encoded protein forms homo- or hetero-dimers that localize to the nucleus and interact with a histone deacetylase complex to repress transcription. Expression of this gene is induced by the Notch signaling pathway. Two similar and redundant genes in mouse are required for embryonic cardiovascular development, and are also implicated in neurogenesis and somitogenesis. Alternatively spliced transcript variants have been found, but their biological validity has not been determined.

# Clinical significance
Common variants of SCN5A, SCN10A, and HEY2 (this gene) are associated with Brugada syndrome.

# Interactions
HEY2 has been shown to interact with Sirtuin 1 and Nuclear receptor co-repressor 1.
HHEX
Hematopoietically-expressed homeobox protein HHEX is a protein that in humans is encoded by the HHEX gene.
This gene encodes a member of the homeobox family of transcription factors, many of which are involved in developmental processes. Expression in specific hematopoietic lineages suggests that this protein may play a role in hematopoietic differentiation.

# Function
The HHEX transcription factor acts as a promoter in some instances and an inhibitor others. It interacts with a number of other signaling molecules to play an important role in the development of multiple organs, such as the liver, thyroid and forebrain. HHEX serves to repress VEGFA, another protein which is important in endothelial cell development. SCL, a significant transcription factor for blood and endothelial cell differentiation, is shown to interact with HHEX to promote the correct development of the hematopoiesis process. HHEX appears to work together with another molecule, -catenin, for the development of the anterior organizer. It also contributes to developmental remodeling and stabilization of endothelial cells in an unborn organism. The importance of this transcription factor is illustrated by the inability of HHEX knockout mice embryos to survive gestation. Without the expression of HHEX, these mice embryos die in utero between Day 13 and Day 16. HHEX knockout mice display a range of abnormalities including forebrain abnormalities in various levels of severity, as well as a number of other defects including heart, vasculature, liver, monocyte, and thyroid abnormalities.

# Interactions
HHEX has been shown to interact with Promyelocytic leukemia protein.
HIRA
Protein HIRA is a protein that in humans is encoded by the HIRA gene. This gene is mapped to 22q11.21, centromeric to COMT.

# Function
The specific function of this protein has yet to be determined; however, it has been speculated to play a role in transcriptional regulation and/or chromatin and histone metabolism.
Research done by Salome Adam, Sophie E. Polo, and Genevieve Almouzni indicate that HIRA proteins are involved in restarting transcription after UVC damage Function of HIRA gene can be effectively examined by siRNA knockdown based on an independent validation.

# Clinical significance
It is considered the primary candidate gene in some haploinsufficiency syndromes such as DiGeorge syndrome, and insufficient production of the gene may disrupt normal embryonic development.

# Model organisms
Model organisms have been used in the study of HIRA function. A conditional knockout mouse line, called Hiratm1a(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 two tests were carried out on mutant mice and two significant abnormalities were observed. No homozygous mutant mice survived until weaning. The remaining tests were carried out on heterozygous mutant adult mice and a decreased leukocyte cell number was recorded in male animals.

# Interactions
HIRA has been shown to interact with HIST1H2BK.
HLTF
Helicase-like transcription factor is an enzyme that in humans is encoded by the HLTF gene.

# Function
This gene encodes a member of the SWI/SNF family. Members of this family have helicase and ATPase activities and are thought to regulate transcription of certain genes by altering the chromatin structure around those genes. The encoded protein contains a RING finger DNA binding motif. Two transcript variants encoding the same protein have been found for this gene. However, use of an alternative translation start site produces an isoform that is truncated at the N-terminus compared to the full-length protein.
HLTF is a double-stranded DNA translocase, one of two human homologs of Saccharomyces cerevisiae RAD5 besides SHPRH (SNF2 histone linker PHD RING helicase), that is able to carry out fork regression, similarly to Rad5.

# Interactions
HLTF has been shown to interact with UBE2N,.
HM13
Minor histocompatibility antigen H13 is a protein that in humans is encoded by the HM13 gene.

# Function
The minor histocompatibility antigen 13 is a nonamer peptide that originates from a protein encoded by the H13 gene. The peptide is generated by the cytosol by the proteasome, enters the endoplasmic reticulum (ER) lumen by the transporter associated with antigen processing (TAP) and is presented on the cell surface on H2-Db major histocompatibility anigen I (MHC I) molecules. The alloreactivity, which leads to transplant rejection in mice, is conferred by Val/Ile polymorphism in the SSV(V/I)GVWYL peptide. The orthologue gene in humans is called HM13. If a related polymorphism exists, and if the HM13 serves as a Minor histocompatibility antigen, however, remains to be addressed.
The protein encoded by the M13/HM13 gene is the signal peptide peptidase (SPP), an ER-resident intramembrane protease.
SPP localizes to the endoplasmic reticulum, catalyzes intramembrane proteolysis of some signal peptides after they have been cleaved from a preprotein. This activity is required to generate signal sequence-derived human lymphocyte antigen-E epitopes that are recognized by the immune system, and to process hepatitis C virus core protein. The encoded protein is an integral membrane protein with sequence motifs characteristic of the presenilin-type aspartic proteases. Multiple transcript variants encoding several different isoforms have been found for this gene.
HPS4
Hermansky-Pudlak syndrome 4 protein is a protein that in humans is encoded by the HPS4 gene.
Hermansky-Pudlak syndrome is a disorder of organelle biogenesis in which oculocutaneous albinism, bleeding, and pulmonary fibrosis result from defects of melanosomes, platelet dense granules, and lysosomes. Mutations in this gene as well as several others can cause this syndrome. The protein encoded by this gene appears to be important in organelle biogenesis and is similar to the mouse 'light ear' protein. Five transcript variants encoding different isoforms have been found for this gene. In addition, transcript variants utilizing alternative polyadenylation signals exist.
In melanocytic cells HPS4 gene expression may be regulated by MITF.
HPS6
Hermansky-Pudlak syndrome 6 (HPS6) also known as ruby-eye protein homolog (Ru) is a protein that in humans is encoded by the HPS6 gene.

# Function
This intronless gene encodes a protein that may play a role in organelle biogenesis associated with melanosomes, platelet dense granules, and lysosomes. HPS6 along with HPS3 and HPS5 form a stable protein complex named Biogenesis of Lysosome-related Organelles Complex-2 (BLOC-2).

# Clinical significance
Mutations in this gene are associated with HermanskyPudlak syndrome type 6  characterized by albinism and prolonged bleeding.
HSF2
Heat shock factor protein 2 is a protein that in humans is encoded by the HSF2 gene.

# Function
HSF2, as well as the related gene HSF1, encodes a protein that binds specifically to the heat-shock element and has homology to HSFs of other species. Heat shock transcription factors activate heat-shock response genes under conditions of heat or other stresses. Although the names HSF1 and HSF2 were chosen for historical reasons, these peptides should be referred to as heat-shock transcription factors.

# Interactions
HSF2 has been shown to interact with Nucleoporin 62 and HSF1.
TSC1
Tuberous sclerosis 1 (TSC1), also known as Hamartin, is a protein that in humans is encoded by the TSC1 gene.

# Function
TSC1 functions as a co-chaperone which inhibits the ATPase activity of the chaperone Hsp90 (heat shock protein-90) and decelerates its chaperone cycle.  Tsc1 functions as a facilitator of Hsp90 in chaperoning the kinase and non-kinase clients including Tsc2, therefore preventing their ubiquitination and degradation in the proteasome. TSC1, TSC2 and TBC1D7 is a multi-protein complex also known as the TSC complex. This complex negatively regulates mTORC1 signaling by functioning as a GTPase-activating protein (GAP) for the small GTPase Rheb, an essential activator of mTORC1. The TSC complex has been implicated as a tumor suppressor.

# Clinical significance
Defects in this gene can cause tuberous sclerosis, due to a functional impairment of the TSC complex. Defects in TSC1 may also be a cause of focal cortical dysplasia. TSC1 may be involved in protecting brain neurons in the CA3 region of the hippocampus from the effects of stroke.

# Interactions
TSC1 has been shown to interact with:
- AKT1,
- HSP70 
- HSP90 
- NEFL,
- PLK1,  and
- TSC2.