Persius/hicric huggingface dataset:
ICAM2
Intercellular adhesion molecule 2 (ICAM2), also known as CD102 (Cluster of Differentiation 102), is a human gene, and the protein resulting from it.

# Protein structure
The protein encoded by this gene is a member of the intercellular adhesion molecule (ICAM) family. All ICAM proteins are type I transmembrane glycoproteins, contain 29 immunoglobulin-like C2-type domains, and bind to the leukocyte adhesion LFA-1 protein.

# Protein functions
ICAM-2 molecules regulate spermatid adhesion on Sertoli cell on the apical side of the blood-testis barrier (towards the lumen), thus playing a major role in spermatogenesis.
This protein may also play a role in lymphocyte recirculation by blocking LFA-1-dependent cell adhesion. It mediates adhesive interactions important for antigen-specific immune response, NK-cell mediated clearance, lymphocyte recirculation, and other cellular interactions important for immune response and surveillance.

# Interactions
ICAM2 has been shown to interact with EZR.
ICAM4
The LW blood system was first described by Landsteiner and Wiener in 1940. It was often confused with the Rh system, not becoming a separate antigen system until 1982. The LW and RhD antigens are genetically independent though they are phenotypically related and the LW antigen is expressed more strongly on RhD positive cells than on RhD negative cells. In most populations, the antithetical LW antigens, LWa and LWb are present as very high and very low frequency, respectively.

# Genomics
The LW locus is located on the short arm of chromosome 19 (19p13.3).

# Molecular biology
LW antigens reside on a 40- to 42-kiloDalton red cell membrane glycoprotein named CD242. The LW glycoprotein has recently been renamed ICAM-4 due to its similarity to intercellular adhesion molecule, although exactly which integrins bind to ICAM-4 is subject to controversy.
The function of ICAM-4 is not fully understood but appears to be restricted to erythroid cells. During in vitro erythropoesis, LW appears at either the erythroid colony forming stage or later at the proerythroblast stage. A vital part of erythropoesis is the clustering of erythroblasts around bone marrow macrophages to form erythroblastic islands. The erythroblast is then able to remove its nucleus, which is in turn ingested and broken down by the macrophages, to become a mature erythrocyte. During this process ICAM-4 binds to VLA-4, an erythroblast binding site, on adjacent erythroblasts and to v integrins on macrophages to help stabilise the erythroblastic islands. The binding of red cells to macrophages in the spleen by ICAM-4 could also play a part in the removal of senescent red cells.
Despite the functional aspects of ICAM-4, its apparent absence in LW(a-b-) and Rhnull phenotypes does not appear to lead to any obvious pathological effects. ICAM-4 expression is elevated on sickle red cells and its binding to v integrins on the endothelial cells may cause the pain associated with sickle cell crises.
Auto anti-LW is not uncommon as an autoantibody but usually presents with transient suppression of the LW antigen in genetically LW+ individuals, and so appears to be an alloantibody. True alloanti-LW is a very rare occurrence, with only two known examples of alloanti-LWab, produced by patients with an LW(a-b-) phenotype. Anti-LW can be present as a clinically insignificant autoantibody and not be associated with increased red cell destruction. Anti-LW has also been associated with cases of warm type autoimmune haemolytic anaemia; Philip Levine suggested that it was the most common antibody in cases of AIHA with a positive Coombs test.

# Transfusion medicine
Haemolytic disease of the newborn (HDFN) due to alloanti-LW is described as mild and very rare, even the very potent anti-LWab of one known patient caused minimal evidence of HDFN in her three pregnancies. To date auto anti-LW has only been implicated as the cause of one case of HDFN.
IFRD1
Interferon-related developmental regulator 1 is a protein that in humans is encoded by the IFRD1 gene. The gene is expressed mostly in neutrophils, skeletal and cardiac muscle, brain, pancreas.
The rat and the mouse homolog genes of interferon-related developmental regulator 1 gene (and their proteins) are also known with the name PC4  and Tis21, respectively. 
IFRD1 is member of a gene family that comprises a second gene, IFRD2, also known as SKmc15.

# Clinical significance
IFRD1 has been identified as a modifier gene for cystic fibrosis lung disease. In humans, neutrophil effector function is dependent on the type of IRFD1 polymorphism present in the individual. Human and mouse data both indicate that IFRD1 has a sizable impact on cystic fibrosis pathogenesis by regulating neutrophil effector function. 

# Inducer of muscle regeneration
IFRD1(also known as PC4 or Tis7, see above) participates to the process of skeletal muscle cell differentiation. In fact, inhibition of IFRD1 function in C2C12 myoblasts, by antisense IFRD1 cDNA transfection or microinjection of anti-IFRD1 antibodies, prevents their morphological and biochemical differentiation by inhibiting the expression of MyoD and myogenin, key master genes of muscle development. A role for IFRD1 in muscle differentiation has been observed also in vivo. Muscles from mice lacking IFRD1 display decreased protein and mRNA levels of MyoD, and myogenin, and after muscle crash damage in young mice there was a delay in regeneration.
Recently it has been shown that upregulation of IFRD1 in vivo in injured muscle potentiates muscle regeneration by increasing the production of staminal muscle cells (satellite cells). The underlying molecular mechanism lies in the ability of IFRD1 to cooperate with MyoD at inducing the transcriptional activity of MEF2C. This relies on the ability of IFRD1 to bind selectively MEF2C, thus inhibiting its interaction with HDAC4. Therefore, IFRD1 appears to act as a positive cofactor of MyoD. More recently it has been shown that IFRD1 potentiates muscle regeneration by a second mechanism that potentiates MyoD, i.e., by repressing the transcriptional activity of NF-B, which is known to inhibit MyoD mRNA accumulation. IFRD1 represses the activity of NF-B p65 by enhancing the HDAC-mediated deacetylation of the p65 subunit,  by favoring the recruitment of HDAC3 to p65. In fact IFRD1 forms trimolecular complexes with p65 and HDAC3.
Thus, IFRD1 can induce muscle regeneration acting as a pivotal regulator of the MyoD pathway through multiple mechanisms.
Given the dramatic decrease of myogenic cells occurring in muscle degenerative pathologies such as Duchenne dystrophy, the ability of IFRD1 to potentiate the regenerative process suggests that IFRD1 might be a therapeutic target.

# Interactions
IFRD1 has been shown to interact with several proteins in the SIN3 complex including SIN3B, SAP30, NCOR1, and HDAC1. Moreover, IFRD1 protein binds MyoD, MEF2C, HDAC4, HDAC3 and the p65 subunit of NF-B, forming trimolecular complexes with HDAC3 and p65 NF-B proteins. IFRD1 protein also forms homodimers.
IFT20
Intraflagellar transport protein 20 homolog is a protein that in humans is encoded by the IFT20 gene. The gene is composed of 6 exons and is
located on human chromosome 17p11.1. This gene is expressed in human brain, lung, kidney and pancreas, and lower expression were also detected in human placenta, liver, thymus, prostate and testis.
Intraflagellar transport (IFT), in which molecular motors and IFT particle proteins participate, is very important in assembling and maintaining many cilia/flagella, such as the motile cilia that drive the swimming of cells and embryos, the nodal cilia that generate left-right asymmetry in vertebrate embryos, and the sensory cilia that detect sensory stimuli in some animals. IFT20 subunit of the particle is localized to the Golgi complex in addition to the basal body and cilia where all previous IFT particle proteins had been found. In living cells, fluorescently tagged IFT20 is highly dynamic and moves between the Golgi complex and the cilium as well as along ciliary microtubules. IFT20 has been shown to interact with SPEF2 in the testis, and plays a role in sperm motility.
IFT80
Intraflagellar transport protein 80 homolog (IFT80), also known as WD repeat-containing protein 56, is a protein that in humans is encoded by the IFT80 gene.

# Function
IFT80 is part of the intraflagellar transport complex B and is necessary for the function of motile and sensory cilia.

# Clinical significance
Mutations in the IFT80 gene are associated with asphyxiating thoracic dysplasia.
IGBP1
Immunoglobulin-binding protein 1 is a protein that in humans is encoded by the IGBP1 gene.

# Function
The proliferation and differentiation of B cells is dependent upon a B-cell antigen receptor (BCR) complex. Binding of antigens to specific B-cell receptors results in a tyrosine phosphorylation reaction through the BCR complex and leads to multiple signal transduction pathways.

# Interactions
IGBP1 has been shown to interact with PPP4C, PPP6C and PPP2CA.
IGSF1
Immunoglobulin superfamily, member 1 is a plasma membrane glycoprotein encoded by the IGSF1 gene, which maps to the X chromosome in humans and other mammalian species.

# Function
IGSF1's function in normal cells is unresolved.  The protein is a member of the immunoglobulin (Ig) superfamily. It was predicted to contain 12 Ig loops, a transmembrane domain, and a short cytoplasmic tail. However, during translation of the protein, it is cleaved into amino- and carboxy-terminal domains (NTD and CTD, respectively). Only the CTD is trafficked to the plasma membrane. The NTD is trapped within the endoplasmic reticulum (ER). Pathogenic mutations in the IGSF1 gene block the transport of the CTD to the plasma membrane.

# Clinical Relevance
Mutations in IGSF1 cause a condition called IGSF1 deficiency syndrome or central hypothyroidism/testicular enlargement (CHTE). The condition, which affects an estimated 1:100,000 people, is more common in males than females. Most affected males are discovered through neonatal screening for hypothyroidism. The extent of hypothyroidism is variable, but most male cases require treatment with thyroid hormone replacement. Males with IGSF1 deficiency exhibit enlarged testicles (also known as macroorchidism) and a delay in the development of secondary sexual characteristics. Post-pubertally, there is no evidence of impaired fertility in these men.
The IGSF1 gene is also active in the brain and in the developing liver. It can also become reactivated in liver cancer (hepatocellular carcinoma).

# Animal Model
Mice lacking a functional Igsf1 gene similarly exhibit hypothyroidism of central origin. The IGSF1 gene is particularly active in the pituitary gland. The pituitary synthesizes and secretes thyroid-stimulating hormone (TSH). TSH, in turn, stimulates production of the thyroid hormones, thyroxine and triiodothyronine, by the thyroid gland. TSH secretion is controlled by thyrotropin-releasing hormone (TRH), which is released by neurons in the hypothalamus of the brain. In Igsf1 deficient mice, the receptor for TRH is downregulated in the pituitary. This decrease could explain, at least in part, the central hypothyroidism observed in both humans and mice with IGSF1 deficiency. How the loss of IGSF1 causes a decrease in TRH receptors is presently unknown.
IKBKE
Inhibitor of nuclear factor kappa-B kinase subunit epsilon also known as I-kappa-B kinase epsilon or  IKK-epsilon is an enzyme that in humans is encoded by the IKBKE gene.

# Interactions
IKBKE has been shown to interact with TANK.

# Function
Serine/threonine kinase that plays an essential role in regulating inflammatory responses to viral infection, through the activation of the type I IFN, NF-kappa-B and STAT signaling. Also involved in TNFA and inflammatory cytokines, like Interleukin-1, signaling. Following activation of viral RNA sensors, such as RIG-I-like receptors, associates with DDX3X and phosphorylates interferon regulatory factors (IRFs), IRF3 and IRF7, as well as DDX3X. This activity allows subsequent homodimerization and nuclear translocation of the IRF3 leading to transcriptional activation of pro-inflammatory and antiviral genes including IFNB. In order to establish such an antiviral state, IKBKE forms several different complexes whose composition depends on the type of cell and cellular stimuli. Thus, several scaffolding molecules including IPS1/MAVS, TANK, AZI2/NAP1 or TBKBP1/SINTBAD (TANK-binding kinase 1-binding protein 1) can be recruited to the IKBKE-containing-complexes. Activated by polyubiquitination in response to TNFA and interleukin-1, regulates the NF-kappa-B signaling pathway through, at least, the phosphorylation of CYLD. Phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor. In addition, is also required for the induction of a subset of ISGs which displays antiviral activity, may be through the phosphorylation of STAT1 at 'Ser-708'. Phosphorylation of STAT1 at 'Ser-708' seems also to promote the assembly and DNA binding of ISGF3 (STAT1:STAT2:IRF9) complexes compared to GAF (gamma-activation factor) (STAT1:STAT1) complexes, in this way regulating the balance between type I and type II IFN responses. Protects cells against DNA damage-induced cell death. Also plays an important role in energy balance regulation by sustaining a state of chronic, low-grade inflammation in obesity, which leads to a negative impact on insulin sensitivity. Phosphorylates AKT1.

# Clinical significance
Inhibition of IB kinase (IKK) and  IKK-related kinases, IKBKE (IKK) and TANK-binding kinase 1 (TBK1), has been investigated as a therapeutic option for the treatment of inflammatory diseases and cancer.
IKZF3
Zinc finger protein Aiolos also known as Ikaros family zinc finger protein 3 is a protein that in humans is encoded by the IKZF3 gene.

# Function
This gene encodes a member of the Ikaros family of zinc-finger proteins. Three members of this protein family (Ikaros, Aiolos and Helios) are hematopoietic-specific transcription factors involved in the regulation of lymphocyte development. This gene product is a transcription factor that is important in the regulation of B lymphocyte proliferation and differentiation. Both Ikaros and Aiolos can participate in chromatin remodeling. Regulation of gene expression in B lymphocytes by Aiolos is complex as it appears to require the sequential formation of Ikaros homodimers, Ikaros/Aiolos heterodimers, and Aiolos homodimers. At least six alternative transcripts encoding different isoforms have been described.

# Interactions
IKZF3 has been shown to interact with BCL2-like 1 and HRAS.
IL2RA
Interleukin-2 receptor alpha chain (also called CD25) is a protein that in humans is encoded by the IL2RA gene.
The interleukin 2 (IL2) receptor alpha (IL2RA) and beta (IL2RB) chains, together with the common gamma chain (IL2RG), constitute the high-affinity IL2 receptor. Homodimeric alpha chains (IL2RA) result in low-affinity receptor, while homodimeric beta (IL2RB) chains produce a medium-affinity receptor. Normally an integral-membrane protein, soluble IL2RA has been isolated and determined to result from extracellular proteolysis.  Alternately-spliced IL2RA mRNAs have been isolated, but the significance of each is currently unknown.

# Description
It is a type I transmembrane protein present on activated T cells, activated B cells, some thymocytes, myeloid precursors, and oligodendrocytes. Though IL2RA has been used as a marker to identify CD4+FoxP3+ regulatory T cells in mice, it has been found that a large proportion of resting memory T cells constitutively express IL2RA in humans.
IL2RA is expressed in most B-cell neoplasms, some acute nonlymphocytic leukemias,  neuroblastomas, mastocytosis and tumor infiltrating lymphocytes. It functions as the receptor for HTLV-1 and is consequently expressed on neoplastic cells in adult T cell lymphoma/leukemia. Its soluble form, called sIL-2R may be elevated in these diseases and is occasionally used to track disease progression.

# Clinical significance

## Chagas disease
Infection by the protozoan Trypanosoma cruzi causes Chagas disease, characterized by a reduction in the amount of IL2RA expressed on the surface of immune cells.  This leads to chronic immune suppression, becoming increasingly severe over the course of many years and ultimately resulting in death if left untreated.

## Multiple sclerosis
The multiple sclerosis drug daclizumab binds to and blocks IL2RA.
Sarcoidosis
IL2RA has been shown to be elevated in Sarcoidosis with a sensitivity of 88% and specificity of 85%.
IL2RB
Interleukin-2 receptor subunit beta is a protein that in humans is encoded by the IL2RB gene. Also known as CD122; IL15RB; P70-75.

# Function
The interleukin 2 receptor, which is involved in T cell-mediated immune responses, is present in 3 forms with respect to ability to bind interleukin 2. The low affinity form is a monomer of the alpha subunit (also called CD25) and is not involved in signal transduction. The intermediate affinity form consists of a gamma/beta subunit heterodimer, while the high affinity form consists of an alpha/beta/gamma subunit heterotrimer. Both the intermediate and high affinity forms of the receptor are involved in receptor-mediated endocytosis and transduction of mitogenic signals from interleukin 2. The protein encoded by this gene represents the beta subunit and is a type I membrane protein.
This protein also forms one of the three subunits of the IL-15 receptor.
Activation of the receptor increases proliferation of CD8+ effector T cells.

# Interactions
IL2RB has been shown to interact with:
- CISH,
- HGS,
- Janus kinase 1,  and
- SHC1.
IMViC
The IMViC tests are a group of individual tests used in microbiology lab testing to identify an organism.
These four tests include:
- Indole production
- Methyl Red test
- Voges-Proskauer test
- Citrate Production
These IMViC tests are useful for differentiating the the family Enterobacteriaceae, especially when used alongside the Urease test.
Except for the lowercase i, which is added for ease of pronunciation, each of the letters in IMViC stands for one of these tests. I is for indole; M is for methyl red; V is for Voges-Proskauer, and C is for citrate.
INHBB
Inhibin, beta B, also known as INHBB, is a protein which in humans is encoded by the INHBB gene. INHBB is a subunit of both activin and inhibin, two closely related glycoproteins with opposing biological effects.

# Function

## Inhibin
Inhibins are heterodimeric glycoproteins composed of an  subunit (INHA) and one of two homologous, but distinct,  subunits (A or B, this protein). mRNA for the two subunits has been demonstrated in the testes of adult rats.  Inhibin can bind specifically to testicular interstitial cells throughout development and may be an important regulator of Leydig cell testosterone production or interstitial cell function.
The inhibin beta B subunit joins the  subunit to form a pituitary FSH secretion inhibitor.  Inhibin has been shown to regulate gonadal stromal cell proliferation negatively and to have tumour-suppressor activity.  In addition, serum levels of inhibin have been shown to reflect the size of granulosa-cell tumors and can therefore be used as a marker for primary as well as recurrent disease.   Because expression in gonadal and various extragonadal tissues may vary severalfold in a tissue-specific fashion, it is proposed that inhibin may be both a growth/differentiation factor and a hormone.

## Activin
Furthermore, the beta B subunit forms a homodimer, activin B, and also joins with the beta A subunit to form a heterodimer, activin AB, both of which stimulate FSH secretion.

# Tissue distribution
Sections of testicular tissue from rat revealed positive immunoreactivity against anti-inhibin intensely appeared in Leydig cells. In adult animals, binding of 125I inhibin was localized primarily to the interstitial compartment of the testis.  Also, Jin et al., (2001) reported that Leydig cells showed strong positive staining for the inhibin A subunit in pigs testis.

# Receptors
In situ ligand binding studies have shown that 125I inhibin A binds specifically to Leydig cells throughout rat testis development. These results suggest that inhibin has been considered as a regulator of Leydig cell differentiated function. Recently, additional inhibin specific binding proteins were identified in inhibin target tissues, including pituitary and Leydig cells. From these receptors -glycan (the TGF type III receptor) and InhBP/p120 (a membrane-tethered proteoglycan) were identified as putative inhibin receptors and they are all present in Leydig cells. However, a faint positive reaction was detected in Leydig cell cytoplasm in rats treated with anise oil. This may be related to the damaged Leydig cells, as a result of the decreasing of inhibin expression. This may be related to its content of safrole.
INPP1
Inositol polyphosphate 1-phosphatase is an enzyme that, in humans, is encoded by the INPP1 gene.
INPP1 encodes the enzyme inositol polyphosphate-1-phosphatase, one of the enzymes involved in phosphatidylinositol signaling pathways. This enzyme removes the phosphate group at position 1 of the inositol ring from the polyphosphates inositol 1,4-bisphosphate and inositol 1,3,4-trisphophosphate.

# Model organisms
Model organisms have been used in the study of INPP1 function. A conditional knockout mouse line, called Inpp1tm1a(KOMP)Wtsi was generated as part of the International Knockout Mouse Consortium program  a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Twenty four tests were carried out on mutant mice, and one significant abnormality was observed: a decreased susceptibility to bacterial infection.