Persius/hicric huggingface dataset:
SH3TC2
SH3 domain and tetratricopeptide repeats-containing protein 2 is a protein that in humans is encoded by the SH3TC2 gene. It is believed to be expressed in the Schwann cells that wrap the myelin sheath around nerves.

# Function
This gene encodes a protein with two N-terminal Src homology 3 (SH3) domains and 10 tetratricopeptide repeat (TPR) motifs, and is a member of a small gene family. The gene product has been proposed to be an adapter or docking molecule.
The mouse version (orthologue) of SH3TC2 is believed to be expressed in Schwann cells. The tagged protein localizes to the plasma membrane and to the perinuclear endocytic recycling compartment. Mice lacking Sh3tc2 have an abnormal organization of the node of Ranvier consistent with the idea that the protein might have a role in myelination or in axon  glial cell interactions.

# Clinical significance
Mutations in this gene result in autosomal recessive Charcot-Marie-Tooth disease type 4C, a childhood-onset neurodegenerative disease characterized by demyelination of motor and sensory neurons.
SHANK2
SH3 and multiple ankyrin repeat domains protein 2 is a protein that in humans is encoded by the SHANK2 gene. Two alternative splice variants, encoding distinct isoforms, are reported. Additional splice variants exist but their full-length nature has not been determined.

# Function
This gene encodes a protein that is a member of the Shank family of synaptic proteins that may function as molecular scaffolds in the postsynaptic density (PSD). Shank proteins contain multiple domains for protein-protein interaction, including ankyrin repeats, an SH3 domain, a PSD-95/Dlg/ZO-1 domain, a sterile alpha motif domain, and a proline-rich region. This particular family member contains a PDZ domain, a consensus sequence for cortactin SH3 domain-binding peptides and a sterile alpha motif. The alternative splicing demonstrated in Shank genes has been suggested as a mechanism for regulating the molecular structure of Shank and the spectrum of Shank-interacting proteins in the PSDs of adult and developing brain.
It is thought that SHANK2 might play a role in synaptogenesis by attaching metabotropic glutamate receptors (mGluRs) to an existing pool of NMDA receptors (NMDA-R), bylinking to the NMDA-R through PSD-95, and the mGluRs through HOMER1. An alternative hypothesis is that the Homer/Shank/GKAP/PSD-95 assembly mediates physical association of the NMDAR with IP3R/RYR and intracellular Ca2+ stores.

# Interactions
SHANK2 has been shown to interact with:
- ARHGEF7,
- Cortactin,
- DLG4,
- DLGAP1, and
- DNM2.
SHANK3
SH3 and multiple ankyrin repeat domains 3 (Shank3), also known as proline-rich synapse-associated protein 2 (ProSAP2), is a protein that in humans is encoded by the SHANK3 gene on chromosome 22.  Additional isoforms have been described for this gene but they have not yet been experimentally verified.

# Function
This gene is a member of the Shank gene family. The gene encodes a protein that contains 5 interaction domains or motifs including the ankyrin repeats domain (ANK), a src 3 domain (SH3), a proline-rich domain, a PDZ domain and a SAM (sterile  motif) domain. Shank proteins are multidomain scaffold proteins of the postsynaptic density that connect neurotransmitter receptors, ion channels, and other membrane proteins to the actin cytoskeleton and G-protein-coupled signaling pathways. Shank proteins also play a role in synapse formation and dendritic spine maturation.

# Clinical significance
Mutations in this gene are associated with autism spectrum disorder. This gene is often missing in patients with 22q13.3 deletion syndrome, although not in all cases.

# Interactions
SHANK3 has been shown to interact with ARHGEF7.

# Mouse models
Mouse models of SHANK3 include N-terminal knock-outs and a PDZ domain knock-out all of which also show social interaction deficits and variable other phenotypes. Most of these mice are homozygous knock-outs whereas all the human Shank3 mutations have been heterozygous.
In an inducible knockout, restoration of Shank3 expression in adult mice promoted dendritic spine growth and recovered normal grooming behaviour and voluntary social interaction. However, the reduced locomotion, anxiety and rotarod deficits remained. Germline restoration of the gene's expression rescued all measured phenotypes. Experiments on different developmental windows suggested that early intervention was more effective in restoring behavioural traits.

# Rat Models
A rat model of SHANK3 was developed using zinc finger nucleases targeting exon 6 of the ankyrin (ANK) repeat domain. The deletion (-68bp) resulted in reduction of the full length SHANK3a protein. It is unclear if the expression of other isoforms (b and c) of SHANK3 is affected in this rodent model. The shank3 mutant rats have deficits in long-term social recognition memory but not short-term social recognition memory as well as deficits in attention. These mutant also have impaired synaptic plasticity. In humans, 5 patients have been described harboring varying mutations in exon 6 of the SHANK3 protein.
SLAMF1
Signaling lymphocytic activation molecule 1 is a protein that in humans is encoded by the SLAMF1 gene. Recently SLAMF1 has also been designated CD150 (cluster of differentiation 150).
SLAMF1 belongs to the signaling lymphocytic activation molecule family. The interaction of SLAMF1 promoter and enhancers with the Early B-cell factor 1 (EBF1) is required for the expression of SLAMF1 gene in B cells. STAT6, IRF4, and NF-kB factors involved in the transfer of the signals from the B-cell receptor, its co-receptors and IL-4R, also play important role in the regulation of SLAMF1 expression.

# Interactions
SLAMF1 has been shown to interact with PTPN11, SH2D1A and SH2D1B.
SLC2A9
Solute carrier family 2, facilitated glucose transporter member 9 is a protein that in humans is encoded by the SLC2A9 gene.
This gene encodes a member of the SLC2A facilitative glucose transporter family. Members of this family play a significant role in maintaining glucose homeostasis.  The encoded protein may play a role in the development and survival of chondrocytes in cartilage matrices. Two transcript variants encoding distinct isoforms have been identified for this gene.
SLC2A9 has also recently been found to transport uric acid, and genetic variants of the transporter have been linked to increased risk of development of both hyperuricemia, gout and Alzheimer's disease.
SLC3A2
4F2 cell-surface antigen heavy chain  is a protein that in humans is encoded by the SLC3A2 (solute carrier family 3 member 2) gene.
SLC3A2 comprises the heavy subunit of the large neutral amino acid transporter (LAT1) that is also known as CD98 (cluster of differentiation 98).

# Function
SLC3A2 is a member of the solute carrier family and encodes a cell surface, transmembrane protein with an alpha-amylase domain. The protein exists as the heavy chain of a heterodimer, covalently bound through di-sulfide bonds to one of several possible light chains. It associates with integrins and mediates integrin-dependent signaling related to normal cell growth and tumorigenesis. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.
LAT1 is a heterodimeric membrane transport protein that preferentially transports neutral branched (valine, leucine, isoleucine) and aromatic (tryptophan, tyrosine) amino acids. LAT is highly expressed in brain capillaries (which form the blood brain barrier) relative to other tissues.
A functional LAT1 transporter is composed of two proteins encoded by two distinct genes:
- 4F2hc/CD98 heavy subunit protein encoded by the SLC3A2 gene (this gene)
- CD98 light subunit protein encoded by the SLC7A5 gene

# Interactions
SLC3A2 has been shown to interact with SLC7A7.
Additionally, SLC3A2 is a constituent member of the system xc- cystine/glutamate antiporter, complexing with SLC7A11.
SLC4A2
Anion exchange protein 2 (AE2) is a membrane transport protein that in humans is encoded by the SLC4A2 gene. AE2 is functionally similar to the Band 3 Cl/HCO3 exchange protein.
Mice have been used to explore the function of AE2. AE2 contributes to basolateral membrane HCO3 transport in the gastrointestinal tract. AE2 is required for spermiogenesis in mice. AE2 is required for normal osteoclast function. The activity of AE2 is sensitive to pH.
AE3 has been suggested as a target for prevention of diabetic vasculopathy.
SLC4A4
Electrogenic sodium bicarbonate cotransporter 1 is a membrane transport protein that in humans is encoded by the SLC4A4 gene.

# Function
Sodium bicarbonate cotransporters (NBCs) mediate the coupled movement of sodium and bicarbonate ions across the plasma membrane of many cells. This is an electrogenic process with an apparent stoichiometry of 3 bicarbonate ions per sodium ion. Sodium bicarbonate cotransport is involved in bicarbonate secretion/absorption and intracellular pH regulation. Romero and Boron (1999) reviewed NBCs. Soleimani and Burnham (2000) reviewed NBCs and their regulation in physiologic and pathophysiologic states.

# Clinical significance
NBCe1 may participate in regulation of brain extracellular space pH. Some mutations in NBCe1 have been associated with Familial hemiplegic migraine. Other NBCe1 mutations disrupt kidney bicarbonate transport and cause proximal renal tubular acidosis.

# Splice variants
NBCe1-A aka kNBC1 (mainly expressed in the kidney)
NBCe1-B aka pNBC1 (expressed in the pancreas and elsewhere)
NBCe1-C (expressed in the brain)

# Distribution
The renal SLC4A4 gene product NBCe1-A is specifically expressed in the basolateral membranes of proximal tubule epithelia.
SLC4A5
Electrogenic sodium bicarbonate cotransporter 4 is a protein that in humans is encoded by the SLC4A5 gene.

# Function
This gene encodes a member of the sodium bicarbonate cotransporter (NBC) family, part of the bicarbonate transporter superfamily. Sodium bicarbonate cotransporters are involved in intracellular pH regulation and electroneural or electrogenic sodium bicarbonate transport. This protein is thought to be an integral membrane protein. Multiple transcript variants encoding different isoforms have been found for this gene, but the biological validity of some variants has not been determined.

# Clinical significance
This human gene has been identified as a hypertension susceptibility gene based on the association of single nucleotide polymorphisms with blood pressure (BP) levels and hypertension status.
SLC5A1
Sodium/glucose cotransporter 1 also known as solute carrier family 5 member 1 is a protein that in humans is encoded by the SLC5A1 gene.

# Function
Glucose transporters are integral membrane proteins that mediate the transport of glucose and structurally related substances across cellular membranes. The role of the sodium-glucose cotransporters is to not only absorb glucose, but to also absorb sodium and to then reabsorb the sodium and glucose from the tubule of the nephron. Two families of glucose transporter have been identified: the facilitated diffusion glucose transporter family (GLUT family), also known as 'uniporters,' and the sodium-dependent glucose transporter family (SGLT family), also known as 'cotransporters' or 'symporters. The SLC5A1 gene encodes a protein that is involved in the active transport of glucose and galactose into eukaryotic and some prokaryotic cells.

# Cloning
Co-transport proteins of mammalian cell membranes had eluded efforts of purification with classical biochemical methods until the late 1980s. These proteins had proven difficult to isolate because they contain hydrophilic and hydrophobic sequences and exist in membranes only in very low abundance (<0.2% of membrane proteins). The rabbit form of SGLT1 was the first mammalian co-transport protein ever to be cloned and sequenced, and this  was reported in 1987. To circumvent the difficulties with traditional isolation methods, a novel expression cloning technique was used. Size-fractionation of large amounts of rabbit intestinal mRNA with preparative gel electrophoresis were then sequentially injected into Xenopus oocytes to ultimately find the RNA species that induced the expression of sodium-glucose cotransport.

# Mutations
SLC5A1 is important  because of its role in the absorption of glucose and sodium, however, mutations in the gene can cause serious effects. A mutation in the SLC5A1 gene can cause problems creating the SGLT1 protein, leading to a rare glucose-galactose malabsorption disease. Glucose-galactose malabsorption occurs when the lining of the intestinal cells can't take in glucose and galactose which prevents the use of those molecules in catabolism and anabolism. The disease has symptoms that consist of watery and/or acidic diarrhea which is the result of water retention in the intestinal lumen and osmotic loss created by non-absorbed glucose, galactose and sodium. Glucose-Galactose malabsorption can cause death, due to loss of water from diarrhea, if the disease isn't treated soon. To counteract the disease, oral rehydration therapy is performed using sodium, glucose, and water for intestinal reabsorption.

# Tissue distribution
The SLC5A1 cotransporter is mainly expressed in the lumen of the small intestine, kidney, parotid glands, submandibular glands and in the heart.
SLC7A9
Solute carrier family 7 (cationic amino acid transporter, y+ system), member 9 also known as SLC7A9 is a protein which in humans is encoded by the SLC7A9 gene.

# Function
This gene encodes a protein that belongs to a family of light subunits of amino acid transporters. This protein plays a role in the high-affinity and sodium-independent transport of cystine and neutral and dibasic amino acids, and appears to function in the reabsorption of cystine in the kidney tubule. The protein associates with the protein coded for by SLC3A1.

# Clinical significance
Mutations in this gene cause non-type I cystinuria, a disease that leads to cystine stones in the urinary system due to impaired transport of cystine and dibasic amino acids.
SLC9A8
Sodium/hydrogen exchanger 8 is a protein that in humans is encoded by the SLC9A8 gene.

# Model organisms
Model organisms have been used in the study of SLC9A8 function. A conditional knockout mouse line, called Slc9a8tm1a(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 one tests were carried out on mutant mice and one significant abnormality was observed: homozygous mutant animals had abnormal retinal morphology and pigmentation.
SLURP1
Secreted Ly-6/uPAR-related protein 1 is a protein that in humans is encoded by the SLURP1 gene. It exerts anti-inflammatory effects and acts as a tumor suppressor and antagonist of nicotine.

# Function
The protein encoded by this gene is a member of the Ly6/uPAR family but lacks a GPI-anchoring signal sequence. It is secreted into the blood and binds to the 7-acetylcholine receptor. It is shown to act as an endogenous tumor suppressor by reducing cell migration and invasion by mediating its own anti-tumor effect and by antagonizing the pro-malignant effects of nicotine.
Mutations in this gene have been associated with Mal de Meleda, a rare autosomal recessive skin disorder characterized by an inflammatory palmoplantar hyperkeratosis. This is the consequence of a loss of SLURP1 which leads to a dysfunctional epithelial differentiation and an increased secretion of the inflammatory cytokines TNF, IL1, IL-6, and IL-8.
This gene maps to the same chromosomal region as several members of the Ly6/uPAR family of glycoprotein receptors.
SNAP23
Synaptosomal-associated protein 23 is a protein that in humans is encoded by the SNAP23 gene. Two alternative transcript variants encoding different protein isoforms have been described for this gene.

# Function
Specificity of vesicular transport is regulated, in part, by the interaction of a vesicle-associated membrane protein termed synaptobrevin/VAMP with a target compartment membrane protein termed syntaxin. These proteins, together with SNAP25 (synaptosome-associated protein of 25 kDa), form a complex which serves as a binding site for the general membrane fusion machinery. Synaptobrevin/VAMP and syntaxin are believed to be involved in vesicular transport in most, if not all cells, while SNAP25 is present almost exclusively in the brain, suggesting that a ubiquitously expressed homolog of SNAP25 exists to facilitate transport vesicle/target membrane fusion in other tissues.
SNAP23 is structurally and functionally similar to SNAP25 and binds tightly to multiple syntaxins and synaptobrevins/VAMPs. It is an essential component of the high affinity receptor for the general membrane fusion machinery and is an important regulator of transport vesicle docking and fusion.

# Clinical significance
In individuals with insulin resistance, SNAP23 is found to be translocated from the plasma membrane to the cytosol where it becomes associated with lipid droplets and is therefore unable to translocate GLUT-4 to the membrane, hindering glucose transport.

# Interactions
SNAP23 has been shown to interact with:
- Cystic fibrosis transmembrane conductance regulator,
- KIF5B,
- NAPA,
- SNAPAP,
- STX11,
- STX1A,
- STX2,
- STX4,
- STX6,
- SYBL1,
- Syntaxin 3,
- VAMP2,
- VAMP3, and
- Vesicle-associated membrane protein 8.
SNAP29
Synaptosomal-associated protein 29 is a protein that in humans is encoded by the SNAP29 gene.

# Function
This gene, a member of the SNAP25 gene family, encodes a protein involved in multiple membrane trafficking steps. Two other members of this gene family, SNAP23 and SNAP25, encode proteins that bind a syntaxin protein and mediate synaptic vesicle membrane docking and fusion to the plasma membrane. The protein encoded by this gene binds tightly to multiple syntaxins and is localized to intracellular membrane structures rather than to the plasma membrane. While the protein is mostly membrane-bound, a significant fraction of it is found free in the cytoplasm. Use of multiple polyadenylation sites has been noted for this gene.

# Model organisms
Model organisms have been used in the study of SNAP29 function. A conditional knockout mouse line, called Snap29tm1a(EUCOMM)Wtsi was generated as part of the International Knockout Mouse Consortium programa 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 significant abnormalities were observed in these animals.

# Interactions
SNAP29 has been shown to interact with Syntaxin 3 and EHD1.
SNAPAP
SNARE-associated protein Snapin is a protein that in humans is encoded by the SNAPIN gene.

# Function
SNAPAP is a component of the SNARE complex of proteins that is required for synaptic vesicle docking and fusion. SNAPAP is also a component of the ubiquitously expressed BLOC1 multisubunit protein complex. BLOC1 is required for normal biogenesis of specialized organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules.
Snapin has been established to be a promoter of vesicle docking, as it plays a role in binding to SNAP-25, which together stabilize and favor SNARE complex assembly and vesicle docking. Specifically, the degree to which snapin is necessary for proper synaptic release varies across species. The functions of snapin have been reported to be independent of synaptotagmin, and works through the SNAP-25 pathway to stabilize, prime, and dock vesicles.

# Interactions
SNAPAP has been shown to interact with:
- BLOC1S1,
- BLOC1S2,
- Dysbindin,
- PLDN,
- RGS7,
- SNAP-25,
- SNAP23,  and
- TRPV1.
SNAPC4
snRNA-activating protein complex subunit 4 is a protein that in humans is encoded by the SNAPC4 gene.

# Model organisms
Model organisms have been used in the study of SNAPC4 function. A conditional knockout mouse line, called Snapc4tm1a(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 six tests were carried out on mutant mice and two significant abnormalities were observed. No homozygous mutant embryos were recorded during gestation and, in a separate study, no homozygous animals were observed at weaning. The remaining tests were carried out on adult heterozygous mutant animals and no further abnormalities were observed.

# Interactions
SNAPC4 has been shown to interact with SNAPC1, POU2F1 and SNAPC2.
SNC-80
SNC-80 is an opioid analgesic drug used in scientific research. It was invented in 1994.
SNC-80 was the first non-peptide drug developed that is a highly selective agonist for the -opioid receptor.
It has been shown to produce useful analgesic, antidepressant and anxiolytic effects in animal studies, but its usefulness is limited by producing convulsions at high doses, and so SNC-80 is not used medically, although it is a useful drug in scientific research.
SNCAIP
Synphilin-1 is a protein that in humans is encoded by the SNCAIP gene. SNCAIP stands for "synuclein, alpha interacting protein" and can be signified by SNCAP_HUMAN, synphilin 1, synuclein, alpha interacting protein (synphilin), and SYPH1.

# Function
This gene encodes a protein containing several protein-protein interaction domains, including ankyrin-like repeats, a coiled-coil domain, and an ATP/GTP-binding motif. The encoded protein interacts with alpha-synuclein in neuronal tissue and may play a role in the formation of cytoplasmic inclusions and neurodegeneration. A mutation in this gene has been associated with Parkinson's disease. Alternatively spliced transcript variants encoding different isoforms of this gene have been described, but their full-length nature has yet to be determined.
The SNCAIP gene provides instructions for making a protein called synphilin-1 and a slightly different version of this protein called synphilin-1A. These proteins are produced in the brain. They are usually located in specialized structures called presynaptic terminals, found at the tips of nerve cells. In nerve cells, synphilin-1 and synphilin-1A interact with another protein called alpha-synuclein. The functions of synphilin-1 and synphilin-1A, however, are unknown.

# Interactions
SNCAIP has been shown to interact with:
- Alpha-synuclein  and
- Parkin (ligase).