Persius/hicric huggingface dataset:
SART3
Squamous cell carcinoma antigen recognized by T-cells 3 is a protein that in humans is encoded by the SART3 gene.
The protein encoded by this gene is an RNA-binding nuclear protein that is a tumor-rejection antigen. This antigen possesses tumor epitopes capable of inducing HLA-A24-restricted and tumor-specific cytotoxic T lymphocytes in cancer patients and may be useful for specific immunotherapy. This gene product is found to be an important cellular factor for HIV-1 gene expression and viral replication. It also associates transiently with U6 and U4/U6 snRNPs during the recycling phase of the spliceosome cycle. This encoded protein is thought to be involved in the regulation of mRNA splicing.

# Interactions
SART3 has been shown to interact with RNPS1 and Androgen receptor.
SASS6
Spindle assembly abnormal protein 6 homolog (SAS-6) is a protein that in humans is encoded by the SASS6 gene.

# Function
SAS-6 is necessary for centrosome duplication and functions during procentriole formation; SAS-6 functions to ensure that each centriole seeds the formation of a single procentriole per cell cycle.

# Clinical significance
Mutations in  SASS6 are associated to                 MCPH            .
SCN1B
Sodium channel subunit beta-1 is a protein that in humans is encoded by the SCN1B gene.
Voltage-gated sodium channels are essential for the generation and propagation of action potentials in striated muscle and neuronal tissues. Biochemically, they consist of a large alpha subunit and 1 or 2 smaller beta subunits, such as SCN1B. The alpha subunit alone can exhibit all the functional attributes of a voltage-gated Na+ channel, but requires a beta-1 subunit for normal inactivation kinetics.

# Clinical significance
Mutation in the SCN1B gene are  associated with disorders such as Brugada syndrome and GEFS.
SCN3A
Sodium channel, voltage-gated, type III, alpha subunit (SCN3A) is a  protein that in humans is encoded by the Nav1.3 gene.

# Function
Voltage-gated sodium channels are transmembrane glycoprotein complexes composed of a large alpha subunit with 24 transmembrane domains and one or more regulatory beta subunits. They are responsible for the generation and propagation of action potentials in neurons and muscle. This gene encodes one member of the sodium channel alpha subunit gene family, and is found in a cluster of five alpha subunit genes on chromosome 2. Multiple transcript variants encoding different isoforms have been found for this gene.
SCN3A is involved in folding the human cerebral cortex, a process called "gyrification".
SCYL1
SCY1-like 1 (S. cerevisiae), also known as SCYL1, is a human gene which is highly conserved throughout evolution.

# Function
This gene encodes a transcriptional regulator belonging to the SCY1-like family of kinase-like proteins. The protein has a divergent N-terminal kinase domain that is thought to be catalytically inactive, and can bind specific DNA sequences through its C-terminal domain. It activates transcription of the telomerase reverse transcriptase and DNA polymerase beta genes. The protein has been localized to the nucleus, and also to the cytoplasm and centrosomes during mitosis. Multiple transcript variants encoding different isoforms have been found for this gene. At least three of the transcripts code for a protein containing all exons, referred to as full-length (FL).
The mouse homolog of FL-Scyl1 is 90% identical and 93% similar in amino acid content to human FL-Scyl1. In Mus Musculus FL-Scyl1 encodes an 806-amino acid polypeptide. The FL protein contains HEAT repeats and a C-terminal coiled coil domain that also contains multiple dibasic motifs, and ends in the dibasic motif RKLD-COOH.
Scyl1 localizes to the cis-Golgi and ER-Golgi Intermediate Compartment (ERGIC). Scyl1 binds to Coatomer I (COPI) and colocalizes with beta-COPI and ERGIC53. siRNA mediated knockdown of the protein disrupted retrograde flow of the KDEL receptor from the Golgi to the ER. Furthermore, Scyl1 localization in rat hippocampal neurons also demonstrates a similar relationship to COPI.

# Clinical significance
Mutations in Scyl1 are the genetic defect resulting in the phenotype of muscle deficient mice (mdf mice) that suffer from a progressive neurodegeneration of the cerebellum and lower motor neurons. Mdf mice model human spinocerebellar ataxia type disorders.
SEC63
Translocation protein SEC63 homolog is a protein that in humans is encoded by the SEC63 gene.

# Function
The Sec61 complex is the central component of the protein translocation apparatus of the endoplasmic reticulum (ER) membrane. The protein encoded by this gene and SEC62 protein are found to be associated with ribosome-free SEC61 complex. It is speculated that Sec61-Sec62-Sec63 may perform post-translational protein translocation into the ER. The Sec61-Sec62-Sec63 complex might also perform the backward transport of ER proteins that are subject to the ubiquitin-proteasome-dependent degradation pathway. The encoded protein is an integral membrane protein located in the rough ER.

# Clinical significance
Mutations of this gene have been linked with autosomal dominant polycystic liver disease.
SENP1
Sentrin-specific protease 1 is an enzyme that in humans is encoded by the SENP1 gene.

# General
So far there are six SUMO proteases in humans that have been designated SENP1-3 and SENP5-7 (sentrin/SUMO-specific protease).1 The six proteases possess a conserved C-terminal domain which are variable in size, and with a distinct N-terminal domain between them. The C-terminal domain shows catalytic activity and N-terminal domain regulates cell localization and substrate specificity.

# Features
SENP1 (Sentrin-specific protease 1) is a human protease of 643 amino acids with a weight of 73 kDa, EC number in humans 3.4.22.B70, which adopts a conformation that identifies it as a member of the superfamily of cysteine proteases contain a catalytic triad with characterized three amino acids: a cysteine at position 602, a histidine at position 533 and aspartic acid at position 550.
The important nucleophile is cysteine located at the N-terminal alpha helix of the protein core, the other two amino acids, aspartate and histidine, are located in a beta sheet end.

# Location
Both SENP1 are located in the nucleus and cytosol depending on the cell type, although it has been seen that is exported out from the nucleus to the cytosol through a sequence of nuclear export (NES) that is located at the C-terminus. The mammalian SENP1 is localized mainly in the nucleus.

# Function
SENP1 catalyzes maturation SUMO protein (small ubiquitin-related modifier), which causes hydrolysis peptide bond of SUMO is in a conserved sequence Gly-Gly-|-Ala-Thr-Tyr at the C-terminal  to be added to the conjugation of other proteins (sumoylation). 
In vertebrates there are three members of the family of SUMO: SUMO-1, -2 and -3. SENP1 can catalyze any of these three.
This conjugation of SUMO toward other proteins is a lot like ubiquitination, however these modifications leads to different results depending on the type of protein been modified.
SEP15
15 kDa selenoprotein is a protein that in humans is encoded by the SEP15 gene. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.

# Function
This gene encodes a selenoprotein, which contains a selenocysteine (Sec) residue at its active site. The selenocysteine is encoded by the UGA codon that normally signals translation termination. The 3' UTR of selenoprotein genes have a common stem-loop structure, the sec insertion sequence (SECIS), that is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. Studies in mouse suggest that this selenoprotein may have redox function and may be involved in the quality control of protein folding.

# Clinical significance
This gene is localized on chromosome 1p31, a genetic locus commonly mutated or deleted in human cancers.

# Protein domain
The protein this gene encodes for is often called Sep15 however in the case of mice, it is named SelM. This protein is an selenoprotein only found in eukaryotes. This domain has a  thioredoxin-like domain and a surface accessible active site redox motif. This suggests that they function as thiol-disulfide isomerases involved in disulfide bond formation in the endoplasmic reticulum.

## Function
Recent studies have shown in mice, where the SEP15 gene has been silenced the mice subsequently became deficient in SEP15 and were able to inhibit the development of colorectal cancer.

## Structure
The particular structure has an alpha/beta central domain which is actually made up of three alpha helices and a mixed parallel/anti-parallel four-stranded beta-sheet.
SEPN1
Selenoprotein N is a protein that in humans is encoded by the SEPN1 gene.

# Function
This gene encodes a selenoprotein, which contains a selenocysteine (Sec) residue at its active site. The selenocysteine is encoded by the UGA codon that normally signals translation termination. The 3' UTR of selenoprotein genes have a common stem-loop structure, the sec insertion sequence (SECIS), that is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. Mutations in this gene cause the classical phenotype of multiminicore disease and congenital muscular dystrophy with spinal rigidity and restrictive respiratory syndrome. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.

# Model organisms
Model organisms have been used in the study of SEPN1 function. A conditional knockout mouse line, called Sepn1tm1a(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 five tests were carried out on homozygous mutant mice and one significant abnormality was observed: than animals displayed vertebral fusion.
SEPT6
Septin-6 is a protein that in humans is encoded by the SEPT6 gene.

# Function
This gene is a member of the septin family of GTPases. Members of this family are required for cytokinesis. This gene encodes four transcript variants encoding three distinct isoforms. An additional transcript variant has been identified, but its biological validity has not been determined.

# Clinical significance
One version of pediatric acute myeloid leukemia is the result of a reciprocal translocation between chromosomes 11 and X, with the breakpoint associated with the genes encoding the mixed-lineage leukemia and septin 2 proteins.

# Interactions
SEPT6 has been shown to interact with SEPT2.
SEPT9
Septin-9 is a protein that in humans is encoded by the SEPT9 gene.

# Interactions
SEPT9 has been shown to interact with SEPT2 and SEPT7.

# Function
Along with AHNAK, eIF4E and S100A11, SEPT9 has been shown to be essential for pseudopod protrusion, tumor cell migration and invasion.

# Clinical significance
The v2 region of the SEPT9 promoter has been shown to be methylated in colorectal cancer tissue compared with normal colonic mucosa.  Using highly sensitive real time PCR assays, methylated SEPT9 was detected in the blood of colorectal cancer patients. This alternate methylation pattern in cancer samples is suggestive of an aberrant activation or repression of the gene compared to normal tissue samples.
Testing to detect methylated SEPT9 is not indicated as a first option for colorectal cancer screening. It is similar in specificity and sensitivity to the stool guaiac test or fecal immune tests, and those tests should be used in preference. In cases when the physician aggressively has recommended a colonoscopy and the patient has declined that and these other tests, then this test has advantages over patients having no screening at all.
SESN1
Sestrin 1, also known as p53-regulated protein PA26, is a protein that in humans is encoded by the SESN1 gene. 
This gene encodes a member of the sestrin family. Sestrins are induced by the p53 tumor suppressor protein and play a role in the cellular response to DNA damage and oxidative stress. 
The encoded protein mediates p53 inhibition of cell growth by activating AMP-activated protein kinase, which results in the inhibition of the mammalian target of rapamycin protein. The encoded protein also plays a critical role in antioxidant defense by regenerating overoxidized peroxiredoxins, and the expression of this gene is a potential marker for exposure to radiation. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.
SESN2
Sestrin-2 also known as Hi95 is a protein that in humans is encoded by the SESN2 gene.

# Function
This gene encodes a member of the sestrin family of PA26-related proteins. The encoded protein may function in the regulation of cell growth and survival. This protein may be involved in cellular response to different stress conditions. The Sestrins constitute a family of evolutionarily-conserved stress-inducible proteins that suppress oxidative stress and regulate adenosine monophosphate-dependent protein kinase (AMPK)-mammalian target of rapamycin (mTOR) signaling. By virtue of these activities, the Sestrins serve as important regulators of metabolic homeostasis. Accordingly, inactivation of Sestrin genes in invertebrates resulted in diverse metabolic pathologies, including oxidative damage, fat accumulation, mitochondrial dysfunction and muscle degeneration that resemble accelerated tissue aging.

# Ligands
The NMDA receptor antagonist ketamine has been found to activate the mammalian target of rapamycin complex 1 (mTORC1) pathway in the medial prefrontal cortex (mPFC) of the brain as an essential downstream mechanism in the mediation of its rapid-acting antidepressant effects. NV-5138 is a ligand and modulator of sestrin2, a leucine amino acid sensor and upstream regulatory pathway of mTORC1, and is under development for the treatment of depression. The drug has been found to directly and selectively activate the mTORC1 pathway, including in the mPFC, and to produce rapid-acting antidepressant effects similar to those of ketamine.
SETD2
SET domain containing 2 is an enzyme that in humans is encoded by the SETD2 gene.

# Function
SETD2 protein is a histone methyltransferase that is specific for lysine-36 of histone H3, and methylation of this residue is associated with active chromatin. This protein also contains a novel transcriptional activation domain and has been found associated with hyperphosphorylated RNA polymerase II.

# Clinical significance
The SETD2 gene is located on the short arm of chromosome 3 and has been shown to play a tumour suppressor role in human cancer.

# Interactions
SETD2 has been shown to interact with Huntingtin. Huntington's disease (HD), a neurodegenerative disorder characterized by loss of striatal neurons, is caused by an expansion of a polyglutamine tract in the HD protein huntingtin. SETD2 belongs to a class of huntingtin interacting proteins characterized by WW motifs.
SF3B1
Splicing factor 3B subunit 1 is a protein that in humans is encoded by the SF3B1 gene.

# Function
This gene encodes subunit 1 of the splicing factor 3b protein complex. Splicing factor 3b, together with splicing factor 3a and a 12S RNA unit, forms the U2 small nuclear ribonucleoproteins complex (U2 snRNP). The splicing factor 3b/3a complex binds pre-mRNA upstream of the intron's branch site in a sequence independent manner and may anchor the U2 snRNP to the pre-mRNA. Splicing factor 3b is also a component of the minor U12-type spliceosome. The carboxy-terminal two-thirds of subunit 1 have 22 non-identical, tandem HEAT repeats that form rod-like, helical structures. Alternative splicing results in multiple transcript variants encoding different isoforms.

# Interactions
SF3B1 has been shown to interact with:
- CDC5L,
- DDX42,
- PPP1R8,
- SF3B2,
- SF3B3,
- SF3B14,

# Clinical relevance
Mutations in this gene have been recurrently seen in cases of advanced chronic lymphocytic leukemia, myelodysplastic syndromes and breast cancer. SF3B1 mutations are found in 60%-80% of patients with refractory anemia with ring sideroblasts (RARS; which is a myelodysplastic syndrome) or RARS with thrombocytosis (RARS-T; which is a myelodysplastic syndrome/myeloproliferative neoplasm). There is also an emerging body of evidence to suggest implications of SF3B1 mutations being involved in orbital melanoma.
SF3B2
Splicing factor 3B subunit 2 is a protein that in humans is encoded by the SF3B2 gene.

# Function
This gene encodes subunit 2 of the splicing factor 3b protein complex. Splicing factor 3b, together with splicing factor 3a and a 12S RNA unit, forms the U2 small nuclear ribonucleoproteins complex (U2 snRNP). The splicing factor 3b/3a complex binds pre-mRNA upstream of the intron's branch site in a sequence-independent manner and may anchor the U2 snRNP to the pre-mRNA. Splicing factor 3b is also a component of the minor U12-type spliceosome. Subunit 2 associates with pre-mRNA upstream of the branch site at the anchoring site. Subunit 2 also interacts directly with subunit 4 of the splicing factor 3b complex. Subunit 2 is a highly hydrophilic protein with a proline-rich N-terminus and a glutamate-rich stretch in the C-terminus.

# Interactions
SF3B2 has been shown to interact with SF3B4, RBM7, SF3B1 and CDC5L.
SF3B3
Splicing factor 3B subunit 3 is a protein that in humans is encoded by the SF3B3 gene.
This gene encodes subunit 3 of the splicing factor 3b protein complex. Splicing factor 3b, together with splicing factor 3a and a 12S RNA unit, forms the U2 small nuclear ribonucleoproteins complex (U2 snRNP). The splicing factor 3b/3a complex binds pre-mRNA upstream of the intron's branch site in a sequence independent manner and may anchor the U2 snRNP to the pre-mRNA. Splicing factor 3b is also a component of the minor U12-type spliceosome. Subunit 3 has also been identified as a component of the STAGA (SPT3-TAF(II)31-GCN5L acetylase) transcription coactivator-HAT (histone acetyltransferase) complex, and the TFTC (TATA-binding-protein-free TAF(II)-containing complex). These complexes may function in chromatin modification, transcription, splicing, and DNA repair.

# Interactions
SF3B3 has been shown to interact with SF3B1, Transcription initiation protein SPT3 homolog and TAF9.
SF3B4
Splicing factor 3B subunit 4 is a protein that in humans is encoded by the SF3B4 gene.

# Function
This gene encodes one of four subunits of the splicing factor 3B. The protein encoded by this gene cross-links to a region in the pre-mRNA immediately upstream of the branchpoint sequence in pre-mRNA in the prespliceosomal complex A. It also may be involved in the assembly of the B, C and E spliceosomal complexes. In addition to RNA-binding activity, this protein interacts directly and highly specifically with subunit 2 of the splicing factor 3B. This protein contains two N-terminal RNA-recognition motifs (RRMs), consistent with the observation that it binds directly to pre-mRNA.

# Disease associations
In 2012, Canadian researchers belonging to the FORGE (Finding of Rare disease GEnes) consortium identified new dominant mutations in SF3B4 as the cause of Nager syndrome, a rare type of mandibulofacial dysostosis with associated limb malformations.

# Interactions
SF3B4 has been shown to interact with CDC5L, BMPR1A and SF3B2.
SFRP4
Secreted frizzled-related protein 4 is a protein that in humans is encoded by the SFRP4 gene.

# Function
Secreted frizzled-related protein 4 (SFRP4) is a member of the SFRP family that contains a cysteine-rich domain homologous to the putative Wnt-binding site of Frizzled proteins. SFRPs act as soluble modulators of Wnt signaling. The expression of SFRP4 in ventricular myocardium correlates with apoptosis related gene expression.
SFRP4 is a hub gene in a Type 2 Diabetes-associated gene coexpression module in human islets, and reduces glucose-induced insulin secretion through decreased -cell exocytosis. Expression and release of SFRP4 from islets is enhanced by interleukin-1. SFRP4 is elevated in serum several years before clinical diagnosis of Type 2 Diabetes. Individuals who have above-average levels of SFRP4 in the blood are five times more likely to develop diabetes in the next few years than those with below-average levels.
SFRS7
Serine/arginine-rich splicing factor 7 (SRSF7) also known as splicing factor, arginine/serine-rich 7 (SFRS7) or splicing factor 9G8 is a protein that in humans is encoded by the SRSF7 gene.

# Function
The protein encoded by this gene is a member of the serine/arginine (SR)-rich family of pre-mRNA splicing factors, which constitute part of the spliceosome. Each of these factors contains an RNA recognition motif (RRM) for binding RNA and an RS domain for binding other proteins. The RS domain is rich in serine and arginine residues and facilitates interaction between different SR splicing factors. In addition to being critical for mRNA splicing, the SR proteins have also been shown to be involved in mRNA export from the nucleus and in translation.

# Model organisms
Model organisms have been used in the study of SRSF7 function. A conditional knockout mouse line called Srsf7tm1a(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
SGLT2
The  sodium/glucose cotransporter 2 (SGLT2) is a protein that in humans is encoded by the SLC5A2 (solute carrier family 5 (sodium/glucose cotransporter)) gene.

# Function
SGLT2 is a member of the sodium glucose cotransporter family which are sodium-dependent glucose transport proteins. SGLT2 is the major cotransporter involved in glucose reabsorption in the kidney.

# SGLT2 inhibitors for diabetes
SGLT2 inhibitors are called gliflozins. They lead to a reduction in blood glucose levels. Therefore, SGLT2 inhibitors have potential use in the treatment of type II diabetes. Gliflozins enhance glycemic control as well as reduce body weight and systolic and diastolic blood pressure. They reduce some cardiovascular complications, especially but not exclusively among patients with established cardiovascular disease
The gliflozins canagliflozin, dapagliflozin, and empagliflozin may lead to euglycemic ketoacidosis. Other side effects of gliflozins include increased risk of (generally mild) genital infections, such as candidal vulvovaginitis.

# Clinical significance
Mutations in this gene are also associated with renal glucosuria.

# Model organisms
Model organisms have been used in the study of SLC5A2 function. A conditional knockout mouse line, called Slc5a2tm1a(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 two tests were carried out on homozygous mutant mice and one significant abnormality was observed: males displayed increased drinking behaviour.
SGMS1
Phosphatidylcholine:ceramide cholinephosphotransferase 1 is an enzyme that in humans is encoded by the SGMS1 gene.

# Function
The protein encoded by this gene is predicted to be a five-pass transmembrane protein. This gene may be predominately expressed in brain.

# Model organisms
Model organisms have been used in the study of SGMS1 function. A conditional knockout mouse line called Sgms1tm1a(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