Persius/hicric huggingface dataset:
S100A7
S100 calcium-binding protein A7 (S100A7), also known as psoriasin, is a protein that in humans is encoded by the S100A7 gene.

# Function
S100A7 is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells, and involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100 genes include at least 13 members which are located as a cluster on chromosome 1q21. This protein differs from the other S100 proteins of known structure in its lack of calcium binding ability in one EF-hand at the N-terminus.  The protein functions as a prominent antimicrobial peptide mainly against E. coli.
S100A7 also displays antimicrobial properties. It is secreted by epithelial cells of the skin and is a key antimicrobial protein against Escherichia coli by disrupting their cell membranes. This is the reason that in countries with poor sanitation, human skin is exposed to E. coli strains from faecal matter but it does not usually result in an infection.
S100A7 is highly homologous to S100A15 (koebnerisin) but distinct in expression, tissue distribution and function.

# Clinical significance
This protein is markedly over-expressed in the skin lesions of psoriatic patients, but is excluded as a candidate gene for familial psoriasis susceptibility. The expression of psoriasin is induced in skin wounds through activation of the epidermal growth factor receptor.

# Interactions
S100A7 has been shown to interact with COP9 constitutive photomorphogenic homolog subunit 5, FABP5 and RANBP9.
S100A7 interacts with RAGE (receptor of advanced glycated end products).
SADDAN

# Overview
SADDAN (severe achondroplasia with developmental delay and acanthosis nigricans) is a rare inherited disorder of bone growth characterized by skeletal, brain, and skin abnormalities.
All people with this condition are extremely short with particularly short arms and legs. Other signs and symptoms include unusual bowing of the leg bones; a small chest with short ribs and curved collar bones; short, broad fingers; and folds of extra skin on the arms and legs. Structural abnormalities of the brain lead to seizures, profound developmental delay, and mental retardation. Acanthosis nigricans, a progressive skin disorder characterized by thick, dark, velvety skin, develops in infancy or early childhood. People with SADDAN often live into childhood and adulthood.
Many of the features of SADDAN are similar to those seen in other skeletal disorders, specifically achondroplasia and thanatophoric dysplasia.

# Epidemiology
This disorder is very rare; it has been described in only a small number of individuals worldwide.

# Genetics
Mutations in the FGFR3 gene cause SADDAN. The protein made by the FGFR3 gene is a receptor that plays a role in the development and maintenance of bone and brain tissue. A mutation in the gene may overactivate the receptor, which leads to disturbances in bone growth. Researchers have not determined how the mutation disrupts brain development or causes acanthosis nigricans.
SADDAN is considered an autosomal dominant disorder because one mutated copy of the FGFR3 gene in each cell is sufficient to cause the condition. The few described cases of SADDAN have been caused by new mutations in the FGFR3 gene. No individuals with this disorder are known to have had children; therefore, the disorder has not been passed to the next generation.
SAP130
Histone deacetylase complex subunit SAP130 is an enzyme that in humans is encoded by the SAP130 gene.

# Function
SAP130 is a subunit of the histone deacetylase (see HDAC1; MIM 601241)-dependent SIN3A (MIM 607776) corepressor complex (Fleischer et al., 2003).

# Interactions
SAP130 has been shown to interact with:
- CSN1S1,
- CUL2,
- Myc,
- SIN3A,  and
- Von Hippel-Lindau tumor suppressor and

# Model organisms
Model organisms have been used in the study of SAP130 function. A conditional knockout mouse line called Sap130tm1a(KOMP)Mbp 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
SDHAF2
Succinate dehydrogenase complex assembly factor 2, formerly known as SDH5 and also known as SDH assembly factor 2 or SDHAF2 is a protein that in humans is encoded by the SDHAF2 gene. This gene encodes a mitochondrial protein needed for the flavination of a succinate dehydrogenase complex subunit required for activity of the complex. Mutations in this gene are associated with paraganglioma.

# Structure
SDHAF2 is located on the q arm of Chromosome 11 in position 12.2 and spans 16,642 base pairs. The SDHAF2 gene produces a 6.7 kDa protein composed of 65 amino acids. This highly conserved protein is a cofactor of flavin adenine dinucleotide (FAD). The structure represents a five-helix bundle with a region of well-defined conserved surface residues. This conserved region includes a negatively charged periphery and a positively charged surface, and a patch that is hydrophobic. The region is located in  -helices I, II, and the connecting band.

# Function
The SDHAF2 gene encodes a mitochondrial protein associated with the  succinate dehydrogenase (SDH) complex (mitochondrial complex II) in the mitochondrial respiratory chain, which plays essential roles in both the electron transport chain and the  Krebs(tricarboxylic acid) cycle. SDHAF2 is integral in the proper function of the SDH complex, mainly in SDH-dependent respiration, and interacts with the catalytic subunit of the complex. SDHAF2 participates in the flavination of SDH1(SDHA), another subunit of the  SDH complex. It does so by incorporating the flavin adenine dinucleotide (FAD) cofactor into SDHA. Such flavination is required for a fully functional SDH complex. Knockdown of SDHAF2 leads to the loss-of-function of the SDH complex, a decrease in the enzyme complex stability, and a substantial reduction in all subunits. SDHAF2 was also found to function as a tumor suppressor.

# Clinical significance
SDHAF2 is a tumor suppressor gene. Constitutional mutations in this gene cause hereditary paraganglioma, a neuroendocrine tumor formerly known to be linked to SDH subunit mutations. paraganglioma is a neural crest tumor usually derived from the chemoreceptor tissue of a paraganglion, and may develop at various body sites, including the head, neck, thorax and abdomen. Most commonly, they are located in the head and neck region, specifically at the carotid bifurcation, the jugular foramen, the vagus nerve, and in the middle ear. Phenotypes include excessive catecholamine induced hypertension, dysfunction of major blood vessels and  cranial nerves, significant morbidity, sweating, and palpitations. In cases of extra-adrenal localization, the tumor may turn metastatic and aggressive. Loss of SDH complex function has been known to be responsible for paraganglioma. Mutations in this gene are found in the DNA of only a small fraction of patients with the disease.

# Interactions
SDHAF2 interacts with SDHA within the SDH catalytic dimer. In addition to SDHA, SDHAF2 has 17 protein-protein interactions, including interactions with proteins such as IMMT, SUCLG2, UBINEDDSUMO1, SSX2IP, and others.
SEC16B
Protein transport protein Sec16B also known as regucalcin gene promoter region-related protein p117 (RGPR-p117) and leucine zipper transcription regulator 2 (LZTR2) is a protein that in humans is encoded by the SEC16B gene.

# Discovery
RGPR-p117/SEC16B, which was named as a regucalcin gene promoter region-related protein, was originally discovered as a novel transcription factor that specifically binds to a nuclear factor I (NFI) consensus motif TTGGC(N)6CC that is located on the 5-flanking region of the regucalcin gene (rgn) in 2001. This gene is a highly conserved a leucine zipper motif, and it was also named as the leucine zipper transcription regulator 2 (LZTR2). In 2007, RGPR-p117 was also renamed as Sec16 homologue B (SEC16B), an endoplasmic reticulum export factor.

# Gene
The gene consists of 26 exons spanning approximately 4.1 kbp and is localized on human chromosome 1q25.2. This gene expression is stimulated through various signaling factors in cells. RGPR-p117 is present in the plasma membranes, cytoplasm, mitochondria, microsomes and nucleus of the cells. Cytoplasm RGPR-p117 is translocated to nucleus. Phosphorylated RGPR-p117 specifically binds to the TTGGC motif in the promoter region of various genes to enhance the gene expression of various proteins, and plays a crucial role as a transcription factor in the cells.

# Function
In the role in the regulation of cell regulation, RGPR-p117 possesses protective effects on apoptotic cell death induced by various signaling factors. Overexpression of RGPR-p117 did not cause an alteration of cell proliferation and led to significant decreases in protein and DNA contents in cloned normal rat kidney proximal tubular epithelial NRK52E cells. It also plays a role as an endoplasmic reticulum export factor to deliver to newly synthesized proteins and lipids to the Golgi. RGPR-p117/SEC16B may be involved in human obesity to possess an association between single nucleotide polymorphisms and different measures of obesity.

# Model organisms
Model organisms have been used in the study of SEC16B function. A conditional knockout mouse line, called Sec16btm1a(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 one tests were carried out on mutant mice and one significant abnormality was observed: homozygote mutants had decreased circulating cholesterol levels.
SEC23A
Sec23 homolog A (S. cerevisiae), also known as SEC23A, is a protein which in humans is encoded by the SEC23A gene.

# Function
The protein encoded by this gene is a member of the SEC23 subfamily of the SEC23/SEC24 family. It contains a gelsolin domain. It is part of a protein complex and found in the ribosome-free transitional face of the endoplasmic reticulum (ER) and associated vesicles. This protein has similarity to yeast Sec23p component of COPII. COPII is the coat protein complex responsible for vesicle budding from the ER. The encoded protein is suggested to play a role in the ER-Golgi protein trafficking.
SEC23 interacts with both SEC16A and SEC16B.

# Interactions
SEC23A has been shown to interact with SEC24C, Sec16A/p250 and iPLA1/p125.
Sec23 has also been shown to interact with TRAPPI, Grh1p also known as GRASP65 and Dynactin. Because they are involved in anterograde vesicle transport from ER to Golgi, Sec23 is involved in vesicle transport.
SEC23B
Protein transport protein Sec23B is a protein that in humans is encoded by the SEC23B gene.
The protein encoded by this gene is a member of the SEC23 subfamily of the SEC23/SEC24 family, which is involved in vesicle trafficking. The encoded protein has similarity to yeast Sec23p component of COPII. COPII is the coat protein complex responsible for vesicle budding from the ER. The function of this gene product has been implicated in cargo selection and concentration.
Multiple alternatively spliced transcript variants encoding the same protein have been found for this gene. Mutations in SEC23B cause an autosomal recessive disorder called congenital dyserythropoietic anemia type II (CDAII).
SEC24A
SEC24 family, member A (S. cerevisiae) is a protein that in humans is encoded by the SEC24A gene. The protein belongs to a protein family that are homologous to yeast Sec24. It is a component of coat protein II (COPII)-coated vesicles that mediate protein transport from the endoplasmic reticulum.

# Model organisms
Model organisms have been used in the study of SEC24A function. A conditional knockout mouse line, called Sec24atm1a(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 mutant mice and one significant abnormality was observed. Male homozygotes had decreased circulating cholesterol and LDL cholesterol levels.
SEMA3A
Semaphorin-3A is a protein that in humans is encoded by the SEMA3A gene.

# Function
The SEMA3A gene is a member of the semaphorin family and encodes a protein with an Ig-like C2-type (immunoglobulin-like) domain, a PSI domain and a Sema domain. This secreted Sema3A protein can function as either a chemorepulsive agent, inhibiting axonal outgrowth, or as a chemoattractive agent, stimulating the growth of apical dendrites. In both cases, the protein is vital for normal neuronal pattern development.
Semaphorin-3A is secreted by neurons and surrounding tissue to guide migrating cells and axons in the developing nervous system.  Axon pathfinding is the process by which neurons follow very precise paths, sends out axons, and react to specific chemical environments to reach the correct endpoint. The guidance is critical for the precise formation of neurons and the surrounding vasculature. Guidance cues, such as Sema3A, induce the collapse and paralysis of neuronal growth cones during development of the nervous system.
This guidance cue for axons of neurons is signaled through receptor complexes containing Neuropilin-1 (NRP1) and a co-receptor. One of the first identified intracellular messenger required for the growth cone-collapse induced by Sema3A is the CRMP protein called CRMP2.
In addition to its role in the nervous system, Sema3A also acts as an inhibitor of angiogenesis, the process by which new blood vessels develop.

# Clinical significance
The protein Sema3A is highly expressed in scar tissue after traumatic central nervous system injuries, such as spinal cord injury. Sema3A, and the other class 3 semaphorins, contributes to the failure of neuronal regeneration after CNS injury by regulating axonal re-growth, re-myelination, re-vascularisation, and the immune response.
Increased expression of Sema3A is associated with schizophrenia and is seen in a variety of human tumor cell lines. Also, aberrant release of this protein is associated with the progression of Alzheimer's disease.
Additionally, the terminal Schwann cells of ALS mice (SOD1 mutant) express Sema3A at fast-fatigable fiber neuromuscular junctions greater than wild-type mice. This expression is greatest pre-symptomatically corresponding to ALS progression in which fast-fatigable fiber denervation precedes clinical symptoms. Because Sema3A is involved in growth cone collapse and axon pruning and repulsion, it potentially holds a causal relationship to synaptic weakening and denervation that precedes motor neuron apoptosis in ALS.
SEMA4A
Semaphorin-4A is a protein that in humans is encoded by the SEMA4A gene.

# Function
SEMA4A is a member of the semaphorin family of soluble and transmembrane proteins. Semaphorins are involved in guidance of axonal migration during neuronal development and in immune responses.

# Clinical significance
A germline variant in SEMA4A (V78M) has been demonstrated to confer risk for colorectal cancer type X.
SEMA4D
Semaphorin-4D (SEMA4D) also known as Cluster of Differentiation 100 (CD100), is a protein of the semaphorin family that in humans is encoded by the SEMA4D gene.

# Function
Semaphorin 4D (Sema 4D) is an axon guidance molecule which is secreted by oligodendrocytes and induces growth cone collapse in the central nervous system. By binding plexin B1 receptor it functions as an R-Ras GTPase-activating protein (GAP) and repels axon growth cones in both the mature central nervous system.
In the immune system, CD100 binds CD72 to activate B cells and dendritic cells, though much about this interaction is still under investigation.
During skin damage repairs, SEMA4D interacts with Plexin B2 on gamma delta t cells  to play a role in the healing process.
SEMA5A
Semaphorin-5A is a protein that in humans is encoded by the SEMA5A gene.
Members of the semaphorin protein family, such as SEMA5A, are involved in axonal guidance during neural development (Adams et al., 1996).
Semaphorine 5A also plays a role in autism, reducing the ability of neurons to form connections with other neurons in certain brain regions (Mosca-Boidron et al 2016).
SETBP1
SET binding protein 1 is a protein that in humans is encoded by the SETBP1 gene.

# Gene
The gene is located on Chromosome 18, specifically on the long (q) arm of the chromosome at position 12.3. This is also written as 18q12.3.

# Function
The SETBP1 gene provides instructions for making a protein known as the SET binding protein 1, which is widely distributed throughout somatic cells. The protein is known to bind to another protein called SET. SETBP1 is a DNA-binding protein that forms part of a group of proteins that act together on histone methylation to make chromatin more accessible and regulate gene expression. There is still more to learn about the overall function of the SETBP1 protein 
and the effect of SET binding.

# Clinical significance
Gain-of-function mutations in the SETBP1 gene are associated with SchinzelGiedion syndrome.
Loss-of-function mutations in the SETBP1 gene are associated with a SETBP1-related developmental delay called SETBP1 disorder which causes a spectrum of symptoms including absent speech/expressive language delays, mild-severe intellectual disability, autistic-traits/autism, developmental delays, ADHD, and seizures. 
SETBP1 is a oncogene; specific somatic mutations of this gene were discovered in patients affected by atypical Chronic Myeloid Leukemia (aCML) and related diseases. These mutations, which are identical to the ones present in SGS as germ line mutations, impair the degradation of SETBP1 and therefore cause increased cellular levels of the protein.
SETDB1
Histone-lysine N-methyltransferase SETDB1 is an enzyme that in humans is encoded by the SETDB1 gene.SETDB1 is also known as KMT1E or H3K9 methyltransferase ESET.

# Function
The SET domain is a highly conserved, approximately 150-amino acid motif implicated in the modulation of chromatin structure. It was originally identified as part of a larger conserved region present in the Drosophila Trithorax protein and was subsequently identified in the Drosophila Su(var)3-9 and 'Enhancer of zeste' proteins, from which the acronym SET is derived. Studies have suggested that the SET domain may be a signature of proteins that modulate transcriptionally active or repressed chromatin states through chromatin remodeling activities.

# Model organisms
Model organisms have been used in the study of SETDB1 function. A conditional knockout mouse line, called Setdb1tm1a(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 seven tests were carried out on mutant mice and four 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 and two significant abnormalities were observed. Females had abnormal peripheral blood lymphocytes data and both sexes displayed increased bone strength and mineral content.

# Interactions
SETDB1 has been shown to interact with TRIM28.>
SETMAR
Histone-lysine N-methyltransferase SETMAR is an enzyme that in humans is encoded by the SETMAR gene.

# Model organisms
Model organisms have been used in the study of SETMAR function. A conditional knockout mouse line, called Setmartm1a(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 five tests were carried out on mutant mice and two significant abnormalities were observed. Homozygous mutant animals of both sex had abnormal retinal pigmentation and morphology, while males also had atypical peripheral blood lymphocyte parameters.
SH2D3C
SH2 domain containing 3C, also known as SH2D3C, is a protein that in humans is encoded by the SH2D3C gene.

# Function
Sh2d3c is a gene on human chromosome 9 that encodes an SH2 domain containing protein known as NSP3.  The mouse homologue is found on chromosome 2.  The NSP (Novel SH2-containing Protein) family of proteins contains three members, NSP1, NSP2, and NSP3 (this protein), all of which have a similar architecture, with an N-terminal SH2 domain, a proline serine rich region, which contains consensus sequences for MAP kinase substrates, and a conserved C-terminus, which binds to the Cas family of adapter proteins, and also shows homology to GEF domains.
NSP3 was originally identified by three independent groups of researchers.  The mouse homologue of NSP3 has been shown to have two distinct isoforms, generated by alternative splicing, that are expressed in different tissues.  The shorter isoform, known as Chat (Cas/Hef1 associated signal transducer) is expressed in brain, lung, heart, kidney, muscle, liver, and intestine, while the larger isoform, known as Chat-H (the "H" is for Hematopoietic), is expressed in spleen, thymus, and lymph nodes.  The two isoforms differ only in their N-terminus, which has been shown by one group to be important for membrane localization.
Through its interaction with Hef1, Chat-H, has been shown to be an important regulator of lymphocyte adhesion, acting upstream of Rap1 in the integrin activation pathway.
SH3D21
SH3D21 is a nuclear protein that is encoded by the SH3D21 gene. In humans, this gene is located on chromosome 1 p34.3. The human mRNA transcript is 2527 base pairs and the final protein product is 756 amino acids.   While the exact function of this protein remains unknown, due to the presence of three SH3 domains, it has been implicated in protein-protein interactions.

# Gene
SH3D21 is expressed in low levels in most tissue.  Microarray analysis has shown SH3D21 expression to be decreased in TP63 knockout mice. SH3D21 has been shown to be expressed highly in the superior cervical ganglion, the dorsal root ganglia and the trigeminal ganglion.  Transcription of SH3D21 is known to be upregulated in the presence of testosterone.

# Protein
SH3D21 contains three SH3 domains. These domains are located near the N-terminus of the protein. In humans, these SH3 domains have a common amino acid sequence Asp-Glu-Leu. This sequence motif is also conserved in other species. SH3D21 has been found to interact with Adenylate Kinase 2, Artemin, and Importin 13. The human protein has two isoforms and no paralogs. The second isoform is 645 amino acids long and is identical to the first isoform, except it is missing the first 111 amino acids.  Due to this, the second isoform is missing the first, and half of the second, N-terminal SH3 domain. Secondary structure analysis of SH3D21 indicates a long alpha helical structure near the C-terminus.  The purpose of this structure is unknown. SH3D21 is predicted to have many phosphorylation sites and multiple sumolyation sites throughout the entirety of the protein.

# Function
The function of this gene is still unclear. However, research has linked SH3D21 expression changes to male infertility and Ataxia Telangiectasia.
Further studies have implicated the chromosomal region of 1p34.3 in Intracranial Aneurysm and as a negative prognosis sign in colorectal cancer. These studies do not, however, directly mention SH3D21.

# Homology
SH3D21 is well-conserved in mammals. BLAST analysis found distant orthologs in Osteichthyes with a max identity of 28%. Sequence identity was calculated using available sequence data and ALIGN software.