Persius/hicric huggingface dataset:
RGS14
Regulator of G-protein signaling 14 (RGS14) is a protein that in humans is encoded by the RGS14 gene.

# Function
RGS14 is a member of the regulator of G protein signalling family. This protein contains one RGS domain, two Raf-like Ras-binding domains (RBDs), and one GoLoco motif. The protein attenuates the signaling activity of G-proteins by binding, through its GoLoco domain, to specific types of activated, GTP-bound G alpha subunits. Acting as a GTPase activating protein (GAP), the protein increases the rate of conversion of the GTP to GDP. This hydrolysis allows the G alpha subunits to bind G beta/gamma subunit heterodimers, forming inactive G-protein heterotrimers, thereby terminating the signal. Alternate transcriptional splice variants of this gene have been observed but have not been thoroughly characterized.
Increasing the expression of the RGS14 protein in the V2 secondary visual cortex of mice promotes the conversion of short-term to long-term object-recognition memory. Conversely RGS14 is enriched in CA2 pyramidal neurons and suppresses synaptic plasticity of these synapses and hippocampal-based learning and memory.

# Interactions
RGS14 has been shown to interact with:
- GNAI1 and
- GNAI3.
RGS17
Regulator of G-protein signaling 17 is a protein that in humans is encoded by the RGS17 gene.

# Function
This gene encodes a member of the regulator of G-protein signaling family. This protein contains a conserved, 120 amino acid motif called the RGS domain and a cysteine-rich region. The protein attenuates the signaling activity of G-proteins by binding to activated, GTP-bound G alpha subunits and acting as a GTPase activating protein (GAP), increasing the rate of conversion of the GTP to GDP. This hydrolysis allows the G alpha subunits to bind G beta/gamma subunit heterodimers, forming inactive G-protein heterotrimers, thereby terminating the signal. Along with RGS4, RGS9 and RGS14, RGS17 plays an important role in termination of signalling by mu opioid receptors and development of tolerance to opioid analgesic drugs.

# Clinical significance
RGS17 is a putative lung cancer susceptibility gene in the lung cancer associated locus on chromosome 6q in humans.  RGS17 is overexpressed in lung and prostate cancers, induces cAMP production, CREB phosphorylation and CREB responsive gene expression.  Expression of RGS17 is required for maintenance of  proliferation in lung tumor cell lines.
RGS19
Regulator of G-protein signaling 19 is a protein that in humans is encoded by the RGS19 gene.
G proteins mediate a number of cellular processes. The protein encoded by this gene belongs to the RGS (regulators of G-protein signaling) family and specifically interacts with G protein, GAI3. This protein is a guanosine triphosphatase-activating protein that functions to down-regulate Galpha i/Galpha q-linked signaling.

# Interactions
RGS19 has been shown to interact with GNAO1, GIPC1, OSTM1, GNAI1, GNAI3 and GNAZ.
RGS20
Regulator of G-protein signaling 20 is a protein that in humans is encoded by the RGS20 gene.
Regulator of G protein signaling (RGS) proteins are regulatory and structural components of G protein-coupled receptor complexes. RGS proteins are GTPase-activating proteins for Gi (see GNAI1; MIM 139310) and Gq (see GNAQ; MIM 600998) class G-alpha proteins. They accelerate transit through the cycle of GTP binding and hydrolysis and thereby accelerate signaling kinetics and termination.
In melanocytic cells RGS20 gene expression may be regulated by MITF.

# Interactions
RGS20 has been shown to interact with GNAO1 and GNAZ.
RING1
E3 ubiquitin-protein ligase RING1 is an enzyme that in humans is encoded by the RING1 gene.

# Function
This gene belongs to the RING finger family, members of which encode proteins characterized by a RING domain, a zinc-binding motif related to the zinc finger domain. The gene product can bind DNA and can act as a transcriptional repressor. It is associated with the multimeric polycomb group protein complex. The gene product interacts with the polycomb group proteins BMI1, EDR1, and CBX4, and colocalizes with these proteins in large nuclear domains. It interacts with the CBX4 protein via its glycine-rich C-terminal domain. The gene maps to the HLA class II region, where it is contiguous with the RING finger genes FABGL and HKE4.

# Interactions
RING1 has been shown to interact with CBX8, BMI1 and RYBP.
RIPK3
Receptor-interacting serine/threonine-protein kinase 3 is an enzyme that in humans is encoded by the RIPK3 gene.
The product of this gene is a member of the receptor-interacting protein (RIP) family of serine/threonine protein kinases, and contains a C-terminal domain unique from other RIP family members. The encoded protein is predominantly localized to the cytoplasm, and can undergo nucleocytoplasmic shuttling dependent on novel nuclear localization and export signals. It is a component of the tumor necrosis factor (TNF) receptor-I signaling complex, and can induce apoptosis and weakly activate the NF-kappaB transcription factor.

# Interactions
RIPK3 has been shown to interact with RIPK1 to form an amyloid spine
RIPK5
Dual serine/threonine and tyrosine protein kinase is an enzyme that in humans is encoded by the DSTYK gene.
This protein is also known as the Dusty protein kinase and the Receptor interacting protein 5 (RIP5).
This gene encodes a dual serine/threonine and tyrosine protein kinase which is expressed in multiple tissues. Multiple alternatively spliced transcript variants have been found, but the biological validity of some variants has not been determined.
In melanocytic cells RIPK5 gene expression may be regulated by MITF.
Mutations in this gene have been associated with hereditary spastic paraplegia type 23.
RNF10
RING finger protein 10 is a protein that in humans is encoded by the RNF10 gene.

# Function
The protein encoded by this gene contains a ring finger motif, which is known to be involved in protein-protein interactions. The specific function of this protein has not yet been determined. EST data suggests the existence of multiple alternatively spliced transcript variants, however, their full length nature is not known.

# Model organisms
Model organisms have been used in the study of RNF10 function. A conditional knockout mouse line, called Rnf10tm1a(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 mutant mice and five significant abnormalities were observed. Homozygous mutant animals displayed increased chromosomal stability in a micronucleus test. Females also had increased body weight,  an increased amount of total body fat and an abnormal complete blood count. Males additionally displayed an increase in eating behavior.
ROBO1
Roundabout homolog 1 is a protein that in humans is encoded by the ROBO1 gene.

# Function
Bilateral symmetric nervous systems have special midline structures that establish a partition between the two mirror image halves. Some axons project toward and across the midline in response to long-range chemoattractants emanating from the midline]. In Drosophila, the roundabout gene, a member of the immunoglobulin gene superfamily, encodes an integral membrane protein that is both an axon guidance receptor and a cell adhesion receptor. This receptor is involved in the decision by axons to cross the central nervous system midline. The protein encoded by this gene is structurally similar to the Drosophila roundabout protein. Two transcript variants encoding different isoforms have been found for this gene.

# Clinical significance
ROBO1 was implicated in communication disorder based on a Finnish pedigree with severe dyslexia. Analyses revealed a translocation had occurred disrupting ROBO1. Study of the  phonological memory component of  the language acquisition system suggests that ROBO1 polymorphisms are associated with functioning  in this system.
RPAP2
RNA polymerase II associated protein 2, also known as RPAP2, is a human gene.

# Model organisms
Model organisms have been used in the study of RPAP2 function. A conditional knockout mouse line, called Rpap2tm1a(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 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 additional significant abnormalities were observed in these animals.
RRBP1
Ribosome-binding protein 1, also referred to as p180, is a protein that in humans is encoded by the RRBP1 gene.
RRBP1 is a membrane-bound protein found in the endoplasmic reticulum (ER). It was originally identified as the ribosome receptor for the ER, however several groups later demonstrated that this activity did not co-fractionate with RRBP1  
 but rather with Sec61 (i.e. the translocon). RRBP1 can enhance the association of certain mRNAs to the endoplasmic reticulum in a manner that does not require ribosome activity, likely by directly associating the mRNA's phosphate backbone. In addition, RRBP1 may promote the association of polysomes with the translocon  and play a role in ER morphology. RRBP1 may also bind to microtubules. Although the p180 isoform is the most abundant, it may exist in different forms due to removal of tandem repeats by partial intraexonic splicing. RRBP1 has been excluded as a candidate gene in the cause of Alagille syndrome.
RRM2B
Ribonucleoside-diphosphate reductase subunit M2 B is an enzyme that in humans is encoded by the RRM2B gene. The gene encoding the RRM2B protein is located on chromosome 8, at position 8q23.1. The gene and its products are also known by designations MTDPS8A, MTDPS8B, and p53R2.

# Function
RRM2B codes for one of two versions of the R2 subunit of ribonucleotide reductase, which generates nucleotide precursors required for DNA replication by reducing ribonucleoside diphosphates to deoxyribonucloside diphosphates.  The version of R2 encoded by RRM2B is induced by p53, and is required for normal DNA repair and mtDNA synthesis in non-proliferating cells.  The other form of R2 is expressed only in dividing cells.

# Interactions
RRM2B has been shown to interact with Mdm2 and Ataxia telangiectasia mutated.

# Clinical relevance
Abnormalities in this gene are one of the causes of mitochondrial DNA depletion syndrome (MDDS). Neonatal hypotonia, developmental delay, encephalopathy, with seizures, deafness and lactic acidosis have been associated with mutations in this gene.  MDDS is fatal, with death occurring from respiratory failure in early childhood.
It has been associated with some cases of pediatric acute liver failure.
Mutations in this gene have been shown to cause progressive external ophthalmoplegia.
Increased expression of RRM2B has been correlated with gemcitabine resistance in human cholangiocarcinoma cells and may be predictive of lack of clinical benefit from gemcitabine for human cancers.
RSPO1
R-spondin-1 is a secreted protein that in humans is encoded by the Rspo1 gene, found on chromosome 1.  In humans, it interacts with WNT4 in the process of female sex development.  Loss of function can cause female to male sex reversal.  Furthermore, it promotes canonical WNT/ catenin signaling.

# Structure
The protein has two cysteine-rich, furin-like domains and one thrombospondin type 1 domain.

# Function

## Sex Development

### Early Gonads
RSPO1 is required for the early development of gonads, regardless of sex.  It has been found in mice only eleven days after fertilization.  To induce cell proliferation, it acts synergistically with WNT4.  They help stabilize -catenin, which activates downstream targets.  If both are deficient in XY mice, there is less expression of SRY and a reduction in the amount of SOX9.  Moreover, defects in vascularization are found.  These occurrences result in testicular hypoplasia.  Male to female sex reversal, however, does not occur because Leydig cells remain normal.  They are maintained by steroidogenic cells, now unrepressed.

### Ovaries
RSPO1 is necessary in female sex development.  It augments the WNT/ catenin pathway to oppose male sex development.  In critical gonadal stages, between six and nine weeks after fertilization, the ovaries upregulate it while the testes downregulate it.

## Mucositis
Oral mucosa has been identified as a target tissue for RSPO1.  When administered to normal mice, it causes nuclear translocation of -catenin to this region.  Modulation of the WNT/ catenin pathway occurs through the relief of Dkk1 inhibition.  This occurrence results in increased basal cellularity, thickened mucosa, and elevated epithelial cell proliferation in the tongue.  RSPO1 can therefore potentially aid in the treatment of mucositis, which is characterized by inflammation of the oral cavity.  This unfortunate condition often accompanies chemotherapy and radiation in cancer patients with head and neck tumors.  RSPO1 has also been shown to promote gastrointestinal epithelial cell proliferation in mice.
RSPO3
R-spondin-3 is a protein that in humans is encoded by the RSPO3 gene.

# Function
This gene encodes a member of the thrombospondin type 1 repeat supergene family. In addition, the protein contains a furin-like cysteine-rich region. Furin-like repeat domains have been found in a variety of eukaryotic proteins involved in the mechanism of signal transduction by receptor tyrosine kinases.
During embryonic development, RSPO3 is expressed in the tail bud and the posterior presomitic mesoderm of the embryo. In tissue engineering, R-spondin 3 has been used to differentiate pluripotent stem cells into paraxial mesoderm progenitors
RUNX3
Runt-related transcription factor 3 is a protein that in humans is encoded by the RUNX3 gene.

# Function
This gene encodes a member of the runt domain-containing family of transcription factors. A heterodimer of this protein and a beta subunit forms a complex that binds to the core DNA sequence 5'-YGYGGT-3' found in a number of enhancers and promoters, and can either activate or suppress transcription. It also interacts with other transcription factors. It functions as a tumor suppressor, and the gene is frequently deleted or transcriptionally silenced in cancer. Multiple transcript variants encoding different isoforms have been found for this gene.
In melanocytic cells RUNX3 gene expression may be regulated by MITF.

# Knockout mouse
Runx3 null mouse gastric mucosa exhibits hyperplasia due to stimulated proliferation and suppressed apoptosis in epithelial cells, and the cells are resistant to TGF-beta stimulation.

# The RUNX3 controversy
In 2011 serious doubt was cast over the tumor suppressor function of Runx3 originated from the earlier publication by Li and co-workers.
On the basis of the original study by Li and co-workers (2002), the majority of later literature citing Li and co-workers (2002) assumed that RUNX3 was expressed in the normal gut epithelium and that it is therefore likely to act as a tumor suppressor in the particular epithelial cancer investigated. Most of this literature used RUNX3 promoter methylation status in various cancers as a proxy for its expression. However, quite many genes are known to be methylated in tumor cell genomes, and the majority of these genes are not expressed in the normal tissue of origin of these cancers. Others used poorly characterized (or fully invalidated) antibodies to detect the RUNX3 protein, or used RT-PCR or validated antibodies and failed to detect RUNX3 in the gut epithelium but still did not question the original finding by Li and co-workers (2002). This facts have recently been discussed in a novel by Ulo Maivali.

# Interactions
RUNX3 has been shown to interact with TLE1.
Rad50
DNA repair protein RAD50, also known as RAD50, is a protein that in humans is encoded by the RAD50 gene.

# Function
The protein encoded by this gene is highly similar to Saccharomyces cerevisiae Rad50, a protein involved in DNA double-strand break repair. This protein forms a complex with MRE11 and NBS1 (also known as Xrs2 in yeast). This MRN complex (MRX complex in yeast) binds to broken DNA ends and displays numerous enzymatic activities that are required for double-strand break repair by nonhomologous end-joining or homologous recombination. Gene knockout studies of the mouse homolog of Rad50 suggest it is essential for cell growth and viability. Two alternatively spliced transcript variants of Rad50, which encode distinct proteins, have been reported.

# Structure
Rad50 is a member of the structural maintenance of chromosomes (SMC) family of proteins.  Like other SMC proteins, Rad50 contains a long internal coiled-coil domain that folds back on itself, bringing the N- and C-termini together to form a globular ABC ATPase head domain.  Rad50 can dimerize both through its head domain and through a zinc-binding dimerization motif at the opposite end of the coiled-coil known as the zinc-hook.  Results from atomic force microscopy suggest that in free Mre11-Rad50-Nbs1 complexes, the zinc-hooks of a single Rad50 dimer associate to form a closed loop, while the zinc-hooks snap apart upon binding DNA, adopting a conformation that is thought to enable zinc-hook-mediated tethering of broken DNA ends.

# Interactions
Rad50 has been shown to interact with:
- BRCA1,
- MRE11A,
- NBN,
- RINT1,
- TERF2IP,  and
- TERF2.

# Evolutionary ancestry
Rad50 protein has been mainly studied in eukaryotes.  However, recent work has shown that orthologs of the Rad50 protein are also conserved in extant prokaryotic archaea where they likely function in homologous recombinational repair.  In the hyperthermophilic archeon Sulfolobus acidocaldarius, the Rad50 and Mre11 proteins interact and appear to have an active role in repair of DNA damages introduced by gamma radiation.  These findings suggest that eukaryotic Rad50 may be descended from an ancestral archaeal Rad50 protein that served a role in homologous recombinational repair of DNA damage.
Ramus
Ramus can refer to:
- A portion of a bone (from Latin ramus, "branch"), as in the Ramus mandibul or Superior pubic ramus
- A nerve ramus such as the Dorsal ramus of spinal nerve
- An arterial branch such as the ramus intermedius in the heart
Raphe
A raphe has different uses:

# In science
Pronounced "RAY-fee" Template:IPA), it is most commonly used when describing diatoms, seeds, and human anatomy.
In the field of anatomy, the term refers to a continuous ridge of tissue. There are several different significant raphes:
- The perineal raphe extends from the anus, through the mid-line of the scrotum (scrotal raphe) and upwards through the posterior mid-line aspect of the penis (penile raphe).
- The buccal raphe which is on the cheek and evidence of the fusion of the maxillary and mandibular processes.
- The lingual raphe on the tongue. Obvious physical evidence of the lingual raphe includes the frenulum (also called the frenum), or band of mucous membrane that is visible under the tongue attaching it to the floor of the mouth. If this raphe is too tight at birth, movement of the tongue is restricted and the child is said to be "tongue tied".
- The palatine raphe on the roof of the mouth (or palate). Incomplete fusion of the palatine raphe results in a congenital defect known as cleft palate.
- The pharyngeal raphe is near the pharyngeal constrictors.
- The raphe nucleus is a moderate-size cluster of nuclei found in the brain stem which releases serotonin to the rest of the brain. Selective serotonin reuptake inhibitor (SSRI) antidepressants are believed to act at these nuclei.
- The anococcygeal raphe
- The pterygomandibular raphe
- The lateral palpebral raphe
S100P
S100 calcium-binding protein P (S100P) is a protein that in humans is encoded by the S100P gene.

# Function
The protein encoded by this gene 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; however, this gene is located at 4p16. This protein, in addition to binding Ca2+, also binds Zn2+ and Mg2+. This protein may play a role in the etiology of prostate cancer.

# Interactions
S100P has been shown to interact with EZR  and RAGE. The interactions between S100P and RAGE are disrupted by  cromolyn and pentamidine.
SALL1
Sal-like 1 (Drosophila), also known as SALL1, is a protein which in humans is encoded by the SALL1 gene. As the full name suggests, it is one of the human versions of the spalt (sal) gene known in Drosophila.

# Function
The protein encoded by this gene is a zinc finger transcriptional repressor and may be part of the NuRD histone deacetylase (HDAC) complex.

# Clinical significance
Defects in this gene are a cause of TownesBrocks syndrome (TBS) as well as branchio-oto-renal syndrome (BOR). Two transcript variants encoding different isoforms have been found for this gene.

# Interactions
SALL1 has been shown to interact with TERF1 and UBE2I.
SAP30
Sin3A-associated protein, 30kDa, also known as SAP30, is a protein which in humans is encoded by the SAP30 gene.

# Function
Histone acetylation plays a key role in the regulation of eukaryotic gene expression. Histone acetylation and deacetylation are catalyzed by multisubunit complexes. The protein encoded by this gene is a component of the histone deacetylase complex, which includes SIN3A, SAP18, HDAC1, HDAC2, RbAp46, RbAp48, and other polypeptides. This complex is active in deacetylating core histone octamers, but inactive in deacetylating nucleosomal histones. A pseudogene of this gene is located on chromosome 3.
Mammals have one paralog of SAP30, named SAP30-like (SAP30L), which shares 70% sequence identity with SAP30. SAP30 and SAP30L together constitute a well-conserved SAP30 protein family. Also SAP30L interacts with several components of the Sin3A corepressor complex and induces transcriptional repression via recruitment of Sin3A and histone deacetylases.
Proteins of the SAP30 family (SAP30 proteins) have a functional nucleolar localization signal and they are able to target Sin3A to the nucleolus. SAP30 proteins have sequence-independent contact with DNA by their N-terminal zinc-dependent module and their acidic central region contributes to histone and nucleosome interactions. The DNA binding of SAP30 proteins is regulated by the nuclear signalling lipids, phosphoinositides (PI). SAP30 proteins provide the first example in which the DNA and PIs seem to stand in a mutually antagonizing interrelationship in regard to their interaction with zinc finger proteins and thus exemplifies the molecular mechanism how these lipids can contribute for gene regulation.

# Interactions
SAP30 has been shown to interact with:
- HDAC1,
- Histone deacetylase 2,
- ING1 and
- Nuclear receptor co-repressor 1,
- RBBP4,
- RBBP7,
- SIN3A,  and
- YY1.
SAR1B
SAR1 gene homolog B (S. cerevisiae), also known as SAR1B, is a protein which in humans is encoded by the SAR1B gene.

# Function
SAR1B belongs to the Sar1-ADP ribosylation factor family of small GTPases, which govern the intracellular trafficking of proteins in coat protein (COP)-coated vesicles.

# Clinical significance
Mutations in the SAR1B gene are associated with chylomicron retention disease (also known as Anderson disease) which is an autosomal recessive disorder of severe fat malabsorption.